PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22405765-12 2012 The deposition of safranin O-stained proteoglycans and type II collagen was highly detected in chondrogenic pellets derived from ROCKi-pretreated chondrocytes. phenosafranine 18-28 Rho associated coiled-coil containing protein kinase 1 Homo sapiens 129-134 7721838-16 1995 It is demonstrated here that under optimized compositions of redox agents, including the use of cysteine/cystine and protein disulfide isomerase, the in vitro folding of EGF could be achieved quantitatively within 1 min. Cysteine 96-104 epidermal growth factor Homo sapiens 170-173 7731044-7 1995 The same reaction was detected in the folding of Fab/-cys but an additional rate-limiting step is involved that is due to a unimolecular step in the folding of the isolated light chain. Cysteine 54-57 FA complementation group B Homo sapiens 49-52 7731044-8 1995 This implies that, during Fab reactivation, Fd associates with the light chain at the stage of an earlier folding intermediate, thus eliminating the additional slow folding step of the light chain observed with Fab/-cys. Cysteine 216-219 FA complementation group B Homo sapiens 26-29 7731044-9 1995 Both in Fab and Fab/-cys renaturation, the folding reaction after association is determined by prolyl isomerization. Cysteine 21-24 FA complementation group B Homo sapiens 16-19 7733663-2 1995 Trx1p supports a normal rate of DNA replication only if the active site contains the redox active cysteines. Cysteine 98-107 thioredoxin TRX1 Saccharomyces cerevisiae S288C 0-5 7703236-4 1995 Of the six cysteine residues present in 3-hydroxyisobutyrate dehydrogenase, only cysteine 215 was found to be critical to catalysis. Cysteine 11-19 3-hydroxyisobutyrate dehydrogenase Rattus norvegicus 40-74 7703236-4 1995 Of the six cysteine residues present in 3-hydroxyisobutyrate dehydrogenase, only cysteine 215 was found to be critical to catalysis. Cysteine 81-89 3-hydroxyisobutyrate dehydrogenase Rattus norvegicus 40-74 7703236-8 1995 The present data suggest that 3-hydroxyisobutyrate dehydrogenase differs in mechanism from other short-chain alcohol dehydrogenases studied to date and that cysteine 215 has a critical function in catalysis, possibly as a general base catalyst. Cysteine 157-165 3-hydroxyisobutyrate dehydrogenase Rattus norvegicus 30-64 7713918-7 1995 Analysis of the distribution of Cys residues in aligned sequences of cloned human alpha 1-->3fucosyltransferases indicated one site, Cys143 of FucT-III and Cys156 of FucT-V, corresponded to the highly conservative replacement of Ser178 in FucT-IV, an enzyme insensitive to N-ethylmaleimide. Cysteine 32-35 fucosyltransferase 3 (Lewis blood group) Homo sapiens 146-154 7713918-11 1995 These results support the importance of Ser178 of FucT-IV in donor substrate binding and strongly suggest analogous Cys residues are the GDP-fucose protectable, N-ethylmaleimide-sensitive sites present in FucT-III and -V. Cysteine 116-119 fucosyltransferase 3 (Lewis blood group) Homo sapiens 205-220 7706490-4 1995 The second mutation, located in exon 46, substituted a cysteine proximal to the NC1 domain of COL4A5 for an arginine. Cysteine 55-63 collagen type IV alpha 5 chain Homo sapiens 94-100 7613471-4 1995 The positions of the three free cysteines of factor VIII are the same as three of the four cysteines present in ceruloplasmin. Cysteine 91-100 ceruloplasmin Homo sapiens 112-125 7702578-0 1995 Mutagenic structure/function analysis of the cytoplasmic cysteines of the insulin receptor. Cysteine 57-66 insulin receptor Cricetulus griseus 74-90 7890653-2 1995 A mutant recombinant plasminogen activator inhibitor 1 (PAI-1) was created (Ser-338-->Cys) in which cysteine was placed at the P9 position of the reactive center loop. Cysteine 89-92 serpin family E member 1 Homo sapiens 21-54 7890653-2 1995 A mutant recombinant plasminogen activator inhibitor 1 (PAI-1) was created (Ser-338-->Cys) in which cysteine was placed at the P9 position of the reactive center loop. Cysteine 89-92 serpin family E member 1 Homo sapiens 56-61 7890653-2 1995 A mutant recombinant plasminogen activator inhibitor 1 (PAI-1) was created (Ser-338-->Cys) in which cysteine was placed at the P9 position of the reactive center loop. Cysteine 103-111 serpin family E member 1 Homo sapiens 21-54 7890653-2 1995 A mutant recombinant plasminogen activator inhibitor 1 (PAI-1) was created (Ser-338-->Cys) in which cysteine was placed at the P9 position of the reactive center loop. Cysteine 103-111 serpin family E member 1 Homo sapiens 56-61 7873540-0 1995 Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Cysteine 33-41 aldehyde dehydrogenase 2 family member Rattus norvegicus 63-99 7849038-6 1995 One or both cysteine residues are located at the interface of the Gin dimer, which maps the dimerization domain in the N-terminal part of the protein. Cysteine 12-20 recombinase family protein Escherichia phage Mu 66-69 7849038-8 1995 In the protein-DNA complex, however, oxidation of cysteine residues still seems to be possible, indicating that the N-terminal parts of two Gin subunits are also in close proximity when bound to DNA. Cysteine 50-58 recombinase family protein Escherichia phage Mu 140-143 7856691-5 1995 The de novo secretion of monocyte chemotactic protein-1 in the culture supernatants was analyzed by immunoprecipitation and electrophoresis after metabolic labeling with sulfur 35-labeled cysteine. Cysteine 188-196 C-C motif chemokine ligand 2 Homo sapiens 25-55 7532583-0 1995 Methanethiolation of the liberated cysteine residues of human alpha 2-macroglobulin treated with methylamine generates a derivative with similar functional characteristics as native alpha 2-macroglobulin. Cysteine 35-43 alpha-2-macroglobulin Homo sapiens 62-83 7532583-0 1995 Methanethiolation of the liberated cysteine residues of human alpha 2-macroglobulin treated with methylamine generates a derivative with similar functional characteristics as native alpha 2-macroglobulin. Cysteine 35-43 alpha-2-macroglobulin Homo sapiens 182-203 7532583-1 1995 The thiol-modifying reagent methyl methanethiosulfonate reacts with the cysteine residues of thiol esters released upon treatment of human alpha 2-macroglobulin with methylamine. Cysteine 72-80 alpha-2-macroglobulin Homo sapiens 139-160 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. Cysteine 151-154 natriuretic peptide receptor 3 Homo sapiens 58-63 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. Cysteine 185-188 natriuretic peptide receptor 3 Homo sapiens 58-63 7721952-1 1995 SPARC (secreted protein, acidic and rich in cysteine, also known as osteonectin and BM-40) is a metal-binding glycoprotein secreted by a variety of cultured cells and characteristic of tissues undergoing morphogenesis, remodeling, and repair. Cysteine 44-52 secreted protein acidic and cysteine rich Bos taurus 0-5 7721952-1 1995 SPARC (secreted protein, acidic and rich in cysteine, also known as osteonectin and BM-40) is a metal-binding glycoprotein secreted by a variety of cultured cells and characteristic of tissues undergoing morphogenesis, remodeling, and repair. Cysteine 44-52 secreted protein acidic and cysteine rich Bos taurus 68-79 7721952-1 1995 SPARC (secreted protein, acidic and rich in cysteine, also known as osteonectin and BM-40) is a metal-binding glycoprotein secreted by a variety of cultured cells and characteristic of tissues undergoing morphogenesis, remodeling, and repair. Cysteine 44-52 secreted protein acidic and cysteine rich Bos taurus 84-89 7749197-0 1995 Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines. Cysteine 71-80 RAB5A, member RAS oncogene family Homo sapiens 14-18 7749197-2 1995 We report here that an N-terminal domain contained within the first 22 amino acids of Rab5 is critical for efficient geranylgeranylation of the protein"s C-terminal cysteines. Cysteine 165-174 RAB5A, member RAS oncogene family Homo sapiens 86-90 8600671-3 1995 Recently, germline point-mutations in RET cysteine codons of the extracellular cysteine-rich domain (encoded by exons 10 and 11) and in the tyrosine-kinase domain (encoded by exon 16) at codon 918, have been associated with the syndromes of multiple endocrine neoplasia (MEN) type 2A, MEN type 2B and familial medullary thyroid carcinoma (FMTC). Cysteine 42-50 ret proto-oncogene Homo sapiens 38-41 8600671-3 1995 Recently, germline point-mutations in RET cysteine codons of the extracellular cysteine-rich domain (encoded by exons 10 and 11) and in the tyrosine-kinase domain (encoded by exon 16) at codon 918, have been associated with the syndromes of multiple endocrine neoplasia (MEN) type 2A, MEN type 2B and familial medullary thyroid carcinoma (FMTC). Cysteine 79-87 ret proto-oncogene Homo sapiens 38-41 8600671-7 1995 In all 19 MEN 2A patients we found RET germline point-mutations either at cysteine codons 634 (14), 630 (1) in exon 11 or at codon 618 (4) in exon 10. Cysteine 74-82 ret proto-oncogene Homo sapiens 35-38 7524561-4 1994 We have identified 2 cysteines in the NR1 subunit that are required for redox modulation of NMDA-gated currents in oocytes expressing NR1-NR2B, NR1-NR2C, or NR1-NR2D receptors. Cysteine 21-30 glutamate ionotropic receptor NMDA type subunit 2D Homo sapiens 161-165 7945308-1 1994 Members of the Wnt gene family code for cysteine-rich, secreted proteins, which are differentially expressed in the developing brain and possibly act as an intercellular signaling molecule. Cysteine 40-48 Wnt family member 4 Gallus gallus 15-18 8090735-5 1994 The guest molecule is bound by the R-state monomer through the formation of two hydrogen bonds from the hydroxy group of Tylenol to the carbonyl oxygen and the nitrogen of A6 Cys and A11 Cys, respectively. Cysteine 187-190 DXS435E Homo sapiens 183-186 7520910-3 1994 Replacement of Gly166 and Tyr167 in this epitope of the substance P receptor by the corresponding substance K receptor amino acids (Cys and Phe) increases the affinity toward substance P 2-fold and toward substance K and neurokinin B 11- and 21-fold, respectively. Cysteine 132-135 tachykinin receptor 1 Homo sapiens 56-76 7520910-3 1994 Replacement of Gly166 and Tyr167 in this epitope of the substance P receptor by the corresponding substance K receptor amino acids (Cys and Phe) increases the affinity toward substance P 2-fold and toward substance K and neurokinin B 11- and 21-fold, respectively. Cysteine 132-135 tachykinin precursor 3 Homo sapiens 221-233 8082776-1 1994 cDNAs encoding for two isoforms of O-acetylserine (thiol) lyase (OAS-TL), which catalyzes the synthesis of cysteine, have been isolated from Arabidopsis thaliana. Cysteine 107-115 O-acetylserine (thiol) lyase (OAS-TL) Arabidopsis thaliana 35-63 7810879-4 1994 The concentration of phenylacetylglutamine is calculated from the natural 13C signals of all carbons of its benzene ring and C-2 of its acetyl moiety. Cysteine 27-33 complement C2 Homo sapiens 125-128 8080280-1 1994 Triosephosphate isomerase from rabbit has 5 Cys and 2 Met, while triosephosphate isomerase from yeast has 2 Cys (present in the rabbit enzyme in equivalent positions) and no Met. Cysteine 44-47 triosephosphate isomerase Oryctolagus cuniculus 0-25 8080280-1 1994 Triosephosphate isomerase from rabbit has 5 Cys and 2 Met, while triosephosphate isomerase from yeast has 2 Cys (present in the rabbit enzyme in equivalent positions) and no Met. Cysteine 44-47 triosephosphate isomerase Oryctolagus cuniculus 65-90 8080280-1 1994 Triosephosphate isomerase from rabbit has 5 Cys and 2 Met, while triosephosphate isomerase from yeast has 2 Cys (present in the rabbit enzyme in equivalent positions) and no Met. Cysteine 108-111 triosephosphate isomerase Oryctolagus cuniculus 0-25 8080280-1 1994 Triosephosphate isomerase from rabbit has 5 Cys and 2 Met, while triosephosphate isomerase from yeast has 2 Cys (present in the rabbit enzyme in equivalent positions) and no Met. Cysteine 108-111 triosephosphate isomerase Oryctolagus cuniculus 65-90 8080280-4 1994 An initial effect of chloramine-T on triosephosphate isomerase was the oxidation of Cys and the formation of catalytically active acidic isoforms. Cysteine 84-87 triosephosphate isomerase Oryctolagus cuniculus 37-62 8062268-7 1994 administration of TGF alpha-delta Cys-PE40 via an osmotic minipump at a dose of 0.4 microgram/g/day over 7 days inhibited MDA-468, MA-231, and BT-20 but not MCF-7 tumor growth in female athymic mice. Cysteine 34-37 transforming growth factor alpha Mus musculus 18-27 8080215-7 1994 Anti-Rmp blocking antibodies may harbor specificity for OmpA sequences shared with other neisserial species or Enterobacteriaceae or may be directed against unique Rmp upstream cysteine loop specific sequences, or both. Cysteine 177-185 URI1 prefoldin like chaperone Homo sapiens 5-8 8049267-1 1994 Full-length clones encoding a novel member of the metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family of proteins have been isolated from a monkey (Macaca fascicularis) testicular cDNA library. Cysteine 92-100 C-C motif chemokine ligand 22 Rattus norvegicus 107-110 8051084-2 1994 The regulatory domain of protein kinase C gamma (PKC gamma) contains the following functional elements which can interact with lipids: the pseudosubstrate motif within the first variable region (V1), cysteine-rich domains, Cys1 and Cys2 which contain zinc and bind phorbol dibutyrate (PDBu)/diacylglycerol, and the calcium-dependent lipid binding domain (CaLB). Cysteine 200-208 protein kinase C gamma Homo sapiens 25-47 8051084-2 1994 The regulatory domain of protein kinase C gamma (PKC gamma) contains the following functional elements which can interact with lipids: the pseudosubstrate motif within the first variable region (V1), cysteine-rich domains, Cys1 and Cys2 which contain zinc and bind phorbol dibutyrate (PDBu)/diacylglycerol, and the calcium-dependent lipid binding domain (CaLB). Cysteine 200-208 protein kinase C gamma Homo sapiens 49-58 8068046-3 1994 The cysteine adduct (SCC) of 2-chloroethyl isocyanate (CEIC) was a strong inhibitor of GR (27 +/- 1% activity remaining after a 1-hr incubation at 0.1 mM) and was essentially equipotent with the antitumor agent N,N"-bis(2-chloroethyl)-N-nitrosourea (BCNU). Cysteine 4-12 glutathione-disulfide reductase Rattus norvegicus 87-89 7948687-1 1994 Apocytochrome c derived from horse heart cytochrome c was spin-labeled on the cysteine residue at position 14 or 17 in the N-terminal region of the primary sequence, and cytochrome c from yeast was spin-labeled on the single cysteine residue at sequence position 102 in the C-terminal region. Cysteine 78-86 cytochrome c, somatic Equus caballus 3-15 7948687-6 1994 On binding to dioleoylphosphatidylglycerol, the labeled cysteine residue in yeast cytochrome c is located closest to the phospholipid headgroups but possibly between the polar group region and the 5-C atom of the acyl chains. Cysteine 56-64 cytochrome c, somatic Equus caballus 82-94 8055960-5 1994 The aim of this study was to characterize the involvement of the four cysteine-rich repeats of the human p55 TNF receptor in TNF and LT binding by both membrane-bound and soluble forms of the receptor. Cysteine 70-78 TNF receptor superfamily member 1A Homo sapiens 105-108 7987299-1 1994 Mutations in FMTC and MEN 2A exclusively affect cysteine residues in exon 10 and 11 of RET, whereas in MEN 2B codon 918 in exon 16 is involved. Cysteine 48-56 ret proto-oncogene Homo sapiens 22-28 7987299-1 1994 Mutations in FMTC and MEN 2A exclusively affect cysteine residues in exon 10 and 11 of RET, whereas in MEN 2B codon 918 in exon 16 is involved. Cysteine 48-56 ret proto-oncogene Homo sapiens 87-90 8035816-7 1994 Analysis of mutants indicated that p56lck was nearly quantitatively palmitoylated at Cys-5 but not palmitoylated at Cys-3. Cysteine 85-88 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 35-41 8035816-8 1994 The nonpalmitoylated cysteine at position 3 was very important for association of p56lck with the membrane fraction, while palmitoylation at Cys-5 promoted only a low level of interaction. Cysteine 21-29 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 82-88 7972490-2 1994 The cDNA library was made from poly(A)+ RNA from leaves challenged with mercuric chloride for 2 d. The two clones, pCh2 and pCh11, appear to encode class I chitinase isoforms with cysteine-rich domains (not found in pCh11 due to the incomplete sequence) and proline-/glycine-rich or proline-rich hinge domains, respectively. Cysteine 180-188 chitinase chem 5 Zea mays 156-165 7933622-8 1994 We have also found that ADF/hTRX promotes L-cysteine transport into the cells and increases intracellular GSH content, indicating the close association between ADF/hTRX and GSH systems. Cysteine 42-52 thioredoxin Homo sapiens 24-27 7933622-8 1994 We have also found that ADF/hTRX promotes L-cysteine transport into the cells and increases intracellular GSH content, indicating the close association between ADF/hTRX and GSH systems. Cysteine 42-52 thioredoxin Homo sapiens 28-32 7933622-8 1994 We have also found that ADF/hTRX promotes L-cysteine transport into the cells and increases intracellular GSH content, indicating the close association between ADF/hTRX and GSH systems. Cysteine 42-52 thioredoxin Homo sapiens 160-163 7933622-8 1994 We have also found that ADF/hTRX promotes L-cysteine transport into the cells and increases intracellular GSH content, indicating the close association between ADF/hTRX and GSH systems. Cysteine 42-52 thioredoxin Homo sapiens 164-168 7518927-1 1994 The prolactin (PRL) receptor is a member of the family of cytokine receptors that lack intrinsic tyrosine kinase activity but contain two conserved cysteines in their N-terminal regions and a WSXWS motif adjacent to their transmembrane domains. Cysteine 148-157 prolactin receptor Rattus norvegicus 4-28 8043603-7 1994 Characterization of the chimeric enzymes revealed that residues between residues 54-110 and 229-317, namely, Val-55 and/or Ala-81, and Arg-242 and/or Cys-264 of PRS I also contribute to the strong GDP inhibition. Cysteine 150-153 phosphoribosyl pyrophosphate synthetase 1 Rattus norvegicus 161-166 8043603-9 1994 Regarding the physical properties, chimeric enzymes bearing residues 12-53 of PRS I were stable at 49 degrees C and with digestion with papain and proteinase K. Our observations suggest that Lys-17, Ile-18, and/or Cys-40 of PRS I contribute to stability of the enzyme. Cysteine 214-217 phosphoribosyl pyrophosphate synthetase 1 Rattus norvegicus 78-83 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Cysteine 143-149 serpin family C member 1 Homo sapiens 200-216 8033888-3 1994 We have replaced the amino acids at these two positions by cysteine in Saccharomyces cerevisiae iso-1-cytochrome c; in an earlier study, Cys102 was replaced by threonine without negatively influencing the physical or enzymic properties of the protein. Cysteine 59-67 threonine ammonia-lyase ILV1 Saccharomyces cerevisiae S288C 96-101 7518463-1 1994 Recent work has demonstrated that p56lck, a member of the Src family of protein tyrosine kinases (PTKs), is modified by palmitoylation of a cysteine residue(s) within the first 10 amino acids of the protein (in addition to amino-terminal myristoylation that is a common modification of the Src family of PTKs). Cysteine 140-148 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 34-40 7518463-4 1994 Individual replacement of the two cysteine residues within the first 10 amino acids of p59fyn and p56lck with serine indicated that Cys3 was the major determinant of palmitoylation, as well as association of the PTK with glycosyl-phosphatidylinositol-anchored proteins. Cysteine 34-42 FYN proto-oncogene, Src family tyrosine kinase Homo sapiens 87-93 7518463-4 1994 Individual replacement of the two cysteine residues within the first 10 amino acids of p59fyn and p56lck with serine indicated that Cys3 was the major determinant of palmitoylation, as well as association of the PTK with glycosyl-phosphatidylinositol-anchored proteins. Cysteine 34-42 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 98-104 7515969-0 1994 The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins. Cysteine 4-7 Mdv1p Saccharomyces cerevisiae S288C 50-54 7515969-0 1994 The Cys-His motif of Ty3 NC can be contributed by Gag3 or Gag3-Pol3 polyproteins. Cysteine 4-7 Mdv1p Saccharomyces cerevisiae S288C 58-62 7968721-3 1994 In the arthritic patient it is proposed that there is an inappropriate amount of a copper donor form of ceruloplasmin which contains a reduced copper that was formed during ceruloplasmin"s oxidation of plasma cysteine. Cysteine 209-217 ceruloplasmin Homo sapiens 104-117 7968721-3 1994 In the arthritic patient it is proposed that there is an inappropriate amount of a copper donor form of ceruloplasmin which contains a reduced copper that was formed during ceruloplasmin"s oxidation of plasma cysteine. Cysteine 209-217 ceruloplasmin Homo sapiens 173-186 7911344-8 1994 Time-course studies of nine patients after Cy +/- granulocyte-macrophage CSF (GM-CSF) showed that CD34+ cells, CFCs, and LTC-ICs fell from normal to undetectable levels after Cy, and increased at the time of white blood cell (WBC) recovery: LTC-ICs to a mean of sixfold and CFCs to a mean of 26-fold higher than normal. Cysteine 43-47 colony stimulating factor 2 Homo sapiens 78-84 7922028-10 1994 The conformational change between oxidized and reduced human thioredoxin is very small and localized to areas in spatial proximity to the redox active cysteines. Cysteine 151-160 thioredoxin Homo sapiens 61-72 7515061-9 1994 A minireceptor containing the cluster of eight complement-type cysteine-rich repeats followed by four epidermal growth factor precursor homologous domains binds and internalizes 125I-labeled plasminogen activator-PAI-1 complexes. Cysteine 63-71 serpin family E member 1 Homo sapiens 213-218 7514405-0 1994 The role of cysteine-949 in the binding of transforming growth factor-beta 1 and transforming growth factor-beta 2 to alpha 2-macroglobulin. Cysteine 12-20 alpha-2-macroglobulin Homo sapiens 118-139 7514405-2 1994 The resulting free Cys residues (Cys-949) contain the only free thiol groups in alpha 2M. Cysteine 19-22 alpha-2-macroglobulin Homo sapiens 80-88 7514405-2 1994 The resulting free Cys residues (Cys-949) contain the only free thiol groups in alpha 2M. Cysteine 33-36 alpha-2-macroglobulin Homo sapiens 80-88 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. Cysteine 173-176 alpha-2-macroglobulin Homo sapiens 98-106 7514405-7 1994 These studies demonstrate that Cys-949 in alpha 2M is not essential for binding of TGF-beta 1 and TGF-beta 2 noncovalently; however, this residue plays a critical role in the covalent stabilization step of the reaction mechanism. Cysteine 31-34 alpha-2-macroglobulin Homo sapiens 42-50 7909779-12 1994 CONCLUSIONS: Extracellular GSH protects cultured gastric cells from H2O2 damage by accelerating intracellular GSH synthesis; this is mediated by membrane-bound gamma-glutamyl transpeptidase acting on extracellular GSH (which supplies these cells with cysteine) and then by intracellular gamma-glutamylcysteine synthetase. Cysteine 251-259 gamma-glutamyltransferase 1 Rattus norvegicus 160-189 8151774-5 1994 Our results indicate that the portion of the cytoplasmic domain required for the down-regulation of CD4 by Nef overlaps with the binding site of p56lck, but the cysteine residues which are essential for the association of CD4 with p56lck are not required. Cysteine 161-169 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 231-237 8178437-5 1994 Excluding the predicted N-terminal signal sequences, 8 of 9 potential N-linked glycosylation sites and all 10 cysteine residues in gB-1 are conserved in both gB-2 and gB-3. Cysteine 110-118 alpha 1,4-galactosyltransferase (P blood group) Homo sapiens 167-171 7908986-1 1994 A search for co-ordinated amino acid changes in the hsp60 family of chaperonins suggested that cysteine residues at positions 137 and 518 in the Escherichia coli chaperonin GroEL may interact with each other. Cysteine 95-103 chaperonin GroEL Escherichia coli 162-178 8163468-0 1994 Site-directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin. Cysteine 41-50 thioredoxin Homo sapiens 60-71 8163468-0 1994 Site-directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin. Cysteine 41-50 thioredoxin Homo sapiens 113-124 8163468-0 1994 Site-directed mutagenesis of active site cysteines in human thioredoxin produces competitive inhibitors of human thioredoxin reductase and elimination of mitogenic properties of thioredoxin. Cysteine 41-50 thioredoxin Homo sapiens 113-124 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Cysteine 109-112 serpin family C member 1 Homo sapiens 37-49 8045680-4 1994 The antigen belongs to the three-disulfide epidermal growth factor (EGF) family based on the alignment of the six cysteines. Cysteine 114-123 epidermal growth factor Homo sapiens 43-66 8045680-4 1994 The antigen belongs to the three-disulfide epidermal growth factor (EGF) family based on the alignment of the six cysteines. Cysteine 114-123 epidermal growth factor Homo sapiens 68-71 8045680-5 1994 In the K1 strain there are, however, only four cysteines corresponding to the four carboxyl cysteines of EGF. Cysteine 47-56 epidermal growth factor Homo sapiens 105-108 8045680-10 1994 The other contains an EGF-like, three-disulfide [Cys-9,14]VK-50 peptide. Cysteine 49-52 epidermal growth factor Homo sapiens 22-25 8045680-13 1994 The specific pairing pattern of 1-3, 2-4 and 5-6 in [Cys 9,14]VK-50 corresponding to EGF in [Cys 9,14]VK-50 was obtained using a "knowledge-based" (KB) strategy for their formation. Cysteine 53-56 epidermal growth factor Homo sapiens 85-88 8045680-13 1994 The specific pairing pattern of 1-3, 2-4 and 5-6 in [Cys 9,14]VK-50 corresponding to EGF in [Cys 9,14]VK-50 was obtained using a "knowledge-based" (KB) strategy for their formation. Cysteine 93-96 epidermal growth factor Homo sapiens 85-88 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. Cysteine 22-31 Cuticle collagen sqt-1 Caenorhabditis elegans 35-40 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Cysteine 98-106 serpin family C member 1 Homo sapiens 4-20 8017095-1 1994 Employing the Fmoc solid phase strategy, analogues of pituitary adenylate cyclase activating polypeptide (PACAP) were synthesized containing single cysteine residues. Cysteine 148-156 adenylate cyclase activating polypeptide 1 Sus scrofa 54-112 7510758-1 1994 A radioimmunoassay specific for the C-terminus of human prothymosin alpha was developed using the synthetic peptide [Cys-Aca degrees]-human prothymosin alpha (90-109)-OH coupled to KLH as antigen and the analogue [Tyr-Aca degrees]-human prothymosin alpha (90-109)-OH labelled with 125I as tracer. Cysteine 117-120 prothymosin alpha pseudogene 9 Homo sapiens 56-73 7510758-1 1994 A radioimmunoassay specific for the C-terminus of human prothymosin alpha was developed using the synthetic peptide [Cys-Aca degrees]-human prothymosin alpha (90-109)-OH coupled to KLH as antigen and the analogue [Tyr-Aca degrees]-human prothymosin alpha (90-109)-OH labelled with 125I as tracer. Cysteine 117-120 prothymosin alpha pseudogene 9 Homo sapiens 140-157 7510758-1 1994 A radioimmunoassay specific for the C-terminus of human prothymosin alpha was developed using the synthetic peptide [Cys-Aca degrees]-human prothymosin alpha (90-109)-OH coupled to KLH as antigen and the analogue [Tyr-Aca degrees]-human prothymosin alpha (90-109)-OH labelled with 125I as tracer. Cysteine 117-120 prothymosin alpha pseudogene 9 Homo sapiens 140-157 8125086-5 1994 Although at least one of the binding sites of this protein resides within the cysteine-rich domain of dystrophin, a contribution of additional amino acid residues within the first half of the C-terminal domain was also suggested for more secure binding. Cysteine 78-86 dystrophin Homo sapiens 102-112 8125086-8 1994 Previously, based on the enzyme digestion experiments, we showed that the binding site for the glycoprotein complex on dystrophin is present within the cysteine-rich domain and the first half of the C-terminal domain [Suzuki, A., Yoshida, M., Yamamoto, H. & Ozawa, E. (1992) FEBS Lett. Cysteine 152-160 dystrophin Homo sapiens 119-129 8125121-5 1994 Downstream of the basic region, another cysteine-rich motif (C-X2-C-X13-C-X9-C), a putative zinc-finger, was found to be well conserved in the PARP of Sarcophaga, Drosophila and human. Cysteine 40-48 Poly-(ADP-ribose) polymerase Drosophila melanogaster 143-147 7509297-2 1994 To determine the role of the thiol ester in the folding of human alpha 2-macroglobulin (alpha 2M) in the active conformation, we have characterized a recombinant variant of alpha 2M, C949S, expressed in baby hamster kidney cells, that lacks the thiol ester-forming cysteine. Cysteine 265-273 alpha-2-macroglobulin Homo sapiens 173-181 7509599-2 1994 IGFBP-3 contains vicinal cysteines in sequence which is similar to the active sites in thioredoxin and protein disulfide isomerase. Cysteine 25-34 insulin like growth factor binding protein 3 Homo sapiens 0-7 7509599-2 1994 IGFBP-3 contains vicinal cysteines in sequence which is similar to the active sites in thioredoxin and protein disulfide isomerase. Cysteine 25-34 thioredoxin Homo sapiens 87-98 8203728-0 1994 Biotinylated and cysteine-modified peptides as useful reagents for studying the inhibition of cathepsin G. Cysteine 17-25 cathepsin G Homo sapiens 94-105 8112293-8 1994 Results from experiments with a CD4 construct containing mutations of the cysteine residues which are responsible for association of CD4 with p56lck demonstrate that p56lck is implicated in the transduction of the signal negatively regulating HIV replication. Cysteine 74-82 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 142-148 8112293-8 1994 Results from experiments with a CD4 construct containing mutations of the cysteine residues which are responsible for association of CD4 with p56lck demonstrate that p56lck is implicated in the transduction of the signal negatively regulating HIV replication. Cysteine 74-82 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 166-172 8313381-4 1994 From the fact that preincubation of GST P1-1 with 1-chloro-2,4-dinitrobenzene reduced the incorporation of [14C]EA from 0.94 +/- 0.21 (SD) to 0.16 +/- 0.02 mol EA/mol subunit and from automated Edman degradation of the major radioactive peptide isolated after pepsin digestion of the [14C]EA-labeled enzyme, it was concluded that the reaction of EA takes place with cysteine 47 of GST P1-1. Cysteine 366-374 glutathione S-transferase pi 1 Homo sapiens 36-44 7508914-3 1994 In this work, we expressed [35S]cysteine-labeled recombinant pro-MSP in MSP cDNA-transfected Chinese hamster ovary cells and studied proteolytic processing of pro-MSP and the requirement of cleavage for biological activity. Cysteine 32-40 macrophage stimulating 1 Homo sapiens 65-68 7508914-3 1994 In this work, we expressed [35S]cysteine-labeled recombinant pro-MSP in MSP cDNA-transfected Chinese hamster ovary cells and studied proteolytic processing of pro-MSP and the requirement of cleavage for biological activity. Cysteine 32-40 macrophage stimulating 1 Homo sapiens 72-75 7508914-3 1994 In this work, we expressed [35S]cysteine-labeled recombinant pro-MSP in MSP cDNA-transfected Chinese hamster ovary cells and studied proteolytic processing of pro-MSP and the requirement of cleavage for biological activity. Cysteine 32-40 macrophage stimulating 1 Homo sapiens 72-75 7911697-2 1994 The majority of MEN 2A and familial medullary thyroid carcinoma results from missense mutations within one of five cysteine codons in the extracellular domain of the RET proto-oncogene. Cysteine 115-123 ret proto-oncogene Homo sapiens 16-22 7911697-2 1994 The majority of MEN 2A and familial medullary thyroid carcinoma results from missense mutations within one of five cysteine codons in the extracellular domain of the RET proto-oncogene. Cysteine 115-123 ret proto-oncogene Homo sapiens 166-169 8169523-6 1994 Mouse apoJ contains six potential N-glycosylation sites, a potential Arg-Ser cleavage site to generate alpha and beta subunits, a cluster of five cysteine residues in each subunit, three putative amphipathic helices, and four potential heparin-binding domains. Cysteine 146-154 clusterin Mus musculus 6-10 8290256-5 1994 Two mutations were identified in the p53 cDNA from HC11 cells: a missense mutation at codon 138, substituting Trp for Cys, and a microdeletion, codon 123 to 130, of exon 5. Cysteine 118-121 C-C motif chemokine ligand 2 Homo sapiens 51-55 8114938-6 1994 Mutations in the extracellular cysteine-rich domain of Ret have been identified previously in patients with multiple endocrine neoplasia type 2A, and a targeted mutation in the tyrosine kinase domain of the same gene produces intestinal aganglionosis and kidney agenesis in homozygous transgenic mice. Cysteine 31-39 ret proto-oncogene Homo sapiens 55-58 7906866-6 1994 All mutations occurred within codons specifying cysteine residues in the transition point between the RET protein extracellular and transmembrane domains. Cysteine 48-56 ret proto-oncogene Homo sapiens 102-105 8300622-2 1994 It also associates with the Torpedo M(r) 87,000 postsynaptic protein (87K), the core of which is a superdomain homologous to the cysteine-rich (CR) and COOH-terminal (CT) domains of human dystrophin. Cysteine 129-137 dystrophin Homo sapiens 188-198 8300628-3 1994 A glutathione S-transferase fusion protein containing the second cysteine-rich region, Cys2, of PKC gamma with bound zinc with a stoichiometry of 1.8 +/- 0.1 mol of zinc/mol of protein. Cysteine 65-73 protein kinase C gamma Homo sapiens 96-105 8300628-6 1994 Both represent the ultimate residues of a 50-amino acid consensus motif with six conserved cysteines and two conserved histidines present in the cysteine-rich regions of all PKC isoforms. Cysteine 91-100 protein kinase C gamma Homo sapiens 174-177 8300628-6 1994 Both represent the ultimate residues of a 50-amino acid consensus motif with six conserved cysteines and two conserved histidines present in the cysteine-rich regions of all PKC isoforms. Cysteine 91-99 protein kinase C gamma Homo sapiens 174-177 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. Cysteine 126-134 lactotransferrin Bos taurus 163-174 7584011-9 1994 RET, a transmembrane receptor protein, has a large glycosylated extracellular domain containing clustered cysteine residues and calcium-binding motifs, a single hydrophobic transmembrane domain, and a cytoplasmic domain with tyrosine kinase catalytic activity. Cysteine 106-114 ret proto-oncogene Homo sapiens 0-3 7584011-10 1994 Several germline missense mutations in a codon specifying one of these highly conserved cysteine residues have been detected in patients affected with MEN-2A. Cysteine 88-96 ret proto-oncogene Homo sapiens 151-157 8119654-3 1994 When the mice were treated with CY alone, the total number of cells, and NK and LAK precursor cell activities per spleen were reduced to the nadir on day 3, and they eventually recovered, reaching normal levels on day 7. Cysteine 32-34 alpha-kinase 1 Mus musculus 80-83 7981713-4 1994 This point mutation results in an amino acid change from glutamic acid to lysine at amino acid residue 119 in the third repeat of the cysteine-rich ligand binding domain of the mature LDL receptor. Cysteine 134-142 low density lipoprotein receptor Homo sapiens 184-196 8019555-2 1994 An A-to-G transition was detected which leads to an exchange of a tyrosine by a cysteine in the SRY protein. Cysteine 80-88 sex determining region Y Homo sapiens 96-99 8138354-4 1994 Upon direct sequence analysis of intact bovine insulin, the PTH derivatives of cystine from both Cys-A7 and Cys-B7 were significantly released after Edman cycle 7 and gave approximately 20% recovery of common PTH amino acids. Cysteine 97-100 insulin Bos taurus 47-54 7620223-4 1994 Site-directed mutagenesis of the active-site cysteines of thioredoxin has shown that redox activity is necessary for the stimulation of cell proliferation. Cysteine 45-54 thioredoxin Homo sapiens 58-69 7764619-1 1994 In order to examine the role of cysteine (Cys)-rich domains in the accumulation of maize (Zea mays L.) gamma-zein within the endoplasmic-reticulum-derived protein bodies, we studied the localization of gamma-zein and of two truncated forms of gamma-zein in Xenopus laevis oocytes. Cysteine 32-40 prolamin 50 kDa gamma zein Zea mays 103-113 7764619-1 1994 In order to examine the role of cysteine (Cys)-rich domains in the accumulation of maize (Zea mays L.) gamma-zein within the endoplasmic-reticulum-derived protein bodies, we studied the localization of gamma-zein and of two truncated forms of gamma-zein in Xenopus laevis oocytes. Cysteine 42-45 prolamin 50 kDa gamma zein Zea mays 103-113 14731825-2 1994 Dystrophin-related proteins are identical or homologous to the cysteine-rich and C-terminal domains of dystrophin. Cysteine 63-71 dystrophin Homo sapiens 0-10 14731825-2 1994 Dystrophin-related proteins are identical or homologous to the cysteine-rich and C-terminal domains of dystrophin. Cysteine 63-71 dystrophin Homo sapiens 103-113 8128610-8 1994 Three Cys residues are conserved in all compared mature IL-2 molecules. Cysteine 6-9 interleukin 2 Mus musculus 56-60 8260505-11 1993 The higher pKa of the meta I to meta II transition in gecko P521 compared to a rod pigment like bovine rhodopsin (pKa = 6.4) probably is due to a cysteine residue at position 211 in gecko rather than a histidine residue in bovine rhodopsin. Cysteine 146-154 rhodopsin Bos taurus 103-112 8262047-2 1993 ACE1 and AMT1 are "copper-fist" transcription factors which possess a conserved cysteine-rich copper binding domain required for DNA binding. Cysteine 80-88 Cup2p Saccharomyces cerevisiae S288C 0-4 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. Cysteine 107-115 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. Cysteine 107-115 glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis 155-203 7903251-5 1993 These cysteine residues in the putative extracellular domain of the NR1 subunit may form a disulfide bridge important for agonist interaction. Cysteine 6-14 glutamate ionotropic receptor NMDA type subunit 1 L homeolog Xenopus laevis 68-71 7505617-8 1993 A sugar chain of human G-CSF, by standing close by Cys-17, may prevent free radicals from attacking the deprotonated sulfhydryl group. Cysteine 51-54 colony stimulating factor 3 Homo sapiens 23-28 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-. Cysteine 202-205 glutaredoxin-1 Bos taurus 0-12 8258344-2 1993 HLA-B27, which sequencing predicts has a free cysteine at position 67, reacts rapidly with the positively charged thiol reagent monobromotrimethyl-ammoniobimane bromide (qBBr) to give products which are identifiable by isoelectric focusing. Cysteine 46-54 major histocompatibility complex, class I, B Homo sapiens 0-7 8307321-3 1993 Three mutations in sqt-1 and one in rol-6 that cause dominant right-handed helical twisting (RRol) of animals are arginine to cysteine replacements. Cysteine 126-134 Cuticle collagen sqt-1 Caenorhabditis elegans 19-24 8307321-6 1993 In contrast, three sqt-1 mutations that cause recessive left-handed helical twisting (LRol) are replacements of a conserved carboxy-terminal cysteine residue with either tyrosine or serine. Cysteine 141-149 Cuticle collagen sqt-1 Caenorhabditis elegans 19-24 8245130-5 1993 The NH2-terminal 408 residues, unique to fibulin-2, showed no sequence homology to other known proteins and presumably form two additional domains that differ in their cysteine content. Cysteine 168-176 fibulin 2 Mus musculus 41-50 8298464-1 1993 The two sulfur-containing amino acids, methionine and cysteine, occur frequently among functional alleles in random mutant libraries of Saccharomyces cerevisiae iso-1-cytochrome c genes at positions that form a weakly polar aromatic-aromatic interaction, the wild-type protein. Cysteine 54-62 threonine ammonia-lyase ILV1 Saccharomyces cerevisiae S288C 161-166 8142620-5 1993 RBTN1/Ttg-1 and RBTN2/Ttg-2 encode related proteins consisting of two cysteine-rich regions called LIM domains. Cysteine 70-78 LIM domain only 1 Homo sapiens 0-5 8142620-5 1993 RBTN1/Ttg-1 and RBTN2/Ttg-2 encode related proteins consisting of two cysteine-rich regions called LIM domains. Cysteine 70-78 LIM domain only 1 Homo sapiens 6-11 7916692-6 1993 Chicken SPARC can be defined by four sequence signatures: (a) a conserved spacing of 11 cysteine residues in domain II, (b) the pentapeptide KKGHK in domain II, which is contained within a larger region of 31 identical residues, (c) a 100% conserved region of 10 residues in domain III, and (d) a C-terminal, calcium-binding EF-hand motif. Cysteine 88-96 secreted protein acidic and cysteine rich Gallus gallus 8-13 8226909-2 1993 Like other Ras-related proteins, Rab5 is prenylated on C-terminal cysteine residues, although it lacks the typical C-terminal CAAX motif (where A is any aliphatic amino acid and X is any amino acid) to direct this post-translational modification. Cysteine 66-74 RAB5A, member RAS oncogene family Homo sapiens 33-37 7902568-8 1993 The mutation at position 723, which changes the amino acid sequence from Arg to Cys at residue 220, showed complete association with the PGM1 2/1 protein polymorphism: DNA from individuals showing the PGM1 1 isozyme carried the Arg codon CGT, whereas individuals showing the PGM1 2 isozyme carried the Cys codon TGT. Cysteine 80-83 phosphoglucomutase 1 Homo sapiens 137-141 7902568-8 1993 The mutation at position 723, which changes the amino acid sequence from Arg to Cys at residue 220, showed complete association with the PGM1 2/1 protein polymorphism: DNA from individuals showing the PGM1 1 isozyme carried the Arg codon CGT, whereas individuals showing the PGM1 2 isozyme carried the Cys codon TGT. Cysteine 80-83 phosphoglucomutase 1 Homo sapiens 201-205 7902568-8 1993 The mutation at position 723, which changes the amino acid sequence from Arg to Cys at residue 220, showed complete association with the PGM1 2/1 protein polymorphism: DNA from individuals showing the PGM1 1 isozyme carried the Arg codon CGT, whereas individuals showing the PGM1 2 isozyme carried the Cys codon TGT. Cysteine 80-83 phosphoglucomutase 1 Homo sapiens 201-205 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. Cysteine 101-109 myosin light chain 2 Homo sapiens 45-65 8226834-9 1993 Instead, mutants containing cysteines in the NH2-terminal domain formed intermolecular disulfide bonds between the two heads of myosin. Cysteine 28-37 myosin heavy chain 14 Homo sapiens 128-134 8099202-7 1993 Further, 19 of these 20 mutations affect the same conserved cysteine residue at the boundary of the RET extracellular and transmembrane domains. Cysteine 60-68 ret proto-oncogene Homo sapiens 100-103 8363656-4 1993 We have found that the cysteine-rich, carboxyl-terminal region of the MSP-1 protein from the rodent malarial parasite Plasmodium yoelii yoelii can be expressed in a native configuration as a fusion protein in Escherichia coli. Cysteine 23-31 salivary protein electrophoretic 1, regulator Mus musculus 70-75 7684381-0 1993 P-selectin is acylated with palmitic acid and stearic acid at cysteine 766 through a thioester linkage. Cysteine 62-70 selectin P Homo sapiens 0-10 8506140-4 1993 For the EcoRII methyltransferase, it has been shown that substitution of this catalytic cysteine by glycine is cytotoxic to E.coli cells expressing the mutant methyltransferase (Wyszynski et al. Cysteine 88-96 EcoRII methyltransferase Escherichia coli 8-32 8214349-1 1993 Significance of a cysteine-rich domain for functional expression of dystrophin protein. Cysteine 18-26 dystrophin Homo sapiens 68-78 8214349-3 1993 From the polymerase chain reaction and immunochemical analysis data, the expressed dystrophin protein was predicted to lack the portion comprising the tail of the rod-like domain, the cysteine-rich domain, and the head of the C-terminal domain. Cysteine 184-192 dystrophin Homo sapiens 83-93 8214349-4 1993 These results indicated the functional importance of the cysteine-rich domain in the dystrophin protein. Cysteine 57-65 dystrophin Homo sapiens 85-95 8491377-6 1993 Analysis of DNA binding by deletion mutants of EBF identified an amino-terminal cysteine-rich DNA-binding domain lacking obvious sequence similarity to known transcription factors. Cysteine 80-88 EBF transcription factor 1 Homo sapiens 47-50 8097110-11 1993 It appears that cysteine-73 is responsible for the abstraction of the C-2 hydrogen from (R)-glutamate and cysteine-184 abstracts the proton from (S)-glutamate in the racemization reaction of the wild-type enzyme. Cysteine 16-24 complement C2 Homo sapiens 70-73 8385131-2 1993 Like most members of the G-protein-coupled receptor superfamily, the primary structure of the alpha 2AAR possesses a putative consensus sequence for palmitoylation in the COOH terminus at Cys-442. Cysteine 188-191 adrenoceptor alpha 2A Canis lupus familiaris 94-104 8484715-1 1993 Activity of the cysteine adducts of the cysteine proteinases papain and thaumatopain can be recovered by treatment with thioredoxin, thioredoxin reductase and NADPH. Cysteine 16-24 thioredoxin Homo sapiens 120-131 8484715-1 1993 Activity of the cysteine adducts of the cysteine proteinases papain and thaumatopain can be recovered by treatment with thioredoxin, thioredoxin reductase and NADPH. Cysteine 16-24 peroxiredoxin 5 Homo sapiens 133-154 7680388-0 1993 Mutation of a cysteine residue in polyomavirus middle T antigen abolishes interactions with protein phosphatase 2A, pp60c-src, and phosphatidylinositol-3 kinase, activation of c-fos expression, and cellular transformation. Cysteine 14-22 FBJ osteosarcoma oncogene Mus musculus 176-181 8385052-3 1993 All Cys residues previously found in mature u-PA and u-PAR from these different species are also conserved in the bovine molecules. Cysteine 4-7 plasminogen activator, urokinase Bos taurus 44-48 7680577-5 1993 Cys-949, being one constituent of the internal thiol ester site of members of the family of proteins related to alpha 2-macroglobulin, is an Asn-residue in hen egg-white ovostatin, but the other constituent, Gln-952, is preserved. Cysteine 0-3 alpha-2-macroglobulin Homo sapiens 112-133 8449215-8 1993 It was found that the generation of IFN-gamma pc in normal BN and Lewis splenocyte cultures was strongly dependent on GSH or its precursor cysteine in the culture medium. Cysteine 139-147 interferon gamma Rattus norvegicus 36-45 8432869-3 1993 The loss of 18 amino acids and the change of 6 amino acids, including a cysteine at position 80 in the carboxy terminus of beta 2-mu, are likely to cause marked changes in the structure of the polypeptide. Cysteine 72-80 beta-2-microglobulin Homo sapiens 123-132 8422260-6 1993 Cys-containing hFSH-beta-(33-53) and hFSH-beta-(81-95) did not increase influx of extracellular calcium over basal levels, whereas [Ser-51]-hFSH-beta-(33-53) and [Ser-82, 84, 87, 94]-hFSH-beta-(81-95) induced 2.8- and 1.8-fold increases, respectively. Cysteine 0-3 follicle stimulating hormone subunit beta Homo sapiens 15-24 8419339-3 1993 The enzyme attaches farnesyl groups to cysteines in p21ras and other proteins that contain cysteine residues at the fourth position from the COOH terminus. Cysteine 39-48 HRas proto-oncogene, GTPase Rattus norvegicus 52-58 8419339-3 1993 The enzyme attaches farnesyl groups to cysteines in p21ras and other proteins that contain cysteine residues at the fourth position from the COOH terminus. Cysteine 39-47 HRas proto-oncogene, GTPase Rattus norvegicus 52-58 7677994-0 1993 The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel. Cysteine 33-41 aquaporin 1 (Colton blood group) S homeolog Xenopus laevis 53-59 7677994-7 1993 These studies demonstrated: (i) CHIP28 water channel activity is retained despite substitution of individual cysteines with serine; (ii) cysteine 189 is the Hg(2+)-sensitive residue; (iii) the subunits of the CHIP28 complex are individually active water pores; (iv) residue 189 is critical to proper processing of the CHIP28 protein. Cysteine 109-118 aquaporin 1 (Colton blood group) S homeolog Xenopus laevis 209-215 7509109-3 1993 A strong EPR signal is observed from the dye in solution or when specifically attached to myosin following irradiation in the presence of dithiothreitol or cysteine. Cysteine 156-164 myosin heavy chain 14 Homo sapiens 90-96 7678970-7 1993 The results are consistent with a proposed molecular model of the two env regions which predicts the presence, within the C5 region of gp120, of a large intramolecular pocket that is contacted by the gp41 cysteine loop. Cysteine 205-213 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 135-140 7907856-2 1993 The mechanism of PAP nephrotoxicity has not been fully elucidated, although it has been suggested to involve glutathione (GSH)-dependent S-conjugation followed by processing by the enzyme gamma-glutamyl transpeptidase (gamma GT) to the corresponding cysteine S-conjugate. Cysteine 250-258 gamma-glutamyltransferase 1 Rattus norvegicus 188-217 7907856-2 1993 The mechanism of PAP nephrotoxicity has not been fully elucidated, although it has been suggested to involve glutathione (GSH)-dependent S-conjugation followed by processing by the enzyme gamma-glutamyl transpeptidase (gamma GT) to the corresponding cysteine S-conjugate. Cysteine 250-258 gamma-glutamyltransferase 1 Rattus norvegicus 219-227 8454579-8 1993 (2) The remaining disulfide linkage linked Cys 31 of one subunit to Cys 31 of the second subunit of M-CSF. Cysteine 43-46 colony stimulating factor 1 Homo sapiens 100-105 8454579-8 1993 (2) The remaining disulfide linkage linked Cys 31 of one subunit to Cys 31 of the second subunit of M-CSF. Cysteine 68-71 colony stimulating factor 1 Homo sapiens 100-105 8419942-1 1993 Previously, bovine rhodopsin has been shown to be palmitoylated at cysteine residues 322 and 323. Cysteine 67-75 rhodopsin Bos taurus 19-28 1334106-10 1992 However, a comparison of the splice sites within the regions encoding the respective ligand-binding domains of the CD27 and nerve growth factor receptor genes identifies the archetypal cysteine-rich building blocks, from which the members of this family may have arisen during the course of evolution. Cysteine 185-193 CD27 molecule Homo sapiens 115-119 1334106-10 1992 However, a comparison of the splice sites within the regions encoding the respective ligand-binding domains of the CD27 and nerve growth factor receptor genes identifies the archetypal cysteine-rich building blocks, from which the members of this family may have arisen during the course of evolution. Cysteine 185-193 nerve growth factor receptor Homo sapiens 124-152 1460023-4 1992 Substitution of the putative fatty acylation sites, cysteines 3 and 4, abolished membrane association as well as [3H]palmitic acid labeling of neuromodulin. Cysteine 52-61 neuromodulin Cricetulus griseus 143-155 1447205-0 1992 P-domains as shuffled cysteine-rich modules in integumentary mucin C.1 (FIM-C.1) from Xenopus laevis. Cysteine 22-30 Integumentary mucin C.1 Xenopus laevis 72-79 1284248-0 1992 Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing non-collagenous segments. Cysteine 137-145 adrenoceptor alpha 1D Homo sapiens 74-86 1427856-7 1992 However, despite this high homology, the predicted feline ARSB polypeptide has nine cysteine residues, while the human enzyme has eight. Cysteine 84-92 arylsulfatase B Homo sapiens 58-62 1427856-8 1992 The presence of the extra cysteine residue at position 451 in the feline enzyme may explain why feline ARSB is a homodimer and the human enzyme is a monomer. Cysteine 26-34 arylsulfatase B Homo sapiens 103-107 1501882-1 1992 rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region. Cysteine 123-131 RAP1A, member of RAS oncogene family Homo sapiens 0-11 1501882-1 1992 rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region. Cysteine 123-131 H3 histone pseudogene 16 Homo sapiens 16-19 1501882-1 1992 rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region. Cysteine 123-131 H3 histone pseudogene 16 Homo sapiens 25-28 1325644-1 1992 Tissue-type plasminogen activator (t-PA) reacts upon exposure to endothelium-derived relaxing factor (EDRF) by way of the enzyme"s single free sulfhydryl (Cys-83) to form a stable S-nitrosothiol protein adduct. Cysteine 155-158 alpha hemoglobin stabilizing protein Homo sapiens 65-100 1325644-1 1992 Tissue-type plasminogen activator (t-PA) reacts upon exposure to endothelium-derived relaxing factor (EDRF) by way of the enzyme"s single free sulfhydryl (Cys-83) to form a stable S-nitrosothiol protein adduct. Cysteine 155-158 alpha hemoglobin stabilizing protein Homo sapiens 102-106 1412509-3 1992 The GSH adduct of EA (EA-GSH) was the most potent inhibitor of GSTs; EA-GSH was approximately one order of magnitude more potent than the parent EA, while L-cysteine conjugate of EA (EA-cysteine) and N-acetyl-L-cysteine conjugate of EA (EA-mercapturate) were approximately two orders of magnitude less potent than the parent EA. Cysteine 155-165 glutathione S-transferase kappa 1 Homo sapiens 63-67 1387320-4 1992 Both Ig have a carboxy (C)-terminal domain (C gamma 3*) which contains genetically introduced cysteine residues. Cysteine 94-102 immunoglobulin heavy constant gamma 3 (G3m marker) Homo sapiens 44-54 1512231-2 1992 Bovine rhodopsin has been reported to be S-palmitylated at cysteines 322 and 323 (Ovchinnikov, Y. Cysteine 59-68 rhodopsin Bos taurus 7-16 1512231-6 1992 Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327). Cysteine 205-208 rhodopsin Bos taurus 7-16 1512231-10 1992 These results prove the modification of cysteines 322 and 323 with palmitic acid in bovine rhodopsin, and illustrate the utility of mass spectrometry to characterize the post-translational modifications in G-protein coupled receptors. Cysteine 40-49 rhodopsin Bos taurus 91-100 1637185-0 1992 Site-directed mutagenesis of glutathione S-transferase YaYa: functional studies of histidine, cysteine, and tryptophan mutants. Cysteine 94-102 hematopoietic prostaglandin D synthase Rattus norvegicus 29-54 1637185-1 1992 The rat cytosolic glutathione S-transferase Ya subunit contains three histidine residues (at positions 8, 143, and 159), two cysteine residues (at positions 18 and 112), and a single tryptophan residue (at position 21). Cysteine 125-133 hematopoietic prostaglandin D synthase Rattus norvegicus 18-43 1637185-2 1992 Histidine, cysteine, and tryptophan have been proposed to be present either near or at the active site of other glutathione S-transferase subunits. Cysteine 11-19 hematopoietic prostaglandin D synthase Rattus norvegicus 112-137 1637185-7 1992 These results indicate that histidine, cysteine, and tryptophan in the glutathione S-transferase Ya subunit are not essential for catalysis nor are they involved in the binding of heme to the YaYa homodimer. Cysteine 39-47 hematopoietic prostaglandin D synthase Rattus norvegicus 71-96 1323835-5 1992 The extracellular portion of human PTP zeta contains two striking structural features: the N-terminal 280-amino acid sequence that is homologous to carbonic anhydrases (carbonate hydro-lyase, EC 4.2.1.1), and a sequence of 1048 amino acids without a cysteine residue. Cysteine 250-258 protein tyrosine phosphatase receptor type Z1 Homo sapiens 35-43 1380160-2 1992 This transcript, approximately 4.5 kb long, corresponds to the cysteine-rich and carboxyl-terminal domains of dystrophin. Cysteine 63-71 dystrophin Homo sapiens 110-120 1380167-5 1992 The sequence was found to correspond to that of a tryptic peptide of the EGF receptor beginning with Gly-85, which is in domain I, a region N terminal to the first cysteine-rich region of the receptor. Cysteine 164-172 epidermal growth factor Mus musculus 73-76 1508666-0 1992 Thioredoxin regulates the DNA binding activity of NF-kappa B by reduction of a disulphide bond involving cysteine 62. Cysteine 105-113 thioredoxin Homo sapiens 0-11 1508666-3 1992 DNA binding activity of the wild type protein but not the amino acid 62 mutant was also stimulated by thioredoxin while detection of disulphide cross linked dimers in p50 but not the amino acid 62 mutant suggests that thioredoxin stimulates DNA binding by reduction of a disulphide bond involving cysteine 62. Cysteine 297-305 thioredoxin Homo sapiens 218-229 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 0-3 thioredoxin Homo sapiens 29-32 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 0-3 thioredoxin Homo sapiens 39-50 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 0-3 thioredoxin Homo sapiens 123-134 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 103-106 thioredoxin Homo sapiens 29-32 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 103-106 thioredoxin Homo sapiens 39-50 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 103-106 thioredoxin Homo sapiens 113-116 1510657-4 1992 Cys-31 at the active site of ADF/human thioredoxin proved essential for reducing activity, and loss of Cys-31 in ADF/human thioredoxin attenuated the protein-refolding activity. Cysteine 103-106 thioredoxin Homo sapiens 123-134 1329679-1 1992 The spondylitis associated HLA-B27 epitope includes a characteristic unpaired cysteine at amino acid position 67. Cysteine 78-86 major histocompatibility complex, class I, B Homo sapiens 27-34 1530290-4 1992 LAK cell-accumulation (% dose/g) at the tumor site was only 2.7% in untreated mice and 19.7 in CY-treated mice. Cysteine 95-97 alpha-kinase 1 Mus musculus 0-3 1279778-5 1992 Amylase synthesis rate did not change during the 1st h of incubation but decreased slightly when incubated for 2 h. Incubation of pancreatic lobules with dbcAMP (1 mM) for 1 h also stimulated the incorporation of cysteine into lipase and colipase by 21% and 25%, respectively, whereas incubation with dbcGMP had no effect on the synthesis rates of lipase and colipase. Cysteine 213-221 lipase G, endothelial type Rattus norvegicus 240-246 1321599-7 1992 Two cysteines in PPA2 and one in the S. pombe enzyme are located at the catalytic cleft. Cysteine 4-13 inorganic diphosphatase PPA2 Saccharomyces cerevisiae S288C 17-21 1322127-5 1992 In contrast, when serine was substituted for the last cysteine in the RAS extension, transfer of the [3H]farnesyl group from [3H] farnesyl pyrophosphate to the modified Ub-cRAS was not observed. Cysteine 54-62 ubiquitin Oryctolagus cuniculus 169-171 1333237-6 1992 In the case either of excimer formation or of ground-state pyrene-pyrene interactions in doubly labelled gelsolin molecules, the modified Cys residues must be in close proximity in the folded protein structure. Cysteine 138-141 gelsolin Equus caballus 105-113 1644864-2 1992 Since the glycoprotein SPARC (secreted protein, acidic and rich in cysteine) is associated with remodeling, cellular migration, and angiogenesis in vitro, we questioned whether SPARC might influence the motility of endothelial cells. Cysteine 67-75 secreted protein acidic and cysteine rich Bos taurus 23-28 1283687-1 1992 Cysteine 949 and glutamine 952 are known to be part of the thiol ester site of each of the four subunits of human alpha 2-macroglobulin (alpha 2M). Cysteine 0-8 alpha-2-macroglobulin Homo sapiens 114-135 1283687-1 1992 Cysteine 949 and glutamine 952 are known to be part of the thiol ester site of each of the four subunits of human alpha 2-macroglobulin (alpha 2M). Cysteine 0-8 alpha-2-macroglobulin Homo sapiens 137-145 1333414-0 1992 The amino-terminal fragment of gelsolin is cross-linked to Cys-374 of actin in the EGTA-resistant actin-gelsolin complex. Cysteine 59-62 GSN Sus scrofa 31-39 1333414-0 1992 The amino-terminal fragment of gelsolin is cross-linked to Cys-374 of actin in the EGTA-resistant actin-gelsolin complex. Cysteine 59-62 GSN Sus scrofa 104-112 1333414-1 1992 It has been shown that the EGTA-resistant actin, one of the two actin molecules associated to gelsolin, can be predominantly cross-linked to gelsolin by benzophenone-4-maleimide (BPM), a photoaffinity-labeling reagent, which was conjugated to Cys-374 of actin prior to cross-linking (Doi, Y., Banba, M. and Vertut-Doi, A. Cysteine 243-246 GSN Sus scrofa 94-102 1333414-1 1992 It has been shown that the EGTA-resistant actin, one of the two actin molecules associated to gelsolin, can be predominantly cross-linked to gelsolin by benzophenone-4-maleimide (BPM), a photoaffinity-labeling reagent, which was conjugated to Cys-374 of actin prior to cross-linking (Doi, Y., Banba, M. and Vertut-Doi, A. Cysteine 243-246 GSN Sus scrofa 141-149 1554726-13 1992 The stabilization of a thiolate anion at physiological pH can be explained by the interaction of the S gamma of Cys-32 with the amide of Cys-35 observed in the previously determined high-resolution solution structure of reduced human thioredoxin [Forman-Kay, J. D., Clore, G. M., Wingfield, P. T., & Gronenborn, A. M. (1991) Biochemistry 30, 2685-2698]. Cysteine 112-115 thioredoxin Homo sapiens 234-245 1554726-13 1992 The stabilization of a thiolate anion at physiological pH can be explained by the interaction of the S gamma of Cys-32 with the amide of Cys-35 observed in the previously determined high-resolution solution structure of reduced human thioredoxin [Forman-Kay, J. D., Clore, G. M., Wingfield, P. T., & Gronenborn, A. M. (1991) Biochemistry 30, 2685-2698]. Cysteine 137-140 thioredoxin Homo sapiens 234-245 1550123-7 1992 Proband 1 was homoallelic for a T-to-C transition in nucleotide (nt) 349, which predicted a cysteine-to-arginine substitution in the ASB polypeptide at residue 117 (C117R). Cysteine 92-100 arylsulfatase B Homo sapiens 133-136 1375018-0 1992 Sulphydryl reactivity of the HLA-B27 epitope: accessibility of the free cysteine studied by flow cytometry. Cysteine 72-80 major histocompatibility complex, class I, B Homo sapiens 29-36 1375018-1 1992 HLA-B27 has an unpaired cysteine on or near its serologically defined spondylitis associated epitope, and it has been argued that its sulphydryl side chain may be chemically reactive. Cysteine 24-32 major histocompatibility complex, class I, B Homo sapiens 0-7 1377655-3 1992 The novel transcript shares with dystrophin most of the sequence coding for the cysteine-rich and C-terminal domains. Cysteine 80-88 dystrophin Homo sapiens 33-43 1377655-4 1992 Here we used cDNA cloning to identify the divergence point between the common region and the sequence unique to the novel mRNA at the 5" end of the sequence encoding the cysteine-rich domain of dystrophin. Cysteine 170-178 dystrophin Homo sapiens 194-204 1555584-4 1992 The cleavage sites for alpha-chymotrypsin are located in or near to the EF-hand domain IV of calcium-depleted BM-40 (also known as SPARC, i.e. secreted protein acidic and rich in cysteine, and osteonectin). Cysteine 179-187 secreted protein acidic and cysteine rich Homo sapiens 110-115 1555584-4 1992 The cleavage sites for alpha-chymotrypsin are located in or near to the EF-hand domain IV of calcium-depleted BM-40 (also known as SPARC, i.e. secreted protein acidic and rich in cysteine, and osteonectin). Cysteine 179-187 secreted protein acidic and cysteine rich Homo sapiens 131-136 1346974-11 1992 5-CLA-PBGS is shown to be modified at cysteine-223 on half of the subunits. Cysteine 38-46 selectin P ligand Homo sapiens 2-5 1740442-1 1992 p21ras and several other ras-related GTP-binding proteins are modified post-translationally by addition of 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenoids to cysteines within a conserved carboxyl-terminal sequence motif, Caa(M/S/L), where a is an aliphatic amino acid. Cysteine 169-178 HRas proto-oncogene, GTPase Homo sapiens 0-6 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. Cysteine 12-15 G protein subunit gamma 7 Bos taurus 63-71 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. Cysteine 19-22 G protein subunit gamma 7 Bos taurus 63-71 1419069-2 1992 As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2. Cysteine 20-23 interleukin 2 Mus musculus 38-51 1419069-2 1992 As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2. Cysteine 20-23 interleukin 2 Mus musculus 53-57 1419069-2 1992 As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2. Cysteine 20-23 interleukin 2 Mus musculus 209-213 1419069-2 1992 As the nonessential Cys-140 of murine interleukin 2 (mIL2) is located in the hydrophobic interface of the amphiphilic F domain it was successfully used to stabilize hydrophobic amino acid contacts between two mIL2 cores yielding biologically active cystine-bonded dimeric mIL2. Cysteine 20-23 interleukin 2 Mus musculus 209-213 1301946-0 1992 Clustering of fibrillin (FBN1) missense mutations in Marfan syndrome patients at cysteine residues in EGF-like domains. Cysteine 81-89 fibrillin 1 Homo sapiens 25-29 1480032-0 1992 The latency of the human fibroblast collagenase precursor depends on an internal cysteine residue. Cysteine 81-89 matrix metallopeptidase 1 Homo sapiens 25-47 1939117-1 1991 smg p21B, a member of the ras p21-like small GTP-binding protein superfamily, undergoes post-translational modifications, which are geranylgeranylation of the cysteine residue in the C-terminal region followed by removal of the three C-terminal amino acids (QLL) and the subsequent carboxyl methylation of the exposed prenylated cysteine residue. Cysteine 159-167 H3 histone pseudogene 16 Homo sapiens 4-7 1939117-1 1991 smg p21B, a member of the ras p21-like small GTP-binding protein superfamily, undergoes post-translational modifications, which are geranylgeranylation of the cysteine residue in the C-terminal region followed by removal of the three C-terminal amino acids (QLL) and the subsequent carboxyl methylation of the exposed prenylated cysteine residue. Cysteine 329-337 H3 histone pseudogene 16 Homo sapiens 4-7 1953663-2 1991 The co-operative binding of myosin subfragment 1 (S1) to reconstituted skeletal-muscle thin filaments has been examined by monitoring the fluorescence of a pyrene probe on Cys-374 of actin. Cysteine 172-175 myosin heavy chain 14 Homo sapiens 28-34 1936989-9 1991 Substitution of serine for cysteine in each of the putative fingers abolishes RME1 function; serine substitutions in the second and third putative fingers do not affect RME1 stability. Cysteine 27-35 Rme1p Saccharomyces cerevisiae S288C 78-82 1656067-5 1991 The env genes of CAEV-63 and CAEV-Co encode 28 conserved cysteines and 25 conserved potential N-linked glycosylation sites. Cysteine 57-66 envelope polyprotein;trans-regulatory splicing-like protein Caprine arthritis encephalitis virus 4-7 1957313-5 1991 2-Br-3-(CYS)HQ and 2-Br-5&6-(CYS)HQ caused increases in the biochemical indices of nephrotoxicity at doses between 50 and 150 mumol/kg whereas 2-Br-5-(NAC)HQ and 2-Br-6-(NAC)HQ required doses of 150-200 mumol/kg to cause smaller, though significant increases in urinary glucose, gamma-GT, and LDH excretion. Cysteine 8-11 gamma-glutamyltransferase 1 Rattus norvegicus 283-291 1957313-5 1991 2-Br-3-(CYS)HQ and 2-Br-5&6-(CYS)HQ caused increases in the biochemical indices of nephrotoxicity at doses between 50 and 150 mumol/kg whereas 2-Br-5-(NAC)HQ and 2-Br-6-(NAC)HQ required doses of 150-200 mumol/kg to cause smaller, though significant increases in urinary glucose, gamma-GT, and LDH excretion. Cysteine 33-36 gamma-glutamyltransferase 1 Rattus norvegicus 283-291 1834643-3 1991 Since myosin also binds to actin in the vicinity of Cys-374 and since caldesmon inhibits actomyosin ATPase activity by the reduction of myosin binding to actin, then the inhibition might be by caldesmon sterically hindering or blocking myosin"s interaction with actin. Cysteine 52-55 myosin heavy chain 14 Homo sapiens 6-12 1930211-0 1991 Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: characterization and their catalytic activities. Cysteine 52-60 myoglobin Homo sapiens 20-29 1918072-10 1991 Six of the 56 cysteine residues that are conserved within the extracellular domains of beta 1, beta 2, beta 3, beta 5, beta 6, and the beta subunit from Drosophila are absent in the beta 8 polypeptide. Cysteine 14-22 myospheroid Drosophila melanogaster 87-117 1918082-0 1991 Engineered cysteine mutants of myosin light chain 2. Cysteine 11-19 myosin light chain 2 Homo sapiens 31-51 1918082-2 1991 Site-directed mutagenesis has been used to insert cysteine residues at specific locations in the myosin light chain 2 (LC2) sequence. Cysteine 50-58 myosin light chain 2 Homo sapiens 97-117 1924354-6 1991 These observations indicate that the amino acid occupying the terminal position (Xaa) in the Cys-Ali-Ali-Xaa motif constitutes a key structural feature by which Ha-ras p21 and other proteins with ras-like COOH-terminal isoprenylation sites are distinguished as substrates for farnesyl- or geranylgeranyltransferases. Cysteine 93-96 H3 histone pseudogene 16 Homo sapiens 168-171 1655274-4 1991 Moreover, the phosphatase activity of the cdc25 protein is eliminated by treatment with N-ethylmaleimide or by alteration of a single conserved cysteine residue by site-directed mutagenesis. Cysteine 144-152 cell division cycle 25C Homo sapiens 42-47 1658333-2 1991 To evaluate the biological relevance of the thioester adduct between RAD6 protein and ubiquitin, formed as an obligatory, transient intermediate during ubiquitin conjugation to substrates, we altered cysteine 88 in RAD6 to serine. Cysteine 200-208 E2 ubiquitin-conjugating protein RAD6 Saccharomyces cerevisiae S288C 69-73 1658333-2 1991 To evaluate the biological relevance of the thioester adduct between RAD6 protein and ubiquitin, formed as an obligatory, transient intermediate during ubiquitin conjugation to substrates, we altered cysteine 88 in RAD6 to serine. Cysteine 200-208 E2 ubiquitin-conjugating protein RAD6 Saccharomyces cerevisiae S288C 215-219 1885608-8 1991 We converted yeast actin to a class II species by inserting a Cys codon between the Met-1 and Asp-2 codons. Cysteine 62-65 uroporphyrinogen-III C-methyltransferase Saccharomyces cerevisiae S288C 84-89 1912278-1 1991 It is not definitively known whether the highly conserved region of myosin heavy chain around SH1 (Cys 707) is part of the actin-binding site. Cysteine 99-102 myosin heavy chain 14 Homo sapiens 68-74 1713450-7 1991 Carboxymethylation of hIGFBP-3 suggests that all 18 cysteines are involved in disulfide linkages. Cysteine 52-61 insulin like growth factor binding protein 3 Homo sapiens 22-30 2071895-2 1991 We probed the functional significance of the region around Cys-241 in human C2 by testing the hemolytic activity of a series of mutant rC2. Cysteine 59-62 complement C2 Rattus norvegicus 76-78 2071895-2 1991 We probed the functional significance of the region around Cys-241 in human C2 by testing the hemolytic activity of a series of mutant rC2. Cysteine 59-62 complement C2 Rattus norvegicus 135-138 2071895-11 1991 They also confirm that Cys-241 is the residue responsible for the increased activity of C2 reacted with I2. Cysteine 23-26 complement C2 Rattus norvegicus 88-90 2068090-5 1991 Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1. Cysteine 163-171 Cup2p Saccharomyces cerevisiae S288C 106-110 2068090-5 1991 Sequence comparison of AMT1 protein to the S. cerevisiae copper- or silver-activated DNA-binding protein, ACE1, indicates that AMT1 contains the 11 amino terminal cysteine residues known to be critical for the metal-activated DNA-binding activity of ACE1. Cysteine 163-171 Cup2p Saccharomyces cerevisiae S288C 250-254 2068090-7 1991 These results suggest that the amino-terminal cysteines, and other conserved residues, play an important role in the ability of AMT1 and ACE1 to sense intracellular copper levels and assume a metal-activated DNA-binding structure. Cysteine 46-55 Cup2p Saccharomyces cerevisiae S288C 137-141 1906066-6 1991 Partial secretion of PrtM into the culture medium was observed after Cys-24, the target residue for lipid modification, was replaced by an Ala residue by means of site-directed mutagenesis. Cysteine 69-72 prtM Lactococcus lactis 21-25 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. Cysteine 180-188 chondroitin sulfate proteoglycan 4 Rattus norvegicus 97-100 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. Cysteine 355-363 chondroitin sulfate proteoglycan 4 Rattus norvegicus 97-100 1646820-1 1991 Nerve growth factor (NGF) binds to a low affinity cell surface receptor (p75NGFR) which contains four extracellular repeats, rich in cysteine residues and negatively charged. Cysteine 133-141 CD177 molecule Homo sapiens 50-71 1863993-3 1991 Two of these delete part of the cysteine rich domain, which comprises the ligand binding region of the LDL-receptor. Cysteine 32-40 low density lipoprotein receptor Homo sapiens 103-115 2034676-5 1991 Human and mouse Rhom-2 are highly conserved and, like rhombotin, encode two tandem cysteine-rich LIM domains. Cysteine 83-91 LIM domain only 2 Mus musculus 16-22 1850747-3 1991 Herein, we demonstrate that terminal cysteine residues in the rab1B, rab2, and rab5 proteins undergo thioether modification by isoprenyl groups when these proteins are translated in vitro in the presence of a radiolabeled isoprenoid precursor, [3H]mevalonate. Cysteine 37-45 RAB5A, member RAS oncogene family Homo sapiens 79-83 1648005-1 1991 Each strain contains a single, unique base-pair substitution at the Cys-22 codon of the CYC1 gene, which codes for iso-1-cytochrome c. These mutations encode replacements of the functionally critical Cys-22 and render each strain unable to grow on media containing nonfermentable carbon sources (Cyc-). Cysteine 68-71 cytochrome c isoform 1 Saccharomyces cerevisiae S288C 88-92 1648005-1 1991 Each strain contains a single, unique base-pair substitution at the Cys-22 codon of the CYC1 gene, which codes for iso-1-cytochrome c. These mutations encode replacements of the functionally critical Cys-22 and render each strain unable to grow on media containing nonfermentable carbon sources (Cyc-). Cysteine 200-203 cytochrome c isoform 1 Saccharomyces cerevisiae S288C 88-92 1873469-0 1991 Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1. Cysteine 34-37 myosin heavy chain 14 Homo sapiens 61-67 1873469-0 1991 Conformational flexibility of the Cys 697-Cys 707 segment of myosin subfragment-1. Cysteine 42-45 myosin heavy chain 14 Homo sapiens 61-67 1873469-2 1991 The separation between Cys 697 (SH1) and Cys 707 (SH2) of the heavy chain of myosin subfragment-1 was previously measured by fluorescence resonance energy transfer with a donor linked to SH1 and an acceptor to SH2. Cysteine 23-26 myosin heavy chain 14 Homo sapiens 77-83 1873469-2 1991 The separation between Cys 697 (SH1) and Cys 707 (SH2) of the heavy chain of myosin subfragment-1 was previously measured by fluorescence resonance energy transfer with a donor linked to SH1 and an acceptor to SH2. Cysteine 41-44 myosin heavy chain 14 Homo sapiens 77-83 1993699-6 1991 T. thermophilus MetRS has a zinc finger-like sequence with all the three cysteine residues and a histidine residue. Cysteine 73-81 methionine--tRNA ligase Thermus thermophilus HB8 16-21 1993699-7 1991 By site-directed mutagenesis of one of the cysteine residues (Cys127) of T. thermophilus MetRS, the SH group was found to be important for methionyl-tRNA synthesis. Cysteine 43-51 methionine--tRNA ligase Thermus thermophilus HB8 89-94 1671341-1 1991 The T cell-specific transmembrane glycoprotein CD4 interacts with class II MHC molecules via its external domain and is associated with tyrosine kinase p56lck via a cysteine motif in its cytoplasmic domain. Cysteine 165-173 LCK proto-oncogene, Src family tyrosine kinase Homo sapiens 152-158 2124349-0 1990 Conserved cysteine to serine mutation in tyrosinase is responsible for the classical albino mutation in laboratory mice. Cysteine 10-18 tyrosinase Mus musculus 41-51 2167439-2 1990 In the presence of Cu+ and Ag+) ions its DNA-binding domain is thought to fold as a cysteine-coordinated Cu cluster which recognizes the palindromic CUP1 upstream activation sequence (UASc). Cysteine 84-92 metallothionein CUP1 Saccharomyces cerevisiae S288C 149-153 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. Cysteine 84-91 interleukin 5 Mus musculus 169-173 2143760-0 1990 Alkylation of cysteine 82 of p11 abolishes the complex formation with the tyrosine-protein kinase substrate p36 (annexin 2, calpactin 1, lipocortin 2). Cysteine 14-22 annexin A2 Homo sapiens 108-111 2143760-0 1990 Alkylation of cysteine 82 of p11 abolishes the complex formation with the tyrosine-protein kinase substrate p36 (annexin 2, calpactin 1, lipocortin 2). Cysteine 14-22 annexin A2 Homo sapiens 113-122 1702992-0 1990 Separation and localization of the four cysteine-949 residues in human alpha 2-macroglobulin using fluorescence energy transfer. Cysteine 40-48 alpha-2-macroglobulin Homo sapiens 71-92 2116409-6 1990 Also, 18 of the 23 cysteine residues of TFIIIA reacted with 5,5"-dithiobis-(2-nitrobenzoic acid). Cysteine 19-27 general transcription factor 3A L homeolog Xenopus laevis 40-46 2116409-10 1990 This further indicates exposure of cysteine residues from Zn2+ binding domains in TFIIIA. Cysteine 35-43 general transcription factor 3A L homeolog Xenopus laevis 82-88 2116409-12 1990 Limited papain cleavage of the AEDANS-labeled 7 S particle indicated that the modified cysteine is located within a 34-kDa TFIIIA fragment. Cysteine 87-95 general transcription factor 3A L homeolog Xenopus laevis 123-129 2116409-14 1990 Thus, Zn2+ binding domains and all but 1 cysteine residue are buried in the 7 S particle, thereby facilitating site-specific labeling of TFIIIA. Cysteine 41-49 general transcription factor 3A L homeolog Xenopus laevis 137-143 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 68-71 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 68-71 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 70-73 serpin family C member 1 Homo sapiens 57-63 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 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. Cysteine 132-141 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. Cysteine 132-141 complement C1q A chain Homo sapiens 109-112 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. Cysteine 132-141 complement C1q A chain Homo sapiens 109-112 2116011-2 1990 These include p21ras, fungal mating factors, and nuclear lamins, which are isoprenylated at carboxyl-terminal cysteine residues with a 15-carbon farnesyl group. Cysteine 110-118 HRas proto-oncogene, GTPase Rattus norvegicus 14-20 1695508-0 1990 Cysteine-108 is an acylation site in myelin proteolipid protein. Cysteine 0-8 proteolipid protein 1 Bos taurus 37-63 1695508-7 1990 Furthermore, as in rhodopsin and other members of the G protein-coupled receptor family, this Cys residue is located within a hydrophilic, basic, and possibly cytoplasmic, domain. Cysteine 94-97 rhodopsin Bos taurus 19-28 2194674-0 1990 Inhibition of purified p21ras farnesyl:protein transferase by Cys-AAX tetrapeptides. Cysteine 62-65 HRas proto-oncogene, GTPase Rattus norvegicus 23-29 2194674-1 1990 We report the identification, purification, and characterization of a farnesyl:protein transferase that transfers the farnesyl moiety from farnesyl pyrophosphate to a cysteine in p21ras proteins. Cysteine 167-175 HRas proto-oncogene, GTPase Rattus norvegicus 179-185 2088443-8 1990 Since loricrin is rich in cysteine, L-granules account for the sulfur-rich keratohyalin granules described earlier. Cysteine 26-34 loricrin Mus musculus 6-14 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. Cysteine 8-16 cystin 1 Homo sapiens 52-63 2115173-6 1990 Our results revealed that all identified disulfide linkages are located in the trypsin-releasable regions and that all except Cys-1-Cys-3 and Cys-2-Cys-4 are linked to the neighboring cysteine. Cysteine 184-192 cystin 1 Homo sapiens 126-137 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. Cysteine 244-247 rhodopsin Bos taurus 55-64 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. Cysteine 256-259 rhodopsin Bos taurus 55-64 2351676-7 1990 The deduced CRS1C and CRS4C polypeptides are apparent precursors of secreted, cationic, proline- and cysteine-rich peptides that contain Cys-Pro-X repeats. Cysteine 137-140 defensin, alpha, related sequence 2 Mus musculus 22-27 1972865-10 1990 Formation of cysteine during ischemia was suppressed in rats pretreated with acivicin, an inhibitor of gamma-glutamyltransferase (gamma-GT), although the degree of suppression was small in comparison to the extent of gamma-GT inhibition. Cysteine 13-21 gamma-glutamyltransferase 1 Rattus norvegicus 103-128 1972865-10 1990 Formation of cysteine during ischemia was suppressed in rats pretreated with acivicin, an inhibitor of gamma-glutamyltransferase (gamma-GT), although the degree of suppression was small in comparison to the extent of gamma-GT inhibition. Cysteine 13-21 gamma-glutamyltransferase 1 Rattus norvegicus 130-138 2157209-0 1990 Mutation of cysteine-88 in the Saccharomyces cerevisiae RAD6 protein abolishes its ubiquitin-conjugating activity and its various biological functions. Cysteine 12-20 E2 ubiquitin-conjugating protein RAD6 Saccharomyces cerevisiae S288C 56-60 2157209-4 1990 Since the formation of a thioester adduct between E2 and ubiquitin is necessary for E2 activity, the single cysteine residue (Cys-88) present in RAD6 was changed to alanine or valine. Cysteine 108-116 E2 ubiquitin-conjugating protein RAD6 Saccharomyces cerevisiae S288C 145-149 2157209-4 1990 Since the formation of a thioester adduct between E2 and ubiquitin is necessary for E2 activity, the single cysteine residue (Cys-88) present in RAD6 was changed to alanine or valine. Cysteine 126-129 E2 ubiquitin-conjugating protein RAD6 Saccharomyces cerevisiae S288C 145-149 2183224-2 1990 Palmitic acid and an isoprenoid (farnesol) intermediate in cholesterol biosynthesis are attached to separate cysteine residues near the C termini of H-ras, N-ras, and Kirsten-ras (K-ras) exon 4A-encoded proteins. Cysteine 109-117 HRas proto-oncogene, GTPase Homo sapiens 149-154 2138623-0 1990 Inhibition of actomyosin subfragment 1 ATPase activity by analog peptides of the actin-binding site around the Cys(SH1) of myosin heavy chain. Cysteine 111-114 myosin heavy chain 14 Homo sapiens 18-24 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. Cysteine 33-36 colony stimulating factor 3 Homo sapiens 14-20 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. Cysteine 91-94 colony stimulating factor 3 Homo sapiens 14-20 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. Cysteine 91-94 colony stimulating factor 3 Homo sapiens 14-20 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. Cysteine 91-94 colony stimulating factor 3 Homo sapiens 14-20 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. Cysteine 91-94 colony stimulating factor 3 Homo sapiens 14-20 2315290-7 1990 Kinetic studies showed that the incorporation of [35S]cysteine into amylase, lipase, and colipase was linear until up to 2 h of incubation in normal pancreatic lobules, while in the diabetic lobules the incorporation into lipase and colipase was accelerated, reaching a plateau level already after 1 h of incubation. Cysteine 54-62 lipase G, endothelial type Rattus norvegicus 77-83 2315290-7 1990 Kinetic studies showed that the incorporation of [35S]cysteine into amylase, lipase, and colipase was linear until up to 2 h of incubation in normal pancreatic lobules, while in the diabetic lobules the incorporation into lipase and colipase was accelerated, reaching a plateau level already after 1 h of incubation. Cysteine 54-62 lipase G, endothelial type Rattus norvegicus 91-97 2137453-9 1990 Comparison of this sequence with the derived sequence of caldesmon demonstrates, unequivocally, that the myosin-binding region of caldesmon begins at the amino terminus and extends beyond the first Cys residue. Cysteine 198-201 myosin heavy chain 14 Homo sapiens 105-111 1688857-3 1990 OMgp consists of four domains: (a) a short cysteine-rich motif at the NH2 terminus; (b) a series of tandem leucine-rich repeats (LRs) present in several other proteins where they may play roles in adhesion; (c) a serine/threonine-rich region that contains probable attachment sites for O-linked carbohydrates; and (d) a hydrophobic COOH-terminal segment that is likely to be cleaved concomitant with the attachment of lipid during biosynthesis of OMgp. Cysteine 43-51 oligodendrocyte myelin glycoprotein Homo sapiens 0-4 1688857-5 1990 Together with glycoprotein Ib and several other proteins, OMgp belongs to a family of proteins that contain both an NH2-terminal cysteine-rich motif and an adjacent series of LRs. Cysteine 129-137 oligodendrocyte myelin glycoprotein Homo sapiens 58-62 2406590-4 1990 Sequence analysis and alignment showed significant sequence similarity to other members of the eukaryotic cysteine protease family (45% identical to chicken cathepsin L) and conservation of the cysteine, histidine, and asparagine residues which form the catalytic triad. Cysteine 106-114 cathepsin V Gallus gallus 157-168 1689154-5 1990 The amino acid sequence is over 80% homologous with the equivalent human IGFBP-3 form and shows complete conservation of 18 cysteine residues that are clustered at the amino and carboxy ends of the protein. Cysteine 124-132 insulin like growth factor binding protein 3 Homo sapiens 73-80 2183181-4 1990 By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids. Cysteine 216-223 SKI proto-oncogene Homo sapiens 42-45 2183181-4 1990 By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids. Cysteine 216-223 SKI proto-oncogene Homo sapiens 109-112 2183181-4 1990 By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids. Cysteine 216-223 SKI proto-oncogene Homo sapiens 109-112 2268499-3 1990 The human IL-3 gene encodes a protein of 133 amino acids with two conserved cysteine residues and 2 potential N-linked glycosylation sites; human native IL-3 has not been characterized. Cysteine 76-84 interleukin 3 Homo sapiens 10-14 1693535-3 1990 GMP-140 is cysteine-rich and heavily glycosylated. Cysteine 11-19 selectin P Homo sapiens 0-7 2300550-7 1990 Significantly, within the five contiguous consensus residues of the transglutaminase active site, Gly-Gln-Cys-Trp-Val, band 4.2 has an alanine substituted for cysteine (which is apparently essential for activity). Cysteine 159-167 protein-glutamine gamma-glutamyltransferase 2 Cavia porcellus 68-84 33766578-5 2021 Domain analysis indicated that two Fab variants, each containing two unpaired cysteines, were present while the third variant contained two unpaired cysteines on the Fc region. Cysteine 78-87 FA complementation group B Homo sapiens 35-38 33775773-2 2021 Massive ROS production can induce cell death or activate protective pathways such as Keap1/Nrf2 pathway, which regulates intracellular cysteine availability through upregulation of SLC7A11, a subunit of xCT transporter, and subsequently glutathione synthesis, thus improving antioxidative defense. Cysteine 135-143 solute carrier family 7 member 11 Homo sapiens 181-188 33763603-4 2019 In contrast with previous reports on Ru(II)(bpy)3-mediated photolabelling, tandem mass spectrometry experiments reveal that the labelling site is a cysteine residue of MCL-1. Cysteine 148-156 MCL1 apoptosis regulator, BCL2 family member Homo sapiens 168-173 27996375-0 2017 Trimeric gp120-specific bovine monoclonal antibodies require cysteine and aromatic residues in CDRH3 for high affinity binding to HIV Env. Cysteine 61-69 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 9-14 25747310-1 2015 The aim of the present study is to construct a cysteine modified polyion complex micelles made of Pluronic F127-chitosan (PF127-CS), Pluronic F127-cysteine (PF127-cysteine) and sodium cholate (NaC) and to evaluate the potential of the micelles as an oral drug delivery system for paclitaxel. Cysteine 47-55 synuclein alpha Homo sapiens 193-196 25747310-3 2015 Compared with Pluronic micelles, drug-loading capacity of PF127-CS/PF127-cysteine/NaC micelles was increased from 3.35% to 12.77%. Cysteine 73-81 synuclein alpha Homo sapiens 82-85 25747310-4 2015 Both the critical micelle concentration and the stability test confirmed that the PF127-CS/PF127-cysteine/NaC micelles were more stable in aqueous solution than sodium cholate micelles. Cysteine 97-105 synuclein alpha Homo sapiens 106-109 23587639-4 2013 CADASIL is caused mostly by missense mutations in the NOTCH3 gene, invariably involving a cysteine residue. Cysteine 90-98 notch receptor 3 Homo sapiens 54-60 23662831-1 2013 BACKGROUND AND AIMS: Metallothionein (MT)-1 and -2 are low-molecular weight, cysteine-rich, intracellular metal-binding proteins involved in diverse functions, such as metal homeostasis, cell cycle progression, cell differentiation, and carcinogenesis. Cysteine 77-85 metallothionein 2A Homo sapiens 21-50 22653842-0 2012 Cysteine cathepsin S processes leptin, inactivating its biological activity. Cysteine 0-8 leptin Homo sapiens 31-37 22653842-2 2012 The search for proteolytic enzymes capable of processing leptin prompted us to investigate the action of cysteine cathepsins on human leptin degradation. Cysteine 105-113 leptin Homo sapiens 134-140 22653842-7 2012 Taken together, these results suggest that cysteine cathepsins may be putative leptin activity regulators in WAT. Cysteine 43-51 leptin Homo sapiens 79-85 15039438-0 2004 Proteasomal degradation of N-acetyltransferase 1 is prevented by acetylation of the active site cysteine: a mechanism for the slow acetylator phenotype and substrate-dependent down-regulation. Cysteine 96-104 N-acetyltransferase 1 Homo sapiens 27-48 7579175-7 1995 The coding region of the genomic sequence, AVA-P3, was interrupted by two introns located at the codons for Cys-26 and Arg-121. Cysteine 108-111 vacuolar-type H[+]-ATPase C3 Arabidopsis thaliana 43-49 34894577-7 2022 In site-specific profiling, NLRP3 was identified as a covalent target of 1 and 2 for the first time, and the Cys483 of NLRP3 NACHT domain was identified as one active-site of NLRP3 cysteine residues that can be covalently modified by the alpha-methylene-gamma-lactone moiety. Cysteine 181-189 NLR family, pyrin domain containing 3 Mus musculus 28-33 34894577-7 2022 In site-specific profiling, NLRP3 was identified as a covalent target of 1 and 2 for the first time, and the Cys483 of NLRP3 NACHT domain was identified as one active-site of NLRP3 cysteine residues that can be covalently modified by the alpha-methylene-gamma-lactone moiety. Cysteine 181-189 NLR family, pyrin domain containing 3 Mus musculus 119-124 34894577-7 2022 In site-specific profiling, NLRP3 was identified as a covalent target of 1 and 2 for the first time, and the Cys483 of NLRP3 NACHT domain was identified as one active-site of NLRP3 cysteine residues that can be covalently modified by the alpha-methylene-gamma-lactone moiety. Cysteine 181-189 NLR family, pyrin domain containing 3 Mus musculus 175-180 34413458-4 2022 In participants without prevalent myeloid neoplasms, eGFR.cys was associated with myeloid mCA (n = 148, beta = -3.36, P = 0.01) and somatic driver mutations (n = 3241, beta = -1.08, P = 6.25 x 10-5) associated with myeloid neoplasia (myeloid CH), specifically mutations in CBL, TET2, JAK2, PPM1D and GNB1 but not DNMT3A or ASXL1. Cysteine 58-61 Cbl proto-oncogene Homo sapiens 273-276 34297860-1 2022 AIMS: CADASIL, the most prevalent hereditary cerebral small vessel disease, is caused by cysteine-altering NOTCH3 variants (NOTCH3cys ) leading to vascular NOTCH3 protein aggregation. Cysteine 89-97 notch receptor 3 Homo sapiens 107-113 34297860-1 2022 AIMS: CADASIL, the most prevalent hereditary cerebral small vessel disease, is caused by cysteine-altering NOTCH3 variants (NOTCH3cys ) leading to vascular NOTCH3 protein aggregation. Cysteine 89-97 notch receptor 3 Homo sapiens 156-162 34902580-0 2022 The role of l-cysteine/Hydrogen sulfide pathway on beta3-Adrenoceptor- induced relaxation in mouse gastric fundus. Cysteine 12-22 adrenergic receptor, beta 3 Mus musculus 51-69 34902580-5 2022 In addition, cystathionine-gamma-lyase (CSE) inhibitor D,L-propargylglycine (PAG, 10-2 M), cystathionine-beta-synthase inhibitor (CBS) aminooxyacetic acid (AOAA, 10-2 M), and the combination of these inhibitors significantly reduced the relaxant responses induced by l-cysteine and BRL 37344. Cysteine 267-277 cystathionine beta-synthase Mus musculus 91-118 34992680-0 2022 Research progress on SLC7A11 in the regulation of cystine/cysteine metabolism in tumors. Cysteine 58-66 solute carrier family 7 member 11 Homo sapiens 21-28 34992680-1 2022 Solute carrier family 7 member 11 (SLC7A11) is a major transporter regulating cysteine metabolism and is widely expressed in a variety of tumor cells. Cysteine 78-86 solute carrier family 7 member 11 Homo sapiens 0-33 34992680-1 2022 Solute carrier family 7 member 11 (SLC7A11) is a major transporter regulating cysteine metabolism and is widely expressed in a variety of tumor cells. Cysteine 78-86 solute carrier family 7 member 11 Homo sapiens 35-42 34992680-2 2022 SLC7A11 plays an important role in the occurrence, development, invasion and metastasis of tumors by regulating the transport of cysteine in the tumor microenvironment. Cysteine 129-137 solute carrier family 7 member 11 Homo sapiens 0-7 34695570-2 2022 The ubiquitin-associated (UBA) domain of human HOIP contains three cysteine residues, Cys504, Cys551, and Cys572. Cysteine 67-75 ring finger protein 31 Homo sapiens 47-51 34767654-3 2022 Here we show that Arabidopsis PTOX contains a conserved C-terminus domain (CTD) with cysteines that evolved progressively following plants colonization of the land. Cysteine 85-94 Alternative oxidase family protein Arabidopsis thaliana 30-34 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). Cysteine 140-148 solute carrier family 7 member 5 Homo sapiens 55-59 34907017-6 2021 We found that f-type Trx and two types of Trx-like proteins, Trx-like 2 and atypical Cys His-rich Trx (ACHT), seemed to serve as oxidation factors for Trx-targeted proteins, such as fructose-1,6-bisphosphatase, Rubisco activase, and the gamma-subunit of ATP synthase. Cysteine 85-88 rubisco activase Arabidopsis thaliana 211-266 34560573-5 2021 Despite these differences, both proteins maintain the six conserved cysteine residues important for the function of EGF. Cysteine 68-76 epidermal growth factor Homo sapiens 116-119 34752700-7 2021 Instead, PutA/PRODH oxidation of T4C leads to cysteine formation, whereas oxidation of T2C generates an apparently stable Delta4-thiazoline-2-carboxylate species. Cysteine 46-54 proline dehydrogenase 1 Homo sapiens 14-19 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). Cysteine 131-140 peptidylprolyl isomerase A Homo sapiens 22-26 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). Cysteine 131-140 peptidylprolyl isomerase A Homo sapiens 144-148 34363702-1 2021 The tumour necrosis factor receptor superfamily (TNFRSF) members contain cysteine-rich domains (CRD) in their extra-cellular regions, and the membrane-distal CRD-1 forms homologous interactions in the absence of ligand. Cysteine 73-81 TNF receptor superfamily member 1A Homo sapiens 49-55 34656563-0 2021 Flipping the switch: how cysteine oxidation directs tau amyloid conformations. Cysteine 25-33 microtubule associated protein tau Homo sapiens 52-55 34427100-2 2021 SLC7A11-mediated cystine taken up is reduced to cysteine, a precursor amino acid for glutathione synthesis and antioxidant cellular defense. Cysteine 48-56 solute carrier family 7 member 11 Homo sapiens 0-7 34678655-0 2021 GSNOR facilitates antiviral innate immunity by restricting TBK1 cysteine S-nitrosation. Cysteine 64-72 alcohol dehydrogenase 5 (class III), chi polypeptide Mus musculus 0-5 34547902-9 2021 Glutathionylation of cysteine 691 residue in H/R exposes 735QRYRL739 motif for interaction with HSC70, and consequent transportation to LAMP2A vesicle, where it is degraded by lysosomal proteases. Cysteine 21-29 lysosomal-associated membrane protein 2 Mus musculus 136-142 34657120-7 2021 Our data revealed that the detrimental impact of cofilin1 on mitochondria depends on the oxidation of cysteine residues at positions 139 and 147. Cysteine 102-110 cofilin 1, non-muscle Mus musculus 49-57 34515295-4 2021 Human DJ-1 has three cysteine residues (Cys46, Cys53 and Cys106). Cysteine 21-29 Parkinsonism associated deglycase Homo sapiens 6-10 34515295-5 2021 We found that, in addition to Cys106, Cys46 is the most reactive cysteine residue in DJ-1, which was identified employing an NPSB-B chemical probe that selectively reacts with redox sensitive cysteine sulfhydryl. Cysteine 65-73 Parkinsonism associated deglycase Homo sapiens 85-89 34720880-11 2021 Further, recombinant 2N3R and 2N4R tau isoforms were found to be CoAlated in vitro and the site of CoAlation mapped by mass spectrometry to conserved cysteine 322, located in the microtubule binding region. Cysteine 150-158 microtubule associated protein tau Homo sapiens 35-38 34720880-15 2021 Covalent modification of recombinant tau at cysteine 322 suggests that CoAlation may play an important role in protecting redox-sensitive tau cysteine from irreversible overoxidation and may modulate its acetyltransferase activity and functional interactions. Cysteine 44-52 microtubule associated protein tau Homo sapiens 37-40 34720880-15 2021 Covalent modification of recombinant tau at cysteine 322 suggests that CoAlation may play an important role in protecting redox-sensitive tau cysteine from irreversible overoxidation and may modulate its acetyltransferase activity and functional interactions. Cysteine 44-52 microtubule associated protein tau Homo sapiens 138-141 34679713-7 2021 Cysteine 277 is required for most of the disulfide-dependent interactions of p53, including those with 14-3-3theta and 53BP1. Cysteine 0-8 tumor protein p53 binding protein 1 Homo sapiens 119-124 34680099-7 2021 Using relaxation-based NMR, we have identified the binding site on DJ-1 for glycated and native ac-alphaSyn as the catalytic pocket and established that the oxidation state of the catalytic cysteine is imperative for binding. Cysteine 190-198 Parkinsonism associated deglycase Homo sapiens 67-71 34680099-7 2021 Using relaxation-based NMR, we have identified the binding site on DJ-1 for glycated and native ac-alphaSyn as the catalytic pocket and established that the oxidation state of the catalytic cysteine is imperative for binding. Cysteine 190-198 synuclein alpha Homo sapiens 99-107 34426153-3 2021 Our laboratory has also recently reported functional derivatizations of the A ring and studied its effect on the inhibition of cysteine cathepsin L. Cysteine 127-135 cathepsin L Mus musculus 136-147 34688462-9 2021 Meanwhile, the levels of P53 and P16 protein were down-regulated in the treatment and prevention groups compared with those in the CY/BUS groups. Cysteine 131-133 transformation related protein 53, pseudogene Mus musculus 25-28 34324979-0 2021 Carnosine dipeptidase II (CNDP2) protects cells under cysteine insufficiency by hydrolyzing glutathione-related peptides. Cysteine 54-62 CNDP dipeptidase 2 (metallopeptidase M20 family) Mus musculus 26-31 34324979-9 2021 These collective data imply that cytosolic CNDP2, in conjugation with the removal of the gamma-glutamyl group, recruits Cys from extracellular GSH and supports redox homeostasis of cells, particularly in epithelial cells of proximal tubules that are continuously exposed to oxidative insult from metabolic wastes that are produced in the body. Cysteine 120-123 CNDP dipeptidase 2 (metallopeptidase M20 family) Mus musculus 43-48 34245655-7 2021 Our further transcriptional analyses indicated that cysteine residues in the fourth zinc finger (ZF4) are required for the NO-responsive activation of Fzf1. Cysteine 52-60 Fzf1p Saccharomyces cerevisiae S288C 151-155 34390831-6 2021 HTT is palmitoylated at cysteine 214 by the huntingtin-interacting protein 14 (HIP14 or ZDHHC17) and 14-like (HIP14L or ZDHHC13) acyltransferases. Cysteine 24-32 huntingtin Mus musculus 0-3 34390831-6 2021 HTT is palmitoylated at cysteine 214 by the huntingtin-interacting protein 14 (HIP14 or ZDHHC17) and 14-like (HIP14L or ZDHHC13) acyltransferases. Cysteine 24-32 zinc finger, DHHC domain containing 13 Mus musculus 110-116 34445118-9 2021 As in CD8+ CTLs, cysteine cathepsins C and H were the major targets of cystatin F in CD4+ T-cell clones. Cysteine 17-25 cystatin F Homo sapiens 71-81 34090877-8 2021 Importantly, LC-MS/MS analysis further demonstrated that TA covalently bound to the cysteine 514 residue (Cys514) of NLRP3. Cysteine 84-92 NLR family, pyrin domain containing 3 Mus musculus 117-122 34228591-1 2021 AbstractSecreted protein acidic and rich in cysteine (SPARC), an exercise-induced myokine, has been suggested as a potential endogenous factor that suppresses colon tumorigenesis. Cysteine 44-52 secreted protein acidic and cysteine rich Homo sapiens 54-59 34062408-9 2021 Moreover, we identified protein PTM "hot spots", such as the single cysteine residue of vimentin, which was detected in seven modified forms, thus, supporting its role in PTM crosstalk and redox sensing. Cysteine 68-76 vimentin Homo sapiens 88-96 34294713-3 2021 Here, we show increased levels of S-nitrosylation of guanine nucleotide-binding protein G(i) subunit alpha-2 (SNO-GNAI2) at Cysteine 66 in coronary artery samples from diabetic patients with atherosclerosis, consistently with results from mice. Cysteine 124-132 G protein subunit alpha i2 Homo sapiens 53-108 34294713-3 2021 Here, we show increased levels of S-nitrosylation of guanine nucleotide-binding protein G(i) subunit alpha-2 (SNO-GNAI2) at Cysteine 66 in coronary artery samples from diabetic patients with atherosclerosis, consistently with results from mice. Cysteine 124-132 G protein subunit alpha i2 Homo sapiens 114-119 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. Cysteine 0-3 immunoglobulin kappa variable 2D-24 (non-functional) Homo sapiens 90-95 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. Cysteine 0-3 heat shock protein family B (small) member 1 Homo sapiens 149-154 34704055-3 2021 Here, we present studies on short analogues of p21 peptides (143-151) conformationally constrained with a covalent linker between i, i + 4 separated cysteine residues at positions 145 and 149 to access peptidomimetics that target PCNA. Cysteine 149-157 proliferating cell nuclear antigen Homo sapiens 230-234 34283874-4 2021 We found that degradation of L-cysteine by putative cystathionine beta-synthase (CBS) is the major source of endogenous H2S in V. cholerae. Cysteine 29-39 cystathionine beta-synthase Mus musculus 81-84 34335700-2 2021 Archetypal disease-causing mutations are cysteine-affecting variants within the 34 epidermal growth factor-like repeat (EGFr) region of the Notch3 extracellular subunit. Cysteine 41-49 notch receptor 3 Homo sapiens 140-146 34335700-7 2021 We identified 23 different NOTCH3 variants including 14 cysteine-affecting pathogenic variants, five cysteine-sparing pathogenic variants, two reported cysteine-sparing variants of unknown significance (VUS), and two novel VUS outside EGFr region. Cysteine 101-109 notch receptor 3 Homo sapiens 27-33 34262438-2 2021 Mutations in neuroligin genes, including the arginine to cystein substitution at the 451st amino acid residue (R451C) of neuroligin-3 (NLGN3), have been identified in patients with autism spectrum disorder (ASD). Cysteine 57-64 neuroligin 3 Homo sapiens 121-133 34262438-2 2021 Mutations in neuroligin genes, including the arginine to cystein substitution at the 451st amino acid residue (R451C) of neuroligin-3 (NLGN3), have been identified in patients with autism spectrum disorder (ASD). Cysteine 57-64 neuroligin 3 Homo sapiens 135-140 34095874-5 2021 In particular, Cc6 detects changes in amino acid residues, including phenylalanine, tyrosine, tryptophan, cysteine, aspartate, and glutamate. Cysteine 106-114 NADH:ubiquinone oxidoreductase subunit A9 Homo sapiens 15-18 34776648-5 2021 Furthermore, using DEER, we were able to measure a single cysteine pair distance in a three cysteine domain within HD-PTP. Cysteine 58-66 protein tyrosine phosphatase non-receptor type 23 Homo sapiens 115-121 34776648-5 2021 Furthermore, using DEER, we were able to measure a single cysteine pair distance in a three cysteine domain within HD-PTP. Cysteine 92-100 protein tyrosine phosphatase non-receptor type 23 Homo sapiens 115-121 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. Cysteine 98-106 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. Cysteine 107-115 synuclein alpha Homo sapiens 58-73 35447412-9 2022 This was abolished in BMDMs from glutamate-cysteine ligase modifier subunit-deficient (Gclm-/-) mice in which glutathione biosynthesis is impaired. Cysteine 43-51 glutamate-cysteine ligase, modifier subunit Mus musculus 87-91 35609862-4 2022 The C-terminal cytosolic domain of mitoNEET binds a (2Fe-2S) cluster via three cysteine and one histidine residues. Cysteine 79-87 CDGSH iron sulfur domain 1 Homo sapiens 35-43 35594310-2 2022 Trivalent arsenic (As3+) is known to cure APL by binding to cysteine residues of PML and enhance the degradation of PML-retinoic acid receptor alpha (RARalpha), a t(15;17) gene translocation product in APL cells, and restore PML-nuclear bodies (NBs). Cysteine 60-68 PML nuclear body scaffold Homo sapiens 81-84 35543500-6 2022 The lower exposure of CYS reduces the activation of Toll-like receptors 4 (TLR4), which down-regulates the expression of myeloid differentiation factor (Myd88)-TNF receptor associated factor 6 (TRAF6) to inhibit nuclear factor kappa B (NF-kappaB) signaling. Cysteine 22-25 toll like receptor 4 Homo sapiens 52-73 35543500-6 2022 The lower exposure of CYS reduces the activation of Toll-like receptors 4 (TLR4), which down-regulates the expression of myeloid differentiation factor (Myd88)-TNF receptor associated factor 6 (TRAF6) to inhibit nuclear factor kappa B (NF-kappaB) signaling. Cysteine 22-25 toll like receptor 4 Homo sapiens 75-79 35543500-6 2022 The lower exposure of CYS reduces the activation of Toll-like receptors 4 (TLR4), which down-regulates the expression of myeloid differentiation factor (Myd88)-TNF receptor associated factor 6 (TRAF6) to inhibit nuclear factor kappa B (NF-kappaB) signaling. Cysteine 22-25 TNF receptor associated factor 6 Homo sapiens 194-199 35020809-0 2022 Novel cysteine substitution p.(Cys1084Tyr) causes variable expressivity of qualitative and quantitative VWF defects. Cysteine 6-14 Von Willebrand factor Mus musculus 104-107 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. Cysteine 4-12 Von Willebrand factor Mus musculus 25-28 35626640-3 2022 When the transsulfuration pathway is activated, the sulfur atom of methionine (Met) is utilized to generate Cys, which can then suppress Cys-starvation-induced ferroptosis. Cysteine 108-111 SAFB like transcription modulator Homo sapiens 79-82 35626640-3 2022 When the transsulfuration pathway is activated, the sulfur atom of methionine (Met) is utilized to generate Cys, which can then suppress Cys-starvation-induced ferroptosis. Cysteine 137-140 SAFB like transcription modulator Homo sapiens 79-82 35608094-1 2022 The outer mitochondrial membrane protein mitoNEET (mNT) is a recently identified iron-sulfur protein containing a unique Fe2 S2 (His)1 (Cys)3 metal cluster with a single Fe-N(His87) coordinating bond. Cysteine 136-139 CDGSH iron sulfur domain 1 Homo sapiens 41-49 35180474-3 2022 Electrophysiological studies on VDAC3 carrying selective cysteine mutations and mass spectrometry data about the redox state of such sulfur containing amino acids are consistent with a putative involvement of isoform 3 in mitochondrial ROS homeostasis. Cysteine 57-65 voltage dependent anion channel 3 Homo sapiens 32-37 35180474-6 2022 High-resolution respirometry of transiently transfected HAP1-DeltaVDAC3 cells expressing the wild type or the cysteine-null mutant VDAC3 protein, unequivocally confirmed that VDAC3 cysteines are indispensable for protein ability to counteract ROS-induced oxidative stress. Cysteine 110-118 voltage dependent anion channel 3 Homo sapiens 131-136 35180474-6 2022 High-resolution respirometry of transiently transfected HAP1-DeltaVDAC3 cells expressing the wild type or the cysteine-null mutant VDAC3 protein, unequivocally confirmed that VDAC3 cysteines are indispensable for protein ability to counteract ROS-induced oxidative stress. Cysteine 110-118 voltage dependent anion channel 3 Homo sapiens 175-180 35557955-1 2022 Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster. Cysteine 117-125 nuclear assembly factor 1 ribonucleoprotein Homo sapiens 29-34 35557955-1 2022 Human NEET proteins, such as NAF-1 and mitoNEET, are homodimeric, redox iron-sulfur proteins characterized by triple cysteine and one histidine-coordinated (2Fe-2S) cluster. Cysteine 117-125 CDGSH iron sulfur domain 1 Homo sapiens 39-47 35403927-2 2022 GPxs and TPxs generally use GSH or Trx, respectively, to recycle the oxidized cysteine (Cys) residue in the protein. Cysteine 78-86 thioredoxin Homo sapiens 35-38 35403927-2 2022 GPxs and TPxs generally use GSH or Trx, respectively, to recycle the oxidized cysteine (Cys) residue in the protein. Cysteine 88-91 thioredoxin Homo sapiens 35-38 35403927-3 2022 However, it is unclear why unlike human GPxs, the Schizosaccharomyces pombe Gpx1 (spGpx1) prefers Trx over GSH for recycling of the active-site peroxidatic Cys residue. Cysteine 156-159 thioredoxin Homo sapiens 98-101 35403927-6 2022 These two conserved Cys residues are named peroxidatic and resolving Cys residues, respectively, and are found only in GPxs and TPxs that prefer Trx as an electron donor. Cysteine 20-23 thioredoxin Homo sapiens 145-148 35403927-6 2022 These two conserved Cys residues are named peroxidatic and resolving Cys residues, respectively, and are found only in GPxs and TPxs that prefer Trx as an electron donor. Cysteine 69-72 thioredoxin Homo sapiens 145-148 35393494-2 2022 The most commonly inherited SVD, CADASIL, is caused by dominantly acting cysteine-altering mutations in NOTCH3. Cysteine 73-81 notch receptor 3 Homo sapiens 104-110 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. Cysteine 180-189 notch receptor 3 Homo sapiens 87-93 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. Cysteine 205-214 notch receptor 3 Homo sapiens 63-69 35393494-7 2022 In sum, these studies identify specific cysteine residues alterations and quaternary structure induced by CADASIL mutations in NOTCH3; further, we validate that reductive factors alter the structure and stability of this small vessel disease protein. Cysteine 40-48 notch receptor 3 Homo sapiens 127-133 35216667-4 2022 Mechanistically, fumarate directly reacts with PTEN at cysteine 211 (C211) to form S-(2-succino)-cysteine. Cysteine 55-63 phosphatase and tensin homolog Homo sapiens 47-51 35149380-6 2022 We review cys-loop ligand gated ion channels (LGICs), including nicotinic acetylcholine receptors (nAChRs), acetylcholine-chloride gated ion channels (ACCs), glutamate-gated chloride channels (GluCls), and GABA (gamma-aminobutyric acid) receptors, and other ionotropic receptors (transient receptor potential (TRP) channels and potassium ion channels). Cysteine 10-13 1-aminocyclopropane-1-carboxylate synthase homolog (inactive) Homo sapiens 151-155 35401228-2 2022 The extracellular region of DR6 contains four cysteine-rich domains, followed by a single-pass transmembrane domain and an intracellular region. Cysteine 46-54 TNF receptor superfamily member 21 Homo sapiens 28-31 35225603-0 2022 Chemo-Selective Cys-Pen Disulfide for Proximity-Induced Cysteine Cross-Linking. Cysteine 56-64 proprotein convertase subtilisin/kexin type 1 inhibitor Homo sapiens 20-23 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. Cysteine 146-154 proprotein convertase subtilisin/kexin type 1 inhibitor Homo sapiens 22-25 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. Cysteine 124-127 proprotein convertase subtilisin/kexin type 1 inhibitor Homo sapiens 92-95 35254894-3 2022 This mechanism involves direct acylation of FIT2 cysteine residues, which then marks the FIT2 protein for endoplasmic reticulum (ER)-associated degradation. Cysteine 49-57 fat storage-inducing transmembrane protein 2 Mus musculus 44-48 35254894-3 2022 This mechanism involves direct acylation of FIT2 cysteine residues, which then marks the FIT2 protein for endoplasmic reticulum (ER)-associated degradation. Cysteine 49-57 fat storage-inducing transmembrane protein 2 Mus musculus 89-93 35237611-0 2021 Cysteine Substitution and Calcium-Binding Mutations in FBN1 cbEGF-Like Domains Are Associated With Severe Ocular Involvement in Patients With Congenital Ectopia Lentis. Cysteine 0-8 fibrillin 1 Homo sapiens 55-59 35256959-7 2022 FL-18 selectively modified cysteine residues located within the D2 ATP site of p97. Cysteine 27-35 melanotransferrin Homo sapiens 79-82 35256959-8 2022 This covalent labeling of cysteine residue in p97 was verified by LC-MS/MS-based site-mapping and site-directed mutagenesis. Cysteine 26-34 melanotransferrin Homo sapiens 46-49 34870817-1 2022 The scavenger receptor cysteine-rich SRCR domain is an ancient protein domain found in SR-A and SR-I scavenger receptors, which is characterized by a conserved arrangement of cysteines (Martinez et al., Pharmacol Rev 63(4):967-1000, 2011; Sarrias et al., Crit Rev Immunol 24(1):1-37, 2004; Telfer and Baldwin, Cell Immunol 296(1):76-86, 2015; PrabhuDas et al., J Immunol, 2017. Cysteine 23-31 macrophage scavenger receptor 1 Homo sapiens 87-91 34870817-1 2022 The scavenger receptor cysteine-rich SRCR domain is an ancient protein domain found in SR-A and SR-I scavenger receptors, which is characterized by a conserved arrangement of cysteines (Martinez et al., Pharmacol Rev 63(4):967-1000, 2011; Sarrias et al., Crit Rev Immunol 24(1):1-37, 2004; Telfer and Baldwin, Cell Immunol 296(1):76-86, 2015; PrabhuDas et al., J Immunol, 2017. Cysteine 175-184 macrophage scavenger receptor 1 Homo sapiens 87-91 35222920-4 2022 Such reducible solubilizing tags (RSTs) are compatible with peptide salicylaldehyde ester-mediated Ser/Thr ligation and Cys/Pen ligation for purifying and ligating peptides with poor solubility. Cysteine 120-123 proprotein convertase subtilisin/kexin type 1 inhibitor Homo sapiens 124-127 35187416-6 2022 Cys-528 in the elephant shark PR corresponds to Gly-722 in the human PR, which is essential for RU486 inhibition of the human PR. Cysteine 0-3 transmembrane protein 37 Homo sapiens 69-71 35187416-6 2022 Cys-528 in the elephant shark PR corresponds to Gly-722 in the human PR, which is essential for RU486 inhibition of the human PR. Cysteine 0-3 transmembrane protein 37 Homo sapiens 126-128 2597675-1 1989 The low-density Lipoprotein receptor-related protein (LRP) is a 4544-amino-acid membrane protein which closely resembles the LDL receptor in its arrangement of cysteine-rich motifs. Cysteine 160-168 low density lipoprotein receptor Homo sapiens 125-137 2611263-8 1989 These results indicate that the two Zn2+ ions in TFIIIA are coordinated with the cysteine and histidine residues and are required for maintenance of the proper conformation of TFIIIA. Cysteine 81-89 general transcription factor 3A L homeolog Xenopus laevis 49-55 2611263-8 1989 These results indicate that the two Zn2+ ions in TFIIIA are coordinated with the cysteine and histidine residues and are required for maintenance of the proper conformation of TFIIIA. Cysteine 81-89 general transcription factor 3A L homeolog Xenopus laevis 176-182 2592413-6 1989 The predicted amino acid sequence also includes a cluster of four closely spaced cysteine residues, similar to the metal binding domains of some metalloproteins, suggesting that the SNAP-25 polypeptide may have the potential to coordinately bind metal ions. Cysteine 81-89 synaptosome associated protein 25 Homo sapiens 182-189 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. Cysteine 86-95 calcineurin like EF-hand protein 1 Homo sapiens 5-8 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. Cysteine 86-95 calcineurin like EF-hand protein 1 Homo sapiens 101-104 2776214-5 1989 Eryf1 is a basic 38 kd protein containing a pair of highly similar "fingers" with the motif Cys-x-x-Cys-x17-Cys-x-x-Cys. Cysteine 92-95 GATA binding protein 1 (globin transcription factor 1) Gallus gallus 0-5 2776214-5 1989 Eryf1 is a basic 38 kd protein containing a pair of highly similar "fingers" with the motif Cys-x-x-Cys-x17-Cys-x-x-Cys. Cysteine 100-103 GATA binding protein 1 (globin transcription factor 1) Gallus gallus 0-5 2776214-5 1989 Eryf1 is a basic 38 kd protein containing a pair of highly similar "fingers" with the motif Cys-x-x-Cys-x17-Cys-x-x-Cys. Cysteine 100-103 GATA binding protein 1 (globin transcription factor 1) Gallus gallus 0-5 2776214-5 1989 Eryf1 is a basic 38 kd protein containing a pair of highly similar "fingers" with the motif Cys-x-x-Cys-x17-Cys-x-x-Cys. Cysteine 100-103 GATA binding protein 1 (globin transcription factor 1) Gallus gallus 0-5 2674688-3 1989 The CUP2 protein contains a cysteine-rich DNA-binding domain dependent on Cu+ and Ag+ ions which bind the cysteine residues and direct the refolding of the metal-free apoprotein. Cysteine 28-36 Cup2p Saccharomyces cerevisiae S288C 4-8 2664778-3 1989 Analysis of the subunit composition of ACE1 bound to DNA indicates that cooperativity results from the binding of multiple Cu(I) ions to the cysteine-rich DNA-binding domain. Cysteine 141-149 Cup2p Saccharomyces cerevisiae S288C 39-43 2737278-0 1989 The cysteines in position 1 and 86 of rat interferon-alpha 1 are indispensable for antiviral activity. Cysteine 4-13 interferon, alpha 5 Rattus norvegicus 42-60 2737278-3 1989 Changing Cys-86 in rat IFN-alpha 1 into Ser or Tyr virtually abolished antiviral activity. Cysteine 9-12 interferon, alpha 5 Rattus norvegicus 23-34 2565880-6 1989 Sequence analysis indicated that the DNF15S2 locus could potentially code for a previously unreported protein of 67 kDa which has 26 cysteine residues. Cysteine 133-141 macrophage stimulating 1 Homo sapiens 37-44 2704753-6 1989 Determination of the amino acid content and sequence analysis of the R15 alpha 1 peptide demonstrated that this peptide contains 38 residues, including two cysteines. Cysteine 156-165 ribonuclease A family member 2 Rattus norvegicus 69-72 2539162-4 1989 In vivo treatment of KK mice with 1 mg/kg of CY 222 decreased the biosyntheses of type III collagen and of fibronectin to normal levels. Cysteine 45-47 fibronectin 1 Mus musculus 107-118 2703832-3 1989 The experimental data may be explained by the formation of the complexes T1(Cys)-, T1(Cys)H, T1(Pen)-, T1(Pen)H, T1(Acy)-, and T1(Ape)- with log formation constants 3.26, 11.28, 3.60, 12.05, 2.27, and 2.45, respectively. Cysteine 76-79 proprotein convertase subtilisin/kexin type 1 inhibitor Homo sapiens 106-109 2463989-7 1989 The biosynthesis of GMP-140 in HEL cells, which share biochemical features with megakaryocytes, was studied by pulse-chase labeling with [35S]cysteine followed by immunoprecipitation. Cysteine 142-150 selectin P Homo sapiens 20-27 2463989-12 1989 Our studies indicate that GMP-140 is a cysteine-rich, heavily glycosylated protein with a large extracytoplasmic domain. Cysteine 39-47 selectin P Homo sapiens 26-33 2911462-4 1989 Xint-1 shares several characteristics of secreted proteins with the other int-1 homologs: it has a hydrophobic leader, multiple conserved potential N-linked glycosylation sites and is rich in cysteine residues. Cysteine 192-200 Wnt family member 1 S homeolog Xenopus laevis 0-6 2911462-4 1989 Xint-1 shares several characteristics of secreted proteins with the other int-1 homologs: it has a hydrophobic leader, multiple conserved potential N-linked glycosylation sites and is rich in cysteine residues. Cysteine 192-200 Wnt family member 1 S homeolog Xenopus laevis 1-6 2567085-6 1989 Since one would anticipate that the valine/cysteine substitution at position 12 of the ras p21 would occur at only low frequencies in human tumors, our results with DWP are consistent with this hypothesis. Cysteine 43-51 H3 histone pseudogene 16 Homo sapiens 91-94 3143745-5 1988 Substitution of the cysteine residue at position 125 of rIL-2 with serine or alanine led to loss of PGI2-stimulatory activity in HUVECS without affecting thymidine incorporation in lymphocytes. Cysteine 20-28 interleukin 2 Rattus norvegicus 56-61 2845130-2 1988 This activity is principally due to antibodies directed toward a hypervariable region of gp120 between cysteine residues 302 and 337 and is virus isolate specific. Cysteine 103-111 inter-alpha-trypsin inhibitor heavy chain 4 Homo sapiens 89-94 3058966-2 1988 Cysteine substituted analogues of luteinizing hormone releasing hormone (LHRH) were coupled to carrier molecules, and the resulting conjugates used to characterize the immune response to native LHRH generated in BALB/c mice and to formulate vaccines in an effort to maximize titer development. Cysteine 0-8 gonadotropin releasing hormone 1 Mus musculus 34-71 3058966-2 1988 Cysteine substituted analogues of luteinizing hormone releasing hormone (LHRH) were coupled to carrier molecules, and the resulting conjugates used to characterize the immune response to native LHRH generated in BALB/c mice and to formulate vaccines in an effort to maximize titer development. Cysteine 0-8 gonadotropin releasing hormone 1 Mus musculus 73-77 2903444-5 1988 The deduced amino acid sequence of E. histolytica ferredoxin resembles clostridial type of ferredoxins, and shows an arrangement of cysteines characteristic for the coordination of 2[4Fe-4S] centres. Cysteine 132-141 EHI_198670 Entamoeba histolytica HM-1:IMSS 50-60 2848499-10 1988 Dithiothreitol, 2-mercaptoethanol and cysteine restored the phosphotransferase activity of the hexokinase after inactivation by 2-aminothiophenol. Cysteine 38-46 hexokinase Saccharomyces cerevisiae S288C 95-105 2458390-4 1988 To investigate the role of this cysteine residue in the antigenic structure of HLA-B27, we isolated a genomic clone encoding a molecule of the HLA-B27.1 subtype and performed oligonucleotide-directed mutagenesis to convert the cysteine at position 67 to a tyrosine. Cysteine 32-40 major histocompatibility complex, class I, B Homo sapiens 79-86 2458390-4 1988 To investigate the role of this cysteine residue in the antigenic structure of HLA-B27, we isolated a genomic clone encoding a molecule of the HLA-B27.1 subtype and performed oligonucleotide-directed mutagenesis to convert the cysteine at position 67 to a tyrosine. Cysteine 32-40 major histocompatibility complex, class I, B Homo sapiens 143-150 2973411-3 1988 Here we have characterized the p11 binding site on p36 by fluorescence spectroscopy using porcine p36 labelled at cysteine 8 with the fluorophore Prodan (6-proprionyl-2-dimethylamino-naphthalene). Cysteine 114-122 annexin A2 Homo sapiens 51-54 3175343-6 1988 Thus in fasted CD-1 male mice, the intracellular cysteine precursor, OTC, has an apparently selective effect on tissue GSH contents without confounding effects on hepatic GSH utilizing or restoring activities. Cysteine 49-57 CD1 antigen complex Mus musculus 15-19 3167014-1 1988 The amino acid sequences of three essential regions of chicken liver fatty acid synthase have been determined: that around 4"-phosphopantetheine ("carrier" site), the substrate "loading" site containing serine, and a "waiting" site for the growing fatty acid containing cysteine. Cysteine 270-278 fatty acid synthase Gallus gallus 69-88 2836414-1 1988 Beef heart cytochrome c oxidase was labeled at a single sulfhydryl group by treatment with 5 mM N-iodoacetylamidoethyl-1-aminonaphthalene-5-sulfonate (1,5-I-AEDANS) at pH 8.0 for 4 h. Sodium dodecyl sulfate gel electrophoresis revealed that the enzyme was exclusively labeled at subunit III, presumably at Cys-115. Cysteine 306-309 cytochrome c, somatic Equus caballus 11-23 2836414-7 1988 In order to identify the cysteine residues that ligand copper A, a new procedure was developed to specifically remove copper A from cytochrome c oxidase by incubation with 2-mercaptoethanol followed by gel chromatography. Cysteine 25-33 cytochrome c, somatic Equus caballus 132-144 3259134-5 1988 The positions of the cysteine residues in each domain also are conserved, indicating that PS beta G and CEA are two members of the same gene family. Cysteine 21-29 protein S (beta) pseudogene Homo sapiens 90-97 3259134-5 1988 The positions of the cysteine residues in each domain also are conserved, indicating that PS beta G and CEA are two members of the same gene family. Cysteine 21-29 pregnancy specific beta-1-glycoprotein 2 Homo sapiens 104-107 2456780-4 1988 ESR spectra of these alpha 2M derivatives showed that label I is firmly held and label II has limited freedom of rotation consistent with location of the cysteine residue in a narrow cavity. Cysteine 154-162 alpha-2-macroglobulin Homo sapiens 21-29 2900016-4 1988 The amino-acid composition of erythrocyte transglutaminase differed substantially from that of the guinea-pig liver enzyme, notably with respect to the number of histidine, cysteine and acidic amino-acid residues. Cysteine 173-181 protein-glutamine gamma-glutamyltransferase 2 Cavia porcellus 42-58 3042385-0 1988 A carboxyl-terminal cysteine residue is required for palmitic acid binding and biological activity of the ras-related yeast YPT1 protein. Cysteine 20-28 Rab family GTPase YPT1 Saccharomyces cerevisiae S288C 124-128 3042385-3 1988 YPT1 gene mutations were generated that either led to substitutions by serine or the deletion of one or both C-terminal cysteines. Cysteine 120-129 Rab family GTPase YPT1 Saccharomyces cerevisiae S288C 0-4 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. Cysteine 49-52 interleukin 2 Mus musculus 209-213 2450097-8 1988 It binds to a region amino-terminal to cys-324 of avian desmin that is resistant to chymotrypsin and trypsin digestion, and in the electron microscope appears to bind to the ends of tetrameric protofilaments. Cysteine 39-42 desmin Homo sapiens 56-62 3339003-15 1988 The presence of autoantibodies to O-acetyl-GD3 in melanoma sera was confirmed by blocking of the antigen sites on M25 cells by the lectin or preabsorption of the sera with erythrocytes bearing O-acetyl gangliosides. Cysteine 35-42 GRDX Homo sapiens 43-46 2961814-3 1988 FcR material judged to be pure by these criteria was digested with a number of enzymes to identify the cysteine residues engaged in disulfide bonds within the native structure. Cysteine 103-111 Fc receptor Mus musculus 0-3 2831944-3 1987 Comparisons with the sequence of Clr, the other enzymatic subcomponent of Cl, reveal 40% amino acid identity and conservation of all the cysteine residues. Cysteine 137-145 doublecortin like kinase 3 Homo sapiens 33-36 2831944-4 1987 Beside the serine protease domain, the following sequence motifs, previously described in Clr, were also found in Cls: (a) two repeats of the type found in the Ba fragment of complement factor B and in several other complement but also noncomplement proteins, (b) a cysteine-rich segment homologous to the repeats of epidermal growth factor precursor, and (c) a duplicated segment found only in Clr and Cls. Cysteine 266-274 doublecortin like kinase 3 Homo sapiens 90-93 3316228-5 1987 Analysis of the PDR1 deduced amino acid sequence revealed several homologies to four different regulatory proteins involved in the control of gene expression, including a cysteine-rich motif suggested to be a metal-binding domain for DNA recognition. Cysteine 171-179 drug-responsive transcription factor PDR1 Saccharomyces cerevisiae S288C 16-20 3691800-4 1987 gamma-Sm also hydrolyzed the -Phe/Glu- of lysozyme and the -Leu/Cys(SO3H)- of insulin B chain. Cysteine 64-67 kallikrein related peptidase 3 Homo sapiens 0-8 2890582-1 1987 A fragment was obtained by treating Clostridium perfringens enterotoxin with 2-nitro-5-thiocyanobenzoic acid, a reagent which specifically cleaves the amino-terminal peptide bond of cysteine residues. Cysteine 182-190 cpe Clostridium perfringens 60-71 2824697-8 1987 One is a highly sensitive site to NEM (a concentration range of 1-50 microM), which is probably a cysteine residue, IAP-catalyzed ADP-ribosylating site on the alpha-subunit of GTP-binding protein. Cysteine 98-106 magnesium transporter 1 Rattus norvegicus 116-119 3040719-12 1987 Both H1 and H2 were purified to homogeneity when Triton X-100-solubilized membrane proteins from [35S]cysteine-labeled cells were subjected to affinity chromatography on galactose-agarose. Cysteine 102-110 H1.5 linker histone, cluster member Homo sapiens 5-14 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. Cysteine 101-104 interleukin 2 Rattus norvegicus 33-38 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. Cysteine 141-144 interleukin 2 Rattus norvegicus 33-38 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. Cysteine 141-144 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. Cysteine 78-81 interleukin 2 Rattus norvegicus 13-18 3115179-2 1987 Treatment of rIL-2 with 200 mM dithiothreitol resulted in the cleavage of the Cys-58-Cys-105 disulfide bond. Cysteine 85-88 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. Cysteine 50-59 secreted protein acidic and cysteine rich Bos taurus 11-22 2886057-7 1987 Furthermore, in 4-wk-old rats, inhibition of hepatic GGT by acivicin markedly decreased the biliary excretion of Cys-Gly and Cys and increased that of GS without influencing the excretion of total GS-related sulfur in bile. Cysteine 113-116 gamma-glutamyltransferase 1 Rattus norvegicus 53-56 3654593-2 1987 The most predominant amino acid in the phospholipase A2 was cysteine followed by lysine, suggesting that it is a basic one. Cysteine 60-68 phospholipase A2 group IB Rattus norvegicus 39-55 3039013-3 1987 The IFN-alpha protein sequences contain six cysteine residues as well as two or three potential N-glycosylation sites. Cysteine 44-52 interferon, alpha 6 Canis lupus familiaris 4-13 3549727-4 1987 Removal of the acetyl moiety abolishes biological activity, so this reaction may regulate the concentration of PAF and its physiological effects. Cysteine 15-21 PCNA clamp associated factor Homo sapiens 111-114 3106550-5 1987 Unlike human plasma apoA-II, which exists as a disulfide dimer, BALB/c apoA-II lacks cysteine and is a monomer. Cysteine 85-93 apolipoprotein A2 Homo sapiens 71-78 3814605-6 1987 Fluorescence energy transfer was observed from tryptophan to MIANS-labeled cysteines in both gamma-II and gamma-III crystallins, with efficiencies of 86% and 89%, respectively, but not in gamma-IV crystallin. Cysteine 75-84 G protein subunit gamma 7 Bos taurus 93-101 2432068-4 1987 It contains a typical internal thiol ester region and 25 cysteine residues which are conserved between rat and human alpha 2-macroglobulin. Cysteine 57-65 alpha-2-macroglobulin Homo sapiens 117-138 3320533-4 1987 PP12 is a 34-kDa glycoprotein, which has an N-terminal amino acid sequence of Ala-Pro-Trp-Gln-Cys-Ala-Pro-Cys-Ser-Ala. Cysteine 94-97 insulin like growth factor binding protein 1 Homo sapiens 0-4 3330790-6 1987 These data identify the first base of codon 13 as a novel mutation site in ras genes and indicate that cysteine at position 13 of the ras p21 is a transforming substitution. Cysteine 103-111 H3 histone pseudogene 16 Homo sapiens 138-141 3094588-2 1986 In this study we demonstrated increased acetyltransferase activity (i.e., transfer of the acetyl moiety of [3H]acetyl-CoA to lyso-PAF (1-alkyl-sn-glycero-3-phosphocholine) to form PAF) occurring in human platelet microsomes made from platelets stimulated by thrombin or ionophore A-23187. Cysteine 40-46 PCNA clamp associated factor Homo sapiens 130-133 3094588-2 1986 In this study we demonstrated increased acetyltransferase activity (i.e., transfer of the acetyl moiety of [3H]acetyl-CoA to lyso-PAF (1-alkyl-sn-glycero-3-phosphocholine) to form PAF) occurring in human platelet microsomes made from platelets stimulated by thrombin or ionophore A-23187. Cysteine 40-46 PCNA clamp associated factor Homo sapiens 180-183 3021207-3 1986 Fab" fragments are generated from protein-specific, murine monoclonal antibodies by pepsin digestion and mild reduction with cysteine. Cysteine 125-133 FA complementation group B Homo sapiens 0-3 3017933-1 1986 The mechanism by which 2-bromo-4"-nitroacetophenone (BrNAP) inactivates cytochrome P-450c, which involves alkylation primarily at Cys-292, is shown in the present study to involve an uncoupling of NADPH utilization and oxygen consumption from product formation. Cysteine 130-133 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 83-89 3730508-1 1986 Rabbit skeletal alpha alpha-tropomyosin was labeled at Cys-190 with pyrene maleimide to form (S-[N-(1-pyrene)succinimido])2-tropomyosin (pyreneI-Tm). Cysteine 55-58 tropomyosin alpha-1 chain Oryctolagus cuniculus 22-39 3093619-17 1986 Residue 6 of mature rat apoA-II is Asp, while it is Cys in human apoA-II, and this would account for the absence of dimeric forms of rat apoA-II in plasma. Cysteine 52-55 apolipoprotein A2 Homo sapiens 65-72 2424021-0 1986 Antigenic crossreactivity of the alpha subunit of complement component C8 with the cysteine-rich domain shared by complement component C9 and low density lipoprotein receptor. Cysteine 83-91 low density lipoprotein receptor Homo sapiens 142-174 3008820-7 1986 The N-terminal segment of cytochrome c is insensitive to the heme redox state, as in the crystallographic model, except for residues closest to the heme (Cys-14 and Ala-15), which exchange about 15-fold more slowly in the reduced form. Cysteine 154-157 cytochrome c, somatic Equus caballus 26-38 3485286-5 1986 The HLA-B27 mRNA has the structural features and the codon variability typical of an HLA class I transcript but it specifies two uncommon amino acid replacements: a cysteine in position 67 and a serine in position 131. Cysteine 165-173 major histocompatibility complex, class I, B Homo sapiens 4-11 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. Cysteine 66-74 glutaredoxin-1 Bos taurus 46-62 3002789-3 1986 The enzyme contains 238 amino acid residues in the following order: (sequence; see text) The four cysteine residues of AK2 were reinvestigated. Cysteine 98-106 adenylate kinase 2 Bos taurus 119-122 3002789-5 1986 Chemical and model-building studies suggest that the pair Cys-43/Cys-93 forms a disulfide in native AK2. Cysteine 58-61 adenylate kinase 2 Bos taurus 100-103 3002789-5 1986 Chemical and model-building studies suggest that the pair Cys-43/Cys-93 forms a disulfide in native AK2. Cysteine 65-68 adenylate kinase 2 Bos taurus 100-103 3484479-2 1986 In this study, site-specific mutagenesis has been used to modify the cysteine residues of recombinant Escherichia coli-derived IL-2 (rIL-2) to evaluate the functional structure of IL-2. Cysteine 69-77 interleukin 2 Rattus norvegicus 133-138 3484479-3 1986 Substitution or deletion of cysteine 105 disrupted the disulfide bridge and yielded a mutant protein which was 8-10 times less active than wild type rIL-2. Cysteine 28-36 interleukin 2 Rattus norvegicus 149-154 3911945-1 1985 A pyrene label attached to Cys-374 of actin has been shown to be a useful probe for monitoring the interaction of actin with myosin subfragments [Kouyama & Mihashi (1981) Eur. Cysteine 27-30 myosin heavy chain 14 Homo sapiens 125-131 4091793-2 1985 We have used actin labelled at Cys-374 with N-(1-pyrenyl)iodoacetamide [Kouyama & Mihashi (1981) Eur. Cysteine 31-34 actin Oryctolagus cuniculus 13-18 4044546-1 1985 Intestinal and hepatic ornithine decarboxylase (ODC) activities increased to a peak 4 h after administration of a diet containing casein or an amino acid mixture simulating that of casein to rats starved for 12 h. All amino acids except cysteine with a two or three carbon skeleton, including those with a D-configuration, and alpha-amino-isobutyric acid (AIB) strongly induced intestinal ODC when given in the diet or administered intragastrically. Cysteine 237-245 ornithine decarboxylase 1 Rattus norvegicus 23-46 4044546-1 1985 Intestinal and hepatic ornithine decarboxylase (ODC) activities increased to a peak 4 h after administration of a diet containing casein or an amino acid mixture simulating that of casein to rats starved for 12 h. All amino acids except cysteine with a two or three carbon skeleton, including those with a D-configuration, and alpha-amino-isobutyric acid (AIB) strongly induced intestinal ODC when given in the diet or administered intragastrically. Cysteine 237-245 ornithine decarboxylase 1 Rattus norvegicus 48-51 4044546-3 1985 The amino acids that induced hepatic ODC showed no particular structural characteristics: glycine and cysteine were very effective, threonine, tryptophan, methionine, and phenylalanine were less effective, and serine, valine, isoleucine, and histidine were only slightly effective. Cysteine 102-110 ornithine decarboxylase 1 Rattus norvegicus 37-40 3968065-9 1985 The titration of the two apoenzymes with [14C]NEM and that of the holo-short-chain acyl-CoA dehydrogenase with [14C]pCMB indicated that all three acyl-CoA dehydrogenases contain a single essential cysteine residue/subunit. Cysteine 197-205 acyl-CoA dehydrogenase short chain Rattus norvegicus 71-105 3966926-7 1985 Treatment of rats with SKF 525-A or cysteine inhibited the chloroform-induced elevation of serum glutathione S-transferase activity. Cysteine 36-44 hematopoietic prostaglandin D synthase Rattus norvegicus 97-122 2859259-1 1985 AT-125 (Acivicin) is an inhibitor of gamma-glutamyltranspeptidase (gamma-GTP) which initiates glutathione catabolism to cysteine. Cysteine 120-128 gamma-glutamyltransferase 1 Rattus norvegicus 37-65 2859259-1 1985 AT-125 (Acivicin) is an inhibitor of gamma-glutamyltranspeptidase (gamma-GTP) which initiates glutathione catabolism to cysteine. Cysteine 120-128 gamma-glutamyltransferase 1 Rattus norvegicus 67-76 2859259-7 1985 N-acetylcysteine was administered to AT-125 treated rats in an attempt to supply cysteine to the brain in the face of gamma-GTP inhibition. Cysteine 8-16 gamma-glutamyltransferase 1 Rattus norvegicus 118-127 6487641-3 1984 Assuming the random orientation factor, K2, to be 2/3, the distance between Cys-373 residue of actin and SH1 of myosin subfragment-1 was calculated to be about 50 A, in agreement with the values previously reported, 60 A (Takashi, R. (1969) Biochemistry 18, 5164-69) and 50 A (Trayer, H.R. Cysteine 76-79 myosin heavy chain 14 Homo sapiens 112-118 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. Cysteine 131-134 cannabinoid receptor 2 Homo sapiens 0-3 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. Cysteine 143-146 cannabinoid receptor 2 Homo sapiens 0-3 6203905-10 1984 CB12 contains 1 Cys residue (Cys-35), bridged to Cys-1 of CB15. Cysteine 16-19 cystin 1 Homo sapiens 49-54 6203905-10 1984 CB12 contains 1 Cys residue (Cys-35), bridged to Cys-1 of CB15. Cysteine 29-32 cystin 1 Homo sapiens 49-54 6373742-4 1984 Cysteine dependence of the initial strain was determined by two linked and interacting mutations, cys3 and cys1 . Cysteine 0-8 cystathionine gamma-lyase CYS3 Saccharomyces cerevisiae S288C 98-102 6477879-0 1984 Structural analysis of the cysteine-containing peptides from the major 3-methylcholanthrene-induced isozyme of cytochrome P-450 (P-450c) in rat liver microsomes. Cysteine 27-35 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 129-135 6477879-3 1984 One cysteine-containing peptide (Tsa-56) was shown to possess 46-69% homology with a common peptide found in five other cytochromes P-450 but is not anticipated to be the heme-binding segment on the basis of X-ray crystallographic results obtained with Pseudomonas putida cytochrome P-450cam. Cysteine 4-12 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 132-137 6477879-4 1984 Analysis of the other cysteine-containing peptides in cytochrome P-450c revealed two peptides (Tsa-54 and T-46) of only limited homology with the highly conserved region of cytochromes P-450cam, P-450LM2, P-450b, and P-450e that are all presumed to contain the heme-binding cysteine. Cysteine 22-30 cytochrome P450, family 1, subfamily a, polypeptide 1 Rattus norvegicus 65-71 6325433-5 1984 Diglyceride modification of the Cys residue at the site of signal sequence cleavage probably precedes and is a prerequisite for processing of the TraTp signal sequence. Cysteine 32-35 IncI1 conjugal transfer protein TraT Escherichia coli 146-151 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. Cysteine 75-84 Thy-1 cell surface antigen Homo sapiens 177-182 6323443-7 1984 Cysteine-128 is also present in rat and sheep liver fructose 1,6-bisphosphatase and a long stretch of the sequence around this reactive cysteine residue is highly conserved. Cysteine 0-8 fructose-bisphosphatase 1 Sus scrofa 52-79 6713598-7 1984 Covalent binding of the acetaminophen metabolite to bovine alpha s1-casein, a soluble protein which does not contain any cysteine residues, was found to occur to an extent of 37% of that which became bound to native BSA. Cysteine 121-129 casein alpha s1 Bos taurus 59-74 6085260-5 1984 Cysteine (Cys) reduced the frequency of the induced SSB-dependent CAs in all treatments, but had no influence on the SCE frequencies after BLM and H2O2 treatment and had only a slight effect on the UV-induced SCEs. Cysteine 0-8 lupus La protein Cricetulus griseus 52-55 6085260-5 1984 Cysteine (Cys) reduced the frequency of the induced SSB-dependent CAs in all treatments, but had no influence on the SCE frequencies after BLM and H2O2 treatment and had only a slight effect on the UV-induced SCEs. Cysteine 0-3 lupus La protein Cricetulus griseus 52-55 6661183-7 1983 The results obtained with iodoacetamide show that in the dimeric fatty acid synthase modification of one cysteine-SH condensing site and/or one pantetheine-SH site per dimer is sufficient to affect inhibition of condensing activity and the activity for fatty acid synthesis, and are in accord with a recently proposed model for the mechanism of action of animal fatty acid synthases [Kumar (1982) J. Theor. Cysteine 105-113 fatty acid synthase Gallus gallus 65-84 6579541-5 1983 Of the two highly conserved cysteinyl peptides in P-450LM2, P-450b, and bacterial P-450cam, we favor, on the basis of our model, the one nearer the NH2 terminus (Cys-152 in P-450LM2) as the source of the thiolate ligand to the heme iron atom. Cysteine 162-165 cytochrome P450 2B4 Oryctolagus cuniculus 50-58 6579541-5 1983 Of the two highly conserved cysteinyl peptides in P-450LM2, P-450b, and bacterial P-450cam, we favor, on the basis of our model, the one nearer the NH2 terminus (Cys-152 in P-450LM2) as the source of the thiolate ligand to the heme iron atom. Cysteine 162-165 cytochrome P450 2B4 Oryctolagus cuniculus 173-181 187171-0 1976 Identification of cysteine as the reactive group in pyruvate kinase alkylated by 5-chloro-4-oxopentanoic acid. Cysteine 18-26 pyruvate kinase PKLR Oryctolagus cuniculus 52-67 974110-1 1976 A fluorescent probe N-(3-pyrene)maleimide was conjugated to rabbit skeletal F-actin at the site of most reactive sulfhydryl group (Cys-373). Cysteine 131-134 actin Oryctolagus cuniculus 78-83 974110-2 1976 Its fluorescence anisotropy decay showed a single correlation time of 560 ns at 25 degrees C, which is in a very good agreement with the correlation time of the dansyl-L-cysteine group conjugated to the same site of F-actin reported very recently [Wahl, Ph., Mihashi, K, and Auchet, J-C. (1975) FEBS Lett. Cysteine 168-178 actin Oryctolagus cuniculus 218-223 781677-4 1976 p44, p39, and p34 were purified, and comparison of their amino acid compositions showed that the COOH-terminal peptide removed by the first papain cleavage is hydrophilic and contains cysteine that can be alkylated after mild reduction. Cysteine 184-192 zinc finger CCCH-type containing 12D Homo sapiens 14-17 1061133-4 1976 When the complex, (S-1)-F-actin, is formed, the reactivity of SH1 is strongly decreased, and the reactivity of Cys-10 is strongly increased. Cysteine 111-114 actin Oryctolagus cuniculus 26-31 1213659-6 1975 The analgoue [Bmp1, Val8] -HCT, with a deaminated cysteine residue at the N-terminus, was about 6 times more potent than HCT and slightly longer-acting than [Val8] -HCT. Cysteine 50-58 bone morphogenetic protein 1 Homo sapiens 14-18 765256-3 1975 The amino acid composition of [alpha1 (III)]3 purified by CM-cellulose chromatography and agarose-gel chromatography includes two cysteine residues per chain, and the hydroxyproline/proline ratio is greater than 1.0. Cysteine 130-138 adrenoceptor alpha 1D Homo sapiens 30-45 1103145-1 1975 The decrease in amplitude of the electron spin resonance spectrum of the cysteine-bound spin-label, 3-(maleimidomethyl)-2,2,5,5-tetramethyl-1-pyrrolidinoxyl, brought about by the magnetic interaction with tightly bound manganous ion, was used as a probe of conformational change in actin on binding myosin. Cysteine 73-81 myosin heavy chain 14 Homo sapiens 299-305 804325-5 1975 Of a total of 17 cysteine residues, 14 were located in regions of the molecule which were identical or homologous in the alpha1 and alpha2 chains. Cysteine 17-25 adrenoceptor alpha 1D Homo sapiens 121-138 16656864-8 1968 This was verified by reactivation with exogenous cysteine.Based on these current findings, and previous work, it is concluded that nitrate reductase is a single moiety with the ability to utilize either NADH or FMNH(2) as cofactor. Cysteine 49-57 nitrate reductase [NADH] 1 Zea mays 131-148 14253482-6 1965 Papain and cysteine treatment produced Fc (fast) and Fab (slow) fragments. Cysteine 11-19 FA complementation group B Homo sapiens 53-56 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. Cysteine 95-103 thioredoxin Homo sapiens 184-195 33980892-4 2021 Unlike other JAKs, JAK3 possesses a cysteine in its ATP binding pocket and this has allowed the design of isoform selective covalent JAK3 inhibitors targeting this residue. Cysteine 36-44 Janus kinase 3 Homo sapiens 19-23 33980892-4 2021 Unlike other JAKs, JAK3 possesses a cysteine in its ATP binding pocket and this has allowed the design of isoform selective covalent JAK3 inhibitors targeting this residue. Cysteine 36-44 Janus kinase 3 Homo sapiens 133-137 33980892-5 2021 We report here that mutating this cysteine to serine does not prevent JAK3 catalytic activity but does greatly increase the IC50 for covalent JAK3 inhibitors. Cysteine 34-42 Janus kinase 3 Homo sapiens 142-146 33885283-5 2021 Covalent adduct formation with the catalytic cysteine residue was validated by gel analysis and mass spectrometry of intact ABP-treated USP16CDWT and catalytically inactive mutant USP16CDC205A. Cysteine 45-53 ubiquitin specific peptidase 16 Homo sapiens 136-141 33961881-1 2021 Secreted protein acidic and rich in cysteine (SPARC) is an extracellular and non-structural glycoprotein. Cysteine 36-44 secreted protein acidic and cysteine rich Homo sapiens 46-51 33676679-5 2021 These properties make Cy-1 a promising probe for c-myc G-quadruplex recognition in nanotechnology or biology. Cysteine 22-24 MYC proto-oncogene, bHLH transcription factor Homo sapiens 49-54 33898742-0 2021 Novel Cysteine-Sparing Hypomorphic NOTCH3 A1604T Mutation Observed in a Family With Migraine and White Matter Lesions. Cysteine 6-14 notch receptor 3 Homo sapiens 35-41 33898742-6 2021 Most CADASIL mutations alter the number of cysteine residues in the extracellular domain of the NOTCH3 receptor, but in this article, we describe a family in which some members carry a novel cysteine-sparing NOTCH3 mutation (c.4810 G>A, p.Ala1604Thr). Cysteine 43-51 notch receptor 3 Homo sapiens 96-102 33898742-6 2021 Most CADASIL mutations alter the number of cysteine residues in the extracellular domain of the NOTCH3 receptor, but in this article, we describe a family in which some members carry a novel cysteine-sparing NOTCH3 mutation (c.4810 G>A, p.Ala1604Thr). Cysteine 191-199 notch receptor 3 Homo sapiens 96-102 33898742-10 2021 Conclusions: We identify a family with migraine and WML in which some members carry a cysteine-sparing hypomorphic NOTCH3 mutation. Cysteine 86-94 notch receptor 3 Homo sapiens 115-121 33876866-3 2021 A single cysteine (Cys1) was also found thousand times more reactive toward GSSG, making speculate that a single glutathionylation could represent the primordial event of its oxidative folding. Cysteine 9-17 cystin 1 Homo sapiens 19-23 33035318-2 2021 Unlike most SNARE proteins, Ykt6 lacks a transmembrane domain but instead has a tandem cysteine motif at the C-terminus. Cysteine 87-95 YKT6 v-SNARE homolog Homo sapiens 28-32 33035318-3 2021 Recently, we have demonstrated that Ykt6 undergoes double prenylation at the C-terminal two cysteines first by farnesyltransferase and then by a newly identified protein prenyltransferase named geranylgeranyltransferase type-III (GGTase-III). Cysteine 92-101 YKT6 v-SNARE homolog Homo sapiens 36-40 33903070-5 2021 The NDPK activity of NME1 has been shown to be inhibited in vitro and in vivo under oxidative stress, and the inhibitory effect mediated via redox-sensitive cysteine residues. Cysteine 157-165 cytidine/uridine monophosphate kinase 2 Homo sapiens 4-8 33792991-4 2021 The C-terminal Cys-533 was identified as the S-acylation residue and mutation of Cys-533 to Ala-533 of NPC4 (NPC4C533A ) led to the loss of S-acylation and membrane association of NPC4. Cysteine 15-18 non-specific phospholipase C4 Arabidopsis thaliana 103-107 33792991-4 2021 The C-terminal Cys-533 was identified as the S-acylation residue and mutation of Cys-533 to Ala-533 of NPC4 (NPC4C533A ) led to the loss of S-acylation and membrane association of NPC4. Cysteine 15-18 non-specific phospholipase C4 Arabidopsis thaliana 109-118 33792991-4 2021 The C-terminal Cys-533 was identified as the S-acylation residue and mutation of Cys-533 to Ala-533 of NPC4 (NPC4C533A ) led to the loss of S-acylation and membrane association of NPC4. Cysteine 15-18 non-specific phospholipase C4 Arabidopsis thaliana 109-113 33792991-7 2021 In addition, NPC4 in Brassica napus was S-acylated and mutation of the S-acylating cysteine residue of BnaC01.NPC4 led to the loss of S-acylation and its membrane association. Cysteine 83-91 non-specific phospholipase C4 Arabidopsis thaliana 13-17 33792991-7 2021 In addition, NPC4 in Brassica napus was S-acylated and mutation of the S-acylating cysteine residue of BnaC01.NPC4 led to the loss of S-acylation and its membrane association. Cysteine 83-91 non-specific phospholipase C4 Arabidopsis thaliana 110-114 33713778-4 2021 Spatial and temporal fluctuations in total glutathione (GSH) and total cysteine (Cys) redox steady states were seen during a 24 hr period of CD-1 mouse organogenesis in untreated conceptuses and following exposure to VPA and the Nrf2 antioxidant pathway inducer, 1,2-dithiole-3-thione (D3T). Cysteine 71-79 CD1 antigen complex Mus musculus 141-145 33713778-4 2021 Spatial and temporal fluctuations in total glutathione (GSH) and total cysteine (Cys) redox steady states were seen during a 24 hr period of CD-1 mouse organogenesis in untreated conceptuses and following exposure to VPA and the Nrf2 antioxidant pathway inducer, 1,2-dithiole-3-thione (D3T). Cysteine 81-84 CD1 antigen complex Mus musculus 141-145 33781185-2 2021 PCTAIRE kinases (PCTKs) are a CDK subfamily, characterized by serine to cysteine mutation in the consensus PSTAIRE motif, involved in binding to the cyclin. Cysteine 72-80 cyclin dependent kinase 18 Homo sapiens 30-33 33781185-2 2021 PCTAIRE kinases (PCTKs) are a CDK subfamily, characterized by serine to cysteine mutation in the consensus PSTAIRE motif, involved in binding to the cyclin. Cysteine 72-80 proliferating cell nuclear antigen Homo sapiens 149-155 33757126-2 2022 SPARC (Secreted Protein Acidic and Rich in Cysteine)-related modular calcium binding 1 (SMOC1) is a regulator of BMP2 signalling, but the role of SMOC1 in aortic valve calcification under different conditions has not been studied. Cysteine 43-51 secreted protein acidic and cysteine rich Homo sapiens 0-5 33731877-6 2021 In-frame variants could be subdivided according to their impact on the cysteine content of fibrillin-1 with a global higher severity for cysteine loss variants and the highest frequency of EL surgery for cysteine addition variants. Cysteine 71-79 fibrillin 1 Homo sapiens 91-102 33731877-6 2021 In-frame variants could be subdivided according to their impact on the cysteine content of fibrillin-1 with a global higher severity for cysteine loss variants and the highest frequency of EL surgery for cysteine addition variants. Cysteine 137-145 fibrillin 1 Homo sapiens 91-102 33724210-3 2021 The cysteine knot motif of TGF-beta can stabilize the structure of MSTN protein and plays an important regulatory role in the biological function of MSTN. Cysteine 4-12 myostatin Sus scrofa 67-71 33724210-3 2021 The cysteine knot motif of TGF-beta can stabilize the structure of MSTN protein and plays an important regulatory role in the biological function of MSTN. Cysteine 4-12 myostatin Sus scrofa 149-153 33724210-4 2021 Accordingly, in this study, we used the CRISRP/Cas9 to edit the exon 3 of MSTN in the kidney cells of Liang Guang Small Spotted pig (LPKCs), in order to disrupt the cysteine knot motif of MSTN and remove the inhibitory effect of MSTN on its target genes.MSTN-edited LPKCs were obtained through fluorescence-activated cell sorting (FACS) and used as donor cells for somatic cell nuclear transfer (SCNT) to generate cloned embryos, which were then transferred to surrogate sows to finally obtain eight MSTN-edited Liang Guang Small Spotted piglets. Cysteine 165-173 myostatin Sus scrofa 74-78 33724210-4 2021 Accordingly, in this study, we used the CRISRP/Cas9 to edit the exon 3 of MSTN in the kidney cells of Liang Guang Small Spotted pig (LPKCs), in order to disrupt the cysteine knot motif of MSTN and remove the inhibitory effect of MSTN on its target genes.MSTN-edited LPKCs were obtained through fluorescence-activated cell sorting (FACS) and used as donor cells for somatic cell nuclear transfer (SCNT) to generate cloned embryos, which were then transferred to surrogate sows to finally obtain eight MSTN-edited Liang Guang Small Spotted piglets. Cysteine 165-173 myostatin Sus scrofa 188-192 33724210-4 2021 Accordingly, in this study, we used the CRISRP/Cas9 to edit the exon 3 of MSTN in the kidney cells of Liang Guang Small Spotted pig (LPKCs), in order to disrupt the cysteine knot motif of MSTN and remove the inhibitory effect of MSTN on its target genes.MSTN-edited LPKCs were obtained through fluorescence-activated cell sorting (FACS) and used as donor cells for somatic cell nuclear transfer (SCNT) to generate cloned embryos, which were then transferred to surrogate sows to finally obtain eight MSTN-edited Liang Guang Small Spotted piglets. Cysteine 165-173 myostatin Sus scrofa 188-192 33724210-4 2021 Accordingly, in this study, we used the CRISRP/Cas9 to edit the exon 3 of MSTN in the kidney cells of Liang Guang Small Spotted pig (LPKCs), in order to disrupt the cysteine knot motif of MSTN and remove the inhibitory effect of MSTN on its target genes.MSTN-edited LPKCs were obtained through fluorescence-activated cell sorting (FACS) and used as donor cells for somatic cell nuclear transfer (SCNT) to generate cloned embryos, which were then transferred to surrogate sows to finally obtain eight MSTN-edited Liang Guang Small Spotted piglets. Cysteine 165-173 myostatin Sus scrofa 188-192 33724210-4 2021 Accordingly, in this study, we used the CRISRP/Cas9 to edit the exon 3 of MSTN in the kidney cells of Liang Guang Small Spotted pig (LPKCs), in order to disrupt the cysteine knot motif of MSTN and remove the inhibitory effect of MSTN on its target genes.MSTN-edited LPKCs were obtained through fluorescence-activated cell sorting (FACS) and used as donor cells for somatic cell nuclear transfer (SCNT) to generate cloned embryos, which were then transferred to surrogate sows to finally obtain eight MSTN-edited Liang Guang Small Spotted piglets. Cysteine 165-173 myostatin Sus scrofa 188-192 32770227-6 2020 The cysteine 292 of HDAC4 is a key site for its sumo E3 ligase activity. Cysteine 4-12 histone deacetylase 4 Homo sapiens 20-25 33678736-0 2021 Heterozygous Cysteine-sparing NOTCH3 Variant p.Val237Met in a Japanese Patient with Suspected Cerebral Autosomal Dominant Arteriopathy with Subcortical Infarcts and Leukoencephalopathy: A Case Report. Cysteine 13-21 notch receptor 3 Homo sapiens 30-36 33678736-2 2021 The cysteine-sparing variation p.Val237Met was identified in NOTCH3. Cysteine 4-12 notch receptor 3 Homo sapiens 61-67 33480363-3 2021 Taking microRNA-21 (miRNA-21) as an analytical model, a label-free electrochemical sensor was designed according to the properties of the Pl-Cys/MoS2 sensing interface. Cysteine 141-144 microRNA 21 Homo sapiens 7-18 33480363-3 2021 Taking microRNA-21 (miRNA-21) as an analytical model, a label-free electrochemical sensor was designed according to the properties of the Pl-Cys/MoS2 sensing interface. Cysteine 141-144 microRNA 21 Homo sapiens 20-28 33460958-4 2021 We found that L-Cysteine treatment skewed CD11b+/CD45low microglia and CD11b+/CD45high brain monocytes/macrophages towards a more anti-inflammatory property 72 h after HI-injured brain. Cysteine 14-24 protein tyrosine phosphatase, receptor type, C Mus musculus 49-53 33460958-4 2021 We found that L-Cysteine treatment skewed CD11b+/CD45low microglia and CD11b+/CD45high brain monocytes/macrophages towards a more anti-inflammatory property 72 h after HI-injured brain. Cysteine 14-24 protein tyrosine phosphatase, receptor type, C Mus musculus 78-82 33717051-11 2020 Transcripts based on IGHV7-4-1*01 that had undergone somatic hypermutation and class switch had mutated the codon that encoded the unusual residue in framework region 3 (cysteine 92; located far from the antigen binding site). Cysteine 170-178 immunoglobulin heavy variable 7-4-1 Homo sapiens 21-30 33669258-6 2021 Global proteome comparison of cells over-expressing DJ-1 DeltaH8 with native or mutated active site cysteine indicated a strong impact on mitochondrial biology. Cysteine 100-108 Parkinsonism associated deglycase Homo sapiens 52-56 32472188-4 2021 We found that alpha5-containing nAChRs are irreversibly blocked by methanethiosulfonate (MTS) reagents through a covalent reaction with a cysteine present only in alpha5. Cysteine 138-146 immunoglobulin kappa variable 2D-26 Homo sapiens 14-20 32472188-4 2021 We found that alpha5-containing nAChRs are irreversibly blocked by methanethiosulfonate (MTS) reagents through a covalent reaction with a cysteine present only in alpha5. Cysteine 138-146 immunoglobulin kappa variable 2D-26 Homo sapiens 163-169 33285240-2 2021 Cystine taken up by the cells via xCT is reduced to cysteine, which is used to synthesize glutathione for antioxidant cellular defense. Cysteine 52-60 solute carrier family 7 member 11 Homo sapiens 34-37 33001274-5 2021 The use of cysteine as a sulfur source led to the production of methionine via hydrogen sulfide synthesis mediated by CYS4 (CNA06170), CYS3 (CNN01730), and MST1 (CND03690). Cysteine 11-19 threonine--tRNA ligase MST1 Saccharomyces cerevisiae S288C 156-160 33001274-7 2021 Although the hypothesis that hydrogen sulfide is produced from cysteine via CYS4, CYS3, and MST1 warrants further study, the new insight into the metabolic pathway of sulfur-containing amino acids in C. neoformans provided here indicates the usefulness of this system in the development of screening tools for antifungal drug agents. Cysteine 63-71 threonine--tRNA ligase MST1 Saccharomyces cerevisiae S288C 92-96 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 8-oxoguanine DNA glycosylase Homo sapiens 91-96 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 8-oxoguanine DNA glycosylase Homo sapiens 91-96 33372419-10 2021 Interestingly, p53 and EGFR exon 19 deletion mutations were more frequent in patients with hOGG1 Ser/Cys + Cys/Cys hOGG1-Cys variants than with the hOGG1 Ser/Ser genotype (P = 0.010 for p53, P = 0.032 for EGFR). Cysteine 107-110 8-oxoguanine DNA glycosylase Homo sapiens 91-96 33372419-12 2021 KEY POINTS: SIGNIFICANT FINDINGS OF THE STUDY: NSCLC patients with hOGG1-Cys variants may have a higher risk of p53 and EGFR deletion mutations than with hOGG1 Ser/Ser genotype. Cysteine 73-76 8-oxoguanine DNA glycosylase Homo sapiens 67-72 33372419-12 2021 KEY POINTS: SIGNIFICANT FINDINGS OF THE STUDY: NSCLC patients with hOGG1-Cys variants may have a higher risk of p53 and EGFR deletion mutations than with hOGG1 Ser/Ser genotype. Cysteine 73-76 8-oxoguanine DNA glycosylase Homo sapiens 154-159 33372419-13 2021 WHAT THIS STUDY ADDS: NSCLC patients with hOGG1-Cys variants might be helpful to predict patients having higher risk of EGFR exon 19 deletion mutations and these patients who were treated with gefitinib or erlotinib could be a higher risk to occur EGFR T790M mutation. Cysteine 48-51 8-oxoguanine DNA glycosylase Homo sapiens 42-47 32966806-0 2021 Discovery of a Functional Covalent Ligand Targeting an Intrinsically Disordered Cysteine within MYC. Cysteine 80-88 MYC proto-oncogene, bHLH transcription factor Homo sapiens 96-99 32966806-2 2021 Here, we have performed a cysteine-reactive covalent ligand screen to identify compounds that could disrupt the binding of MYC to its DNA consensus sequence in vitro and also impair MYC transcriptional activity in situ in cells. Cysteine 26-34 MYC proto-oncogene, bHLH transcription factor Homo sapiens 123-126 32966806-2 2021 Here, we have performed a cysteine-reactive covalent ligand screen to identify compounds that could disrupt the binding of MYC to its DNA consensus sequence in vitro and also impair MYC transcriptional activity in situ in cells. Cysteine 26-34 MYC proto-oncogene, bHLH transcription factor Homo sapiens 182-185 32966806-3 2021 We have identified a covalent ligand, EN4, that targets cysteine 171 of MYC within a predicted intrinsically disordered region of the protein. Cysteine 56-64 MYC proto-oncogene, bHLH transcription factor Homo sapiens 72-75 33466919-4 2021 Similarly, hVKORC1 is analysed in its native state, where two pairs of cysteine residues are covalently linked, forming two disulphide bridges, as a target for Trx-fold proteins. Cysteine 71-79 vitamin K epoxide reductase complex subunit 1 Homo sapiens 11-18 33466919-4 2021 Similarly, hVKORC1 is analysed in its native state, where two pairs of cysteine residues are covalently linked, forming two disulphide bridges, as a target for Trx-fold proteins. Cysteine 71-79 thioredoxin Homo sapiens 160-163 33365082-6 2021 mRNA expression levels of cystine/glutamate antiporter xCT (SLC7A11), a key component of the cysteine/glutamate antiporter, were measured using reverse transcription-quantitative PCR, while the levels of SLC7A11 protein were measured using western blot analysis. Cysteine 93-101 solute carrier family 7 member 11 Homo sapiens 55-58 33365082-6 2021 mRNA expression levels of cystine/glutamate antiporter xCT (SLC7A11), a key component of the cysteine/glutamate antiporter, were measured using reverse transcription-quantitative PCR, while the levels of SLC7A11 protein were measured using western blot analysis. Cysteine 93-101 solute carrier family 7 member 11 Homo sapiens 60-67 33317395-0 2020 Role of cysteines in accelerating Tau filament formation. Cysteine 8-17 microtubule associated protein tau Homo sapiens 34-37 33317395-3 2020 The two cysteine residues and the two hexapeptide regions of full-length Tau play a key role in initialization and filament formation during Tau aggregation. Cysteine 8-16 microtubule associated protein tau Homo sapiens 73-76 33317395-3 2020 The two cysteine residues and the two hexapeptide regions of full-length Tau play a key role in initialization and filament formation during Tau aggregation. Cysteine 8-16 microtubule associated protein tau Homo sapiens 141-144 33317395-4 2020 The role of cysteine residues in Tau aggregation has been studied by in-vitro aggregation assay that was measured by Thioflavin S fluorescence to observe the kinetics of aggregation. Cysteine 12-20 microtubule associated protein tau Homo sapiens 33-36 33317395-6 2020 Here, we report that cysteine mutant full-length Tau can aggregate to form filaments under in-vitro conditions. Cysteine 21-29 microtubule associated protein tau Homo sapiens 49-52 33317395-9 2020 On the other hand, the cysteine mutant delayed the initial Tau aggregation. Cysteine 23-31 microtubule associated protein tau Homo sapiens 59-62 33317395-10 2020 This indicates the importance of cysteine residues in accelerating initial Tau nucleation for its aggregation. Cysteine 33-41 microtubule associated protein tau Homo sapiens 75-78 33317395-11 2020 The filament morphology of wild-type and cysteine mutant Tau has been characterized using transmission electron microscopy and high-resolution transmission electron microscopy. Cysteine 41-49 microtubule associated protein tau Homo sapiens 57-60 33292080-3 2022 Here, we develop a cysteine-bounded cyclic peptide (CYS-cIHL) and linear peptide (CYS-IHL), using the conserved inhibitory hairpin loop amino acid sequence. Cysteine 19-27 CIHL Homo sapiens 56-60 33292080-3 2022 Here, we develop a cysteine-bounded cyclic peptide (CYS-cIHL) and linear peptide (CYS-IHL), using the conserved inhibitory hairpin loop amino acid sequence. Cysteine 52-55 CIHL Homo sapiens 56-60 33292080-6 2022 CYS-cIHL was able to bind with micromolar affinity to FP-2 and modulate its binding with its substrate, hemoglobin in in vitro and in vivo assays. Cysteine 0-3 CIHL Homo sapiens 4-8 33292080-7 2022 CYS-cIHL could effectively block parasite growth and displayed antimalarial activity in culture assays with no cytotoxicity towards human cells. Cysteine 0-3 CIHL Homo sapiens 4-8 33273012-6 2021 Here we use quantitative mass spectrometry (MS) and electrophoretic mobility analyses to show that KO likely forms a covalent complex with a cysteine mutant mimicking hVKOR in a partially oxidized state. Cysteine 141-149 vitamin K epoxide reductase complex subunit 1 Homo sapiens 167-172 33273012-8 2021 To investigate this activity, we analyze the correlation between the cellular activity and the cellular cysteine status of hVKOR. Cysteine 104-112 vitamin K epoxide reductase complex subunit 1 Homo sapiens 123-128 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. Cysteine 14-22 heat shock protein 90 alpha family class A member 1 Homo sapiens 48-53 32181977-4 2020 We revealed CD9 lipidation at its three most frequent lipidated sites suffices for EWI-F binding, while cysteine to alanine CD9 mutations markedly reduced binding of EWI-F. Cysteine 104-112 prostaglandin F2 receptor inhibitor Homo sapiens 166-171 32876851-6 2020 Target CD34 cells yield of 5 x 106/kg was achieved with single apheresis in 58.6% of patients after B-Cy-GCSF mobilization as compared to 44.3% in Cy-GCSF group (p = 0.07). Cysteine 102-104 colony stimulating factor 3 Homo sapiens 105-109 32876851-8 2020 Addition of bortezomib to Cy-GCSF mobilization showed a trend towards increased CD34 collection and reduced need for apheresis sessions. Cysteine 26-28 colony stimulating factor 3 Homo sapiens 29-33 32780264-0 2020 Aggregation-Induced Emission Properties of Glutathione and L-Cysteine Capped CdS Quantum Dots and their Application as Zn(II) Probe. Cysteine 59-69 CDP-diacylglycerol synthase 1 Homo sapiens 77-80 32780264-1 2020 Targeting to obtain better water solubility and stability and less aggregation-caused quenching effects of quantum dots, two kinds of thiol molecules, glutathione and L-cysteine, were firstly united to offer stabilizing ligands for aqueous synthesized CdS quantum dots, which exhibited sensitive aggregation-induced emission properties. Cysteine 167-177 CDP-diacylglycerol synthase 1 Homo sapiens 252-255 32529779-1 2020 A pair of 9-mesityl-10-phenyl acridinium (Mes-Acr + ) photoredox catalysts were synthesized with an iodoacetamide handle for cysteine bioconjugation. Cysteine 125-133 acrosin Homo sapiens 46-49 32558168-3 2020 Here we probe the interaction of the p66/p66" asymmetric reverse transcriptase precursor with HIV-1 protease by pulsed Q-band double electron-electron resonance EPR spectroscopy to measure distances between nitroxide labels introduced at surface engineered cysteine residues. Cysteine 257-265 DNA polymerase delta 3, accessory subunit Homo sapiens 37-40 32558168-3 2020 Here we probe the interaction of the p66/p66" asymmetric reverse transcriptase precursor with HIV-1 protease by pulsed Q-band double electron-electron resonance EPR spectroscopy to measure distances between nitroxide labels introduced at surface engineered cysteine residues. Cysteine 257-265 DNA polymerase delta 3, accessory subunit Homo sapiens 41-44 33084974-2 2021 Variants are frequently located in the RET extracellular cysteine-rich region domain, mainly affecting cysteines which are replaced by an alternative amino acid, resulting in a mispaired cysteine and the generation of RET dimers. Cysteine 57-65 ret proto-oncogene Homo sapiens 218-221 33084974-2 2021 Variants are frequently located in the RET extracellular cysteine-rich region domain, mainly affecting cysteines which are replaced by an alternative amino acid, resulting in a mispaired cysteine and the generation of RET dimers. Cysteine 103-112 ret proto-oncogene Homo sapiens 39-42 33084974-2 2021 Variants are frequently located in the RET extracellular cysteine-rich region domain, mainly affecting cysteines which are replaced by an alternative amino acid, resulting in a mispaired cysteine and the generation of RET dimers. Cysteine 103-112 ret proto-oncogene Homo sapiens 218-221 33084974-2 2021 Variants are frequently located in the RET extracellular cysteine-rich region domain, mainly affecting cysteines which are replaced by an alternative amino acid, resulting in a mispaired cysteine and the generation of RET dimers. Cysteine 103-111 ret proto-oncogene Homo sapiens 39-42 33084974-2 2021 Variants are frequently located in the RET extracellular cysteine-rich region domain, mainly affecting cysteines which are replaced by an alternative amino acid, resulting in a mispaired cysteine and the generation of RET dimers. Cysteine 103-111 ret proto-oncogene Homo sapiens 218-221 33084974-3 2021 We describe a novel c.1765A > T variant of RET proto-oncogene in a family with medullary thyroid carcinoma (MTC) that predicts the creation of an additional cysteine p.(Ser589Cys) in the cysteine-rich domain. Cysteine 157-165 ret proto-oncogene Homo sapiens 43-46 33084974-3 2021 We describe a novel c.1765A > T variant of RET proto-oncogene in a family with medullary thyroid carcinoma (MTC) that predicts the creation of an additional cysteine p.(Ser589Cys) in the cysteine-rich domain. Cysteine 187-195 ret proto-oncogene Homo sapiens 43-46 32470580-10 2020 In-silico molecular docking study of cobra CRISP with TLR4-MD2 receptor complex reveals Nk-CRISP engages cysteine-rich domain (CRD) to interact with complex. Cysteine 105-113 toll like receptor 4 Homo sapiens 54-58 33000151-5 2020 Excess Cys is oxidized by cysteine dioxygenase 1 (CDO1) and further metabolized to taurine or sulfate. Cysteine 7-10 cysteine dioxygenase type 1 Homo sapiens 26-48 33000151-5 2020 Excess Cys is oxidized by cysteine dioxygenase 1 (CDO1) and further metabolized to taurine or sulfate. Cysteine 7-10 cysteine dioxygenase type 1 Homo sapiens 50-54 32898818-6 2020 In addition, FOCAD promoted the activity of focal adhesion kinase (FAK), which further enhanced the sensitivity of NSCLC cells to cysteine deprivation-induced ferroptosis via promoting the tricarboxylic acid (TCA) cycle and the activity of Complex I in mitochondrial electron transport chain (ETC). Cysteine 130-138 focadhesin Homo sapiens 13-18 32898818-9 2020 Taken together, our study indicates the close association of NRF2-FOCAD-FAK signaling pathway with cysteine deprivation-induced ferroptosis, and elucidates a novel insight into the ferroptosis-based therapeutic approach for the patients with NSCLC. Cysteine 99-107 focadhesin Homo sapiens 66-71 33035814-10 2020 Oxidation of specific cysteines in Proliferating Cell Nuclear Antigen (PCNA) could interfere with entry into mitosis. Cysteine 22-31 proliferating cell nuclear antigen Homo sapiens 35-69 32948239-6 2020 We identified a paternal heterozygous germline mutation c.1852 T > C, which results in the substitution of cysteine by arginine in the RET-receptor tyrosine kinase (p.C618R mutation). Cysteine 107-115 ret proto-oncogene Homo sapiens 135-163 32160317-1 2020 PURPOSE: Hydrogen sulfide, a signaling molecule formed mainly from cysteine, is catabolized by sulfide:quinone oxidoreductase (gene SQOR). Cysteine 67-75 crystallin zeta Homo sapiens 103-125 32160317-1 2020 PURPOSE: Hydrogen sulfide, a signaling molecule formed mainly from cysteine, is catabolized by sulfide:quinone oxidoreductase (gene SQOR). Cysteine 67-75 sulfide quinone oxidoreductase Homo sapiens 132-136 32860670-3 2020 Furthermore, Western blot showed that SFN-Cys downregulated CDK4, CDK6 and p-Rb in a dose-dependent manner and these results were reversed by p-ERK1/2 blocker PD98059 in U87MG and U373MG cells. Cysteine 42-45 RNA exonuclease 2 Homo sapiens 38-41 32860670-5 2020 Interestingly, SFN-Cys decreased CDK4 and CDK6 by phosphorylated ERK1/2-caused proteasomal degradation resulting in decreased Rb phosphorylation contributing to cell cycle arrest in G0/G1 phase. Cysteine 19-22 RNA exonuclease 2 Homo sapiens 15-18 32860670-6 2020 Besides, Western blot showed that SFN-Cys downregulated alpha-tubulin resulting in microtubule disruption and aggregation, and cell cycle arrest in G2/M phase and apoptosis. Cysteine 38-41 RNA exonuclease 2 Homo sapiens 34-37 32860670-6 2020 Besides, Western blot showed that SFN-Cys downregulated alpha-tubulin resulting in microtubule disruption and aggregation, and cell cycle arrest in G2/M phase and apoptosis. Cysteine 38-41 tubulin alpha 1b Homo sapiens 56-69 32255665-0 2020 4PBA Restores Signalling of a Cysteine-substituted Mutant BMPR2 Receptor Found in Patients with PAH. Cysteine 30-38 bone morphogenetic protein receptor type 2 Homo sapiens 58-63 32255665-2 2020 Point mutations in the BMPR2 ligand binding domain involving cysteine residues (such as C118W) are causative of PAH and predicted to cause protein misfolding. Cysteine 61-69 bone morphogenetic protein receptor type 2 Homo sapiens 23-28 32255665-11 2020 These findings demonstrate in primary cells and in a knock-in mouse that the repurposed small molecule chemical chaperone, 4-PBA, might be a promising precision medicine approach to treat PAH in patients with specific subtypes of BMPR2 mutation involving cysteine substitutions in the ligand binding domain. Cysteine 255-263 bone morphogenetic protein receptor type 2 Homo sapiens 230-235 32243901-6 2020 Mechanistically, SFN modifies several cysteine residues, including C204, located in the RBCC domain of PML. Cysteine 38-46 PML nuclear body scaffold Homo sapiens 103-106 31960911-2 2020 Here, we report individuals with a cysteine altering NOTCH3 variant that induces exon 9 skipping, mimicking therapeutic NOTCH3 cysteine correction. Cysteine 127-135 notch receptor 3 Homo sapiens 53-59 31960911-2 2020 Here, we report individuals with a cysteine altering NOTCH3 variant that induces exon 9 skipping, mimicking therapeutic NOTCH3 cysteine correction. Cysteine 127-135 notch receptor 3 Homo sapiens 120-126 31960911-9 2020 In conclusion, this study provides the first in-human evidence that cysteine corrective NOTCH3 exon skipping is associated with less NOTCH3 aggregation and an attenuated phenotype, justifying further therapeutic development of NOTCH3 cysteine correction for CADASIL. Cysteine 68-76 notch receptor 3 Homo sapiens 88-94 31960911-9 2020 In conclusion, this study provides the first in-human evidence that cysteine corrective NOTCH3 exon skipping is associated with less NOTCH3 aggregation and an attenuated phenotype, justifying further therapeutic development of NOTCH3 cysteine correction for CADASIL. Cysteine 68-76 notch receptor 3 Homo sapiens 133-139 31960911-9 2020 In conclusion, this study provides the first in-human evidence that cysteine corrective NOTCH3 exon skipping is associated with less NOTCH3 aggregation and an attenuated phenotype, justifying further therapeutic development of NOTCH3 cysteine correction for CADASIL. Cysteine 68-76 notch receptor 3 Homo sapiens 133-139 31960911-9 2020 In conclusion, this study provides the first in-human evidence that cysteine corrective NOTCH3 exon skipping is associated with less NOTCH3 aggregation and an attenuated phenotype, justifying further therapeutic development of NOTCH3 cysteine correction for CADASIL. Cysteine 234-242 notch receptor 3 Homo sapiens 88-94 32579346-3 2020 IMP-1710 stereoselectively labels the catalytic cysteine of UCHL1 at low nanomolar concentration in cells. Cysteine 48-56 ubiquitin C-terminal hydrolase L1 Homo sapiens 60-65 32552418-4 2020 Methods and Results Forty-nine individuals carrying NOTCH3 cysteine-altering mutations received brain magnetic resonance imaging with T1-weighted and susceptibility-weighted images. Cysteine 59-67 notch receptor 3 Homo sapiens 52-58 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. Cysteine 162-165 aspartate beta-hydroxylase Homo sapiens 0-4 32184133-7 2020 We show that the preservation of brain cysteine level, employing cysteine pro-drug (N-acetyl-L-cysteine, NAC), markedly curtailed effects of HH - not only on endogenous H2S levels but also, impairment of spatial reference memory in our animal model. Cysteine 39-47 synuclein alpha Homo sapiens 105-108 32173650-4 2020 RESULTS: Both Cy/GVAX plus degarelix and degarelix alone led to significant increases in intratumoral CD8+ T cell infiltration and PD-L1 expression as compared to a cohort of untreated, matched controls. Cysteine 14-16 CD274 molecule Homo sapiens 131-136 32173650-6 2020 Although Cy/GVAX followed by degarelix was associated with a modest improvement in time-to-PSA progression and time-to-next treatment as well as an increase in PD-L1, there was no difference in the CD8 T-cell infiltrate as compared to degarelix alone. Cysteine 9-11 CD274 molecule Homo sapiens 160-165 32580473-1 2020 The silencing of SPARC (secreted protein acid and rich in cysteine) gene through methylation of its promoter region represents a common event in many solid tumors and it is frequently associated with tumor progression and an aggressive clinical outcome. Cysteine 58-66 secreted protein acidic and cysteine rich Homo sapiens 17-22 32371394-5 2020 We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation. Cysteine 141-149 sirtuin 2 Homo sapiens 104-109 32371394-5 2020 We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation. Cysteine 141-149 sirtuin 2 Homo sapiens 288-293 32555735-11 2020 CONCLUSIONS: Patients with CADASIL and cysteine-sparing NOTCH3 mutations showed less involvement of the anterior temporal lobes in brain MRI than those with CADASIL and cysteine-involving NOTCH3 mutations, although both groups showed similar clinical characteristics. Cysteine 169-177 notch receptor 3 Homo sapiens 188-194 32247003-4 2020 In addition, Cys-peptide attenuated TNFalpha-induced cytotoxicity by decreasing soluble fms-like tyrosine kinase-1 (sFlt-1), endothelin-1 (ET-1) and tissue plasminogen activator (tPA) mRNA expression in both cells. Cysteine 13-16 plasminogen activator, tissue type Rattus norvegicus 149-177 32354745-4 2020 The VPA-mediated trafficking correction is in part associated with an increase in the acetylation of lysine residues in the cysteine-rich domain of NPC1. Cysteine 124-132 NPC intracellular cholesterol transporter 1 Homo sapiens 148-152 32487602-2 2020 SPARC, secreted protein, acidic and rich in cysteine, is a multifunctional glycoprotein which has been proposed to be a potential diagnostic marker of invasive meningiomas. Cysteine 44-52 secreted protein acidic and cysteine rich Homo sapiens 0-5 32378256-7 2020 Results showed that TNFalpha exposure increased levels of oxidatively modified cysteine(s) of wt OGG1 without impairing its association with promoter and facilitated gene expression. Cysteine 79-87 8-oxoguanine DNA glycosylase Homo sapiens 97-101 32486313-8 2020 The viscosity of the mucus increased in the presence of 1% PAA-Cys-MNA and PAA-Cys-NAC 5.6- and 10.9-fold, respectively, in comparison to only 1% PAA. Cysteine 79-82 synuclein alpha Homo sapiens 83-86 32486313-11 2020 The retention of PAA, PAA-Cys-MNA, and PAA-Cys-NAC on porcine intestinal mucosa was 25%, 49%, and 76% within 3 h, respectively. Cysteine 43-46 synuclein alpha Homo sapiens 47-50 32677757-6 2020 Further, the comparison between the current work and previous analyses involving alkali metal cationized Met as well as cysteine (the other sulfur containing amino acid) cationized with Zn2+ and Cd2+ allows for the elucidation of important metal dependent trends associated with physiologically important metal-sulfur binding. Cysteine 120-128 CD2 molecule Homo sapiens 195-198 32229256-6 2020 Out of many antioxidant candidates, N-acetyl-L-cysteine (a prodrug of L-cysteine) (NAC) is a potent antioxidant as the bioavailability of the parent drug, L-cysteine, determines the production of glutathione; the universal antioxidant that regulates ROS. Cysteine 45-55 synuclein alpha Homo sapiens 83-86 32229256-6 2020 Out of many antioxidant candidates, N-acetyl-L-cysteine (a prodrug of L-cysteine) (NAC) is a potent antioxidant as the bioavailability of the parent drug, L-cysteine, determines the production of glutathione; the universal antioxidant that regulates ROS. Cysteine 70-80 synuclein alpha Homo sapiens 83-86 32229256-10 2020 The results provide evidence that these lipophilic cysteine prodrugs provide increased protection against oxidative stress in human RPE cells compared with NAC. Cysteine 51-59 synuclein alpha Homo sapiens 156-159 32179647-1 2020 3-Mercaptopyruvate sulfur transferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate (3-MP) and transfers sulfane sulfur from an enzyme-bound persulfide intermediate to thiophilic acceptors such as thioredoxin and cysteine. Cysteine 224-232 thioredoxin Homo sapiens 208-219 32008372-9 2020 Increased activities of iNOS and NOX1 enzymes at MEPs in obese mice generated higher levels of NO and superoxide radicals, resulting in increased local peroxynitrite formation and subsequent oxidation of the regulatory protein AKAP150 at cysteine 36, to impair AKAP150-TRPV4 channel signaling at MEPs. Cysteine 238-246 A kinase (PRKA) anchor protein 5 Mus musculus 227-234 32008372-10 2020 Strategies that lowered peroxynitrite levels prevented cysteine 36 oxidation of AKAP150, and rescued endothelial AKAP150-TRPV4 signaling, vasodilation, and blood pressure in obesity. Cysteine 55-63 A kinase (PRKA) anchor protein 5 Mus musculus 80-87 32176468-7 2020 Human liver microsomes and CYP1A2 supersomes showed the highest bioactivation rate for adduct formation, in which all four cysteines of hGSTP reacted with NAPQI. Cysteine 123-132 cytochrome P450 family 1 subfamily A member 2 Homo sapiens 27-33 32176468-7 2020 Human liver microsomes and CYP1A2 supersomes showed the highest bioactivation rate for adduct formation, in which all four cysteines of hGSTP reacted with NAPQI. Cysteine 123-132 glutathione S-transferase pi 1 Homo sapiens 136-141 32260357-3 2020 As a hallmark, TFF1 contains seven cysteine residues with three disulfide bonds stabilizing the conserved TFF domain. Cysteine 35-43 trefoil factor 1 Mus musculus 15-19 31911834-1 2020 Mammalian asparagine endopeptidase (AEP) is a cysteine protease that cleaves its protein substrates on the C-terminal side of asparagine residues. Cysteine 46-54 legumain Homo sapiens 10-34 31911834-1 2020 Mammalian asparagine endopeptidase (AEP) is a cysteine protease that cleaves its protein substrates on the C-terminal side of asparagine residues. Cysteine 46-54 legumain Homo sapiens 36-39 31690182-2 2020 This process is catalyzed by an E1-E2-E3 trienzyme cascade, in which an E1 enzyme, Atg7, directs Atg8 to its E2 enzyme, Atg3, forming a thioester bond-linked Atg3~ Atg8 intermediate; then the composite E3, Atg12-Atg5-Atg16, interacts with the Atg3~ Atg8 intermediate and promotes Atg8 transfer from the catalytic cysteine of Atg3 to the head group of phosphatidylethanolamine (PE) lipids. Cysteine 313-321 autophagy related 3 Homo sapiens 158-162 31690182-2 2020 This process is catalyzed by an E1-E2-E3 trienzyme cascade, in which an E1 enzyme, Atg7, directs Atg8 to its E2 enzyme, Atg3, forming a thioester bond-linked Atg3~ Atg8 intermediate; then the composite E3, Atg12-Atg5-Atg16, interacts with the Atg3~ Atg8 intermediate and promotes Atg8 transfer from the catalytic cysteine of Atg3 to the head group of phosphatidylethanolamine (PE) lipids. Cysteine 313-321 autophagy related 3 Homo sapiens 158-162 31690182-2 2020 This process is catalyzed by an E1-E2-E3 trienzyme cascade, in which an E1 enzyme, Atg7, directs Atg8 to its E2 enzyme, Atg3, forming a thioester bond-linked Atg3~ Atg8 intermediate; then the composite E3, Atg12-Atg5-Atg16, interacts with the Atg3~ Atg8 intermediate and promotes Atg8 transfer from the catalytic cysteine of Atg3 to the head group of phosphatidylethanolamine (PE) lipids. Cysteine 313-321 autophagy related 3 Homo sapiens 158-162 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. Cysteine 34-42 transthyretin Homo sapiens 17-21 31479652-10 2019 hTTR is a tetramer composed of four identical monomers each containing a reduced cysteine residue in position 10. Cysteine 81-89 transthyretin Homo sapiens 0-4 31479652-11 2019 S-sulfonation of hTTR at this cysteine residue can destabilize the hTTR tetramer, an important step in the formation of TTR-related amyloid fibrils. Cysteine 30-38 transthyretin Homo sapiens 17-21 31479652-11 2019 S-sulfonation of hTTR at this cysteine residue can destabilize the hTTR tetramer, an important step in the formation of TTR-related amyloid fibrils. Cysteine 30-38 transthyretin Homo sapiens 67-71 31479652-11 2019 S-sulfonation of hTTR at this cysteine residue can destabilize the hTTR tetramer, an important step in the formation of TTR-related amyloid fibrils. Cysteine 30-38 transthyretin Homo sapiens 18-21 31450413-1 2019 Gamma-glutamyl transpeptidase (GGT) plays an important role in cellular glutathione/cysteine homeostasis and is a potential tumor biomarker. Cysteine 84-92 inactive glutathione hydrolase 2 Homo sapiens 0-29 31450413-1 2019 Gamma-glutamyl transpeptidase (GGT) plays an important role in cellular glutathione/cysteine homeostasis and is a potential tumor biomarker. Cysteine 84-92 inactive glutathione hydrolase 2 Homo sapiens 31-34 31801293-4 2019 The occurrence of monomeric xP1 is unexpected because of its odd number of cysteine residues. Cysteine 75-83 trefoil factor 3, gene 2 S homeolog Xenopus laevis 28-31 31984197-3 2019 A cysteine residue C113 is known to be important for its PPIase activity; a mutation C113A reduced the activity by 130-fold. Cysteine 2-10 peptidylprolyl isomerase like 1 Homo sapiens 57-63 31766501-2 2019 Recent studies of an overall cohort of 381 patients have suggested that the genotype may be the main determinant of the development of OPG, with the risk being higher in patients harbouring NF1 mutations in the 5" tertile and the cysteine/serine-rich domain. Cysteine 230-238 basic transcription factor 3 pseudogene 11 Homo sapiens 135-138 31600047-5 2019 The a-synuclein interaction interface includes the whole N-terminal part up to Gln24; in Atox1, residues around the copper-binding cysteines (positions 11-16) are mostly perturbed, but additional effects are also found for residues elsewhere in both proteins. Cysteine 131-140 antioxidant 1 copper chaperone Homo sapiens 89-94 31542487-8 2019 CYS produced relaxations of HCC and HPRA that were sensitive to ODQ and to inhibition of the H2S synthesizing enzymes, cystathionine gamma-lyase (CSE) and cystathionine beta-synthase (CBS). Cysteine 0-3 cystathionine gamma-lyase Homo sapiens 119-144 31542487-8 2019 CYS produced relaxations of HCC and HPRA that were sensitive to ODQ and to inhibition of the H2S synthesizing enzymes, cystathionine gamma-lyase (CSE) and cystathionine beta-synthase (CBS). Cysteine 0-3 cystathionine gamma-lyase Homo sapiens 146-149 31815017-2 2019 Cathepsin B is a lysosomal cysteine protease that degrades ECM, but its role in the PF remains unclear. Cysteine 27-35 cathepsin B Homo sapiens 0-11 31723224-1 2019 A non-synonymous single nucleotide polymorphism of the human serotonin 5-HT2C receptor (5-HT2CR) gene that converts a cysteine to a serine at amino acid codon 23 (Cys23Ser) appears to impact 5-HT2CR pharmacology at a cellular and systems level. Cysteine 118-126 5-hydroxytryptamine receptor 2C Homo sapiens 61-86 31226617-4 2019 Therefore, a turn off/on fluorescent sensor is constructed using CDs as a fluorescent probe, and the sensor is applied to the detection of Hg2+ and biothiols (glutathione, homocysteine and cysteine). Cysteine 176-184 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 139-142 31609245-4 2019 Rac1 activation requires a posttranslational modification, geranylgeranylation, of the C-terminal cysteine residue. Cysteine 98-106 Rac family small GTPase 1 Homo sapiens 0-4 31653923-7 2019 Ran is predominantly distributed in the nucleus, but TMX2 knockdown disrupted the nucleocytoplasmic Ran gradient, and the cysteine 112 residue of Ran was important in its regulation by TMX2. Cysteine 122-130 thioredoxin related transmembrane protein 2 Homo sapiens 185-189 31653927-0 2019 Binding partner- and force-promoted changes in alphaE-catenin conformation probed by native cysteine labeling. Cysteine 92-100 catenin alpha 1 Homo sapiens 47-61 31653927-3 2019 In this study, labeling of native cysteines combined with mass spectrometry revealed conformational changes in alphaE-catenin upon binding to the E-cadherin beta-catenin complex, vinculin and F-actin. Cysteine 34-43 catenin alpha 1 Homo sapiens 111-125 31653927-5 2019 Comparisons of wild-type alphaE-catenin and a mutant with enhanced vinculin affinity using cysteine labeling and isothermal titration calorimetry provide evidence for allosteric coupling of the N-terminal beta-catenin-binding and the middle (M) vinculin-binding domain of alphaE-catenin. Cysteine 91-99 catenin alpha 1 Homo sapiens 25-39 31532181-0 2019 The Role of the Conserved SUMO-2/3 Cysteine Residue on Domain Structure Investigated Using Protein Chemical Synthesis. Cysteine 35-43 small ubiquitin like modifier 2 Homo sapiens 26-32 31532181-3 2019 In particular, we clarify the role of the conserved cysteine residue on SUMO-2/3 domain stability and properties. Cysteine 52-60 small ubiquitin like modifier 2 Homo sapiens 72-78 31532181-4 2019 Our data reveal that SUMO-2 and -3 proteins behave differently from the Cys Ala modification with SUMO-2 being less impacted than SUMO-3, likely due to a stabilizing interaction occurring in SUMO-2 between its tail and the SUMO core domain. Cysteine 72-75 small ubiquitin like modifier 3 Homo sapiens 132-138 31532181-4 2019 Our data reveal that SUMO-2 and -3 proteins behave differently from the Cys Ala modification with SUMO-2 being less impacted than SUMO-3, likely due to a stabilizing interaction occurring in SUMO-2 between its tail and the SUMO core domain. Cysteine 72-75 small ubiquitin like modifier 2 Homo sapiens 100-106 31532181-5 2019 While the Cys Ala modification has no effect on the enzyme-catalyzed conjugation, it shows a deleterious effect on the enzyme-catalyzed deconjugation process, especially with the SUMO-3 conjugate. Cysteine 10-13 small ubiquitin like modifier 3 Homo sapiens 181-187 31468690-4 2019 CTH promotes NF-kappaB nuclear translocation through H2 S-mediated sulfhydration on cysteine-38 of the NF-kappaB p65 subunit, resulting in increased IL-1beta expression and H2 S-induced cell invasion. Cysteine 84-92 cystathionine gamma-lyase Homo sapiens 0-3 31260699-7 2019 Regulated exocytosis studies using co-transfected human growth hormone (hGH) secretion reporter plasmid revealed that overexpression of SNAP-23 Cys- and P119A mutants significantly inhibits the overall extent of exocytosis from RBL mast cells, whereas expression of SNAP-23 Cys--MDR31-145 fusion protein is able to restore exocytosis. Cysteine 144-147 synaptosome associated protein 23 Homo sapiens 136-143 31260699-7 2019 Regulated exocytosis studies using co-transfected human growth hormone (hGH) secretion reporter plasmid revealed that overexpression of SNAP-23 Cys- and P119A mutants significantly inhibits the overall extent of exocytosis from RBL mast cells, whereas expression of SNAP-23 Cys--MDR31-145 fusion protein is able to restore exocytosis. Cysteine 274-277 synaptosome associated protein 23 Homo sapiens 136-143 31632405-2 2019 In addition, MALT1 is a cysteine protease that further fine tunes proinflammatory signaling by cleaving specific substrates. Cysteine 24-32 MALT1 paracaspase Mus musculus 13-18 31579087-8 2019 The present study observed that miR-873 overexpression decreased the expression of YAP target genes AXL receptor tyrosine kinase, connective tissue growth factor and cysteine rich angiogenic inducer 61 at mRNA and protein levels. Cysteine 166-174 microRNA 873 Homo sapiens 32-39 31418761-0 2019 Chemistry of cysteine assembly on Au(100): electrochemistry, in situ STM and molecular modeling. Cysteine 13-21 sulfotransferase family 1A member 3 Homo sapiens 69-72 31418761-2 2019 We have studied the surface structure and adsorption dynamics of l-cysteine adlayers on Au(100) from aqueous solution using electrochemistry, high-resolution electrochemical scanning tunnelling microscopy (in situ STM), and molecular modelling. Cysteine 65-75 sulfotransferase family 1A member 3 Homo sapiens 214-217 31418761-7 2019 In situ STM showed that the adsorbed Cys is organized in stripes with "fork-like" features which co-exist in (11 x 2)-2Cys and (7 x 2)-2Cys lattices, quite differently from Cys adsorption on Au(111)-electrode surfaces. Cysteine 37-40 sulfotransferase family 1A member 3 Homo sapiens 8-11 31418761-8 2019 Stripe structures with bright STM contrast in the center suggest that a second Cys adlayer on top of a first adlayer is formed, supporting the dual-peak reductive desorption of Cys adlayers. Cysteine 79-82 sulfotransferase family 1A member 3 Homo sapiens 30-33 31418761-8 2019 Stripe structures with bright STM contrast in the center suggest that a second Cys adlayer on top of a first adlayer is formed, supporting the dual-peak reductive desorption of Cys adlayers. Cysteine 177-180 sulfotransferase family 1A member 3 Homo sapiens 30-33 31362979-6 2019 Using peptide truncation studies, we found that both N- and C-terminal acidic residues, as well as the C-terminal Cys residue of the TP53INP1 LIR peptide, are required for its high-affinity binding to LC3A and LC3B, whereas binding to the GABARAP subfamily proteins was facilitated by residues either N-terminal or C-terminal to the core motif. Cysteine 114-117 microtubule associated protein 1 light chain 3 alpha Homo sapiens 201-205 31636803-2 2019 Its activity is regulated by the reversible oxidation of an active-site cysteine residue by H2O2 and thioredoxin. Cysteine 72-80 thioredoxin 1 Mus musculus 101-112 32055360-2 2019 Using SiR, we confirmed that inhibiting cystine (Cys2) transporter system xc - to deplete intracellular Cys is more efficient than inhibiting glutamate-cysteine ligase GCL to deplete intracellular GSH for sensitizing cancer cells to chemotherapy. Cysteine 49-52 germ cell-less 2, spermatogenesis associated Homo sapiens 168-171 32055360-2 2019 Using SiR, we confirmed that inhibiting cystine (Cys2) transporter system xc - to deplete intracellular Cys is more efficient than inhibiting glutamate-cysteine ligase GCL to deplete intracellular GSH for sensitizing cancer cells to chemotherapy. Cysteine 152-160 germ cell-less 2, spermatogenesis associated Homo sapiens 168-171 31337710-8 2019 We focus on JPH2 that has four Cys residues: three flanking the MORN motifs and one in the TMD. Cysteine 31-34 junctophilin 2 Homo sapiens 12-16 31337710-10 2019 Palmitoylated JPH2 binds to lipid-raft domains in PM, whereas palmitoylation of TMD-located Cys stabilizes JPH2"s anchor in the ER/SR membrane. Cysteine 92-95 junctophilin 2 Homo sapiens 107-111 31337710-14 2019 Sequence alignment reveals that the palmitoylatable Cys residues in JPH2 are conserved in other JPHs, suggesting that palmitoylation may also enhance ER/SR-PM tethering by these proteins. Cysteine 52-55 junctophilin 2 Homo sapiens 68-72 31158443-7 2019 However, when the active cysteine residues are oxidized, Prx1 loses its activity as a snoRNA-binding protein. Cysteine 25-33 small nucleolar RNA, C/D box 14E Homo sapiens 86-92 31299423-1 2019 Mouse selenoprotein W (SELENOW) is a small protein containing a selenocysteine (Sec, U) and four cysteine (Cys, C) residues. Cysteine 107-110 selenoprotein W Mus musculus 23-30 31299423-5 2019 In this study, using purified recombinant SELENOW in which Sec13 was changed to Cys, we found that SELENOW was glutathionylated at Cys33 and that this S-glutathionylation was enhanced by oxidative stress. Cysteine 80-83 selenoprotein W Mus musculus 42-49 31299423-5 2019 In this study, using purified recombinant SELENOW in which Sec13 was changed to Cys, we found that SELENOW was glutathionylated at Cys33 and that this S-glutathionylation was enhanced by oxidative stress. Cysteine 80-83 selenoprotein W Mus musculus 99-106 31127934-1 2019 Sulfite oxidase (SO) is encoded by the nuclear SUOX gene and catalyzes the final step in cysteine catabolism thereby oxidizing sulfite to sulfate. Cysteine 89-97 sulfite oxidase Homo sapiens 0-15 31127934-1 2019 Sulfite oxidase (SO) is encoded by the nuclear SUOX gene and catalyzes the final step in cysteine catabolism thereby oxidizing sulfite to sulfate. Cysteine 89-97 sulfite oxidase Homo sapiens 17-19 31127934-1 2019 Sulfite oxidase (SO) is encoded by the nuclear SUOX gene and catalyzes the final step in cysteine catabolism thereby oxidizing sulfite to sulfate. Cysteine 89-97 sulfite oxidase Homo sapiens 47-51 30935989-4 2019 This IL-10 possesses conserved cysteine residues, predicted alpha-helices and a typical IL-10 family signature motif, similar to its mammalian orthologue, and IL-10R1 harbours predicted JAK1 and STAT3 binding sites in the intracellular region. Cysteine 31-39 interleukin 10 Homo sapiens 5-10 31087497-0 2019 Oxidative folding pathways of bovine milk beta-lactoglobulin with odd cysteine residues. Cysteine 70-78 beta-lactoglobulin Bos taurus 42-60 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. Cysteine 116-119 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. Cysteine 116-119 beta-lactoglobulin Bos taurus 27-30 31087497-9 2019 These findings are informative not only for elucidating oxidative folding pathways of other members of the beta-lactoglobulin family, but also for understanding the roles of a redundant Cys thiol in the oxidative folding process of a protein with odd Cys residues. Cysteine 186-189 beta-lactoglobulin Bos taurus 107-125 31087497-9 2019 These findings are informative not only for elucidating oxidative folding pathways of other members of the beta-lactoglobulin family, but also for understanding the roles of a redundant Cys thiol in the oxidative folding process of a protein with odd Cys residues. Cysteine 251-254 beta-lactoglobulin Bos taurus 107-125 31268335-0 2019 Designing an "Off-On" Fluorescence Sensor Based on Cluster-Based CaII-Metal-Organic Frameworks for Detection of l-Cysteine in Biological Fluids. Cysteine 112-122 carbonic anhydrase 2 Homo sapiens 65-69 31268335-6 2019 Then, with the addition of l-cysteine into the CaII-MOFs 1/Pb2+ hybrid system, the fluorescence signal was immediately restored. Cysteine 27-37 carbonic anhydrase 2 Homo sapiens 47-51 31358852-7 2019 Co-deletion of the ADAMTS-5 cysteine-rich domain further reduced versicanase activity to a total 153-fold reduction. Cysteine 28-36 ADAM metallopeptidase with thrombospondin type 1 motif 5 Homo sapiens 19-27 31392096-5 2019 Studies in vitro have shown that NO inhibits the activity of caspases and calpains through S-nitrosylation of a cysteine located in their catalytic site, so we propose to elucidate if the regulatory mechanisms of NO are related with changes in S-nitrosylation of cell death proteins in the ischemic-reperfused myocardium. Cysteine 112-120 caspase 8 Rattus norvegicus 61-69 31413803-0 2019 Rotational Freedom, Steric Hindrance, and Protein Dynamics Explain BLU554 Selectivity for the Hinge Cysteine of FGFR4. Cysteine 100-108 zinc finger MYND-type containing 10 Homo sapiens 67-70 31050059-3 2019 Several commonly used G6PDH cysteine mutants including A45C and K55C have been labeled with CG-maleimide derivative, but inhibition rates of are unsatisfactory. Cysteine 28-36 glucose-6-phosphate dehydrogenase Homo sapiens 22-27 31050059-5 2019 We generated eight cysteine mutants (K106C, Y155C, A201C, T258C, D306C, D375C, G426C, and D480C) of G6PDH, measured their inhibition rates, and evaluated the performance of the D306C mutant using EMIT CG assays. Cysteine 19-27 glucose-6-phosphate dehydrogenase Homo sapiens 100-105 30685490-6 2019 Covalent modification of cysteine in UQCRFS1 was not observed after WA treatment. Cysteine 25-33 ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1 Homo sapiens 37-44 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. Cysteine 11-14 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. Cysteine 11-14 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. Cysteine 11-14 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. Cysteine 11-14 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 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. Cysteine 24-27 insulin II Mus musculus 130-140 31185618-1 2019 Peroxiredoxins (Prxs), a family of peroxidases, are reactive oxygen species scavengers that hydrolyze H2O2 through catalytic cysteine. Cysteine 125-133 peroxiredoxin 4 Homo sapiens 0-14 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. Cysteine 208-216 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. Cysteine 208-216 thioredoxin 1 Mus musculus 135-138 30679029-6 2019 For example, Mst84B (gene CG1988), a very basic cysteine- and lysine-rich nuclear protein and was present in the transition phase from a histone-based to a protamine-based chromatin structure. Cysteine 48-56 Male-specific transcript 84B Drosophila melanogaster 26-32 30959459-4 2019 Mutagenesis of selected cysteine residues in ST6Gal-I mimicked these effects, and also rendered the enzyme inactive. Cysteine 24-32 ST6 beta-galactoside alpha-2,6-sialyltransferase 1 Homo sapiens 45-53 31281521-1 2019 Cysteine-type cathepsins such as cathepsin B are involved in various steps of inflammatory processes such as antigen processing and angiogenesis. Cysteine 0-8 cathepsin B Mus musculus 33-44 31281521-2 2019 Here, we uncovered the role of cysteine-type cathepsins in the effector phase of T cell-driven cutaneous delayed-type hypersensitivity reactions (DTHR) and the implication of this role on therapeutic cathepsin B-specific inhibition. Cysteine 31-39 cathepsin B Mus musculus 200-211 30812058-2 2019 In this work, a quantitative mass spectrometry method is developed to determine the binding ratio of metal-based anticancer complexes with cysteines in human copper chaperone protein Atox1. Cysteine 139-148 antioxidant 1 copper chaperone Homo sapiens 183-188 31160916-8 2019 Results: The distinct metabolites between PDR and NDR groups were significantly enriched in 9 KEGG pathways (P < 0.05, impact > 0.1), namely, alanine, aspartate and glutamate metabolism, caffeine metabolism, beta-alanine metabolism, purine metabolism, cysteine and methionine metabolism, sulfur metabolism, sphingosine metabolism, and arginine and proline metabolism. Cysteine 258-266 serine/threonine kinase 38 Homo sapiens 50-53 30771959-8 2019 Particularly, the probe can avoid the serious interference from cysteine (Cys) found in the rhodamine lactam-based fluorescent NO probes (RB-OPD). Cysteine 64-72 drb Drosophila melanogaster 138-140 30771959-8 2019 Particularly, the probe can avoid the serious interference from cysteine (Cys) found in the rhodamine lactam-based fluorescent NO probes (RB-OPD). Cysteine 74-77 drb Drosophila melanogaster 138-140 31077306-7 2019 Our findings showed that the small loop between two cysteines of the EL2 domain is essential for the binding to one EL2-recognizing mAb and that the recognition regions by three EL1-recognizing mAbs overlap, but are not the same sites of EL1. Cysteine 52-61 spectrin alpha, erythrocytic 1 Homo sapiens 69-72 31077306-7 2019 Our findings showed that the small loop between two cysteines of the EL2 domain is essential for the binding to one EL2-recognizing mAb and that the recognition regions by three EL1-recognizing mAbs overlap, but are not the same sites of EL1. Cysteine 52-61 spectrin alpha, erythrocytic 1 Homo sapiens 116-119 31077306-7 2019 Our findings showed that the small loop between two cysteines of the EL2 domain is essential for the binding to one EL2-recognizing mAb and that the recognition regions by three EL1-recognizing mAbs overlap, but are not the same sites of EL1. Cysteine 52-61 erythrocyte membrane protein band 4.1 Homo sapiens 178-181 31077306-7 2019 Our findings showed that the small loop between two cysteines of the EL2 domain is essential for the binding to one EL2-recognizing mAb and that the recognition regions by three EL1-recognizing mAbs overlap, but are not the same sites of EL1. Cysteine 52-61 erythrocyte membrane protein band 4.1 Homo sapiens 238-241 30668888-1 2019 Sorsby fundus dystrophy (SFD) is a macular degeneration caused by mutations in TIMP3, the majority of which introduce a novel cysteine. Cysteine 126-134 TIMP metallopeptidase inhibitor 3 Homo sapiens 79-84 31218060-3 2019 AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs-Cys-GOx bioconjugate complex. Cysteine 25-35 hydroxyacid oxidase 1 Homo sapiens 127-142 31218060-3 2019 AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs-Cys-GOx bioconjugate complex. Cysteine 25-35 hydroxyacid oxidase 1 Homo sapiens 144-147 31218060-3 2019 AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs-Cys-GOx bioconjugate complex. Cysteine 37-40 hydroxyacid oxidase 1 Homo sapiens 127-142 31218060-3 2019 AuNSs were modified with l-cysteine (Cys) and covalently bound to N-hydroxysulfosuccinimide (sulfo-NHS) activated intermediate glucose oxidase (GOx) to fabricate a stable and sensitive AuNSs-Cys-GOx bioconjugate complex. Cysteine 37-40 hydroxyacid oxidase 1 Homo sapiens 144-147 30945846-6 2019 The bis-Mo-MPT and bis-W-MPT cofactors include metal centers that bind the four sulfurs from the two dithiolene groups in addition to a cysteine and likely a sulfido ligand. Cysteine 136-144 Bis protein Escherichia coli 4-7 30945846-6 2019 The bis-Mo-MPT and bis-W-MPT cofactors include metal centers that bind the four sulfurs from the two dithiolene groups in addition to a cysteine and likely a sulfido ligand. Cysteine 136-144 Bis protein Escherichia coli 19-22 30959951-8 2019 The introduction of a cysteine at the dimer interface is functional for development of new hTS inhibitors through innovative strategies, such as the tethering approach. Cysteine 22-30 APC down-regulated 1 Homo sapiens 91-94 30835068-13 2019 In addition, the results of exposure to AFB1 show a strong significant correlation between KIM-1 and Cys-C that may indicate the toxic renal effect. Cysteine 101-104 hepatitis A virus cellular receptor 1 Homo sapiens 91-96 30718813-4 2019 We applied a fumarate-competitive chemoproteomic probe in concert with LC-MS/MS to discover new cysteines sensitive to fumarate hydratase (FH) mutation in HLRCC cell models. Cysteine 96-105 fumarate hydratase Homo sapiens 119-137 30718813-4 2019 We applied a fumarate-competitive chemoproteomic probe in concert with LC-MS/MS to discover new cysteines sensitive to fumarate hydratase (FH) mutation in HLRCC cell models. Cysteine 96-105 fumarate hydratase Homo sapiens 139-141 30718813-5 2019 Analysis of this dataset revealed an unexpected influence of local environment and pH on fumarate reactivity, and enabled the characterization of a novel FH-regulated cysteine residue that lies at a key protein-protein interface in the SWI-SNF tumor-suppressor complex. Cysteine 167-175 fumarate hydratase Homo sapiens 154-156 30849621-4 2019 In this study, we found that cysteine dioxygenase (CDO), a key enzyme in cysteine oxidative metabolism, was involved in mammary epithelial morphogenesis. Cysteine 29-37 cysteine dioxygenase 1, cytosolic Mus musculus 51-54 30846362-3 2019 KRAS4b plasma membrane (PM) binding is mediated by the insertion of a prenylated moiety that is attached to the terminal carboxy-methylated cysteine, in addition to electrostatic interactions of its positively charged hypervariable region with anionic lipids. Cysteine 140-148 KRAS proto-oncogene, GTPase Homo sapiens 0-6 30824597-1 2019 The formylglycine-generating enzyme (FGE) is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to Calpha-formylglycine. Cysteine 143-151 sulfatase modifying factor 1 Homo sapiens 4-35 30824597-1 2019 The formylglycine-generating enzyme (FGE) is required for the posttranslational activation of type I sulfatases by oxidation of an active-site cysteine to Calpha-formylglycine. Cysteine 143-151 sulfatase modifying factor 1 Homo sapiens 37-40 30776218-2 2019 The spin label links to cysteines via a short thioether tether and has a narrow central transition indicative of small zero-field splitting (ZFS). Cysteine 24-33 spindlin 1 Homo sapiens 4-8 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. Cysteine 94-102 klotho beta Homo sapiens 430-433 30559291-8 2019 Introducing Trp85 or Phe29 to replace Cys or Leu, respectively, disrupts packing in the hydrophobic core and lowers RD3"s apparent affinity for RetGC1. Cysteine 38-41 RD3 regulator of GUCY2D Homo sapiens 116-119 30755663-1 2019 Phytochromes are red/far-red light sensing photoreceptors employing linear tetrapyrroles as chromophores, which are covalently bound to a cysteine (Cys) residue in the chromophore-binding domain (CBD, composed of a PAS and a GAF domain). Cysteine 138-146 fibroblast growth factor 9 Homo sapiens 225-228 30755663-1 2019 Phytochromes are red/far-red light sensing photoreceptors employing linear tetrapyrroles as chromophores, which are covalently bound to a cysteine (Cys) residue in the chromophore-binding domain (CBD, composed of a PAS and a GAF domain). Cysteine 148-151 fibroblast growth factor 9 Homo sapiens 225-228 30381240-2 2019 With seven unpaired cysteines, seroreactivity of E. coli expressed c33 is dependant on reductants. Cysteine 20-29 CD82 molecule Homo sapiens 67-70 30381240-4 2019 A series of cysteine-to-serine substituted variants of a c33-like antigen was constructed and evaluated for reactivity against a panel of HCV-positive sera. Cysteine 12-20 CD82 molecule Homo sapiens 57-60 31148102-2 2019 H2S is synthesized from L-cysteine and/or L-homocysteine by cystathionine beta-synthase, cystathionine gamma-lyase, and cysteine aminotransferase together with 3-mercaptopyruvate sulfurtransferase. Cysteine 24-34 cystathionine gamma-lyase Homo sapiens 89-114 31527362-1 2019 Hydrogen sulfide (H2S), an endogenous gasotransmitter, is generated from L-cysteine by 3 distinct enzymes including cystathionine-gamma-lyase (CSE), and targets multiple molecules, thereby playing various roles in health and disease. Cysteine 73-83 cystathionine gamma-lyase Homo sapiens 116-141 31527362-1 2019 Hydrogen sulfide (H2S), an endogenous gasotransmitter, is generated from L-cysteine by 3 distinct enzymes including cystathionine-gamma-lyase (CSE), and targets multiple molecules, thereby playing various roles in health and disease. Cysteine 73-83 cystathionine gamma-lyase Homo sapiens 143-146 30662667-1 2018 Hydrogen sulfide (H2S) is substantially converted from cysteine by the enzymes cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE). Cysteine 55-63 cystathionine gamma-lyase Homo sapiens 117-142 30662667-1 2018 Hydrogen sulfide (H2S) is substantially converted from cysteine by the enzymes cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE). Cysteine 55-63 cystathionine gamma-lyase Homo sapiens 144-147 30392349-2 2018 We identified a noncatalytic cysteine (Cys481 in KDM5A) near the active sites of KDM5 histone H3 lysine 4 demethylases, which is absent in other histone demethylase families, that could be explored for interaction with the cysteine-reactive electrophile acrylamide. Cysteine 29-37 lysine demethylase 5A Homo sapiens 49-54 30392349-2 2018 We identified a noncatalytic cysteine (Cys481 in KDM5A) near the active sites of KDM5 histone H3 lysine 4 demethylases, which is absent in other histone demethylase families, that could be explored for interaction with the cysteine-reactive electrophile acrylamide. Cysteine 223-231 lysine demethylase 5A Homo sapiens 49-54 30593754-8 2018 Both polymorphisms influenced the methylation status, carriers of OGG1 326Ser/Cys or Ser/Cys+Cys/Cys genotypes demonstrating increased frequency of methylated RUNX3 and ISL1 genes whereas the similar effect of XRCC1 polymorphism concerning methylation of p16 and TIMP3 genes. Cysteine 78-81 X-ray repair cross complementing 1 Homo sapiens 210-215 30593754-8 2018 Both polymorphisms influenced the methylation status, carriers of OGG1 326Ser/Cys or Ser/Cys+Cys/Cys genotypes demonstrating increased frequency of methylated RUNX3 and ISL1 genes whereas the similar effect of XRCC1 polymorphism concerning methylation of p16 and TIMP3 genes. Cysteine 78-81 TIMP metallopeptidase inhibitor 3 Homo sapiens 263-268 30593754-8 2018 Both polymorphisms influenced the methylation status, carriers of OGG1 326Ser/Cys or Ser/Cys+Cys/Cys genotypes demonstrating increased frequency of methylated RUNX3 and ISL1 genes whereas the similar effect of XRCC1 polymorphism concerning methylation of p16 and TIMP3 genes. Cysteine 89-92 X-ray repair cross complementing 1 Homo sapiens 210-215 30593754-8 2018 Both polymorphisms influenced the methylation status, carriers of OGG1 326Ser/Cys or Ser/Cys+Cys/Cys genotypes demonstrating increased frequency of methylated RUNX3 and ISL1 genes whereas the similar effect of XRCC1 polymorphism concerning methylation of p16 and TIMP3 genes. Cysteine 89-92 TIMP metallopeptidase inhibitor 3 Homo sapiens 263-268 30593754-8 2018 Both polymorphisms influenced the methylation status, carriers of OGG1 326Ser/Cys or Ser/Cys+Cys/Cys genotypes demonstrating increased frequency of methylated RUNX3 and ISL1 genes whereas the similar effect of XRCC1 polymorphism concerning methylation of p16 and TIMP3 genes. Cysteine 89-92 X-ray repair cross complementing 1 Homo sapiens 210-215 30300680-4 2018 Cystine is reduced inside the cells and the L-type amino acid transporter 1 (LAT1) transports cysteine from the endothelial cells into the brain, cysteine is transported into the neurons through the excitatory amino acid transporter 3 (EAAT3), also known as excitatory amino acid carrier 1 (EAAC1). Cysteine 94-102 solute carrier family 7 (cationic amino acid transporter, y+ system), member 5 Mus musculus 44-75 30300680-4 2018 Cystine is reduced inside the cells and the L-type amino acid transporter 1 (LAT1) transports cysteine from the endothelial cells into the brain, cysteine is transported into the neurons through the excitatory amino acid transporter 3 (EAAT3), also known as excitatory amino acid carrier 1 (EAAC1). Cysteine 94-102 solute carrier family 7 (cationic amino acid transporter, y+ system), member 5 Mus musculus 77-81 30300680-4 2018 Cystine is reduced inside the cells and the L-type amino acid transporter 1 (LAT1) transports cysteine from the endothelial cells into the brain, cysteine is transported into the neurons through the excitatory amino acid transporter 3 (EAAT3), also known as excitatory amino acid carrier 1 (EAAC1). Cysteine 146-154 solute carrier family 7 (cationic amino acid transporter, y+ system), member 5 Mus musculus 44-75 30300680-4 2018 Cystine is reduced inside the cells and the L-type amino acid transporter 1 (LAT1) transports cysteine from the endothelial cells into the brain, cysteine is transported into the neurons through the excitatory amino acid transporter 3 (EAAT3), also known as excitatory amino acid carrier 1 (EAAC1). Cysteine 146-154 solute carrier family 7 (cationic amino acid transporter, y+ system), member 5 Mus musculus 77-81 30300680-4 2018 Cystine is reduced inside the cells and the L-type amino acid transporter 1 (LAT1) transports cysteine from the endothelial cells into the brain, cysteine is transported into the neurons through the excitatory amino acid transporter 3 (EAAT3), also known as excitatory amino acid carrier 1 (EAAC1). Cysteine 146-154 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 199-234 30533581-3 2018 The central feature of SHP2"s allosteric site is a nonconserved cysteine residue (C333) that can potentially be labeled with electrophilic compounds for selective SHP2 inhibition. Cysteine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 23-27 30533581-3 2018 The central feature of SHP2"s allosteric site is a nonconserved cysteine residue (C333) that can potentially be labeled with electrophilic compounds for selective SHP2 inhibition. Cysteine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 163-167 30809370-5 2019 Crystallographic studies of peptide-MDM2/MDMX complexes structurally validated the chemoselectivity of the dithiocarbamate staple bridging Lys and Cys at (i, i + 4) positions. Cysteine 147-150 MDM2 proto-oncogene Homo sapiens 36-40 30246912-2 2018 Peptide polymerization relies on tyrosinase oxidation of tyrosine residues to Dopaquinones, which rapidly form cysteinyldopa-moieties with free thiols from cysteine residues, thereby linking unimers and generating adhesive polymers. Cysteine 156-164 tyrosinase Homo sapiens 33-43 30287686-9 2018 Finally, we identified a conserved catalytic ensemble comprising Glu-646 and Arg-604 that supports HECT-ubiquitin thioester exchange and isopeptide bond formation at the active-site Cys-922 of NEDD4-2. Cysteine 182-185 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 193-200 30237173-5 2018 Further, we identified a triad of evolutionarily conserved cysteines in the FZD linker domain that is crucial for receptor membrane expression and recruitment of DVL. Cysteine 59-68 dishevelled segment polarity protein 1 pseudogene 1 Homo sapiens 162-165 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. Cysteine 68-77 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. Cysteine 68-77 cytochrome b-245 beta chain Homo sapiens 113-117 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. Cysteine 89-92 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. Cysteine 89-92 cytochrome b-245 beta chain Homo sapiens 113-117 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 . Cysteine 152-160 cytochrome b-245 beta chain Homo sapiens 58-62 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 . Cysteine 175-178 cytochrome b-245 beta chain Homo sapiens 58-62 30217845-6 2018 Cysteine synthase incorporated H2S into O-acetyl-l-homoserine to produce l-homocysteine, which is the precursor for cysteine and methionine in S. cerevisiae Several other rhodaneses replaced Rdl1 and Rdl2 for thiosulfate utilization in the yeast. Cysteine 79-87 thiosulfate sulfurtransferase RDL1 Saccharomyces cerevisiae S288C 191-195 30052299-3 2018 The nuclear isoform of dUTPase is a 164-amino-acids-long protein containing three cysteine residues. Cysteine 82-90 Deoxyuridine triphosphatase Drosophila melanogaster 23-30 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. Cysteine 130-138 Deoxyuridine triphosphatase Drosophila melanogaster 48-55 30319633-3 2018 Here, we report the existence of two amino acids, cysteine at residue 44 and 135 (Cys44 and Cys135, respectively), in ATG10 being related to differential effects of ATG10 on HCV replication and autophagy flux. Cysteine 50-58 autophagy related 10 Homo sapiens 118-123 30319633-3 2018 Here, we report the existence of two amino acids, cysteine at residue 44 and 135 (Cys44 and Cys135, respectively), in ATG10 being related to differential effects of ATG10 on HCV replication and autophagy flux. Cysteine 50-58 autophagy related 10 Homo sapiens 165-170 30345401-3 2018 Formation of AviCys moiety requires an oxidative decarboxylation of the C-terminal Cys of the precursor peptide CypA, and this process is catalyzed by a flavin-containing protein CypD. Cysteine 16-19 peptidylprolyl isomerase A Mus musculus 112-116 29510000-7 2018 The variant allele of BRCA1 Cys39Gly increased breast cancer risk (Gly/Cys versus Cys/Cys, OR: 12.2, 95%CI: 1.53; 98.1), and carriers of the variant allele of CYP17A1 -34T>C had reduced risk (CT+CC versus TT, OR: 0.44, 95%CI: 0.21; 0.93). Cysteine 28-31 BRCA1 DNA repair associated Homo sapiens 22-27 29510000-7 2018 The variant allele of BRCA1 Cys39Gly increased breast cancer risk (Gly/Cys versus Cys/Cys, OR: 12.2, 95%CI: 1.53; 98.1), and carriers of the variant allele of CYP17A1 -34T>C had reduced risk (CT+CC versus TT, OR: 0.44, 95%CI: 0.21; 0.93). Cysteine 71-74 BRCA1 DNA repair associated Homo sapiens 22-27 29510000-7 2018 The variant allele of BRCA1 Cys39Gly increased breast cancer risk (Gly/Cys versus Cys/Cys, OR: 12.2, 95%CI: 1.53; 98.1), and carriers of the variant allele of CYP17A1 -34T>C had reduced risk (CT+CC versus TT, OR: 0.44, 95%CI: 0.21; 0.93). Cysteine 71-74 BRCA1 DNA repair associated Homo sapiens 22-27 29925651-0 2018 Pigs Lacking the Scavenger Receptor Cysteine-Rich Domain 5 of CD163 Are Resistant to Porcine Reproductive and Respiratory Syndrome Virus 1 Infection. Cysteine 36-44 scavenger receptor cysteine-rich type 1 protein M130 Sus scrofa 62-67 29684906-8 2018 The HILIC method was successfully applied for the analysis of commercially available samples of pharmaceutically active thiols such as captopril, N-acetyl-l-cysteine (NAC) and cysteine. Cysteine 157-165 X-linked Kx blood group Homo sapiens 167-170 28980184-5 2018 In order to estimate the maximum velocity (V max) and Michaelis constant (K m) for the uptake of Cys-S-Hg-S-Cys mediated by MRP2, in vitro studies were carried out using radioactive Cys-S-Hg-S-Cys (5 muM) and inside-out membrane vesicles made from Sf9 cells transfected with MRP2. Cysteine 106-111 ATP binding cassette subfamily C member 2 Homo sapiens 124-128 28980184-5 2018 In order to estimate the maximum velocity (V max) and Michaelis constant (K m) for the uptake of Cys-S-Hg-S-Cys mediated by MRP2, in vitro studies were carried out using radioactive Cys-S-Hg-S-Cys (5 muM) and inside-out membrane vesicles made from Sf9 cells transfected with MRP2. Cysteine 106-111 ATP binding cassette subfamily C member 2 Homo sapiens 275-279 28980184-5 2018 In order to estimate the maximum velocity (V max) and Michaelis constant (K m) for the uptake of Cys-S-Hg-S-Cys mediated by MRP2, in vitro studies were carried out using radioactive Cys-S-Hg-S-Cys (5 muM) and inside-out membrane vesicles made from Sf9 cells transfected with MRP2. Cysteine 108-111 ATP binding cassette subfamily C member 2 Homo sapiens 124-128 28980184-5 2018 In order to estimate the maximum velocity (V max) and Michaelis constant (K m) for the uptake of Cys-S-Hg-S-Cys mediated by MRP2, in vitro studies were carried out using radioactive Cys-S-Hg-S-Cys (5 muM) and inside-out membrane vesicles made from Sf9 cells transfected with MRP2. Cysteine 108-111 ATP binding cassette subfamily C member 2 Homo sapiens 275-279 28980184-5 2018 In order to estimate the maximum velocity (V max) and Michaelis constant (K m) for the uptake of Cys-S-Hg-S-Cys mediated by MRP2, in vitro studies were carried out using radioactive Cys-S-Hg-S-Cys (5 muM) and inside-out membrane vesicles made from Sf9 cells transfected with MRP2. Cysteine 191-196 ATP binding cassette subfamily C member 2 Homo sapiens 124-128 28980184-10 2018 Overall, the data indicate that MRP2 transports Cys-S-Hg-S-Cys in a manner that is similar to that of other MRP2 substrates. Cysteine 48-51 ATP binding cassette subfamily C member 2 Homo sapiens 32-36 28980184-10 2018 Overall, the data indicate that MRP2 transports Cys-S-Hg-S-Cys in a manner that is similar to that of other MRP2 substrates. Cysteine 59-62 ATP binding cassette subfamily C member 2 Homo sapiens 32-36 29693775-8 2018 Indeed, SPE-49 and SPE-42 have identical predicted membrane topology and domain structure, including a large extracellular domain with six conserved cysteine residues, a DC-STAMP domain, and a C-terminal cytoplasmic domain containing a C4-C4 RING finger motif. Cysteine 149-157 DC_STAMP domain-containing protein Caenorhabditis elegans 19-25 28527631-3 2018 Adding oxidized glutathione (GSSG), the core cellular stress indicator, to mitochondrial preparations stimulates mitochondrial fusion by inducing disulphide bond-mediated oligomer formation of MFN2 and its homolog MFN1 which involve cysteine 684 (C684) of MFN2. Cysteine 233-241 mitofusin 2 Homo sapiens 193-197 28527631-3 2018 Adding oxidized glutathione (GSSG), the core cellular stress indicator, to mitochondrial preparations stimulates mitochondrial fusion by inducing disulphide bond-mediated oligomer formation of MFN2 and its homolog MFN1 which involve cysteine 684 (C684) of MFN2. Cysteine 233-241 mitofusin 1 Homo sapiens 214-218 28527631-9 2018 Our data indicate that mutation of this cysteine which forms disulphide bridges in an oxidative state, apparently renders MFN2 more susceptible to alterations of the redox environment. Cysteine 40-48 mitofusin 2 Homo sapiens 122-126 29857311-10 2018 Regulatory cysteines were significantly S-glutathionylated on mitochondrial complex I and II, GAPDH, MDH1, ACO2, and mitochondrial complex V among others. Cysteine 11-20 glyceraldehyde-3-phosphate dehydrogenase Mus musculus 94-99 29857311-10 2018 Regulatory cysteines were significantly S-glutathionylated on mitochondrial complex I and II, GAPDH, MDH1, ACO2, and mitochondrial complex V among others. Cysteine 11-20 malate dehydrogenase 1, NAD (soluble) Mus musculus 101-105 29466676-8 2018 Additionally, a tailored MALDI-TOF assay was developed to monitor compound-dependent, irreversible modification of the active cysteine of PTP1B. Cysteine 126-134 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 138-143 29390068-0 2018 Evolutionary relationship between the cysteine and histidine rich domains (CHORDs) and Btk-type zinc fingers. Cysteine 38-46 Bruton tyrosine kinase Homo sapiens 87-90 29532356-4 2018 In vitro bioadhesion results showed that EMC-5-FU exhibited good affinity to the cysteine-rich subdomains of mucin and NMR studies successfully verified the covalent attachment of EMC-5-FU to mucin. Cysteine 81-89 solute carrier family 13 member 2 Rattus norvegicus 109-114 29361137-4 2018 We then produced Cys to Ser mutants at four sites (Cys25, Cys106, Cys183 and Cys278) in the extracellular domains of P2Y2R and examined the effect on dimer formation and receptor activity. Cysteine 17-20 purinergic receptor P2Y2 Homo sapiens 117-122 29326360-4 2018 Here, GK1.5 cys-diabody (cDb), an antimouse CD4 antibody fragment derived from the GK1.5 hybridoma, was used as a PET probe for CD4+ T cells in the dextran sulfate sodium (DSS) mouse model of IBD. Cysteine 12-15 CD4 antigen Mus musculus 44-47 29326360-4 2018 Here, GK1.5 cys-diabody (cDb), an antimouse CD4 antibody fragment derived from the GK1.5 hybridoma, was used as a PET probe for CD4+ T cells in the dextran sulfate sodium (DSS) mouse model of IBD. Cysteine 12-15 CD4 antigen Mus musculus 128-131 30027060-3 2018 A metabolomics analysis of cells exposed to nanosilver (nAg) integrates volcano plots (t-tests and fold change analysis), partial least squares-discriminant analysis (PLS-DA), and significance analysis of microarrays (SAM) and identifies six metabolites (l-aspartic acid, l-malic acid, myoinositol, d-sorbitol, citric acid, and l-cysteine). Cysteine 328-338 NBAS subunit of NRZ tethering complex Homo sapiens 56-59 29786653-1 2018 Earlier, we reported that gestational ethanol (E) can dysregulate neuron glutathione (GSH) homeostasis partially via impairing the EAAC1-mediated inward transport of Cysteine (Cys) and this can affect fetal brain development. Cysteine 166-174 solute carrier family 1 member 1 Rattus norvegicus 131-136 29786653-1 2018 Earlier, we reported that gestational ethanol (E) can dysregulate neuron glutathione (GSH) homeostasis partially via impairing the EAAC1-mediated inward transport of Cysteine (Cys) and this can affect fetal brain development. Cysteine 166-169 solute carrier family 1 member 1 Rattus norvegicus 131-136 29681455-6 2018 Two such beta sheets bind together along a compact hydrophobic interface featuring an unusual ladder of alternating Ser (from RIPK1) and Cys (from RIPK3). Cysteine 137-140 receptor interacting serine/threonine kinase 3 Homo sapiens 147-152 29369431-5 2018 To render a particular target molecule accessible for PELDOR, it can be engineered to contain only one or two surface-exposed cysteine residues, which can be efficiently spin-labelled using thiol-reactive nitroxide compounds. Cysteine 126-134 spindlin 1 Homo sapiens 170-174 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 52-56 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 93-97 29369431-9 2018 Here we describe the concept of "inhibitor-directed spin labelling" (IDSL) as an approach to spin label suitable cysteine-rich proteins in a site-directed and highly specific manner by employing bespoke spin-labelled inhibitors. Cysteine 113-121 spindlin 1 Homo sapiens 93-97 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. Cysteine 87-95 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 43-48 29511087-8 2018 The alanine-scanning experiments revealed that residues Tyr-34, Gln-38, Gly-39, and Leu-45 (in the AB loop) and Pro-153 (in the D-helix) had specific roles in activating OSMR but not LIFR signaling, whereas Leu-40 and Cys-49 (in the AB loop), and Phe-160 and Lys-163 (in the D-helix) were required for activation of both receptors. Cysteine 218-221 oncostatin M receptor Homo sapiens 170-174 29720605-3 2018 In this study, we tested the hypothesis that reduced cysteine transport into neurons by EAAC1 knockout negatively affects adult hippocampal neurogenesis under physiological or pathological states. Cysteine 53-61 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 88-93 29767695-6 2018 Sulfite oxidase, an enzyme found in mitochondria, catalyzes oxidation of sulfite to sulfate, the final step in oxidation of sulfur amino acids (cysteine and methionine). Cysteine 144-152 sulfite oxidase Homo sapiens 0-15 29636310-10 2018 L-cysteine administered with acrylamide decreased multinucleated giant cell number (p<0.001) and reversed the reduced proliferating cell nuclear antigen positivity (p<0.001), but did not restore other parameters compared with the acrylamide alone-treated group. Cysteine 0-10 proliferating cell nuclear antigen Rattus norvegicus 121-155 29616348-9 2018 This nanohybrid was used for modifying a glassy carbon electrode to develop a sensor electrode for detecting L-cysteine that has fast response (less than 2 s), low detection limit (0.15 muM), and good sensitivity (0.092 muA muM-1 cm-2). Cysteine 109-119 PWWP domain containing 3A, DNA repair factor Homo sapiens 224-229 29382726-6 2018 We found that OTUB1 directly interacted with DEPTOR via its N-terminal domain, deubiquitinated DEPTOR, and thereby stabilized DEPTOR in a Cys-91-independent but Asp-88-dependent manner, suggesting that OTUB1 targets DEPTOR for deubiquitination via a deubiquitinase activity-independent non-canonical mechanism. Cysteine 138-141 DEP domain containing MTOR interacting protein Homo sapiens 45-51 29461042-4 2018 Moreover, aided by the enrichment treatment effect of magnetic micronanoelectrodes, an ultrahigh sensitivity up to 102 muA muM-1 cm-2 was achieved, the detection limit is reduced to picomolar level (83 pM) for d-Cys and can be used for the recognition of cysteine enantiomers. Cysteine 255-263 PWWP domain containing 3A, DNA repair factor Homo sapiens 123-128 29429878-0 2018 Raf-1 Cysteine-Rich Domain Increases the Affinity of K-Ras/Raf at the Membrane, Promoting MAPK Signaling. Cysteine 6-14 KRAS proto-oncogene, GTPase Homo sapiens 53-58 29338251-1 2018 Oxytocin (OXT) is a cyclic nonapeptide, two amino acids of which are cysteine, forming an intramolecular disulfide bond. Cysteine 69-77 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. Cysteine 69-77 oxytocin/neurophysin I prepropeptide Homo sapiens 10-13 29203375-4 2018 In this work, the stability of selected Cys mutants of 14-3-3zeta was predicted by free-energy calculations and the obtained data were compared with experimentally determined stabilities. Cysteine 40-43 tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein zeta Homo sapiens 55-65 29031612-6 2018 Alternatively, HLA-A*02:07, which corresponds to the cysteine residue at HLA-A amino acid position 99 (HLA-A Cys99), demonstrated the most significant association with PsV (odds ratio = 4.61, P = 1.2 x 10-10). Cysteine 53-61 major histocompatibility complex, class II, DQ beta 1 Homo sapiens 15-18 29350903-1 2018 In this work, a typical cylinder-shaped tobacco mosaic virus coat protein (TMVCP) is employed as an anisotropic building block to assemble into triclinic and hexagonal close-packed (HCP) protein crystals by introducing cysteine residues at the 1 and 3 sites and four histidine residues at the C-terminal, respectively. Cysteine 219-227 Coat protein Tobacco mosaic virus 61-73 29495336-0 2018 Cys Site-Directed Mutagenesis of the Human SLC1A5 (ASCT2) Transporter: Structure/Function Relationships and Crucial Role of Cys467 for Redox Sensing and Glutamine Transport. Cysteine 0-3 solute carrier family 1 member 5 Homo sapiens 43-49 29495336-0 2018 Cys Site-Directed Mutagenesis of the Human SLC1A5 (ASCT2) Transporter: Structure/Function Relationships and Crucial Role of Cys467 for Redox Sensing and Glutamine Transport. Cysteine 0-3 solute carrier family 1 member 5 Homo sapiens 51-56 29495336-3 2018 WT and Cys mutants of hASCT2 were produced in P. pastoris and purified for functional assay. Cysteine 7-10 solute carrier family 1 member 5 Homo sapiens 22-28 29276047-3 2018 To counter this obstacle, we developed a CDK inhibitor, E9, that is not a substrate for ABC transporters, and by selecting for resistance, determined that it exerts its cytotoxic effects through covalent modification of cysteine 1039 of CDK12. Cysteine 220-228 cyclin dependent kinase 12 Homo sapiens 237-242 29196604-7 2018 By contrast, LTD-induced spine removal of AKAP79/150 required its depalmitoylation on two Cys residues within the N-terminal targeting domain. Cysteine 90-93 A-kinase anchoring protein 5 Homo sapiens 42-48 29400315-7 2018 As Pex5p undergoes recycling and release, the Pex4p-Pex22p complex is essential for monoubiquitination at the conserved cysteine residue of Pex5p. Cysteine 120-128 Pex5p Saccharomyces cerevisiae S288C 3-8 29400315-7 2018 As Pex5p undergoes recycling and release, the Pex4p-Pex22p complex is essential for monoubiquitination at the conserved cysteine residue of Pex5p. Cysteine 120-128 Pex5p Saccharomyces cerevisiae S288C 140-145 29155106-3 2018 The only free cysteine (Cys-121) of beta-lactoglobulin has been tagged with 7-diethylamino-3-(4-maleimidophenyl)-4-methylcoumarin (CPM) for this purpose. Cysteine 14-22 beta-lactoglobulin Bos taurus 36-54 29155106-3 2018 The only free cysteine (Cys-121) of beta-lactoglobulin has been tagged with 7-diethylamino-3-(4-maleimidophenyl)-4-methylcoumarin (CPM) for this purpose. Cysteine 24-27 beta-lactoglobulin Bos taurus 36-54 29195919-9 2018 We then identified the glutathionylation susceptible cysteine residues of p47phox by LC-MS/MS with IAM switch mapping. Cysteine 53-61 neutrophil cytosolic factor 1 Homo sapiens 74-81 29568662-0 2018 S-Nitroso-N-acetyl-L-cysteine ethyl ester (SNACET) and N-acetyl-L-cysteine ethyl ester (NACET)-Cysteine-based drug candidates with unique pharmacological profiles for oral use as NO, H2S and GSH suppliers and as antioxidants: Results and overview. Cysteine 95-103 X-linked Kx blood group Homo sapiens 55-74 29117939-7 2018 Here, a novel complex is identified between TROY and EGFR, which is mediated predominantly by the cysteine-rich CRD3 domain of TROY. Cysteine 98-106 TNF receptor superfamily member 19 Homo sapiens 44-48 29117939-7 2018 Here, a novel complex is identified between TROY and EGFR, which is mediated predominantly by the cysteine-rich CRD3 domain of TROY. Cysteine 98-106 TNF receptor superfamily member 19 Homo sapiens 127-131 29317536-8 2018 Accordingly, we harnessed the monensin-ATF4-signaling cascade to stimulate CSE expression by preconditioning cells with monensin, which restores cysteine metabolism and an optimal stress response in HD. Cysteine 145-153 activating transcription factor 4 Homo sapiens 39-43 29317536-8 2018 Accordingly, we harnessed the monensin-ATF4-signaling cascade to stimulate CSE expression by preconditioning cells with monensin, which restores cysteine metabolism and an optimal stress response in HD. Cysteine 145-153 cystathionine gamma-lyase Homo sapiens 75-78 29360865-1 2018 Cathepsin B (CatB) is a cysteine proteolytic enzyme widely expressed in various cells and mainly located in the lysosomes. Cysteine 24-32 cathepsin B Mus musculus 0-11 29360865-1 2018 Cathepsin B (CatB) is a cysteine proteolytic enzyme widely expressed in various cells and mainly located in the lysosomes. Cysteine 24-32 cathepsin B Mus musculus 13-17 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. Cysteine 140-143 galectin 13 Homo sapiens 0-11 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. Cysteine 152-155 galectin 13 Homo sapiens 0-11 29320680-4 2018 Key to these studies is the fact that K-Ras4B has its native membrane anchor, including both the farnesylation and methylation of the terminal cysteine, enabling detailed exploration of possible effects of cholesterol and lipid composition on K-Ras4B membrane organization. Cysteine 143-151 KRAS proto-oncogene, GTPase Homo sapiens 38-45 30393252-2 2018 H2S is produced from l-cysteine by pyridoxal 5"-phosphate (PLP)-dependent enzymes, cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE). Cysteine 21-31 cystathionine gamma-lyase Homo sapiens 121-146 30393252-2 2018 H2S is produced from l-cysteine by pyridoxal 5"-phosphate (PLP)-dependent enzymes, cystathionine beta-synthase (CBS) and cystathionine gamma-lyase (CSE). Cysteine 21-31 cystathionine gamma-lyase Homo sapiens 148-151 29206135-0 2017 Ethanol (E) Impairs Fetal Brain GSH Homeostasis by Inhibiting Excitatory Amino-Acid Carrier 1 (EAAC1)-Mediated Cysteine Transport. Cysteine 111-119 solute carrier family 1 member 1 Rattus norvegicus 62-93 29206135-0 2017 Ethanol (E) Impairs Fetal Brain GSH Homeostasis by Inhibiting Excitatory Amino-Acid Carrier 1 (EAAC1)-Mediated Cysteine Transport. Cysteine 111-119 solute carrier family 1 member 1 Rattus norvegicus 95-100 29619193-2 2017 It belongs to the widespread Rrf2 super-family of transcriptional regulators and features three conserved Cys residues that characterise the binding of an iron-sulfur cluster in other Rrf2 family regulators. Cysteine 106-109 GTP dependent ribosome recycling factor mitochondrial 2 Homo sapiens 29-33 29619193-2 2017 It belongs to the widespread Rrf2 super-family of transcriptional regulators and features three conserved Cys residues that characterise the binding of an iron-sulfur cluster in other Rrf2 family regulators. Cysteine 106-109 GTP dependent ribosome recycling factor mitochondrial 2 Homo sapiens 184-188 28542722-5 2017 This variant is predicted to change the highly conserved strongly basic arginine at position 538 in the PAX7 binding domain of PAXBP1 to a neutral cysteine (p.Arg538Cys) residue. Cysteine 147-155 paired box 7 Homo sapiens 104-108 29021278-7 2017 Here, we report phenotypic analysis of a complete loss-of-function mutant in the gamma-glutamylcysteine synthetase catalytic subunit (Gclc) gene in the fruit fly Drosophila melanogasterGclc encodes the evolutionarily conserved catalytic component of the enzyme that conjugates glutamate and cysteine in the GSH biosynthesis pathway. Cysteine 95-103 Glutamate-cysteine ligase catalytic subunit Drosophila melanogaster 134-138 28605509-2 2017 We describe the exceptional case of a patient from a consanguineous family carrying a novel homozygous UMOD mutation (p.C120Y) affecting a conserved cysteine residue within the EGF-like domain III of uromodulin. Cysteine 149-157 uromodulin Homo sapiens 103-107 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. Cysteine 145-153 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 157-161 29184177-0 2017 Corrigendum: Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation. Cysteine 50-58 acetyl-CoA acetyltransferase 2 Homo sapiens 77-82 29109265-8 2017 Furthermore, substitution of the redox active cysteine pair C52 and C57 in the N terminus of Sil1 results in the Doa10-dependent ERAD of this mutant protein. Cysteine 46-54 E3 ubiquitin-protein ligase SSM4 Saccharomyces cerevisiae S288C 113-118 28750239-2 2017 In this paper, an "off-on" method for highly sensitive and selective detection of Hg2+ and l-cysteine (l-Cys) or Hg2+ and I- using home-made nitrogen-doped carbon quantum dots (N-CQDs) as fluorescent probe was reported. Cysteine 103-108 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 82-85 28750239-5 2017 When l-Cys or I- was added into the N-CQDs-Hg2+ system, the fluorescence was recovered effectively (turn-on). Cysteine 5-10 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 43-46 28830914-11 2017 The thiol-containing molecules l-cysteine and d-cysteine both mimicked the protective effects of NAC, whereas the thiol-lacking molecule N-acetyl-S-methyl-l-cysteine failed to exert protection or blunt the rise in ubiquitinated proteins. Cysteine 31-41 X-linked Kx blood group Homo sapiens 97-100 29079645-0 2017 Isa1p is a component of the mitochondrial machinery for maturation of cellular iron-sulfur proteins and requires conserved cysteine residues for function. Cysteine 123-131 iron-sulfur cluster assembly 1 Homo sapiens 0-5 29045385-8 2017 Structural studies reveal that GNE-6640 and GNE-6776 non-covalently target USP7 12 A distant from the catalytic cysteine. Cysteine 112-120 glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase Homo sapiens 31-34 29045385-8 2017 Structural studies reveal that GNE-6640 and GNE-6776 non-covalently target USP7 12 A distant from the catalytic cysteine. Cysteine 112-120 glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase Homo sapiens 44-47 29045385-8 2017 Structural studies reveal that GNE-6640 and GNE-6776 non-covalently target USP7 12 A distant from the catalytic cysteine. Cysteine 112-120 ubiquitin specific peptidase 7 Homo sapiens 75-79 28948272-0 2017 Cysteine and glutathione trigger the Cu-Zn swap between Cu(ii)-amyloid-beta4-16 peptide and Zn7-metallothionein-3. Cysteine 0-8 metallothionein 3 Homo sapiens 96-113 28948272-1 2017 Cysteine and glutathione are able to reduce Cu(ii) coordinated to the peptide amyloidbeta4-16, and shuttle the resulting Cu(i) to partially replace Zn(ii) in the protein Zn7-metallothionein-3. Cysteine 0-8 metallothionein 3 Homo sapiens 174-191 28948272-3 2017 Thus cysteine and glutathione are modulators of Cu/Zn-distribution between metallothionein-3 and amyloid-beta4-16. Cysteine 5-13 metallothionein 3 Homo sapiens 75-92 28933855-0 2017 Orthogonal Tyrosine and Cysteine Site-Directed Spin Labeling for Dipolar Pulse EPR Spectroscopy on Proteins. Cysteine 24-32 spindlin 1 Homo sapiens 47-51 28705807-4 2017 The inhibitory effect of l-cysteine, but not NaHS, on PDE5 activity was blocked in cells transfected with CSE siRNA or treated with CSE inhibitor d,l-propargylglycine (dl-PPG), suggesting activation of CSE and generation of H2S in response to l-cysteine. Cysteine 25-35 cystathionine gamma-lyase Homo sapiens 106-109 28705807-4 2017 The inhibitory effect of l-cysteine, but not NaHS, on PDE5 activity was blocked in cells transfected with CSE siRNA or treated with CSE inhibitor d,l-propargylglycine (dl-PPG), suggesting activation of CSE and generation of H2S in response to l-cysteine. Cysteine 25-35 cystathionine gamma-lyase Homo sapiens 132-135 28705807-4 2017 The inhibitory effect of l-cysteine, but not NaHS, on PDE5 activity was blocked in cells transfected with CSE siRNA or treated with CSE inhibitor d,l-propargylglycine (dl-PPG), suggesting activation of CSE and generation of H2S in response to l-cysteine. Cysteine 25-35 cystathionine gamma-lyase Homo sapiens 132-135 28705807-5 2017 H2S levels were increased in response to l-cysteine, and the effect of l-cysteine was augmented by GSNO in a cGMP-dependent protein kinase-sensitive manner, suggesting augmentation of CSE/H2S by cGMP/PKG pathway. Cysteine 71-81 cystathionine gamma-lyase Homo sapiens 184-187 29147508-3 2017 Inspired by the precise Golgi positioning ability of galactosyltransferase and protein kinase D, due to their cysteine residues, we developed a method for long-term Golgi imaging. Cysteine 110-118 protein kinase D1 Homo sapiens 79-95 28662391-2 2017 For this purpose, the original sequence of the incretin GLP-1 was slightly modified in the C-terminal region by adding a cysteine residue to facilitate conjugation to the gold surface. Cysteine 121-129 glucagon Rattus norvegicus 56-61 28837266-6 2017 Modification of a fifth cysteine (C185), unique for ILEI, did not alter protein secretion, but completely inhibited ILEI dimerization. Cysteine 24-32 FAM3 metabolism regulating signaling molecule C Mus musculus 52-56 28837266-6 2017 Modification of a fifth cysteine (C185), unique for ILEI, did not alter protein secretion, but completely inhibited ILEI dimerization. Cysteine 24-32 FAM3 metabolism regulating signaling molecule C Mus musculus 116-120 29066688-5 2017 The ratio of F4/80+ CD8a+ cells in the CY+LEM+MAK treatment group was lower than that in the untreated group. Cysteine 39-41 adhesion G protein-coupled receptor E1 Mus musculus 13-18 28115272-5 2017 We have recently demonstrated the acute and chronic modulation of DA reuptake activity and DAT stability through S-palmitoylation, the linkage of a 16-carbon palmitate group to cysteine via a thioester bond. Cysteine 177-185 solute carrier family 6 member 3 Homo sapiens 91-94 28971603-4 2017 Carbachol (CCh)-induced contraction in rabbit muscle strips and isolated muscle cells was inhibited by l-cysteine (substrate of CSE) and NaHS (an exogenous H2 S donor) in a concentration-dependent fashion. Cysteine 103-113 cystathionine gamma-lyase Oryctolagus cuniculus 128-131 28971603-7 2017 Inhibition of CCh-induced contraction by l-cysteine was blocked by the CSE inhibitor, dl-propargylglycine (DL-PPG) in dispersed muscle cells. Cysteine 41-51 cystathionine gamma-lyase Oryctolagus cuniculus 71-74 28971603-8 2017 Inhibition of CCh-induced Rho kinase activity by l-cysteine was blocked by CSE siRNA in cultured cells and DL-PPG in dispersed muscle cells. Cysteine 49-59 cystathionine gamma-lyase Oryctolagus cuniculus 75-78 28735240-5 2017 L-Cysteine treatment significantly attenuated brain edema and decreased infarct volume and neuronal cell death, as shown by a decrease in the Bax/Bcl-2 ratio, suppression of caspase-3 activation, and reduced phosphorylation of Akt and ERK at 72h after HI. Cysteine 0-10 BCL2-associated X protein Mus musculus 142-145 28735240-5 2017 L-Cysteine treatment significantly attenuated brain edema and decreased infarct volume and neuronal cell death, as shown by a decrease in the Bax/Bcl-2 ratio, suppression of caspase-3 activation, and reduced phosphorylation of Akt and ERK at 72h after HI. Cysteine 0-10 caspase 3 Mus musculus 174-183 28709872-4 2017 In the present study, we sought to determine whether S-nitrosylation of the cysteine residues in IGF-1R is an important post-translational modification that regulates its response to IGF-1. Cysteine 76-84 insulin like growth factor 1 receptor Homo sapiens 97-103 28709872-5 2017 Using cultured SH-SY5Y human neuroblastoma cells as an in vitro model, we found that treatment of cells with S-nitroso-cysteine (SNOC), a NO donor that can nitrosylate the cysteine residues in proteins, induces S-nitrosylation of the beta subunit of IGF-1R but not its alpha-subunit. Cysteine 119-127 insulin like growth factor 1 receptor Homo sapiens 250-256 28709872-9 2017 Together, these results suggest that elevated nitrosative stress may result in dysfunction of cellular IGF-1R signaling through S-nitrosylation of the cysteine residues in the IGF-1Rbeta subunit, thereby disrupting the downstream PI3K and MAPK signaling functions and ultimately resulting in inhibition of cell proliferation and survival. Cysteine 151-159 insulin like growth factor 1 receptor Homo sapiens 103-109 31457864-8 2017 In the cysteine and penicillamine complexes, double thiolate bridges join the Rh(III) ions, with the nonbridging Cys2- and Pen2- ligands in tridentate chelating (S,N,O) mode, which is consistent with the DeltadeltaC = 7.3-8.4 ppm shift of the COO- signal in their carbon-13 cross polarization magic angle spinning (CPMAS) NMR spectra. Cysteine 7-15 presenilin enhancer, gamma-secretase subunit Homo sapiens 123-127 28825794-5 2017 Anti-EGFR Nanofitin B10 was reformatted by genetic engineering to exhibit a unique cysteine moiety at its C-terminus, which allows the development of a fast and site-specific radiolabeling procedure with 18F-4-fluorobenzamido-N-ethylamino-maleimide (18F-FBEM). Cysteine 83-91 ectonucleotide pyrophosphatase/phosphodiesterase 3 Homo sapiens 20-23 28825794-6 2017 The in vivo tumor targeting and imaging profile of the anti-EGFR Cys-B10 Nanofitin was investigated in a double-tumor xenograft model by static small-animal PET at 2 h after tail-vein injection of the radiolabeled Nanofitin 18F-FBEM-Cys-B10. Cysteine 65-68 ectonucleotide pyrophosphatase/phosphodiesterase 3 Homo sapiens 69-72 28825794-8 2017 18F-FBEM-Cys-B10 demonstrated a significantly higher retention in A431 tumors than in H520 tumors at 2.5 h post-injection with a A431-to-H520 uptake ratio of 2.53 +- 0.18 and a tumor-to-blood ratio of 4.55 +- 0.63. Cysteine 9-12 ectonucleotide pyrophosphatase/phosphodiesterase 3 Homo sapiens 13-16 28837777-8 2017 Thus, the results from the present study revealed, for the first time, that arsenite may target cysteine residues in the zinc-finger motif of the TIP60 histone acetyltransferase, thereby altering the H4K16Ac histone epigenetic mark. Cysteine 96-104 lysine acetyltransferase 5 Homo sapiens 146-151 28724772-2 2017 Two-hybrid and pulldown assays demonstrated that UL20, but no other HSV-1 gene-encoded proteins, binds specifically to GODZ (also known as DHHC3), a cellular Golgi apparatus-specific Asp-His-His-Cys (DHHC) zinc finger protein. Cysteine 195-198 envelope protein UL20 Human alphaherpesvirus 1 49-53 28955208-1 2017 The alpha9 and alpha10 nicotinic acetylcholine receptor (nAChR) subunits are likely to be the evolutionary precursors to the entire cys-loop superfamily of ligand-gated ion channels, which includes acetylcholine, GABA, glycine and serotonin ionotropic receptors. Cysteine 132-135 integrin alpha 9 Mus musculus 4-22 28878211-4 2017 By combining proximity ligation assay with chemical labeling of cysteine residues in the sulfenic acid state, we visualize oxidized Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2). Cysteine 64-72 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 197-201 28869585-10 2017 Since beta-hCG belongs to a cysteine knot family of proteins like TGFbeta and TGFbeta signaling is deregulated in BRCA1 defective tumors, we checked whether beta-hCG can mediate signaling through TGFbetaRII in BRCA1 mutated cells. Cysteine 28-36 BRCA1 DNA repair associated Homo sapiens 114-119 28606778-8 2017 The biphasic roles of HMGB1 may be based on the different redox modifications of cysteine residues. Cysteine 81-89 high mobility group box 1 Rattus norvegicus 22-27 28807514-4 2017 Here we show a cysteine residue (Cys306) for selective Hsp70 activation using natural small-molecule handelin. Cysteine 15-23 heat shock protein family A (Hsp70) member 4 Homo sapiens 55-60 28807514-7 2017 Collectively, our study offers some insights into direct pharmacological activation of Hsp70 by specially targeting functional cysteine residue, thus providing a powerful tool for accurately modulating neuroinflammation pathogenesis in human with fewer undesirable adverse effects. Cysteine 127-135 heat shock protein family A (Hsp70) member 4 Homo sapiens 87-92 28623432-1 2017 Involvement of genes (CYS-A1, CYS-C1 and NIT4) encoded with cysteine synthase, beta-cyanoalanine synthase, nitrilase and cyanide metabolisms are evident in Arabidopsis. Cysteine 22-25 cysteine synthase C1 Arabidopsis thaliana 30-36 28734204-6 2017 Results were consistent with previous findings from cysteine accessibility assays used to assess an inhibitor"s DAT conformation preference. Cysteine 52-60 solute carrier family 6 member 3 Homo sapiens 112-115 28581036-6 2017 We also investigated whether cysteine residues of Opi1p were implicated in the H2 O2 -mediated translocation of this protein to the nucleus and identified cysteine residue 159 as essential for this process. Cysteine 29-37 transcriptional regulator OPI1 Saccharomyces cerevisiae S288C 50-55 28581036-6 2017 We also investigated whether cysteine residues of Opi1p were implicated in the H2 O2 -mediated translocation of this protein to the nucleus and identified cysteine residue 159 as essential for this process. Cysteine 155-163 transcriptional regulator OPI1 Saccharomyces cerevisiae S288C 50-55 28609781-6 2017 We reveal that hSSB1 forms a tetramer that is structurally similar to the SSB from Escherichia coli and is stabilized by two cysteines (C81 and C99) as well as a subset of charged and hydrophobic residues. Cysteine 125-134 single-stranded DNA-binding protein Escherichia coli 16-19 28757206-5 2017 Here, we report that NO positively regulates the PRMT5 activity through S-nitrosylation at Cys-125 during stress responses. Cysteine 91-94 SHK1 binding protein 1 Arabidopsis thaliana 49-54 28757206-6 2017 In prmt5-1 plants, a PRMT5C125S transgene, carrying a non-nitrosylatable mutation at Cys-125, fully rescues the developmental defects, but not the stress hypersensitive phenotype and the responsiveness to NO during stress responses. Cysteine 85-88 SHK1 binding protein 1 Arabidopsis thaliana 3-8 28637872-7 2017 The H2S-induced increase in eIF2alpha phosphorylation was mediated at least in part by inhibition of protein phosphatase-1 (PP1c) via persulfidation at Cys-127. Cysteine 152-155 eukaryotic translation initiation factor 2A Homo sapiens 28-37 28637872-7 2017 The H2S-induced increase in eIF2alpha phosphorylation was mediated at least in part by inhibition of protein phosphatase-1 (PP1c) via persulfidation at Cys-127. Cysteine 152-155 protein phosphatase 1 catalytic subunit gamma Homo sapiens 124-128 28637872-8 2017 Overexpression of a PP1c cysteine mutant (C127S-PP1c) abrogated the H2S effect on eIF2alpha phosphorylation. Cysteine 25-33 protein phosphatase 1 catalytic subunit gamma Homo sapiens 20-24 28637872-8 2017 Overexpression of a PP1c cysteine mutant (C127S-PP1c) abrogated the H2S effect on eIF2alpha phosphorylation. Cysteine 25-33 protein phosphatase 1 catalytic subunit gamma Homo sapiens 48-52 28637872-8 2017 Overexpression of a PP1c cysteine mutant (C127S-PP1c) abrogated the H2S effect on eIF2alpha phosphorylation. Cysteine 25-33 eukaryotic translation initiation factor 2A Homo sapiens 82-91 28661582-4 2017 In addition, the structures reveal for the first time that the Cys-rich subdomain, which is unique to vertebrate melanogenic proteins, has an epidermal growth factor-like fold and is tightly associated with the tyrosinase subdomain. Cysteine 63-66 tyrosinase Homo sapiens 211-221 28790335-6 2017 HQ-induced TRPA1 activation was dependent on essential redox-sensitive cysteine and lysine residues within N-terminus of channel protein. Cysteine 71-79 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 11-16 28779110-6 2017 Mutant experiments show that conserved cysteine residues of Fe-S clusters of CDKAL1 are essential for its anti-adipogenic action. Cysteine 39-47 CDK5 regulatory subunit associated protein 1-like 1 Mus musculus 77-83 27371763-4 2017 Instead, nuclear distribution element-like (NDEL1), a protein that regulates dendritic development, is specifically S-nitrosylated at cysteine 203, thereby accelerating dendritic arborization. Cysteine 134-142 nudE neurodevelopment protein 1 like 1 Homo sapiens 44-49 28730604-2 2017 Full activation of c-Raf-1 requires cooperative interaction of the farnesylated C terminus and the activator region of Ras with its cysteine-rich domain (CRD). Cysteine 132-140 TNF receptor associated factor 3 Homo sapiens 19-26 28576974-0 2017 Lecithin:Cholesterol Acyltransferase Activation by Sulfhydryl-Reactive Small Molecules: Role of Cysteine-31. Cysteine 96-104 lecithin-cholesterol acyltransferase Homo sapiens 0-36 27966069-0 2017 ImmunoPET Imaging of Murine CD4+ T Cells Using Anti-CD4 Cys-Diabody: Effects of Protein Dose on T Cell Function and Imaging. Cysteine 56-59 CD4 antigen Mus musculus 28-31 27966069-0 2017 ImmunoPET Imaging of Murine CD4+ T Cells Using Anti-CD4 Cys-Diabody: Effects of Protein Dose on T Cell Function and Imaging. Cysteine 56-59 CD4 antigen Mus musculus 52-55 28570922-10 2017 After sequential amino acid substitution, we found the binding capacity of P14-2 was completely lost by the substitution of cysteine (C) 132 and significantly decreased by the substitution of tryptophan (W) 136, lysine (K) 141, or glycine (G) 142, but still at a high level. Cysteine 124-132 ribonuclease P/MRP subunit p14 Homo sapiens 75-78 28789400-1 2017 WNT1-inducible-signaling pathway protein-1 (WISP-1) belongs to the family of cysteine rich 61/connective tissue growth factor/nephroblastoma overexpressed matricellular proteins, which are involved in various biological processes, including cell adhesion, proliferation, differentiation, angiogenesis and carcinogenesis. Cysteine 77-85 cellular communication network factor 4 Homo sapiens 0-42 28789400-1 2017 WNT1-inducible-signaling pathway protein-1 (WISP-1) belongs to the family of cysteine rich 61/connective tissue growth factor/nephroblastoma overexpressed matricellular proteins, which are involved in various biological processes, including cell adhesion, proliferation, differentiation, angiogenesis and carcinogenesis. Cysteine 77-85 cellular communication network factor 4 Homo sapiens 44-50 26578115-3 2017 The DARC receptor-binding domain lies in a conserved N-terminal cysteine-rich region of PvDBP referred to as region II (PvDBPII). Cysteine 64-72 atypical chemokine receptor 1 (Duffy blood group) Homo sapiens 4-8 28547869-4 2017 Moreover, NMR data and the chemical modification of cysteine residues demonstrated that the RFP141C peptide binds to two zinc atoms in a cross-brace arrangement. Cysteine 52-60 ring finger protein 141 Homo sapiens 92-107 28596420-2 2017 A comparative analysis of the AOX isoenzymes AOX1A, AOX1C, and AOX1D from Arabidopsis (Arabidopsis thaliana) revealed that cysteine residues, CysI and CysII, are both involved in 2-oxo acid activation, with AOX1A activity being more increased by 2-oxo acids than that of AOX1C and AOX1D. Cysteine 123-131 alternative oxidase 1D Arabidopsis thaliana 63-68 28596420-2 2017 A comparative analysis of the AOX isoenzymes AOX1A, AOX1C, and AOX1D from Arabidopsis (Arabidopsis thaliana) revealed that cysteine residues, CysI and CysII, are both involved in 2-oxo acid activation, with AOX1A activity being more increased by 2-oxo acids than that of AOX1C and AOX1D. Cysteine 123-131 alternative oxidase 1D Arabidopsis thaliana 281-286 28391181-1 2017 Ohr and OsmC proteins comprise two subfamilies within a large group of proteins that display Cys-based, thiol dependent peroxidase activity. Cysteine 93-96 peroxidase 24 Musa acuminata 120-130 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. Cysteine 5-8 peroxidase 24 Musa acuminata 44-54 28592540-5 2017 Both cobalt and cysteine coupling resulted in a high-density array of NFL trimers that was stable in both 20% mouse serum and 100 mM EDTA, whereas the nickel-conjugated trimers were not stable under these conditions. Cysteine 16-24 neurofilament light chain Homo sapiens 70-73 28675039-1 2017 Cystathionine gamma-synthase (MetB) condenses O-acetyl-l-homoserine (OAHS) or O-succinyl-l-homoserine (OSHS) with cysteine to produce cystathionine. Cysteine 114-122 cystathionine gamma-synthase 1, chloroplastic-like Nicotiana tabacum 30-34 28034907-1 2017 Purpose: Ibrutinib inhibits Bruton tyrosine kinase (BTK) by irreversibly binding to the Cys-481 residue in the enzyme. Cysteine 88-91 Bruton tyrosine kinase Homo sapiens 28-50 28034907-1 2017 Purpose: Ibrutinib inhibits Bruton tyrosine kinase (BTK) by irreversibly binding to the Cys-481 residue in the enzyme. Cysteine 88-91 Bruton tyrosine kinase Homo sapiens 52-55 28034907-2 2017 However, ibrutinib also inhibits several other enzymes that contain cysteine residues homologous to Cys-481 in BTK. Cysteine 68-76 Bruton tyrosine kinase Homo sapiens 111-114 28034907-2 2017 However, ibrutinib also inhibits several other enzymes that contain cysteine residues homologous to Cys-481 in BTK. Cysteine 100-103 Bruton tyrosine kinase Homo sapiens 111-114 28576969-0 2017 Redox regulation of the yeast voltage-gated Ca2+ channel homolog Cch1p by glutathionylation of specific cysteine residues. Cysteine 104-112 Cch1p Saccharomyces cerevisiae S288C 65-70 28576969-3 2017 Furthermore, through mutational analysis of all 18 exposed cysteine residues in the Cch1p protein, we show that the four mutants C587A, C606A, C636A and C642A, which are clustered together in a common cytoplasmic loop region, were functionally defective for both fast and slow activations, and also showed reduced glutathionylation. Cysteine 59-67 Cch1p Saccharomyces cerevisiae S288C 84-89 28701733-4 2017 Here we identify that the primary enzymatic source of reactive oxygen species, NOX2 oxidase, is activated by single stranded RNA and DNA viruses in endocytic compartments resulting in endosomal hydrogen peroxide generation, which suppresses antiviral and humoral signaling networks via modification of a unique, highly conserved cysteine residue (Cys98) on Toll-like receptor-7. Cysteine 329-337 cytochrome b-245 beta chain Homo sapiens 79-83 28495886-8 2017 Furthermore, cysteine accessibility assays showed that sigma1R agonist preincubation potentiated cocaine-induced changes in DAT conformation, which were blocked by the specific sigma1R antagonist CM304. Cysteine 13-21 sigma non-opioid intracellular receptor 1 Rattus norvegicus 55-62 28495886-8 2017 Furthermore, cysteine accessibility assays showed that sigma1R agonist preincubation potentiated cocaine-induced changes in DAT conformation, which were blocked by the specific sigma1R antagonist CM304. Cysteine 13-21 sigma non-opioid intracellular receptor 1 Rattus norvegicus 177-184 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. Cysteine 16-25 glycoprotein Ib platelet subunit alpha Homo sapiens 69-78 28695845-3 2017 ACHT1 (atypical cysteine/histidine-rich Trx1) is a thylakoid-associated thioredoxin-type protein found in the Arabidopsis thaliana chloroplast. Cysteine 16-24 atypical CYS HIS rich thioredoxin 1 Arabidopsis thaliana 0-5 28526707-5 2017 Reconstitution of VASP knockout myocardial endothelial cells with cysteine mutants of VASP demonstrated that S-nitrosylation of cysteine 64 is associated with PAF-induced hyperpermeability. Cysteine 128-136 patchy fur Mus musculus 159-162 28434967-1 2017 BACKGROUND: The cysteine residue on transthyretin (TTR) is susceptible to be oxidized, and serum cysteinylated TTR (Cys-TTR) level is thought to reflect oxidative stress. Cysteine 16-24 transthyretin Homo sapiens 36-49 28434967-1 2017 BACKGROUND: The cysteine residue on transthyretin (TTR) is susceptible to be oxidized, and serum cysteinylated TTR (Cys-TTR) level is thought to reflect oxidative stress. Cysteine 16-24 transthyretin Homo sapiens 51-54 28434967-2 2017 The purpose of this study was to elucidate the relationship between Cys-TTR and arterial stiffness, a known predictor of cardiovascular disease, in patients with type 2 diabetes. Cysteine 68-71 transthyretin Homo sapiens 72-75 28434967-5 2017 The relationship between CAVI and ratio of Cys-TTR to total TTR (Cys-TTR ratio) was analyzed. Cysteine 43-46 transthyretin Homo sapiens 47-50 28434967-6 2017 RESULTS: Cys-TTR ratio was significantly correlated with CAVI (Pearson"s correlation coefficient: 0.316, p<0.01), and CAVI was significantly higher in the 3rd tertile group for Cys-TTR ratio than in its 1st tertile group. Cysteine 9-12 transthyretin Homo sapiens 13-16 28434967-6 2017 RESULTS: Cys-TTR ratio was significantly correlated with CAVI (Pearson"s correlation coefficient: 0.316, p<0.01), and CAVI was significantly higher in the 3rd tertile group for Cys-TTR ratio than in its 1st tertile group. Cysteine 9-12 transthyretin Homo sapiens 184-187 28434967-6 2017 RESULTS: Cys-TTR ratio was significantly correlated with CAVI (Pearson"s correlation coefficient: 0.316, p<0.01), and CAVI was significantly higher in the 3rd tertile group for Cys-TTR ratio than in its 1st tertile group. Cysteine 180-183 transthyretin Homo sapiens 184-187 28434967-8 2017 Prevalence of high CAVI (>=10.0) was significantly higher in the 3rd tertile for Cys-TTR ratio than in its 1st tertile and tended to be higher with an increase in tertile (28.6% in the 1st tertile, 42.9% in the 2nd tertile and 60.0% in the 3rd tertile). Cysteine 84-87 transthyretin Homo sapiens 88-91 28434967-9 2017 Odds ratio (OR) for high CAVI of the 3rd vs. 1st tertile groups for Cys-TTR ratio was significantly higher than the reference level of 1.00 both before and after adjustment for the above cardiovascular risk factors (crude OR, 3.75 [1.38-10.17]; adjusted OR, 5.09 [1.39-18.64]). Cysteine 68-71 transthyretin Homo sapiens 72-75 28434967-10 2017 CONCLUSIONS: Cys-TTR ratio is associated with arterial stiffness in patients with diabetes and is proposed as a new discriminator of cardiovascular risk. Cysteine 13-16 transthyretin Homo sapiens 17-20 28483671-8 2017 Activation of MMP-9 by acrolein was inhibited by cysteine, and slightly by lysine, because these amino acids inhibited acrolein conjugation with MMP-9. Cysteine 49-57 matrix metallopeptidase 9 Homo sapiens 14-19 28483671-11 2017 These results suggest that activation of 92kDa MMP-9 by acrolein is involved in tissue damage in pSS patients and is regulated by cysteine and histidine, and slightly by lysine. Cysteine 130-138 matrix metallopeptidase 9 Homo sapiens 47-52 28476858-0 2017 Mutating a conserved cysteine in GPIHBP1 reduces amounts of GPIHBP1 in capillaries and abolishes LPL binding. Cysteine 21-29 lipoprotein lipase Mus musculus 97-100 28476858-2 2017 A mutation in a conserved cysteine in CD59 prevented the protein from reaching the surface of blood cells. Cysteine 26-34 CD59a antigen Mus musculus 38-42 28476858-9 2017 We conclude that mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL, resulting in mislocalization of LPL and severe chylomicronemia. Cysteine 41-49 lipoprotein lipase Mus musculus 102-105 28476858-9 2017 We conclude that mutation of a conserved cysteine in GPIHBP1 abolishes the ability of GPIHBP1 to bind LPL, resulting in mislocalization of LPL and severe chylomicronemia. Cysteine 41-49 lipoprotein lipase Mus musculus 139-142 28332258-7 2017 In this work, the recently discovered GOS-TerL intein was explored as the only known naturally split intein that both lacks a cysteine in its N-terminal fragment and is active under ambient conditions. Cysteine 126-134 trans-2,3-enoyl-CoA reductase like Homo sapiens 42-46 28458053-5 2017 Cysteine 53 of GP1, which forms a disulfide bond with GP2, was mutated to serine to avoid potential disulfide bond mispairing. Cysteine 0-8 GTP binding protein 1 Homo sapiens 15-18 28657544-5 2017 NaF induced apoptosis via tumor necrosis factor recpter-1 (TNF-R1) signaling pathway, which was characterized by significantly increasing mRNA and protein expression levels of TNF-R1, Fas associated death domain (FADD), TNFR-associated death domain (TRADD), cysteine aspartate specific protease-8 (caspase-8) and cysteine aspartate specific protease-3 (caspase-3) in dose- and time-dependent manner. Cysteine 258-266 tumor necrosis factor receptor superfamily, member 1a Mus musculus 26-57 28657544-5 2017 NaF induced apoptosis via tumor necrosis factor recpter-1 (TNF-R1) signaling pathway, which was characterized by significantly increasing mRNA and protein expression levels of TNF-R1, Fas associated death domain (FADD), TNFR-associated death domain (TRADD), cysteine aspartate specific protease-8 (caspase-8) and cysteine aspartate specific protease-3 (caspase-3) in dose- and time-dependent manner. Cysteine 258-266 tumor necrosis factor receptor superfamily, member 1a Mus musculus 59-65 28955770-2 2017 In particular, addicsin acts as a negative modulator of neural glutamate transporter excitatory amino acid carrier 1 (EAAC1) and participates in the regulation of intracellular glutathione (GSH) content by negatively modulating EAAC1-mediated cysteine and glutamate uptake. Cysteine 243-251 ADP-ribosylation factor-like 6 interacting protein 5 Mus musculus 15-23 28432123-2 2017 NCX inactivation occurs in the absence of phosphatidylinositol 4,5-bisphosphate and is facilitated by palmitoylation of a single cysteine at position 739 within the large intracellular loop of NCX. Cysteine 129-137 T cell leukemia homeobox 2 Homo sapiens 0-3 28432123-2 2017 NCX inactivation occurs in the absence of phosphatidylinositol 4,5-bisphosphate and is facilitated by palmitoylation of a single cysteine at position 739 within the large intracellular loop of NCX. Cysteine 129-137 T cell leukemia homeobox 2 Homo sapiens 193-196 28485044-6 2017 The A82-L-B272 ligand was selective over related kinases (BTK and GAK), which also contain targetable cysteine residues in the vicinity of the active site. Cysteine 102-110 Bruton tyrosine kinase Homo sapiens 58-61 28485044-6 2017 The A82-L-B272 ligand was selective over related kinases (BTK and GAK), which also contain targetable cysteine residues in the vicinity of the active site. Cysteine 102-110 cyclin G associated kinase Homo sapiens 66-69 28457754-0 2017 Investigation of the structural requirements of K-Ras(G12D) selective inhibitory peptide KRpep-2d using alanine scans and cysteine bridging. Cysteine 122-130 KRAS proto-oncogene, GTPase Homo sapiens 48-53 28219719-6 2017 Expression of stearoyl-CoA desaturase-1 (Scd1), known to be repressed with cysteine depletion, was also reduced with low cysteine. Cysteine 75-83 stearoyl-Coenzyme A desaturase 1 Mus musculus 14-39 28219719-6 2017 Expression of stearoyl-CoA desaturase-1 (Scd1), known to be repressed with cysteine depletion, was also reduced with low cysteine. Cysteine 75-83 stearoyl-Coenzyme A desaturase 1 Mus musculus 41-45 28219719-6 2017 Expression of stearoyl-CoA desaturase-1 (Scd1), known to be repressed with cysteine depletion, was also reduced with low cysteine. Cysteine 121-129 stearoyl-Coenzyme A desaturase 1 Mus musculus 14-39 28219719-6 2017 Expression of stearoyl-CoA desaturase-1 (Scd1), known to be repressed with cysteine depletion, was also reduced with low cysteine. Cysteine 121-129 stearoyl-Coenzyme A desaturase 1 Mus musculus 41-45 28381531-4 2017 Improvements in overall performance ranged from 4-fold for Hcy:Cys to ~8-fold for Hcy:Cys:Cre and were particularly strong in subjects with the common 5,10-methylenetetrahydrofolate reductase (MTHFR) 677CC genotype.Conclusions: Ratios of tHcy to tCys and/or creatinine showed a severalfold improvement over tHcy alone as functional markers of B-vitamin status in Norwegian coronary angiography screenees. Cysteine 63-66 methylenetetrahydrofolate reductase Homo sapiens 193-198 28381531-4 2017 Improvements in overall performance ranged from 4-fold for Hcy:Cys to ~8-fold for Hcy:Cys:Cre and were particularly strong in subjects with the common 5,10-methylenetetrahydrofolate reductase (MTHFR) 677CC genotype.Conclusions: Ratios of tHcy to tCys and/or creatinine showed a severalfold improvement over tHcy alone as functional markers of B-vitamin status in Norwegian coronary angiography screenees. Cysteine 86-89 methylenetetrahydrofolate reductase Homo sapiens 151-191 28381531-4 2017 Improvements in overall performance ranged from 4-fold for Hcy:Cys to ~8-fold for Hcy:Cys:Cre and were particularly strong in subjects with the common 5,10-methylenetetrahydrofolate reductase (MTHFR) 677CC genotype.Conclusions: Ratios of tHcy to tCys and/or creatinine showed a severalfold improvement over tHcy alone as functional markers of B-vitamin status in Norwegian coronary angiography screenees. Cysteine 86-89 methylenetetrahydrofolate reductase Homo sapiens 193-198 28471462-6 2017 Copper is bound at the active site of MOR244-3 by cysteine and histidine, while cysteine, histidine and methionine are involved with OR2T11. Cysteine 80-88 olfactory receptor family 2 subfamily T member 11 Homo sapiens 133-139 28415650-6 2017 Here, we have investigated whether also oxidation of cysteine residues regulates Zap70 functions. Cysteine 53-61 zeta chain of T cell receptor associated protein kinase 70 Homo sapiens 81-86 28300825-0 2017 Cysteine-linked dimerization of BST-2 confers anoikis resistance to breast cancer cells by negating proapoptotic activities to promote tumor cell survival and growth. Cysteine 0-8 bone marrow stromal cell antigen 2 Homo sapiens 32-37 28300825-4 2017 Using structure/function studies, we report that dimerization of BST-2 through cysteine residues located in the BST-2 extracellular domain (ECD), leads to anoikis resistance and cell survival through proteasome-mediated degradation of BIM-a key proapoptotic factor. Cysteine 79-87 bone marrow stromal cell antigen 2 Homo sapiens 65-70 28300825-4 2017 Using structure/function studies, we report that dimerization of BST-2 through cysteine residues located in the BST-2 extracellular domain (ECD), leads to anoikis resistance and cell survival through proteasome-mediated degradation of BIM-a key proapoptotic factor. Cysteine 79-87 bone marrow stromal cell antigen 2 Homo sapiens 112-117 28300825-6 2017 Furthermore, we demonstrate that restoration of the ECD cysteine residues is sufficient to rescue cell survival and tumor growth via a previously unreported pathway-BST-2/GRB2/ERK/BIM/Cas3. Cysteine 56-64 bone marrow stromal cell antigen 2 Homo sapiens 165-170 28219928-5 2017 We show further that SOCE activates a mitochondrial redox transient which is dependent on NCLX and is required for preventing Orai1 inactivation through oxidation of a critical cysteine (Cys195) in the third transmembrane helix of Orai1. Cysteine 177-185 ORAI calcium release-activated calcium modulator 1 Homo sapiens 126-131 28219928-5 2017 We show further that SOCE activates a mitochondrial redox transient which is dependent on NCLX and is required for preventing Orai1 inactivation through oxidation of a critical cysteine (Cys195) in the third transmembrane helix of Orai1. Cysteine 177-185 ORAI calcium release-activated calcium modulator 1 Homo sapiens 231-236 28193858-6 2017 By using 9H4, we observed that senescent primary human fibroblasts express vimentin on their cell surface, and MS analysis revealed a posttranslational modification on cysteine 328 (C328) by the oxidative adduct malondialdehyde (MDA). Cysteine 168-176 vimentin Mus musculus 75-83 28240595-1 2017 The SNAREs SNAP25 and SNAP23 are proteins that are initially cytosolic after translation, but then become stably attached to the cell membrane through palmitoylation of cysteine residues. Cysteine 169-177 synaptosome associated protein 25 Rattus norvegicus 11-17 28240595-3 2017 In experiments with rat neuroendocrine cells, we find that a few basic amino acids in the cysteine-rich region of SNAP25 and SNAP23 are essential for plasma membrane targeting. Cysteine 90-98 synaptosome associated protein 25 Rattus norvegicus 114-120 28231264-5 2017 CD163 has been described as a fusion receptor for PRRSV, whereby the scavenger receptor cysteine-rich domain 5 (SRCR5) region was shown to be an interaction site for the virus in vitro. Cysteine 88-96 CD163 molecule Homo sapiens 0-5 28230807-0 2017 Effect of Reduction of Redox Modifications of Cys-Residues in the Na,K-ATPase alpha1-Subunit on Its Activity. Cysteine 46-49 ATPase Na+/K+ transporting subunit alpha 1 Homo sapiens 66-92 28230807-6 2017 We have found that purified Na,K-ATPase alpha1-subunit contains glutathionylated, nitrosylated, and oxidized cysteines. Cysteine 109-118 ATPase Na+/K+ transporting subunit alpha 1 Homo sapiens 28-54 28230807-10 2017 This suggests that the enzymatic reducing system glutaredoxin/glutathione reductase specifically affects glutathionylation of the regulatory cysteine residues of Na,K-ATPase alpha1-subunit. Cysteine 141-149 ATPase Na+/K+ transporting subunit alpha 1 Homo sapiens 162-188 27935278-5 2017 The glo1 strain also assimilated sulfate inefficiently but grew normally on cysteine. Cysteine 76-84 lactoylglutathione lyase GLO1 Saccharomyces cerevisiae S288C 4-8 28212299-1 2017 Hydrogen sulfide (H2S) is an endogenous mediator, synthesized from l-cysteine by cystathionine gamma-lyase (CSE), cystathionine beta-synthase (CBS) or 3-mercaptopyruvate sulfurtransferase (3-MST). Cysteine 67-77 mercaptopyruvate sulfurtransferase Rattus norvegicus 151-187 28195196-3 2017 The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Cysteine 18-26 dehydroascorbate reductase Arabidopsis thaliana 92-96 28195196-3 2017 The presence of a cysteine at the active site is essential for the catalytic functioning of DHAR, as mutation of this cysteine abolishes the activity. Cysteine 118-126 dehydroascorbate reductase Arabidopsis thaliana 92-96 28182867-2 2017 We have employed cysteine labelling and linkage analysis to the full length of Bak in mitochondria. Cysteine 17-25 BCL2 antagonist/killer 1 Homo sapiens 79-82 28093456-0 2017 Effect of lipid-bound apolipoprotein A-I cysteine mutant on ATF3 in RAW264.7 cells. Cysteine 41-49 apolipoprotein A-I Mus musculus 22-40 28093456-6 2017 In summary, the different anti-inflammatory mechanisms of the ApoA-I cysteine mutants might be associated with the regulation of ATF3 level. Cysteine 69-77 apolipoprotein A-I Mus musculus 62-68 27990559-6 2017 In addition, NAC restores levels of neuronal glutathione (GSH), a potent antioxidant, by providing a cell-permeable source of cysteine. Cysteine 126-134 X-linked Kx blood group Homo sapiens 13-16 26582344-4 2017 The caIGF-I contains all the features of IGF-I peptide with B, C, A, and D domains and the six conservative cysteine residues involved in the stable tertiary structure. Cysteine 108-116 insulin-like growth factor I Alligator sinensis 6-11 28007574-5 2017 For the assembly of this complex, cysteines of the active site of each Grx3/4 glutaredoxins, glutathione and specific cysteine residues from Slt2 provide the ligands. Cysteine 34-43 monothiol glutaredoxin GRX3 Saccharomyces cerevisiae S288C 71-75 28007574-5 2017 For the assembly of this complex, cysteines of the active site of each Grx3/4 glutaredoxins, glutathione and specific cysteine residues from Slt2 provide the ligands. Cysteine 34-42 monothiol glutaredoxin GRX3 Saccharomyces cerevisiae S288C 71-75 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. Cysteine 61-70 GTP binding elongation factor GUF1 Homo sapiens 139-142 27994615-1 2016 As an essential enzyme in the sulfate assimilation reductive pathway, sulfite reductase (SiR) plays important roles in diverse metabolic processes such as sulfur homeostasis and cysteine metabolism. Cysteine 178-186 sulfite reductase Arabidopsis thaliana 70-87 27994615-1 2016 As an essential enzyme in the sulfate assimilation reductive pathway, sulfite reductase (SiR) plays important roles in diverse metabolic processes such as sulfur homeostasis and cysteine metabolism. Cysteine 178-186 sulfite reductase Arabidopsis thaliana 89-92 27753644-0 2016 Tryptophan and Cysteine Mutations in M1 Helices of alpha1beta3gamma2L gamma-Aminobutyric Acid Type A Receptors Indicate Distinct Intersubunit Sites for Four Intravenous Anesthetics and One Orphan Site. Cysteine 15-23 GABA(A) receptor-associated protein L homeolog Xenopus laevis 70-100 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. Cysteine 80-88 lysine demethylase 1A Homo sapiens 212-217 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. Cysteine 150-158 lysine demethylase 1A Homo sapiens 212-217 27831566-2 2016 Cysteine cathepsins (Cathepsin B or S, CTSB/S) execute specific functions in physiological processes, such as protein degradation, having SIRT1 as a substrate. Cysteine 0-8 cathepsin B Mus musculus 21-32 27831566-2 2016 Cysteine cathepsins (Cathepsin B or S, CTSB/S) execute specific functions in physiological processes, such as protein degradation, having SIRT1 as a substrate. Cysteine 0-8 cathepsin B Mus musculus 39-43 27722658-5 2016 In addition, BDB1 and BDB2 were capable of sensing cysteine in aqueous solution with high selectivity and sensitivity, which means that these complexes hold great potential in serving as fluorogenic cysteine sensors for biological application. Cysteine 51-59 receptor tyrosine kinase like orphan receptor 2 Homo sapiens 13-17 27722658-5 2016 In addition, BDB1 and BDB2 were capable of sensing cysteine in aqueous solution with high selectivity and sensitivity, which means that these complexes hold great potential in serving as fluorogenic cysteine sensors for biological application. Cysteine 199-207 receptor tyrosine kinase like orphan receptor 2 Homo sapiens 13-17 27211622-9 2016 Despite the low homology of Pin p 1 sequence with other allergenic 2S albumins from angiosperms, Pin p 1 contains the typical skeleton of 8 cysteine residues, important for its alpha-helixes enriched structure. Cysteine 140-148 crystallin gamma F, pseudogene Homo sapiens 101-104 27428725-3 2016 MS/MS spectra of [(R)2 Sn(Cys-H)]+ complexes are characterized by numerous fragmentation processes, notably associated with elimination of NH3 and (C,H2 ,O2 ). Cysteine 26-29 relaxin 2 Homo sapiens 148-156 27434506-5 2016 TRPA1 activation by crotalphine required intact N-terminal cysteine residues and was followed by strong and long-lasting desensitization of the channel. Cysteine 59-67 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 0-5 27613864-2 2016 The most common mutation in PRCD linked with severe RP phenotype is substitution of the only cysteine to tyrosine (C2Y). Cysteine 93-101 photoreceptor disc component Mus musculus 28-32 27613864-3 2016 In this study, we find that PRCD is post-translationally modified by a palmitoyl lipid group at the cysteine residue linked with RP. Cysteine 100-108 photoreceptor disc component Mus musculus 28-32 27613864-4 2016 Disrupting PRCD palmitoylation either chemically or by genetically eliminating the modified cysteine dramatically affects the stability of PRCD. Cysteine 92-100 photoreceptor disc component Mus musculus 11-15 27613864-4 2016 Disrupting PRCD palmitoylation either chemically or by genetically eliminating the modified cysteine dramatically affects the stability of PRCD. Cysteine 92-100 photoreceptor disc component Mus musculus 139-143 27782882-3 2016 Here we report that C. elegans LGC-46, a member of the Cys-loop acetylcholine (ACh)-gated chloride (ACC) channel family, localizes to presynaptic terminals of cholinergic motor neurons and regulates synaptic vesicle (SV) release kinetics upon evoked release of acetylcholine. Cysteine 55-58 putative ligand-gated ion channel 46 Caenorhabditis elegans 31-37 27609519-3 2016 Mass spectrometric and crystallographic studies of Pt(II) binding to the RecA intein revealed a complex in which two platinum atoms bind at N- and C-terminal catalytic cysteine residues. Cysteine 168-176 RAD51 recombinase Homo sapiens 73-77 27708394-2 2016 It is endogenously synthesized mainly by two pyridoxal-5"-phosphate-dependent enzymes involved in L-cysteine metabolism: cystathionine-ss-synthase (CBS) and cystathionine-gamma-lyase (CSE). Cysteine 98-108 cystathionine gamma-lyase Homo sapiens 157-182 27708394-2 2016 It is endogenously synthesized mainly by two pyridoxal-5"-phosphate-dependent enzymes involved in L-cysteine metabolism: cystathionine-ss-synthase (CBS) and cystathionine-gamma-lyase (CSE). Cysteine 98-108 cystathionine gamma-lyase Homo sapiens 184-187 27703239-5 2016 Co-crystal structures of GSTO1 with our inhibitors demonstrate covalent binding to the active site cysteine. Cysteine 99-107 glutathione S-transferase omega 1 Homo sapiens 25-30 27609313-1 2016 Transforming growth factor beta-induced protein (TGFBIp) is an extracellular matrix protein composed of an NH2-terminal cysteine-rich domain (CRD) annotated as an emilin (EMI) domain and four fasciclin-1 (FAS1-1-FAS1-4) domains. Cysteine 120-128 transforming growth factor beta induced Homo sapiens 49-55 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. Cysteine 19-27 transforming growth factor beta induced Homo sapiens 0-6 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. Cysteine 115-123 transforming growth factor beta induced Homo sapiens 0-6 27609313-8 2016 The NH2-terminal CRD contains six cysteine residues, and one of these (Cys65) was identified as the candidate for the reducible cross-link between TGFBIp and type XII collagen. Cysteine 34-42 transforming growth factor beta induced Homo sapiens 147-153 27521458-7 2016 Focusing on the regulatory role of PTP1B, we showed S-nitrosylation to be the principal Cys reversible redox modification in endothelial insulin signaling. Cysteine 88-91 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 35-40 27195487-3 2016 Molecular dynamics simulation revealed solvent accessible residues within the beta1 strand of the GABAA beta3 homopentamer that might be amenable to analysis using the substituted Cys accessibility method. Cysteine 180-183 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 78-83 27571479-0 2016 Covalent targeting of remote cysteine residues to develop CDK12 and CDK13 inhibitors. Cysteine 29-37 cyclin dependent kinase 12 Homo sapiens 58-63 27571479-4 2016 Co-crystallization of THZ531 with CDK12-cyclin K indicates that THZ531 irreversibly targets a cysteine located outside the kinase domain. Cysteine 94-102 cyclin dependent kinase 12 Homo sapiens 34-39 27585463-3 2016 Recently, in analogy to what is known in the animal field, plant cytosolic glyceraldehyde-3-phosphate dehydrogenase (GAPC), a ubiquitous enzyme involved in glycolysis, has been suggested to fulfill other functions associated with its oxidative post-translational modifications such as S-nitrosylation on cysteine residues. Cysteine 304-312 glyceraldehyde-3-phosphate dehydrogenase, cytosolic-like Nicotiana tabacum 75-115 27693992-10 2016 Glutathionylation of Rac1 on cysteine 81 and 157 located adjacent to guanine nucleotide binding site was required for the metabolic stress to inhibit Rac1 activity and promote endothelial hyperpermeability. Cysteine 29-37 Rac family small GTPase 1 Homo sapiens 21-25 27693992-10 2016 Glutathionylation of Rac1 on cysteine 81 and 157 located adjacent to guanine nucleotide binding site was required for the metabolic stress to inhibit Rac1 activity and promote endothelial hyperpermeability. Cysteine 29-37 Rac family small GTPase 1 Homo sapiens 150-154 27402161-3 2016 Here, we establish human Ku70 as a novel target of cyclin B1-Cdk1, which phosphorylates it in a Cy-motif dependent manner. Cysteine 96-98 X-ray repair cross complementing 6 Homo sapiens 25-29 27481942-1 2016 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine 333-336 adrenoceptor beta 2 Homo sapiens 42-68 27481942-1 2016 We report here that a population of human beta2-adrenergic receptors (beta2AR), a canonical G protein-coupled receptor, traffics along a previously undescribed intracellular itinerary via the Golgi complex that is associated with the sequential S-palmitoylation and depalmitoylation of a previously undescribed site of modification, Cys-265 within the third intracellular loop. Cysteine 333-336 adrenoceptor beta 2 Homo sapiens 70-77 27481942-4 2016 Cys-265 S-palmitoylation is mediated by the Golgi-resident palmitoyl transferases zDHHC9/14/18 and is followed by depalmitoylation by the plasma membrane-localized acyl-protein thioesterase APT1. Cysteine 0-3 lysophospholipase 1 Homo sapiens 190-194 27481942-6 2016 In addition, beta2AR S-palmitoylated at Cys-265 are selectively preserved under a sustained adrenergic stimulation, which results in the down-regulation and degradation of betaAR. Cysteine 40-43 adrenoceptor beta 2 Homo sapiens 13-20 27481942-7 2016 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine 61-64 adrenoceptor beta 2 Homo sapiens 128-135 27481942-7 2016 Cys-265 is not conserved in beta1AR, and S-palmitoylation of Cys-265 may thus be associated with functional differences between beta2AR and beta1AR, including relative resistance of beta2AR to down-regulation in multiple pathophysiologies. Cysteine 61-64 adrenoceptor beta 2 Homo sapiens 182-189 27546061-4 2016 On the basis of the split Soret ultraviolet-visible (UV-vis) spectrum of ferric DGCR8, bis-thiolate sulfur (cysteinate, Cys(-)) heme iron coordination of DGCR8 heme iron was proposed. Cysteine 120-123 DGCR8 microprocessor complex subunit Homo sapiens 154-159 27546061-6 2016 These studies indicate DGCR8 bis-Cys heme iron ligation, with conversion from bis-thiolate (Cys(-)/Cys(-)) axial coordination in ferric DGCR8 to bis-thiol (CysH/CysH) coordination in ferrous DGCR8. Cysteine 33-36 DGCR8 microprocessor complex subunit Homo sapiens 23-28 27546061-6 2016 These studies indicate DGCR8 bis-Cys heme iron ligation, with conversion from bis-thiolate (Cys(-)/Cys(-)) axial coordination in ferric DGCR8 to bis-thiol (CysH/CysH) coordination in ferrous DGCR8. Cysteine 92-95 DGCR8 microprocessor complex subunit Homo sapiens 136-141 27546061-6 2016 These studies indicate DGCR8 bis-Cys heme iron ligation, with conversion from bis-thiolate (Cys(-)/Cys(-)) axial coordination in ferric DGCR8 to bis-thiol (CysH/CysH) coordination in ferrous DGCR8. Cysteine 92-95 DGCR8 microprocessor complex subunit Homo sapiens 136-141 27698946-4 2016 We successfully design a paclitaxel (PTX) and alpha-galactosylceramide (alphaGC) co-loaded TH peptide (AGYLLGHINLHHLAHL(Aib)HHIL-Cys) -modified liposome (PTX/alphaGC-TH-Lip) and introduce a new concept of immuno-chemotherapy combination via accumulation of these liposomes at both spleen and tumor sites naturally and simultaneously. Cysteine 129-132 ANIB1 Homo sapiens 120-123 27545864-4 2016 According to the single-ring mutation of GroEL, we obtained a single-ring version of GroEL bearing cysteine mutations (GroELCys) and modified its 14 apical cysteine residues with merocyanine (MC). Cysteine 99-107 heat shock protein family D (Hsp60) member 1 Homo sapiens 41-46 27545864-4 2016 According to the single-ring mutation of GroEL, we obtained a single-ring version of GroEL bearing cysteine mutations (GroELCys) and modified its 14 apical cysteine residues with merocyanine (MC). Cysteine 99-107 heat shock protein family D (Hsp60) member 1 Homo sapiens 85-90 27545864-4 2016 According to the single-ring mutation of GroEL, we obtained a single-ring version of GroEL bearing cysteine mutations (GroELCys) and modified its 14 apical cysteine residues with merocyanine (MC). Cysteine 156-164 heat shock protein family D (Hsp60) member 1 Homo sapiens 41-46 27545864-4 2016 According to the single-ring mutation of GroEL, we obtained a single-ring version of GroEL bearing cysteine mutations (GroELCys) and modified its 14 apical cysteine residues with merocyanine (MC). Cysteine 156-164 heat shock protein family D (Hsp60) member 1 Homo sapiens 85-90 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. Cysteine 164-173 PDI-like 5-2 Arabidopsis thaliana 38-42 27348438-3 2016 The terminal elimination rate from circulation was dependent on the identity of the OND used, and increased circulation time of gadolinium cargo was achieved for linkers bearing electrophilic fragments designed to react with cysteine-34 of circulating serum albumin. Cysteine 225-233 albumin Rattus norvegicus 258-265 27431616-4 2016 The order of reactivity of nucleophiles was: Tu > l-Met > l-Cys > l-His > 5"-GMP. Cysteine 64-69 5'-nucleotidase, cytosolic II Homo sapiens 89-92 27436896-3 2016 We show here that the master regulator of amino acid homeostasis, activating transcription factor 4 (ATF4), is dysfunctional in HD because of oxidative stress contributed by aberrant cysteine biosynthesis and transport. Cysteine 183-191 activating transcription factor 4 Homo sapiens 66-99 27436896-3 2016 We show here that the master regulator of amino acid homeostasis, activating transcription factor 4 (ATF4), is dysfunctional in HD because of oxidative stress contributed by aberrant cysteine biosynthesis and transport. Cysteine 183-191 activating transcription factor 4 Homo sapiens 101-105 27334685-6 2016 Among the candidate genes, we could find the genes encoding cysteine-rich secretory proteins (CRISP1, CRISP2 and CRISP3). Cysteine 60-68 cysteine rich secretory protein 1 Equus caballus 94-100 27035752-2 2016 Endogenous H2S is synthesized from l-cysteine via cystathionine beta-synthase and cystathionine gamma-lyase and it regulates multiple signaling pathways in mammalian cells. Cysteine 35-45 cystathionine gamma-lyase Homo sapiens 82-107 27482366-5 2016 UbFluor is a mechanism-based probe that undergoes a direct transthiolation reaction with the catalytic cysteine of the model HECT E3 ligase Rsp5, producing the catalytically active Rsp5~Ub (~ indicates thioester) accompanied by release of Fluor-SH. Cysteine 103-111 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 140-144 27482366-5 2016 UbFluor is a mechanism-based probe that undergoes a direct transthiolation reaction with the catalytic cysteine of the model HECT E3 ligase Rsp5, producing the catalytically active Rsp5~Ub (~ indicates thioester) accompanied by release of Fluor-SH. Cysteine 103-111 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 181-185 27030509-15 2016 TRPA1 activation by limonene was abolished in H2 O2 -insensitive cysteine-mutated channels. Cysteine 65-73 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 0-5 27148767-7 2016 These include both reversible and irreversible inhibitors of the kinase, most of which target the cysteine-481 residue of BTK. Cysteine 98-106 Bruton tyrosine kinase Homo sapiens 122-125 27445102-5 2016 Western blotting results showed that alpha4 and beta2 subunits were cross-linked when the agonist-bound receptor encountered H2O2, which could be prevented by the substitution of the conserved cysteine in the M1-M2 linker to an alanine. Cysteine 193-201 immunoglobulin binding protein 1 Homo sapiens 37-43 27180293-1 2016 In this research, keratin was extracted from the disposable chicken feather using l-cysteine as reducing agent. Cysteine 82-92 keratin Gallus gallus 18-25 30090430-5 2016 Results suggest that this cysteine-induced hormesis effect is concentration-dependent; the concentration that make sulfuration rate (ns/nAg) of 6.15 shows strong excitation to cells. Cysteine 26-34 NBAS subunit of NRZ tethering complex Homo sapiens 136-139 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. Cysteine 176-179 chymotrypsin C Homo sapiens 48-52 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. Cysteine 184-187 chymotrypsin C Homo sapiens 48-52 27081212-1 2016 Thioredoxin (Trx) is a ubiquitous oxidoreductase maintaining protein-bound cysteine residues in the reduced thiol state. Cysteine 75-83 oxidoreductase Escherichia coli 34-48 27055119-5 2016 Disease-causing symptoms mainly go back to the lack of sulfite oxidase (SO) activity, an enzyme in cysteine catabolism. Cysteine 99-107 sulfite oxidase Homo sapiens 55-70 27055119-5 2016 Disease-causing symptoms mainly go back to the lack of sulfite oxidase (SO) activity, an enzyme in cysteine catabolism. Cysteine 99-107 sulfite oxidase Homo sapiens 72-74 26921254-3 2016 Supplementation withL-cys up-regulated occludin and claudin-1 expression, reduced caspase-3 activity and enhanced proliferating cell nuclear antigen expression of jejunum and ileum relative to LPS group. Cysteine 21-25 claudin 1 Homo sapiens 52-61 26745957-0 2016 Effect of Cysteamine on Mutant ASL Proteins with Cysteine for Arginine Substitutions. Cysteine 49-57 argininosuccinate lyase Homo sapiens 31-34 26609561-0 2016 Cysteines 208 and 241 in Ero1alpha are required for maximal catalytic turnover. Cysteine 0-9 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 25-34 26609561-2 2016 Besides four catalytic cysteines (Cys(94), Cys(99), Cys(394), Cys(397)), Ero1alpha harbors four regulatory cysteines (Cys(104), Cys(131), Cys(208), Cys(241)). Cysteine 107-116 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 73-82 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. Cysteine 171-180 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 37-46 26609561-6 2016 Specifically, mutation of Cys(208)/Cys(241) does not mechanistically mimic reductive stimulation, as it lowers the turnover rate of Ero1alpha in presence of a reducing agent. Cysteine 26-29 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 132-141 26609561-6 2016 Specifically, mutation of Cys(208)/Cys(241) does not mechanistically mimic reductive stimulation, as it lowers the turnover rate of Ero1alpha in presence of a reducing agent. Cysteine 35-38 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 132-141 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. Cysteine 80-83 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. Cysteine 80-83 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. Cysteine 89-92 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. Cysteine 89-92 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. Cysteine 89-92 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. Cysteine 89-92 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. Cysteine 89-92 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. Cysteine 89-92 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 242-251 27386166-5 2016 In addition to chaperones, also members of the thioredoxin superfamily can influence the folding of proteins by regulation of cysteine reduction/oxidation. Cysteine 126-134 Thioredoxin Caenorhabditis elegans 47-58 26919094-6 2016 A computer-assistant docking showed that B19 may bind TrxR1 protein via formation of a covalent bond with the residue Cys-498. Cysteine 118-121 thioredoxin reductase 1 Homo sapiens 54-59 26845511-10 2016 Two cysteine adducts (CA-1 and CA-2) derived from 10-DMC were found in proteolytically digested microsomal protein samples after incubation with colchicine. Cysteine 4-12 carbonic anhydrase 1 Homo sapiens 22-35 26823467-8 2016 H2O2 inhibited Panx1 function temporarily by formation of disulfide bonds at the thiol group of its terminal cysteine. Cysteine 109-117 pannexin 1 Homo sapiens 15-20 26929335-2 2016 The proposed catalytic mechanism of DNMT1 involves nucleophilic attack of Cys(1226) to cytosine (Cyt) C6, methyl transfer from S-adenosyl-l-methionine (SAM) to Cyt C5, and proton abstraction from C5 to form methylated CpG in DNA. Cysteine 74-77 DNA methyltransferase 1 Homo sapiens 36-41 26929335-5 2016 Methyl transfer occurs after Cys(1226) attack to Cyt C6, and the methyl transfer step is chemically rate-limiting for DNMT1. Cysteine 29-32 DNA methyltransferase 1 Homo sapiens 118-123 27014067-9 2016 Additionally, the peptide-chemical complexes for Cor1-C420-cinnamaldehyde and cysteine-containing heptapeptide-2, 4-dinitrochlorobenzene were partially reversible during 3-days of autosampler storage. Cysteine 78-86 synaptonemal complex protein 3 Homo sapiens 49-53 26840563-10 2016 Affinity blot of BIAM-labeled, immunoprecipitated HSP60 and PDI verified that HGF can decrease the cysteine (-SH) containing HSP60 and PDI. Cysteine 99-107 heat shock protein family D (Hsp60) member 1 Homo sapiens 50-55 26840563-10 2016 Affinity blot of BIAM-labeled, immunoprecipitated HSP60 and PDI verified that HGF can decrease the cysteine (-SH) containing HSP60 and PDI. Cysteine 99-107 heat shock protein family D (Hsp60) member 1 Homo sapiens 125-130 26840563-11 2016 On the other hand, HGF and TPA increased cysteinyl glutathione-containing HSP60, consistent with the decrease of cysteine (-SH)-containing HSP60. Cysteine 113-121 heat shock protein family D (Hsp60) member 1 Homo sapiens 139-144 26840563-12 2016 Moreover, depletion of HSP60 and PDI or expression of dominant negative mutant of HSP60 with alteration of Cys, effectively prevented HGF-induced ERK phosphorylation and HepG2 migration.In conclusion, the redox sensitive HSP60 and PDI are required for HGF-induced ROS signaling and potential targets for preventing HCC progressions. Cysteine 107-110 heat shock protein family D (Hsp60) member 1 Homo sapiens 82-87 26840563-12 2016 Moreover, depletion of HSP60 and PDI or expression of dominant negative mutant of HSP60 with alteration of Cys, effectively prevented HGF-induced ERK phosphorylation and HepG2 migration.In conclusion, the redox sensitive HSP60 and PDI are required for HGF-induced ROS signaling and potential targets for preventing HCC progressions. Cysteine 107-110 heat shock protein family D (Hsp60) member 1 Homo sapiens 82-87 26740626-0 2016 Use of Cysteine Trapping to Map Spatial Approximations between Residues Contributing to the Helix N-capping Motif of Secretin and Distinct Residues within Each of the Extracellular Loops of Its Receptor. Cysteine 7-15 secretin Homo sapiens 117-125 26740626-3 2016 We used cysteine trapping to systematically explore spatial approximations between cysteines replacing each residue in this motif of secretin (sec), Phe(6), Thr(7), and Leu(10), and cysteines incorporated into the extracellular face of the receptor. Cysteine 8-16 secretin Homo sapiens 133-141 26740626-3 2016 We used cysteine trapping to systematically explore spatial approximations between cysteines replacing each residue in this motif of secretin (sec), Phe(6), Thr(7), and Leu(10), and cysteines incorporated into the extracellular face of the receptor. Cysteine 83-92 secretin Homo sapiens 133-141 26481005-1 2016 The cysteine dioxygenase (Cdo1)-null and the cysteine sulfinic acid decarboxylase (Csad)-null mouse are not able to synthesize hypotaurine/taurine by the cysteine/cysteine sulfinate pathway and have very low tissue taurine levels. Cysteine 4-12 cysteine dioxygenase 1, cytosolic Mus musculus 26-30 26699903-1 2016 SCUBE1 (S1), a secreted and membrane-bound glycoprotein, has a modular protein structure composed of an N-terminal signal peptide sequence followed by nine epidermal growth factor (EGF)-like repeats, a spacer region and three cysteine-rich (CR) motifs with multiple potential N-linked glycosylation sites, and one CUB domain at the C-terminus. Cysteine 226-234 signal peptide, CUB domain, EGF-like 1 Danio rerio 0-6 29899936-4 2016 Moreover, if we introduce cystathionine gamma-lyase (CSE), a specific enzyme converting cysteine into H2S, onto the vesicle membrane, the polymersomes can extend their responsive scope from H2S to a specific amino acid bioactivator. Cysteine 88-96 cystathionine gamma-lyase Homo sapiens 26-51 29899936-4 2016 Moreover, if we introduce cystathionine gamma-lyase (CSE), a specific enzyme converting cysteine into H2S, onto the vesicle membrane, the polymersomes can extend their responsive scope from H2S to a specific amino acid bioactivator. Cysteine 88-96 cystathionine gamma-lyase Homo sapiens 53-56 26671999-1 2016 We previously defined that the mitochondria-localized PKCdelta signaling complex stimulates the conversion of pyruvate to acetyl-coenzyme A by the pyruvate dehydrogenase complex. Cysteine 122-128 protein kinase C, delta Mus musculus 54-62 26992682-8 2016 Transfection of CBS and CSE siRNA reversed the stimulatory effect of l-cysteine on VEGF production in placental cells. Cysteine 69-79 cystathionine gamma-lyase Homo sapiens 24-27 26894959-4 2016 Moreover, we found that (55)Cys helps to determine the influence of beta2 on Nav1.2 toxin susceptibility. Cysteine 28-31 sodium voltage-gated channel alpha subunit 2 Homo sapiens 77-83 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. Cysteine 76-79 sodium voltage-gated channel alpha subunit 2 Homo sapiens 124-130 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. Cysteine 113-116 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. Cysteine 103-106 sodium voltage-gated channel alpha subunit 2 Homo sapiens 87-93 26506232-4 2016 Wild-type E6AP promoted proteasome dependent degradation of MNT, while catalytically inactive E6AP having cysteine replaced with alanine at amino-acid 843 position (E6APC843A) rather stabilized it. Cysteine 106-114 ubiquitin protein ligase E3A Homo sapiens 94-98 26903865-7 2016 TRP subtype-targeted pharmacological blockers and siRNAs strategy revealed that suppression of either TRPV1, TRPC1, TRPM2, or TRPM7 reduced APAP-induced ROS formation, Ca(2+) influx, and cell death; the effects of suppression of TRPV1 or TRPC1, known to be activated by oxidative cysteine modifications, were stronger than those of TRPM2 or TRPM7. Cysteine 280-288 transient receptor potential cation channel subfamily C member 1 Homo sapiens 109-114 26903865-7 2016 TRP subtype-targeted pharmacological blockers and siRNAs strategy revealed that suppression of either TRPV1, TRPC1, TRPM2, or TRPM7 reduced APAP-induced ROS formation, Ca(2+) influx, and cell death; the effects of suppression of TRPV1 or TRPC1, known to be activated by oxidative cysteine modifications, were stronger than those of TRPM2 or TRPM7. Cysteine 280-288 transient receptor potential cation channel subfamily M member 2 Homo sapiens 116-121 26903865-7 2016 TRP subtype-targeted pharmacological blockers and siRNAs strategy revealed that suppression of either TRPV1, TRPC1, TRPM2, or TRPM7 reduced APAP-induced ROS formation, Ca(2+) influx, and cell death; the effects of suppression of TRPV1 or TRPC1, known to be activated by oxidative cysteine modifications, were stronger than those of TRPM2 or TRPM7. Cysteine 280-288 transient receptor potential cation channel subfamily M member 7 Homo sapiens 126-131 26903865-8 2016 Interestingly, TRPV1 and TRPC1 were labeled by the cysteine-selective modification reagent, 5,5"-dithiobis (2-nitrobenzoic acid)-2biotin (DTNB-2Bio), and this was attenuated by pretreatment with APAP, suggesting that APAP and/or its oxidized metabolites act directly on the modification target cysteine residues of TRPV1 and TRPC1 proteins. Cysteine 51-59 transient receptor potential cation channel subfamily C member 1 Homo sapiens 25-30 26903865-8 2016 Interestingly, TRPV1 and TRPC1 were labeled by the cysteine-selective modification reagent, 5,5"-dithiobis (2-nitrobenzoic acid)-2biotin (DTNB-2Bio), and this was attenuated by pretreatment with APAP, suggesting that APAP and/or its oxidized metabolites act directly on the modification target cysteine residues of TRPV1 and TRPC1 proteins. Cysteine 51-59 transient receptor potential cation channel subfamily C member 1 Homo sapiens 325-330 26903865-8 2016 Interestingly, TRPV1 and TRPC1 were labeled by the cysteine-selective modification reagent, 5,5"-dithiobis (2-nitrobenzoic acid)-2biotin (DTNB-2Bio), and this was attenuated by pretreatment with APAP, suggesting that APAP and/or its oxidized metabolites act directly on the modification target cysteine residues of TRPV1 and TRPC1 proteins. Cysteine 294-302 transient receptor potential cation channel subfamily C member 1 Homo sapiens 25-30 26629855-2 2016 For example, targeting cysteine residues in the ATP-binding pockets of kinases with thiol-reactive molecules has afforded increased selectivity and potency to drugs like imbrutinib, which inhibits the oncogene BTK, and CO-1686 and AZD9291 that target oncogenic mutant EGFR. Cysteine 23-31 Bruton tyrosine kinase Homo sapiens 210-213 26690702-6 2016 Molecular analysis revealed that the extracellular Kringle domain is required for ROR1/ROR2 heterooligomerization and the cysteine-rich domain or intracellular proline-rich domain is required for Wnt5a-induced recruitment of GEFs to ROR1/ROR2. Cysteine 122-130 wingless-type MMTV integration site family, member 5A Mus musculus 196-201 26685111-4 2016 In this study, we developed an algorithm (named HAL-Cy) which blends previous work with novel implementations to identify reactive Cys from nonreactive. Cysteine 131-134 histidine ammonia-lyase Homo sapiens 48-51 26685111-7 2016 We implemented our algorithm in a web service (Cy-preds), the ultimate product of our work; we provided it with a variety of additional features, tools, and options: Cy-preds is capable of performing fully automated calculations for a thorough analysis of Cys reactivity in proteins, ranging from reactivity predictions (e.g., with HAL-Cy) to functional characterization. Cysteine 256-259 histidine ammonia-lyase Homo sapiens 332-335 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. Cysteine 146-154 Thy-1 cell surface antigen Sus scrofa 4-8 26551598-9 2016 Finally NO-dependent arginase-2 induction was prevented by pre-incubation for 10 min with the cysteine blocker MMTS (10 mM). Cysteine 94-102 arginase 2 Homo sapiens 21-31 26503968-7 2016 Inhibition was mediated by the Dkk-3 C-terminal cysteine-rich domain (Cys2), which also inhibited TGF-beta-induced expression of MMP9 and MMP13. Cysteine 48-56 matrix metallopeptidase 9 Homo sapiens 129-133 26567752-5 2016 N-acetyl-l-cysteine (NAC) acts as a precursor for the substrate cysteine in synthesis of GSH and also as a mucolytic and anti-inflammatory agent. Cysteine 11-19 X-linked Kx blood group Homo sapiens 21-24 26719270-6 2015 Interestingly, two of the isolates, named AII and BV2, have a pair of cysteines located within the randomized region of 11 amino acids similar to that identified within the CP Env, an isolate identified in a previous Env library screen on the human renal carcinoma Caki-1 cell line. Cysteine 70-79 endogenous retrovirus group K member 20 Homo sapiens 176-179 26719270-6 2015 Interestingly, two of the isolates, named AII and BV2, have a pair of cysteines located within the randomized region of 11 amino acids similar to that identified within the CP Env, an isolate identified in a previous Env library screen on the human renal carcinoma Caki-1 cell line. Cysteine 70-79 endogenous retrovirus group K member 20 Homo sapiens 217-220 26701913-2 2015 Only two enzymes - the acyl-protein thioesterases APT1 and APT2 - are known to catalyze palmitate removal from cytosolic cysteine residues. Cysteine 121-129 lysophospholipase 1 Homo sapiens 50-54 26701913-2 2015 Only two enzymes - the acyl-protein thioesterases APT1 and APT2 - are known to catalyze palmitate removal from cytosolic cysteine residues. Cysteine 121-129 lysophospholipase 2 Homo sapiens 59-63 26644582-6 2015 Aph2-mediated palmitoylation of phospholamban on cysteine 36 differentially alters its interaction with PKA and protein phosphatase 1 alpha, augmenting serine 16 phosphorylation, and regulates phospholamban pentamer formation. Cysteine 49-57 zinc finger, DHHC domain containing 16 Mus musculus 0-4 26398879-6 2015 The identified inhibitors are highly potent (IC50(app) = 63 nM), nontoxic at concentrations up to 100 muM, and appear to preferentially target a specific cysteine residue within IDE. Cysteine 154-162 insulin degrading enzyme Homo sapiens 178-181 26492990-0 2015 Cysteine is not a substrate but a specific modulator of human ASCT2 (SLC1A5) transporter. Cysteine 0-8 solute carrier family 1 member 5 Homo sapiens 62-67 26492990-0 2015 Cysteine is not a substrate but a specific modulator of human ASCT2 (SLC1A5) transporter. Cysteine 0-8 solute carrier family 1 member 5 Homo sapiens 69-75 26492990-3 2015 In the present work, the interaction of the putative substrate Cys with the human ASCT2 has been studied using the recombinant hASCT2 over-produced in Pichia pastoris and the native ASCT2 extracted from HeLa in both proteoliposomes and intact cells. Cysteine 63-66 solute carrier family 1 member 5 Homo sapiens 82-87 26492990-3 2015 In the present work, the interaction of the putative substrate Cys with the human ASCT2 has been studied using the recombinant hASCT2 over-produced in Pichia pastoris and the native ASCT2 extracted from HeLa in both proteoliposomes and intact cells. Cysteine 63-66 solute carrier family 1 member 5 Homo sapiens 127-133 26492990-3 2015 In the present work, the interaction of the putative substrate Cys with the human ASCT2 has been studied using the recombinant hASCT2 over-produced in Pichia pastoris and the native ASCT2 extracted from HeLa in both proteoliposomes and intact cells. Cysteine 63-66 solute carrier family 1 member 5 Homo sapiens 128-133 26492990-4 2015 It was found that Cys is a potent competitive inhibitor of hASCT2 but is not a substrate. Cysteine 18-21 solute carrier family 1 member 5 Homo sapiens 59-65 26359516-1 2015 The formation of intramolecular triplex DNA can be regulated by Ag(+) and Cys (cysteine), which switch off/on the fluorescence of the oligonucleotides, 5"-TAMRA-TTC TCT TCC TCT TCC TTC TGA CGA CAG TTG ACT CTT CCT TCT CCT TCT CTT-BHQ-2-3" (Oligo 1) and 3"-GAA GGA AGA GGA AGA GAA-5" (Oligo 2). Cysteine 79-87 CCT Homo sapiens 209-212 26527616-0 2016 Characterizations of Three Major Cysteine Sensors of Keap1 in Stress Response. Cysteine 33-41 kelch-like ECH-associated protein 1 Mus musculus 53-58 26527616-2 2016 Although Cys151, Cys273, and Cys288 of Keap1 are major sensor cysteine residues for detecting these stresses, it has not been technically feasible to evaluate the functionality of Cys273 or Cys288, since Keap1 mutants that harbor substitutions in these residues and maintain the ability to repress Nrf2 accumulation do not exist. Cysteine 62-70 kelch-like ECH-associated protein 1 Mus musculus 39-44 26527616-8 2016 This study thus demonstrates that Keap1 utilizes multiple cysteine residues specifically and/or collaboratively as sensors for the detection of a wide range of environmental stresses. Cysteine 58-66 kelch-like ECH-associated protein 1 Mus musculus 34-39 26081982-7 2015 Both CN1 cysteine residues were nitrosylated, the cysteine at position 102 but not at position 229 regulated CN1 activities. Cysteine 50-58 carnosine dipeptidase 1 (metallopeptidase M20 family) Mus musculus 109-112 26160850-0 2015 A Cys-Gly-Cys triad in the dehydrogenase region of Nox2 plays a key role in the interaction with p67phox. Cysteine 2-5 cytochrome b-245 beta chain Homo sapiens 51-55 26160850-0 2015 A Cys-Gly-Cys triad in the dehydrogenase region of Nox2 plays a key role in the interaction with p67phox. Cysteine 10-13 cytochrome b-245 beta chain Homo sapiens 51-55 26160850-7 2015 Our results reveal an essential role for the Cys-Gly-Cys triad in Nox2 in binding p67(phox), seconded by an additional binding region, comprising residues C terminal to Cys-Gly-Cys. Cysteine 45-48 cytochrome b-245 beta chain Homo sapiens 66-70 26160850-7 2015 Our results reveal an essential role for the Cys-Gly-Cys triad in Nox2 in binding p67(phox), seconded by an additional binding region, comprising residues C terminal to Cys-Gly-Cys. Cysteine 53-56 cytochrome b-245 beta chain Homo sapiens 66-70 32264585-0 2015 Enantiomers of cysteine-modified SeNPs (d/lSeNPs) as inhibitors of metal-induced Abeta aggregation in Alzheimer"s disease. Cysteine 15-23 amyloid beta precursor protein Rattus norvegicus 81-86 32264585-2 2015 Here we use cysteine enantiomer-modified SeNPs (abbreviated as d/lSeNPs) to demonstrate that surface chirality strongly influences the formation of Abeta aggregates in the presence of metal ions, such as Zn2+ or Cu2+. Cysteine 12-20 amyloid beta precursor protein Rattus norvegicus 148-153 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. Cysteine 56-65 microseminoprotein beta Homo sapiens 121-124 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. Cysteine 126-135 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. Cysteine 126-135 quiescin sulfhydryl oxidase 1 Homo sapiens 29-33 26246604-5 2015 Here we show that TMX1, one of the few transmembrane members of the family, forms functional complexes with the ER lectin calnexin and preferentially intervenes during maturation of cysteine-containing, membrane-associated proteins while ignoring the same cysteine-containing ectodomains if not anchored at the ER membrane. Cysteine 182-190 thioredoxin related transmembrane protein 1 Homo sapiens 18-22 26246604-5 2015 Here we show that TMX1, one of the few transmembrane members of the family, forms functional complexes with the ER lectin calnexin and preferentially intervenes during maturation of cysteine-containing, membrane-associated proteins while ignoring the same cysteine-containing ectodomains if not anchored at the ER membrane. Cysteine 256-264 thioredoxin related transmembrane protein 1 Homo sapiens 18-22 26385697-2 2015 Under nitrosative stress, an excess of nitric oxide (NO) radical species induced the S-nitrosylation of PDI cysteines which eliminate its isomerase and oxidoreductase capabilities. Cysteine 108-117 thioredoxin reductase 1 Homo sapiens 152-166 26435880-1 2015 BACKGROUND: Recently a profound depletion of cystathionine gamma-lyase (CSE), the principal enzyme involved in the generation of cysteine from cystathionine, was shown in Huntington disease (HD) patients and several transgenic HD mouse models. Cysteine 129-137 cystathionine gamma-lyase Homo sapiens 45-70 26435880-1 2015 BACKGROUND: Recently a profound depletion of cystathionine gamma-lyase (CSE), the principal enzyme involved in the generation of cysteine from cystathionine, was shown in Huntington disease (HD) patients and several transgenic HD mouse models. Cysteine 129-137 cystathionine gamma-lyase Homo sapiens 72-75 26216878-4 2015 However, the role of posttranslational modifications signaled by the hypervariable region carboxyl-terminal tetrapeptide CAAX motif (C = cysteine, A = aliphatic amino acid, X = terminal residue) in Ral isoform-selective functions has not been addressed. Cysteine 137-145 RAS like proto-oncogene A Homo sapiens 198-201 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. Cysteine 33-36 spleen trypsin inhibitor I Bos taurus 129-133 25930007-4 2015 BARD activates Nrf2 via covalent modification of reactive cysteine residues in the Nrf2 repressor molecule, Keap1. Cysteine 58-66 Kelch-like ECH-associated protein 1 Rattus norvegicus 108-113 26006104-5 2015 The N-terminal cysteine residue on S100A9 was highly susceptible to oxidation which resulted in cross-linking of the protein monomers. Cysteine 15-23 S100 calcium binding protein A9 Homo sapiens 35-41 26044846-0 2015 Impact of cysteine variants on the structure, activity, and stability of recombinant human alpha-galactosidase A. Cysteine 10-18 galactosidase alpha Homo sapiens 91-112 26085103-1 2015 A redox-regulated import pathway consisting of Mia40 and Erv1 mediates the import of cysteine-rich proteins into the mitochondrial intermembrane space. Cysteine 85-93 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 47-52 26085103-3 2015 However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation. Cysteine 36-44 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 9-14 26085103-3 2015 However, Mia40 has one redox-active cysteine pair, resulting in ambiguity about how Mia40 accepts numerous electrons during substrate oxidation. Cysteine 36-44 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 84-89 26086102-4 2015 Here, we show that Cys residues in SOD1 are essential to exerting toxicities of SOD1 in a Caenorhabditis elegans model. Cysteine 19-22 Superoxide dismutase [Cu-Zn] Caenorhabditis elegans 35-39 26086102-4 2015 Here, we show that Cys residues in SOD1 are essential to exerting toxicities of SOD1 in a Caenorhabditis elegans model. Cysteine 19-22 Superoxide dismutase [Cu-Zn] Caenorhabditis elegans 80-84 26086102-6 2015 In contrast, little effects of exogenously expressed SOD1 on the motility were observed when all four Cys residues in SOD1 were replaced with Ser. Cysteine 102-105 Superoxide dismutase [Cu-Zn] Caenorhabditis elegans 118-122 26086102-7 2015 Taken together, we propose that deregulation of Cys chemistry in SOD1 proteins is involved in the pathogenesis of SOD1-related ALS. Cysteine 48-51 Superoxide dismutase [Cu-Zn] Caenorhabditis elegans 65-69 26086102-7 2015 Taken together, we propose that deregulation of Cys chemistry in SOD1 proteins is involved in the pathogenesis of SOD1-related ALS. Cysteine 48-51 Superoxide dismutase [Cu-Zn] Caenorhabditis elegans 114-118 26249349-9 2015 On the basis of the initial hits, the design of reactive fragments targeting the hotspot which would be simultaneously covalently linked to a cysteine residue present only in trypanosomatid HisRS was initiated. Cysteine 142-150 histidyl-tRNA synthetase 2, mitochondrial Homo sapiens 190-195 26551704-6 2015 The proximal regulator of Nrf2 is Keap1 (Kelch-like ECH-associated protein-1), a cysteine (Cys)-rich protein that normally interacts transiently with Nrf2, targeting it for degradation. Cysteine 81-89 kelch-like ECH-associated protein 1 Mus musculus 34-39 26551704-6 2015 The proximal regulator of Nrf2 is Keap1 (Kelch-like ECH-associated protein-1), a cysteine (Cys)-rich protein that normally interacts transiently with Nrf2, targeting it for degradation. Cysteine 81-89 kelch-like ECH-associated protein 1 Mus musculus 41-76 26551704-6 2015 The proximal regulator of Nrf2 is Keap1 (Kelch-like ECH-associated protein-1), a cysteine (Cys)-rich protein that normally interacts transiently with Nrf2, targeting it for degradation. Cysteine 91-94 kelch-like ECH-associated protein 1 Mus musculus 34-39 26551704-6 2015 The proximal regulator of Nrf2 is Keap1 (Kelch-like ECH-associated protein-1), a cysteine (Cys)-rich protein that normally interacts transiently with Nrf2, targeting it for degradation. Cysteine 91-94 kelch-like ECH-associated protein 1 Mus musculus 41-76 25748343-8 2015 RESULTS: Cysteine oxidation was present in children with difficult-to-treat asthma and accompanied by increased reactive oxygen species generation and increased CCL3 and CXCL1 mRNA expression. Cysteine 9-17 C-X-C motif chemokine ligand 1 Homo sapiens 170-175 25952734-0 2015 Immuno-PET of Murine T Cell Reconstitution Postadoptive Stem Cell Transplantation Using Anti-CD4 and Anti-CD8 Cys-Diabodies. Cysteine 110-113 CD8a molecule Homo sapiens 106-109 25952734-2 2015 To study whole-body T lymphocyte dynamics noninvasively in vivo, we generated anti-CD4 and -CD8 cys-diabodies (cDbs) derived from the parental antibody hybridomas GK1.5 and 2.43, respectively, for (89)Zr-immuno-PET detection of helper and cytotoxic T cell populations. Cysteine 96-99 CD8a molecule Homo sapiens 92-95 26080424-2 2015 In large part, the reduction of oxidized protein cysteines is mediated by a small 12-kDa thiol oxidoreductase, thioredoxin (Trx). Cysteine 49-58 thioredoxin reductase 1 Homo sapiens 95-109 26080442-9 2015 Moreover, dimerization and signaling of KRas are both dependent on an intact CAAX (C, cysteine; A, aliphatic; X, any amino acid) motif that is also known to mediate membrane localization. Cysteine 86-94 KRAS proto-oncogene, GTPase Homo sapiens 40-44 26024338-2 2015 In this study, we employed substituted cysteine accessibility methodology (SCAM) to screen the entire TM5 defined by the original topology model and its cytoplasmic extension in a Cysless background. Cysteine 39-47 tropomyosin 3 Homo sapiens 102-105 25731082-6 2015 The mutant of the conserved cysteines in b domain, C272/278A, did not form hyLYS, however, showed predominant reductase activity, implying that P5 functioned as a potent sulfhydryl oxidase and a predominant reductase depending on the circumstance around C272/278. Cysteine 28-37 protein disulfide isomerase family A member 6 Homo sapiens 144-146 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. Cysteine 95-104 NADPH-dependent thioredoxin reductase C Arabidopsis thaliana 182-186 25923079-7 2015 The gene expression of hepatic tumour necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) did not differ among amino acids, NanoAg and uninjected controls in the non-LPS groups, but increased by many folds in the LPS treated NanoAg, Cys and Cys+NanoAg groups. Cysteine 240-243 interleukin 6 Gallus gallus 76-89 25923079-7 2015 The gene expression of hepatic tumour necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) did not differ among amino acids, NanoAg and uninjected controls in the non-LPS groups, but increased by many folds in the LPS treated NanoAg, Cys and Cys+NanoAg groups. Cysteine 240-243 interleukin 6 Gallus gallus 91-95 25923079-7 2015 The gene expression of hepatic tumour necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) did not differ among amino acids, NanoAg and uninjected controls in the non-LPS groups, but increased by many folds in the LPS treated NanoAg, Cys and Cys+NanoAg groups. Cysteine 248-251 interleukin 6 Gallus gallus 76-89 25923079-7 2015 The gene expression of hepatic tumour necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) did not differ among amino acids, NanoAg and uninjected controls in the non-LPS groups, but increased by many folds in the LPS treated NanoAg, Cys and Cys+NanoAg groups. Cysteine 248-251 interleukin 6 Gallus gallus 91-95 25769677-3 2015 duIL-17F is predicted to encode 166 amino acids, including a 26-amino acid signal peptide, a single N-linked glycosylation site, and six cysteine residues that are conserved in mammalian IL-17. Cysteine 137-145 interleukin 17A Homo sapiens 2-7 25578648-0 2015 S-nitrosylation of XIAP at Cys 213 of BIR2 domain impairs XIAP"s anti-caspase 3 activity and anti-apoptotic function. Cysteine 27-30 X-linked inhibitor of apoptosis Homo sapiens 19-23 25578648-0 2015 S-nitrosylation of XIAP at Cys 213 of BIR2 domain impairs XIAP"s anti-caspase 3 activity and anti-apoptotic function. Cysteine 27-30 X-linked inhibitor of apoptosis Homo sapiens 58-62 25578648-5 2015 We found that mutations of Cys 90 and Cys 327 affect the normal structure of XIAP. Cysteine 27-30 X-linked inhibitor of apoptosis Homo sapiens 77-81 25578648-5 2015 We found that mutations of Cys 90 and Cys 327 affect the normal structure of XIAP. Cysteine 38-41 X-linked inhibitor of apoptosis Homo sapiens 77-81 25578648-6 2015 More importantly, we found that S-nitrosylation of XIAP Cys 213 impairs the anti-caspase 3 and anti-apoptotic function of XIAP that we observed in our previous study. Cysteine 56-59 X-linked inhibitor of apoptosis Homo sapiens 51-55 25578648-6 2015 More importantly, we found that S-nitrosylation of XIAP Cys 213 impairs the anti-caspase 3 and anti-apoptotic function of XIAP that we observed in our previous study. Cysteine 56-59 X-linked inhibitor of apoptosis Homo sapiens 122-126 25667317-6 2015 We found that S-nitrosylation of APX1 at cysteine (Cys)-32 enhances its enzymatic activity of scavenging hydrogen peroxide, leading to the increased resistance to oxidative stress, whereas a substitution mutation at Cys-32 causes the reduction of ascorbate peroxidase activity and abolishes its responsiveness to the NO-enhanced enzymatic activity. Cysteine 41-49 ascorbate peroxidase 1 Arabidopsis thaliana 33-37 25667317-6 2015 We found that S-nitrosylation of APX1 at cysteine (Cys)-32 enhances its enzymatic activity of scavenging hydrogen peroxide, leading to the increased resistance to oxidative stress, whereas a substitution mutation at Cys-32 causes the reduction of ascorbate peroxidase activity and abolishes its responsiveness to the NO-enhanced enzymatic activity. Cysteine 51-54 ascorbate peroxidase 1 Arabidopsis thaliana 33-37 25667317-6 2015 We found that S-nitrosylation of APX1 at cysteine (Cys)-32 enhances its enzymatic activity of scavenging hydrogen peroxide, leading to the increased resistance to oxidative stress, whereas a substitution mutation at Cys-32 causes the reduction of ascorbate peroxidase activity and abolishes its responsiveness to the NO-enhanced enzymatic activity. Cysteine 216-219 ascorbate peroxidase 1 Arabidopsis thaliana 33-37 25667317-7 2015 Moreover, S-nitrosylation of APX1 at Cys-32 also plays an important role in regulating immune responses. Cysteine 37-40 ascorbate peroxidase 1 Arabidopsis thaliana 29-33 25789822-1 2015 A novel annexin V derivative (Cys-Annexin V) with a single cysteine residue at its C-terminal has been developed and successfully labeled site-specifically with 18F-FBEM. Cysteine 30-33 annexin A5 Rattus norvegicus 8-17 25789822-1 2015 A novel annexin V derivative (Cys-Annexin V) with a single cysteine residue at its C-terminal has been developed and successfully labeled site-specifically with 18F-FBEM. Cysteine 30-33 annexin A5 Rattus norvegicus 34-43 25789822-1 2015 A novel annexin V derivative (Cys-Annexin V) with a single cysteine residue at its C-terminal has been developed and successfully labeled site-specifically with 18F-FBEM. Cysteine 59-67 annexin A5 Rattus norvegicus 8-17 25789822-1 2015 A novel annexin V derivative (Cys-Annexin V) with a single cysteine residue at its C-terminal has been developed and successfully labeled site-specifically with 18F-FBEM. Cysteine 59-67 annexin A5 Rattus norvegicus 34-43 25789822-6 2015 Like the 1st generation 18F-SFB-Annexin V, the novel 18F-FBEM-Cys-Annexin V mainly shows renal and to a lesser extent, hepatobiliary excretion in normal mice. Cysteine 62-65 annexin A5 Mus musculus 66-75 25789822-9 2015 as measured via microPET correlated with the ratio of apoptotic nuclei in liver observed using TUNEL histochemistry, indicating that the novel 18F-FBEM-Cys-Annexin V is a potential apoptosis imaging agent. Cysteine 152-155 annexin A5 Rattus norvegicus 156-165 25567809-6 2015 The inhibitory effects of l-cysteine, but not NaHS, were blocked upon suppression of CSE expression by siRNA or inhibition of its activity by dl-propargylglycine (PPG) suggesting that the effect of l-cysteine is mediated via activation of CSE. Cysteine 26-36 cystathionine gamma-lyase Oryctolagus cuniculus 85-88 25567809-6 2015 The inhibitory effects of l-cysteine, but not NaHS, were blocked upon suppression of CSE expression by siRNA or inhibition of its activity by dl-propargylglycine (PPG) suggesting that the effect of l-cysteine is mediated via activation of CSE. Cysteine 26-36 cystathionine gamma-lyase Oryctolagus cuniculus 239-242 24681947-3 2015 Under basal conditions, cell surface CDCP1 constitutively internalizes and undergoes palmitoylation-dependent degradation by a mechanism in which it is palmitoylated in at least one of its four cytoplasmic cysteines. Cysteine 206-215 CUB domain containing protein 1 Homo sapiens 37-42 25593320-3 2015 Here we describe a novel ITK/RLK inhibitor, PRN694, which covalently binds to cysteine residues 442 of ITK and 350 of RLK and blocks kinase activity. Cysteine 78-86 TXK tyrosine kinase Homo sapiens 29-32 25593320-3 2015 Here we describe a novel ITK/RLK inhibitor, PRN694, which covalently binds to cysteine residues 442 of ITK and 350 of RLK and blocks kinase activity. Cysteine 78-86 TXK tyrosine kinase Homo sapiens 118-121 28706640-2 2015 Here we report the discovery that C-terminal ubiquitin thioesters can undergo direct transthiolation with the catalytic cysteine of the model HECT E3 ubiquitin ligase Rsp5 to form a catalytically active Rsp5~ubiquitin thioester (Rsp5~Ub). Cysteine 120-128 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 167-171 28706640-2 2015 Here we report the discovery that C-terminal ubiquitin thioesters can undergo direct transthiolation with the catalytic cysteine of the model HECT E3 ubiquitin ligase Rsp5 to form a catalytically active Rsp5~ubiquitin thioester (Rsp5~Ub). Cysteine 120-128 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 203-207 28706640-2 2015 Here we report the discovery that C-terminal ubiquitin thioesters can undergo direct transthiolation with the catalytic cysteine of the model HECT E3 ubiquitin ligase Rsp5 to form a catalytically active Rsp5~ubiquitin thioester (Rsp5~Ub). Cysteine 120-128 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 203-207 25632004-1 2015 WC1 proteins, which are specifically expressed by bovine gammadelta T cells from a gene array containing 13 members, are part of the scavenger receptor cysteine-rich family. Cysteine 152-160 uncharacterized protein LOC751809 Bos taurus 0-3 25468652-3 2015 A change in the codon 118 of the wild-type alpha-Gal sequence, replacing basic arginine by a potentially sulfhydryl-binding cysteine residue - GLA p.(Arg118Cys) -, has been recurrently described in large FD screening studies of high-risk patients. Cysteine 124-132 galactosidase alpha Homo sapiens 43-52 25468652-3 2015 A change in the codon 118 of the wild-type alpha-Gal sequence, replacing basic arginine by a potentially sulfhydryl-binding cysteine residue - GLA p.(Arg118Cys) -, has been recurrently described in large FD screening studies of high-risk patients. Cysteine 124-132 galactosidase alpha Homo sapiens 143-146 25511704-3 2015 GR AF-1 activity is mostly confined to a short unstructured domain called tau1c (amino acids 187-244) that contains three phosphorylation sites and binds a short cysteine rich fragment (CH3) of the coactivator CREB binding protein (CBP). Cysteine 162-170 interferon gamma receptor 2 Homo sapiens 3-7 25606676-2 2015 TDI is known to arise because of five different mutations, all involving the substitution of an amino acid with a cysteine in fibroblast growth factor receptor 3 (FGFR3). Cysteine 114-122 fibroblast growth factor receptor 3 Homo sapiens 126-161 25606676-2 2015 TDI is known to arise because of five different mutations, all involving the substitution of an amino acid with a cysteine in fibroblast growth factor receptor 3 (FGFR3). Cysteine 114-122 fibroblast growth factor receptor 3 Homo sapiens 163-168 25973333-1 2015 [(68)Ga]-DO3A-VS-Cys(40)-Exendin-4 has been shown to be a promising imaging candidate for targeting glucagon like peptide-1 receptor (GLP-1R). Cysteine 17-20 glucagon-like peptide 1 receptor Rattus norvegicus 100-132 25973333-1 2015 [(68)Ga]-DO3A-VS-Cys(40)-Exendin-4 has been shown to be a promising imaging candidate for targeting glucagon like peptide-1 receptor (GLP-1R). Cysteine 17-20 glucagon-like peptide 1 receptor Rattus norvegicus 134-140 25581026-6 2015 Mutagenesis experiments identify cysteine 24 as the catalytic cysteine residue in CLIC1, which is consistent with its structure. Cysteine 33-41 chloride intracellular channel 1 Homo sapiens 82-87 25581026-6 2015 Mutagenesis experiments identify cysteine 24 as the catalytic cysteine residue in CLIC1, which is consistent with its structure. Cysteine 62-70 chloride intracellular channel 1 Homo sapiens 82-87 25444856-5 2015 Spectroscopic analyses revealed that Bach2(331-520) is the heme-binding domain, as it includes three Cys-Pro motifs known to be important for heme binding. Cysteine 101-104 BTB domain and CNC homolog 2 Homo sapiens 37-42 25444857-1 2015 Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA). Cysteine 114-124 cysteine dioxygenase 1, cytosolic Mus musculus 0-20 25444857-1 2015 Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA). Cysteine 114-124 cysteine dioxygenase 1, cytosolic Mus musculus 22-25 25444857-1 2015 Cysteine dioxygenase (CDO) is a non-heme mononuclear iron enzyme that catalyzes the oxygen-dependent oxidation of L-cysteine (Cys) to produce L-cysteine sulfinic acid (CSA). Cysteine 0-3 cysteine dioxygenase 1, cytosolic Mus musculus 22-25 25287889-0 2015 Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding. Cysteine 50-58 zeta chain of T cell receptor associated protein kinase 70 Homo sapiens 97-103 25287889-0 2015 Modification by covalent reaction or oxidation of cysteine residues in the tandem-SH2 domains of ZAP-70 and Syk can block phosphopeptide binding. Cysteine 50-58 spleen associated tyrosine kinase Homo sapiens 108-111 25283348-4 2015 Furthermore, the redox status of cysteine and methionine residues regulated RUNX2 DNA-binding and reversal of oxidative inhibition was consistent with an endogenous Methionine sulfoxide reductase-A (MsrA) activity. Cysteine 33-41 methionine sulfoxide reductase A Homo sapiens 165-197 25283348-4 2015 Furthermore, the redox status of cysteine and methionine residues regulated RUNX2 DNA-binding and reversal of oxidative inhibition was consistent with an endogenous Methionine sulfoxide reductase-A (MsrA) activity. Cysteine 33-41 methionine sulfoxide reductase A Homo sapiens 199-203 25677088-6 2015 Rac1 activity has recently been shown to be modulated by glutathiolation or S-nitrosation via an active site cysteine residue. Cysteine 109-117 Rac family small GTPase 1 Homo sapiens 0-4 25517874-7 2014 HOCl-mediated N-chlorination thus is a cysteine-independent post-translational modification that reversibly turns RidA into an effective chaperone holdase, which plays a crucial role in the protection of cytosolic proteins during oxidative stress. Cysteine 39-47 reactive intermediate imine deaminase A homolog Homo sapiens 114-118 25361011-5 2014 In clonogenic proliferation assays, Huh7-X cells produced a significant number of colonies whereas Huh7-Cys- cells failed to generate them. Cysteine 104-107 MIR7-3 host gene Homo sapiens 99-103 25450419-2 2014 A prior synaptic membrane binding assay suggests that L-cysteine has a strong affinity for the L-2-amino-4-phosphonobutyric acid (L-AP4) binding site. Cysteine 54-64 replication initiator 1 Rattus norvegicus 132-135 25450419-3 2014 The central action of L-cysteine may be vial-AP4 sensitive receptors. Cysteine 22-32 replication initiator 1 Rattus norvegicus 45-48 25450419-7 2014 In contrast, either receptor blockade alone abolished the response to L-AP4, indicating distinct mechanisms between responses to L-cysteine and L-AP4 in the CVLM. Cysteine 129-139 replication initiator 1 Rattus norvegicus 72-75 25450419-9 2014 Central L-cysteine"s action could be independent of the L-AP4 sensitive receptors. Cysteine 8-18 replication initiator 1 Rattus norvegicus 58-61 25039358-4 2014 EXPERIMENTAL APPROACH: Four cysteine-modified GLP-1 analogues (1-4) were prepared using Gly8 -GLP-1(7-36)-NH2 peptide as a starting point. Cysteine 28-36 glucagon Rattus norvegicus 46-51 25039358-4 2014 EXPERIMENTAL APPROACH: Four cysteine-modified GLP-1 analogues (1-4) were prepared using Gly8 -GLP-1(7-36)-NH2 peptide as a starting point. Cysteine 28-36 glucagon Rattus norvegicus 94-99 25039358-11 2014 CONCLUSIONS AND IMPLICATIONS: Cysteine-specific coumarin conjugation with GLP-1 offers a useful approach to the development of long-acting incretin-based antidiabetic agents. Cysteine 30-38 glucagon Rattus norvegicus 74-79 25385787-6 2014 We introduced cysteine mutations into the S4 transmembrane segment of the KCNQ2 VSD and determined that external application of Cd(2+) profoundly reduced the current amplitude of S4 cysteine mutants S195C, R198C, and R201C. Cysteine 14-22 potassium voltage-gated channel subfamily Q member 2 Homo sapiens 74-79 25385787-6 2014 We introduced cysteine mutations into the S4 transmembrane segment of the KCNQ2 VSD and determined that external application of Cd(2+) profoundly reduced the current amplitude of S4 cysteine mutants S195C, R198C, and R201C. Cysteine 182-190 potassium voltage-gated channel subfamily Q member 2 Homo sapiens 74-79 25070180-2 2014 Enhanced ErbB2 signaling induces cysteine cathepsin B and L expression leading to their higher proteolytic activity (zFRase activity), which is crucial for the invasion of ErbB2-positive breast cancer cells in vitro. Cysteine 33-41 cathepsin B Homo sapiens 42-53 25505619-9 2014 These effects were prevented by the TRPA1 antagonist HC-030031, and were dependent on the presence of Cys621, Cys 641, and Cys 665 in hTRPA1. Cysteine 102-105 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 36-41 25505619-9 2014 These effects were prevented by the TRPA1 antagonist HC-030031, and were dependent on the presence of Cys621, Cys 641, and Cys 665 in hTRPA1. Cysteine 110-113 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 36-41 24896355-2 2014 Cystathionine gamma-lyase (CSE) is one major H2S-producing enzyme with L-cysteine as the main substrate in mammalian cells. Cysteine 71-81 cystathionine gamma-lyase Homo sapiens 0-25 24896355-2 2014 Cystathionine gamma-lyase (CSE) is one major H2S-producing enzyme with L-cysteine as the main substrate in mammalian cells. Cysteine 71-81 cystathionine gamma-lyase Homo sapiens 27-30 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. Cysteine 163-171 cathepsin B Homo sapiens 175-179 24661219-9 2014 NADPH-reduced TrxR1 was significantly more sensitive to NAPQI (IC50 = 0.023 muM) than the oxidized enzyme (IC50 = 1.0 muM) or a human TrxR1 Sec498Cys mutant enzyme (IC50 = 17 muM), indicating that cysteine and selenocysteine residues in the redox motifs of TrxR are critical for enzyme inactivation. Cysteine 197-205 thioredoxin reductase 1 Homo sapiens 14-19 24557597-5 2014 Upregulation of both GCLC and GLCM mRNA levels in response to cysteine deprivation was dependent on new protein synthesis, which is consistent with expression of GCLC and GCLM being mediated by proteins whose synthesis depends on activation of the GCN2/ATF4 pathway. Cysteine 62-70 eukaryotic translation initiation factor 2 alpha kinase 4 Homo sapiens 248-252 24557597-5 2014 Upregulation of both GCLC and GLCM mRNA levels in response to cysteine deprivation was dependent on new protein synthesis, which is consistent with expression of GCLC and GCLM being mediated by proteins whose synthesis depends on activation of the GCN2/ATF4 pathway. Cysteine 62-70 activating transcription factor 4 Homo sapiens 253-257 24733836-0 2014 State-dependent block of Orai3 TM1 and TM3 cysteine mutants: insights into 2-APB activation. Cysteine 43-51 tropomyosin 3 Homo sapiens 39-42 24733836-0 2014 State-dependent block of Orai3 TM1 and TM3 cysteine mutants: insights into 2-APB activation. Cysteine 43-51 arginyl aminopeptidase Homo sapiens 77-80 24733836-4 2014 Here we use cysteine scanning mutagenesis, thiol-reactive reagents, and patch-clamp analysis to define the residues that assist in formation of the 2-APB-activated Orai3 pore. Cysteine 12-20 arginyl aminopeptidase Homo sapiens 150-153 24742347-9 2014 ISG activation depends on Tat interaction with MAP2K3, MAP2K6, and IRF7 promoters and a single exon Tat protein more strongly modulated the luciferase activity mediated by MAP2K3, MAP2K6, and IRF7 promoter sequences located 5" of the RNA start site than the wild type two-exon Tat, while a cysteine and lysine Tat mutants, reduced in LTR transactivation, had negligible effects on these promoters. Cysteine 290-298 mitogen-activated protein kinase kinase 3 Homo sapiens 172-178 24451382-3 2014 We show in SirT1-overexpressing HepG2 cells that oxidants (nitrosocysteine and hydrogen peroxide) or metabolic stress (high palmitate and high glucose) inactivated SirT1 by reversible oxidative post-translational modifications (OPTMs) on three cysteines. Cysteine 244-253 sirtuin 1 Homo sapiens 11-16 24639627-7 2014 These proteins all share a cysteine-rich region that is necessary for Mid1 function in yeast. Cysteine 27-35 Mid1p Saccharomyces cerevisiae S288C 70-74 23843187-7 2014 However, the Thr611Cys mutation in the swapped domain, which mimicked conserved cysteine residues between TMEM16A and TMEM16B, reconstituted CaCC activity. Cysteine 80-88 anoctamin 2 Homo sapiens 118-125 23843187-8 2014 In addition, the GDD-causing cysteine mutation made in TMEM16A drastically altered CaCC activity. Cysteine 29-37 anoctamin 5 Homo sapiens 17-20 24330104-8 2014 In addition the sultr3;1 mutant showed a decrease of xanthine dehydrogenase activity, but not of nitrate reductase, strongly indicating that in seedlings cysteine availability limits activity of the molybdenum co-factor sulfurase, ABA3, which requires cysteine as the S-donor for sulfuration. Cysteine 154-162 sulfate transporter 3;1 Arabidopsis thaliana 16-24 24330104-8 2014 In addition the sultr3;1 mutant showed a decrease of xanthine dehydrogenase activity, but not of nitrate reductase, strongly indicating that in seedlings cysteine availability limits activity of the molybdenum co-factor sulfurase, ABA3, which requires cysteine as the S-donor for sulfuration. Cysteine 252-260 sulfate transporter 3;1 Arabidopsis thaliana 16-24 24393022-2 2014 TR1 is highly dependent upon the rare amino acid selenocysteine (Sec) for the reduction of thioredoxin (Trx) and a host of small molecule substrates, as mutation of Sec to cysteine (Cys) results in a large decrease in catalytic activity for all substrate types. Cysteine 55-63 thioredoxin reductase 1 Homo sapiens 0-3 24393022-2 2014 TR1 is highly dependent upon the rare amino acid selenocysteine (Sec) for the reduction of thioredoxin (Trx) and a host of small molecule substrates, as mutation of Sec to cysteine (Cys) results in a large decrease in catalytic activity for all substrate types. Cysteine 182-185 thioredoxin reductase 1 Homo sapiens 0-3 24393022-13 2014 Loss of both Se-electrophilicity and Se-nucleophilicity in the Sec Cys mutant of TR1 greatly reduces catalytic activity. Cysteine 69-72 thioredoxin reductase 1 Homo sapiens 83-86 24472371-3 2014 Ibrutinib (PCI-32765), a potent inhibitor of BTK induces impressive responses in B-cell malignancies through irreversible bond with cysteine-481 in the active site of BTK (TH/SH1 domain) and inhibits BTK phosphorylation on Tyr223. Cysteine 132-140 Bruton tyrosine kinase Homo sapiens 45-48 24472371-3 2014 Ibrutinib (PCI-32765), a potent inhibitor of BTK induces impressive responses in B-cell malignancies through irreversible bond with cysteine-481 in the active site of BTK (TH/SH1 domain) and inhibits BTK phosphorylation on Tyr223. Cysteine 132-140 Bruton tyrosine kinase Homo sapiens 167-170 24472371-3 2014 Ibrutinib (PCI-32765), a potent inhibitor of BTK induces impressive responses in B-cell malignancies through irreversible bond with cysteine-481 in the active site of BTK (TH/SH1 domain) and inhibits BTK phosphorylation on Tyr223. Cysteine 132-140 Bruton tyrosine kinase Homo sapiens 167-170 24489685-8 2014 Cysteine-151, -273 and -288 of Kelch-like ECH-associated protein-1 (Keap1), a cytosolic repressor of Nrf2, have been considered to act as a redox sensor and play a role in Nrf2 activation. Cysteine 0-8 kelch-like ECH-associated protein 1 Mus musculus 31-66 24489685-8 2014 Cysteine-151, -273 and -288 of Kelch-like ECH-associated protein-1 (Keap1), a cytosolic repressor of Nrf2, have been considered to act as a redox sensor and play a role in Nrf2 activation. Cysteine 0-8 kelch-like ECH-associated protein 1 Mus musculus 68-73 24111988-6 2014 We also identified the active-site cysteine in glutathione S-transferase omega-1 (GSTO1) as a potential Zn(2+)-chelation site, albeit with lower metal affinity relative to SORD. Cysteine 35-43 glutathione S-transferase omega 1 Homo sapiens 47-80 24111988-6 2014 We also identified the active-site cysteine in glutathione S-transferase omega-1 (GSTO1) as a potential Zn(2+)-chelation site, albeit with lower metal affinity relative to SORD. Cysteine 35-43 glutathione S-transferase omega 1 Homo sapiens 82-87 24491890-1 2014 gamma-Cystathionase (CTH, EC: 4.4.1.1), an enzyme widely distributed in the world of prokaryotic and eukaryotic organisms, catalyzes the formation and transformations of sulfane sulfur-containing compounds and plays a pivotal role in the L-cysteine desulfuration pathway. Cysteine 238-248 cystathionine gamma-lyase Homo sapiens 0-19 24491890-1 2014 gamma-Cystathionase (CTH, EC: 4.4.1.1), an enzyme widely distributed in the world of prokaryotic and eukaryotic organisms, catalyzes the formation and transformations of sulfane sulfur-containing compounds and plays a pivotal role in the L-cysteine desulfuration pathway. Cysteine 238-248 cystathionine gamma-lyase Homo sapiens 21-24 24491890-6 2014 A decrease of the expression of CTH entails a drop in the level of cysteine , glutathione (GSH), taurine and hydrogen sulfide (H2S) in the cells and, more importantly, leads to cystathioninuria. Cysteine 67-75 cystathionine gamma-lyase Homo sapiens 32-35 24138715-9 2014 Keeping in mind that the glycine present at position 12 can be substituted by valine, aspartic acid or cysteine, it could be well understood that each different substitution plays a different role in K-RAS-dependent processes. Cysteine 103-111 KRAS proto-oncogene, GTPase Homo sapiens 200-205 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. Cysteine 216-224 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. Cysteine 216-224 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. Cysteine 216-224 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. Cysteine 216-224 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. Cysteine 216-224 interleukin 12A Homo sapiens 135-138 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. Cysteine 149-157 interleukin 12A Homo sapiens 129-132 24961969-6 2014 In addition to TRPM2, TRPC5, TRPV1, and TRPA1 are also activated by H2O2 via modification of cysteine (Cys) free sulfhydryl groups. Cysteine 93-101 transient receptor potential cation channel subfamily M member 2 Homo sapiens 15-20 24961969-6 2014 In addition to TRPM2, TRPC5, TRPV1, and TRPA1 are also activated by H2O2 via modification of cysteine (Cys) free sulfhydryl groups. Cysteine 103-106 transient receptor potential cation channel subfamily M member 2 Homo sapiens 15-20 24555646-3 2014 Taking into account that MeHg is found mostly bound to sulfhydryl-containing molecules such as cysteine in the environment and based on the fact that the MeHg-cysteine complex (MeHg-S-Cys) can be transported via the L-type neutral amino acid carrier transport (LAT) system, the potential beneficial effects of L-methionine (L-Met, a well known LAT substrate) against MeHg (administrated as MeHg-S-Cys)-induced neurotoxicity in mice were investigated. Cysteine 182-187 linker for activation of T cells Mus musculus 261-264 24555646-3 2014 Taking into account that MeHg is found mostly bound to sulfhydryl-containing molecules such as cysteine in the environment and based on the fact that the MeHg-cysteine complex (MeHg-S-Cys) can be transported via the L-type neutral amino acid carrier transport (LAT) system, the potential beneficial effects of L-methionine (L-Met, a well known LAT substrate) against MeHg (administrated as MeHg-S-Cys)-induced neurotoxicity in mice were investigated. Cysteine 182-187 linker for activation of T cells Mus musculus 344-347 24155374-7 2014 TAP of UL28 complexes from cells infected with each domain mutant demonstrated that the conserved cysteine residues of the putative UL28 metal-binding domain and conserved amino acids within the UL15 nuclease domain are required for the cleavage and packaging functions of the viral terminase, but not for terminase complex assembly. Cysteine 98-106 DNA packaging terminase subunit 1 Human alphaherpesvirus 1 195-199 24059442-4 2013 This, along with the sensitivity of hSULT2A1 to oxidative modification at cysteine residues, led us to hypothesize that electrophilic PCB-quinones react with hSULT2A1 to alter its catalytic function. Cysteine 74-82 sulfotransferase family 2A member 1 Homo sapiens 36-44 24059442-4 2013 This, along with the sensitivity of hSULT2A1 to oxidative modification at cysteine residues, led us to hypothesize that electrophilic PCB-quinones react with hSULT2A1 to alter its catalytic function. Cysteine 74-82 sulfotransferase family 2A member 1 Homo sapiens 158-166 23350603-1 2013 AIMS: To define the consequences of loss of cysteine dioxygenase (CDO) on cysteine metabolism at the tissue level, we determined levels of relevant metabolites and enzymes and evidence of H2S/HS(-) (gaseous hydrogen sulfide and its conjugate base) toxicity in liver, pancreas, kidney, and lung of CDO(-/-) mice that were fed either a taurine-free or taurine-supplemented diet. Cysteine 44-52 cysteine dioxygenase 1, cytosolic Mus musculus 66-69 23350603-2 2013 RESULTS: CDO(-/-) mice had low tissue and serum taurine and hypotaurine levels and high tissue levels of cysteine, consistent with the loss of CDO. Cysteine 105-113 cysteine dioxygenase 1, cytosolic Mus musculus 9-12 23350603-5 2013 Very high levels of hypotaurine in pancreas of wild-type mice and very high levels of cystathionine and lanthionine in pancreas of CDO(-/-) mice were observed, suggesting a unique cysteine metabolism in the pancreas. Cysteine 180-188 cysteine dioxygenase 1, cytosolic Mus musculus 131-134 23350603-6 2013 INNOVATION: The CDO(-/-) mouse model provides new insights into tissue-specific cysteine metabolism, particularly the role of pancreas in metabolism of excess cysteine by CBS-catalyzed reactions, and will be a useful model for studying the effects of excess endogenous production of H2S/HS(-). Cysteine 80-88 cysteine dioxygenase 1, cytosolic Mus musculus 16-19 23350603-6 2013 INNOVATION: The CDO(-/-) mouse model provides new insights into tissue-specific cysteine metabolism, particularly the role of pancreas in metabolism of excess cysteine by CBS-catalyzed reactions, and will be a useful model for studying the effects of excess endogenous production of H2S/HS(-). Cysteine 159-167 cysteine dioxygenase 1, cytosolic Mus musculus 16-19 23972067-2 2013 Taurine is the major product of cysteine metabolism in mammals, and its biosynthetic pathway consists of cysteine dioxygenase and cysteine sulfinic acid decarboxylase (hCSAD). Cysteine 32-40 cysteine sulfinic acid decarboxylase Homo sapiens 168-173 23972067-8 2013 The fact that CSAD homologues exist in certain bacteria and are frequently found in operons containing the recently discovered bacterial cysteine dioxygenases that oxidize l-cysteine to CSA supports the idea that a bona fide bacterial taurine biosynthetic pathway exists in prokaryotes. Cysteine 172-182 cysteine sulfinic acid decarboxylase Homo sapiens 14-18 24019517-2 2013 In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Deves, R., Angelo, S., and Chavez, P. (1993) J. Physiol. Cysteine 27-35 solute carrier family 7 member 1 Homo sapiens 126-131 23934853-10 2013 LPS caused sulphonylation of SERCA Cys(674) (as measured immunohistochemically and supported by iodoacetamide labeling), which was greater in sGCalpha1(-/-) versus WT mice. Cysteine 35-38 guanylate cyclase 1, soluble, alpha 1 Mus musculus 142-151 23157314-3 2013 For example, it can react with particular protein Cys thiols because of its electrophilicity and can cause unique post-translational modifications of redox-sensor proteins such as Keap1 and H-Ras. Cysteine 50-53 kelch-like ECH-associated protein 1 Mus musculus 180-185 23157314-3 2013 For example, it can react with particular protein Cys thiols because of its electrophilicity and can cause unique post-translational modifications of redox-sensor proteins such as Keap1 and H-Ras. Cysteine 50-53 Harvey rat sarcoma virus oncogene Mus musculus 190-195 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. Cysteine 62-70 transthyretin Homo sapiens 0-3 24339620-2 2013 The gene sulfatase-modifying factor 1 (SUMF1), recently identified, encodes the enzyme responsible for post-translational modification of a cysteine residue, which is essential for the activity of sulfatases. Cysteine 140-148 sulfatase modifying factor 1 Homo sapiens 9-37 24339620-2 2013 The gene sulfatase-modifying factor 1 (SUMF1), recently identified, encodes the enzyme responsible for post-translational modification of a cysteine residue, which is essential for the activity of sulfatases. Cysteine 140-148 sulfatase modifying factor 1 Homo sapiens 39-44 23834247-5 2013 We show that Mia40 binds a [2Fe-2S] cluster in a dimer form with the cluster co-ordinated by the cysteine residues of the CPC motifs. Cysteine 97-105 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 13-18 23834247-6 2013 The biological relevance of the cofactor binding was confirmed in vivo by cysteine redox state and iron uptake analyses, which showed that a significant amount of cellular Mia40 binds iron in vivo. Cysteine 74-82 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 172-177 23733596-5 2013 The effect of LC on PIP3 was prevented by propargylglycine, an inhibitor of cystathionine-gamma-lyase (CSE) that catalyzes H2S formation from LC. Cysteine 14-16 cystathionine gamma-lyase Homo sapiens 76-101 23733596-5 2013 The effect of LC on PIP3 was prevented by propargylglycine, an inhibitor of cystathionine-gamma-lyase (CSE) that catalyzes H2S formation from LC. Cysteine 14-16 cystathionine gamma-lyase Homo sapiens 103-106 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. Cysteine 66-74 tropomyosin 3 Homo sapiens 78-81 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. Cysteine 114-122 tropomyosin 3 Homo sapiens 78-81 23706761-6 2013 An interesting coordination mode has been proposed for the IRT1-Zn(2+) complex, in which imidazoles from two histidines (His-96 and His-116), a cysteine thiolate (Cys-109) and one of a glutamic acid carboxyl group are involved. Cysteine 163-166 iron-regulated transporter 1 Arabidopsis thaliana 59-63 23885084-7 2013 Further studies suggested that the interaction of A19 with the RNA polymerase did not require RAP94 or other intermediate or late viral proteins but was reduced by mutation of cysteines in the putative zinc finger domain. Cysteine 176-185 immunoglobulin kappa variable 2-28 Homo sapiens 50-53 24204192-2 2013 We have previously demonstrated that extracellular acidosis leads to localization of the cysteine pro-tease cathepsin B on the tumor cell membrane and its secretion. Cysteine 89-97 cathepsin B Homo sapiens 108-119 24204192-5 2013 At pHe 6.8, there were increases in pericellular active cysteine cathepsins and in degradation of dye-quenched collagen IV, which was partially blocked by a cathepsin B inhibitor. Cysteine 56-64 cathepsin B Homo sapiens 157-168 23795888-4 2013 In keeping with its role as a PAT, AtPAT10 auto-S-acylates, and partially complements the yeast akr1 PAT mutant, and this requires Cys(192) of the DHHC motif. Cysteine 131-134 DHHC-type zinc finger family protein Arabidopsis thaliana 35-42 23972033-9 2013 Lastly, we demonstrate that the natural cysteine residues of Rce1p are chemically inaccessible and fully dispensable for in vivo enzyme activity, formally eliminating the possibility of a cysteine-based enzymatic mechanism for this protease. Cysteine 188-196 CAAX prenyl protease Saccharomyces cerevisiae S288C 61-66 23888047-4 2013 Mutating the active site cysteine residue (Cys-32) ablated the deglutathionylating activity of GSTO1-1. Cysteine 25-33 glutathione S-transferase omega 1 Homo sapiens 95-102 23888047-4 2013 Mutating the active site cysteine residue (Cys-32) ablated the deglutathionylating activity of GSTO1-1. Cysteine 43-46 glutathione S-transferase omega 1 Homo sapiens 95-102 23403147-3 2013 Although the neuroglobin sequences mostly display conserved Cys at positions CD7, D5 and G18/19, a number of exceptions are known. Cysteine 60-63 neuroglobin Homo sapiens 13-24 23403147-5 2013 All these neuroglobins differ from human neuroglobin in their Cys-positions. Cysteine 62-65 neuroglobin Homo sapiens 10-21 23929665-3 2013 In this study, we have successfully demonstrated that the covalent binding ability of RAL enamides can be tuned by attaching an electron-withdrawing motif, such as an acyl group, to enhance its reactivity toward the cysteine residues at the MNK1/2 binding sites. Cysteine 216-224 RAS like proto-oncogene A Homo sapiens 86-89 23929665-3 2013 In this study, we have successfully demonstrated that the covalent binding ability of RAL enamides can be tuned by attaching an electron-withdrawing motif, such as an acyl group, to enhance its reactivity toward the cysteine residues at the MNK1/2 binding sites. Cysteine 216-224 MAPK interacting serine/threonine kinase 1 Homo sapiens 241-245 23687301-8 2013 As predicted by CSS-Palm 2.0, Cys-3 and Cys-4 are the palmitoylation sites for Ncdn. Cysteine 30-33 neurochondrin Rattus norvegicus 79-83 23687301-8 2013 As predicted by CSS-Palm 2.0, Cys-3 and Cys-4 are the palmitoylation sites for Ncdn. Cysteine 40-43 neurochondrin Rattus norvegicus 79-83 23373818-4 2013 Homocysteine, a precursor in the metabolism of cysteine and methionine, induces the active Ox1 form of Ero1alpha in the OE cancer cell line OE33. Cysteine 4-12 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 103-112 23868209-1 2013 Oxytocin (OT) is a cyclic nonapeptide containing one internal disulfide bond between its Cys(1) and Cys(6) residues. Cysteine 89-92 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. Cysteine 89-92 oxytocin/neurophysin I prepropeptide Homo sapiens 10-12 23868209-1 2013 Oxytocin (OT) is a cyclic nonapeptide containing one internal disulfide bond between its Cys(1) and Cys(6) residues. Cysteine 100-103 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. Cysteine 100-103 oxytocin/neurophysin I prepropeptide Homo sapiens 10-12 23659571-3 2013 Results from site-directed mutagenesis studies suggest that the ability of hBD-3 to inhibit SDF-1alpha-CXCR4 interaction, as assayed either by blocking SDF-1 binding to CXCR4 or antagonizing SDF-1-induced Ca(2+) mobilization, is correlated with the presence of hBD-3 cysteine residues, specific surface-distributed cationic residues, and the electrostatic properties and availability of both hBD-3 termini. Cysteine 267-275 C-X-C motif chemokine receptor 4 Homo sapiens 103-108 23709667-5 2013 In addition, we demonstrate that Cys-40 and Cys-168 are required for the interaction with CsTdx and that CsCyp binds the citrus carboxyl-terminal domain of RNA polymerase II YSPSAP repeat. Cysteine 33-36 tetratricopeptide domain-containing thioredoxin Citrus sinensis 90-95 23709667-5 2013 In addition, we demonstrate that Cys-40 and Cys-168 are required for the interaction with CsTdx and that CsCyp binds the citrus carboxyl-terminal domain of RNA polymerase II YSPSAP repeat. Cysteine 44-47 tetratricopeptide domain-containing thioredoxin Citrus sinensis 90-95 23636452-7 2013 The observation that the cadmium binding ability of rabbit liver MT2A was only slightly increased led to the development of a hypothesis in which the long cysteine-free linker regions present in certain plant metallothioneins may contribute to the accommodation of the respective larger cluster assemblies. Cysteine 155-163 metallothionein-2A Oryctolagus cuniculus 65-69 23721409-2 2013 When a small label was incorporated on the cytosolic interface of transmembrane helix 6 (Cys-265), (19)F NMR spectra of the beta2 adrenergic receptor (beta2AR) reconstituted in maltose/neopentyl glycol detergent micelles revealed two distinct inactive states, an activation intermediate state en route to activation, and, in the presence of a G protein mimic, a predominant active state. Cysteine 89-92 adrenoceptor beta 2 Homo sapiens 124-149 23721409-2 2013 When a small label was incorporated on the cytosolic interface of transmembrane helix 6 (Cys-265), (19)F NMR spectra of the beta2 adrenergic receptor (beta2AR) reconstituted in maltose/neopentyl glycol detergent micelles revealed two distinct inactive states, an activation intermediate state en route to activation, and, in the presence of a G protein mimic, a predominant active state. Cysteine 89-92 adrenoceptor beta 2 Homo sapiens 151-158 23752473-1 2013 A novel annexin A5 derivative (cys-annexin A5) with a single cysteine residue at its C-terminal has been developed and successfully labeled in high labeling yield with (99m)Tc by a ligand exchange reaction. Cysteine 31-34 annexin A5 Mus musculus 8-18 23752473-1 2013 A novel annexin A5 derivative (cys-annexin A5) with a single cysteine residue at its C-terminal has been developed and successfully labeled in high labeling yield with (99m)Tc by a ligand exchange reaction. Cysteine 31-34 annexin A5 Mus musculus 35-45 23752473-1 2013 A novel annexin A5 derivative (cys-annexin A5) with a single cysteine residue at its C-terminal has been developed and successfully labeled in high labeling yield with (99m)Tc by a ligand exchange reaction. Cysteine 61-69 annexin A5 Mus musculus 8-18 23752473-1 2013 A novel annexin A5 derivative (cys-annexin A5) with a single cysteine residue at its C-terminal has been developed and successfully labeled in high labeling yield with (99m)Tc by a ligand exchange reaction. Cysteine 61-69 annexin A5 Mus musculus 35-45 23603511-6 2013 Fine mapping revealed that the cysteine-rich domain of MRC binds to the chondroitin sulfate side chains of CD44. Cysteine 31-39 CD44 antigen Mus musculus 107-111 23717386-4 2013 The structure of the soluble domain of NAF-1 shows that it forms a homodimer with each protomer containing a [2Fe-2S] cluster bound by 3 Cys and one His. Cysteine 137-140 CDGSH iron sulfur domain 2 Homo sapiens 39-44 23176571-9 2013 NaHS S-sulfhydrated Keap1 at cysteine-151, induced Nrf2 dissociation from Keap1, enhanced Nrf2 nuclear translocation, and stimulated mRNA expression of Nrf2-targeted downstream genes, such as glutamate-cysteine ligase and GSH reductase. Cysteine 29-37 kelch-like ECH-associated protein 1 Mus musculus 20-25 22907821-2 2013 It is synthesised from cysteine via cystathionine beta-synthase and cystathionine gamma-lyase. Cysteine 23-31 cystathionine gamma-lyase Homo sapiens 68-93 22907821-12 2013 Cysteine and the G1364T and 844ins68 variants of the cystathionine gamma-lyase and cystathionine beta-synthase genes, respectively, are the biological determinants of H(2)S synthesis, and all three are shown here to influence the hypertensive phenotype. Cysteine 0-8 cystathionine gamma-lyase Homo sapiens 53-78 23197653-3 2013 This system (consisting of two proteins, Gfer and Mia40) is involved in the mitochondrial import of Cys-rich proteins. Cysteine 100-103 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 50-55 23295225-7 2013 The analysis confirmed GSNO concentration-dependent S-glutathionylation of cysteines at positions 122, 150, 226, 227 which was 2-700 times higher compared to wild-type CBR1 (WT-CBR1). Cysteine 75-84 carbonyl reductase 1 Homo sapiens 177-181 23288839-1 2013 Formylglycine-generating enzyme (FGE) post-translationally converts a specific cysteine in newly synthesized sulfatases to formylglycine (FGly). Cysteine 79-87 sulfatase modifying factor 1 Homo sapiens 0-31 23288839-1 2013 Formylglycine-generating enzyme (FGE) post-translationally converts a specific cysteine in newly synthesized sulfatases to formylglycine (FGly). Cysteine 79-87 sulfatase modifying factor 1 Homo sapiens 33-36 23382182-4 2013 Here we report that in neurons and brain tissue NO can S-nitrosylate SHP-2 at its active site cysteine, forming S-nitrosylated SHP-2 (SNO-SHP-2). Cysteine 94-102 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 127-132 23360348-3 2013 We demonstrate, using mass spectrometry and X-ray crystallography, that the selective inhibitor covalently modifies PI3Kalpha on cysteine 862 (C862), an amino acid unique to the alpha isoform, and that PI3Kbeta, -gamma, and -delta are not covalently modified. Cysteine 129-137 phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta Homo sapiens 202-230 23434668-8 2013 For instance, ROS can inhibit SIRT1 activity by evoking oxidative modifications on its cysteine residues. Cysteine 87-95 sirtuin 1 Homo sapiens 30-35 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. Cysteine 124-127 potassium voltage-gated channel subfamily B member 1 Homo sapiens 42-47 22718265-5 2013 Comparative analysis established that cysteine also inhibited GDC and CSADC in a concentration-dependent manner. Cysteine 38-46 cysteine sulfinic acid decarboxylase Homo sapiens 70-75 22718265-8 2013 Cysteine is the building block for protein synthesis and a precursor of cysteine sulfinic acid that is the substrate of CSADC and therefore is present in many cells, but the presence of cysteine (at comparable concentrations to their natural substrates) apparently could severely inhibit ADC, CSADC and GDC activity. Cysteine 0-8 cysteine sulfinic acid decarboxylase Homo sapiens 120-125 22718265-8 2013 Cysteine is the building block for protein synthesis and a precursor of cysteine sulfinic acid that is the substrate of CSADC and therefore is present in many cells, but the presence of cysteine (at comparable concentrations to their natural substrates) apparently could severely inhibit ADC, CSADC and GDC activity. Cysteine 0-8 cysteine sulfinic acid decarboxylase Homo sapiens 293-298 22718265-8 2013 Cysteine is the building block for protein synthesis and a precursor of cysteine sulfinic acid that is the substrate of CSADC and therefore is present in many cells, but the presence of cysteine (at comparable concentrations to their natural substrates) apparently could severely inhibit ADC, CSADC and GDC activity. Cysteine 72-80 cysteine sulfinic acid decarboxylase Homo sapiens 120-125 23264646-1 2013 In yeast (Saccharomyces cerevisiae) and animals, the sulfhydryl oxidase Erv1 functions with Mia40 in the import and oxidative folding of numerous cysteine-rich proteins in the mitochondrial intermembrane space (IMS). Cysteine 146-154 Mia40p Saccharomyces cerevisiae S288C 92-97 23319727-4 2013 Here, we use cadmium metal bridge formation to measure conformational changes reported by substituted cysteines at loci demarcating the intracellular (E109 and L108) and extracellular (Q56) entrance of hemichannels formed by the Cx32 chimera (Cx32*43E1). Cysteine 102-111 gap junction protein beta 1 Homo sapiens 229-233 23319727-4 2013 Here, we use cadmium metal bridge formation to measure conformational changes reported by substituted cysteines at loci demarcating the intracellular (E109 and L108) and extracellular (Q56) entrance of hemichannels formed by the Cx32 chimera (Cx32*43E1). Cysteine 102-111 gap junction protein beta 1 Homo sapiens 243-247 22900493-9 2013 Inhibition was reversed by 1,4-dithioerythritol, L-cysteine (Cys), and N-acetyl-L-cysteine (NAC) indicating that it was caused by covalent reaction of mercurials with Cys residue(s). Cysteine 167-170 X-linked Kx blood group Homo sapiens 92-95 23203293-4 2013 The ability of this unusual prosthetic group to readily introduce the radioisotope within complex (bio)molecular architectures has been demonstrated by (1) the preparation of the first [(18)F]-labelled cyanine 5.5 (Cy 5.5) dye, a suitable precursor for the construction of hybrid positron emission tomography/near-infrared fluorescence (PET/NIRF) imaging probes and (2) the radiolabelling of a biologically relevant peptide bearing a single lysine residue. Cysteine 215-217 interleukin 17B Homo sapiens 341-345 23301676-8 2013 Furthermore, complex 2 is also a good cathepsin B inhibitor (an enzyme implicated in a number of cancer related events), being the enzyme reactivated by cysteine. Cysteine 153-161 cathepsin B Homo sapiens 38-49 23183178-4 2013 By synthetic peptide ELISA, we identified 3BD10 binding to TSHR amino acids E34, E35, and D36 within TSHR cysteine-bonded loop 2 (C31-C41), which includes R38, the most N-terminal contact residue of TSAb M22. Cysteine 106-114 thyroid stimulating hormone receptor Homo sapiens 59-63 23183178-4 2013 By synthetic peptide ELISA, we identified 3BD10 binding to TSHR amino acids E34, E35, and D36 within TSHR cysteine-bonded loop 2 (C31-C41), which includes R38, the most N-terminal contact residue of TSAb M22. Cysteine 106-114 thyroid stimulating hormone receptor Homo sapiens 101-105 22177231-0 2013 Computational study of the covalent bonding of microcystins to cysteine residues--a reaction involved in the inhibition of the PPP family of protein phosphatases. Cysteine 63-71 protein phosphatase 1 regulatory inhibitor subunit 2 Homo sapiens 127-130 23036860-3 2012 The conserved cysteine residues within small TIM members have also been shown to participate in early biogenesis events, with the most N-terminal cysteine residue important for import and retention within the intermembrane space via the receptor and disulfide oxidase, Mia40. Cysteine 146-154 Mia40p Saccharomyces cerevisiae S288C 269-274 23112049-3 2012 Covalent attachment of palmitate to the N-terminal cysteine of Shh is catalyzed by Hedgehog acyltransferase (Hhat) and is critical for proper signaling. Cysteine 51-59 hedgehog acyltransferase Homo sapiens 83-107 23112049-3 2012 Covalent attachment of palmitate to the N-terminal cysteine of Shh is catalyzed by Hedgehog acyltransferase (Hhat) and is critical for proper signaling. Cysteine 51-59 hedgehog acyltransferase Homo sapiens 109-113 22841986-2 2012 H(2)S can be synthesized from l-cysteine by cystathionine beta-synthetase (CBS) or cystathionine gamma-lyase (CSE). Cysteine 30-40 cystathionine gamma-lyase Homo sapiens 83-108 22841986-2 2012 H(2)S can be synthesized from l-cysteine by cystathionine beta-synthetase (CBS) or cystathionine gamma-lyase (CSE). Cysteine 30-40 cystathionine gamma-lyase Homo sapiens 110-113 22995344-9 2012 While probably belonging to the high-sulphur KAP group, the polypeptide had a moderate level of cysteine, but a high content of serine and tyrosine. Cysteine 96-104 cyclin dependent kinase inhibitor 3 Homo sapiens 45-48 23123111-6 2012 In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. Cysteine 30-39 pre-mRNA processing factor 40 homolog B Homo sapiens 43-47 23123111-6 2012 In the complex, the conserved cysteines of HypC and HypD form an Fe binding site. Cysteine 30-39 MAGE family member A3 Homo sapiens 52-56 23123111-7 2012 The conserved C-terminal cysteine of HypE can access the thiol redox cascade of HypD. Cysteine 25-33 MAGE family member A3 Homo sapiens 80-84 23261056-3 2012 Four cysteine residues at positions of C59, C93, C201, or C274 may be involved, at least in part, in the inhibition of hGDH2 by palmitoyl-CoA. Cysteine 5-13 glutamate dehydrogenase 2 Homo sapiens 119-124 22841676-4 2012 It is predominantly formed from L-cysteine by cystathionine-beta-synthase (CBS) and cystathionine-gamma-lyase (CSE). Cysteine 32-42 cystathionine gamma-lyase Homo sapiens 84-109 22841676-4 2012 It is predominantly formed from L-cysteine by cystathionine-beta-synthase (CBS) and cystathionine-gamma-lyase (CSE). Cysteine 32-42 cystathionine gamma-lyase Homo sapiens 111-114 22841676-12 2012 RESULTS AND LIMITATIONS: CBS and CSE are present in the human bladder dome and efficiently convert L-cysteine into H(2)S. Cysteine 99-109 cystathionine gamma-lyase Homo sapiens 33-36 23183700-6 2012 To address this question, we apply cysteine (Cys) scanning mutagenesis to TMDs and EJMs of KCNE1 and KCNE2. Cysteine 35-43 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 91-96 23183700-6 2012 To address this question, we apply cysteine (Cys) scanning mutagenesis to TMDs and EJMs of KCNE1 and KCNE2. Cysteine 45-48 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 91-96 23142976-4 2012 This, along with E1 and E2 conformational variability, allows presentation of "frontside" Atg3 and Atg10 active sites to the catalytic cysteine in the C-terminal domain from the opposite Atg7 protomer in the homodimer. Cysteine 135-143 Atg3p Saccharomyces cerevisiae S288C 90-94 22989881-10 2012 In this study, we confirmed that S100A1 protein is endogenously modified by Cys(85) S-nitrosylation in PC12 cells, which are a well established model system for studying S100A1 function. Cysteine 76-79 S100 calcium binding protein A1 Rattus norvegicus 33-39 23043141-8 2012 Mutation of Arg(638) compromises SDH function only when present in combination with a Cys(630) substitution. Cysteine 86-89 succinate dehydrogenase complex iron sulfur subunit B Homo sapiens 33-36 23177194-0 2012 Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70. Cysteine 0-8 heat shock protein family A (Hsp70) member 4 Homo sapiens 96-117 23064950-6 2012 Impairment of GAPDH was found to be due to glutathionylation of its catalytic site cysteines. Cysteine 83-92 glyceraldehyde-3-phosphate dehydrogenase Mus musculus 14-19 22990235-4 2012 Atp23 contains ten cysteine residues which are oxidized during several rounds of interaction with Mia40. Cysteine 19-27 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 98-103 22990235-8 2012 Thus, Mia40 plays a much broader role in import and folding of polypeptides than previously expected and can serve as folding factor for proteins with complex disulphide patterns as well as for cysteine-free polypeptides. Cysteine 194-202 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 6-11 23047007-4 2012 We were able to determine the structural domains of BST-2 that are essential to restrict XMRV, including the transmembrane domain, the coiled-coil ectodomain, the C-terminal glycosylphosphatidylinositol (GPI) anchor, the two putative N-linked glycosylation sites, and the three extracellular cysteine residues. Cysteine 292-300 bone marrow stromal cell antigen 2 Homo sapiens 52-57 23058916-0 2012 Inhibition of Ca(2+) release-activated Ca(2+) channel (CRAC) by curcumin and caffeic acid phenethyl ester (CAPE) via electrophilic addition to a cysteine residue of Orai1. Cysteine 145-153 ORAI calcium release-activated calcium modulator 1 Homo sapiens 165-170 23058916-5 2012 We investigated the sensitivity of cysteine mutated Orai1 to curcumin and CAPE to delineate their inhibitory mechanism. Cysteine 35-43 ORAI calcium release-activated calcium modulator 1 Homo sapiens 52-57 22955273-5 2012 In the reaction, cysteine residues of recombinant human arsenic (+3 oxidation state) methyltransferase (hAS3MT) coordinate with arsenicals and involve the methyl transfer step. Cysteine 17-25 arsenite methyltransferase Homo sapiens 56-102 22955273-5 2012 In the reaction, cysteine residues of recombinant human arsenic (+3 oxidation state) methyltransferase (hAS3MT) coordinate with arsenicals and involve the methyl transfer step. Cysteine 17-25 arsenite methyltransferase Homo sapiens 104-110 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+)). Cysteine 88-91 arsenite methyltransferase Homo sapiens 128-134 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+)). Cysteine 108-116 arsenite methyltransferase Homo sapiens 128-134 22992729-0 2012 Identification of the cysteine residue responsible for disulfide linkage of Na+ channel alpha and beta2 subunits. Cysteine 22-30 hemoglobin, beta adult minor chain Mus musculus 98-103 22992729-4 2012 Here we generated a series of mutant beta2 cDNA constructs to investigate the cysteine residue(s) responsible for alpha-beta2 subunit covalent linkage. Cysteine 78-86 hemoglobin, beta adult minor chain Mus musculus 120-125 22992729-5 2012 We demonstrate that a single cysteine-to-alanine substitution at extracellular residue Cys-26, located within the immunoglobulin (Ig) domain, abolishes the covalent linkage between alpha and beta2 subunits. Cysteine 29-37 hemoglobin, beta adult minor chain Mus musculus 191-196 22992729-5 2012 We demonstrate that a single cysteine-to-alanine substitution at extracellular residue Cys-26, located within the immunoglobulin (Ig) domain, abolishes the covalent linkage between alpha and beta2 subunits. Cysteine 87-90 hemoglobin, beta adult minor chain Mus musculus 191-196 23002438-10 2012 Thus, CysLT(2)R negatively regulates the development of cys-LT-dependent Th2 pulmonary inflammation by inhibiting both CysLT(1)R signaling and D. farinae-induced LTC(4)S-dependent cell surface expression of CysLT(1)R on DCs. Cysteine 56-59 leukotriene C4 synthase Rattus norvegicus 162-169 22511607-2 2012 In mitochondria, cyanide is a potent inhibitor of the cytochrome c oxidase and is metabolized by the beta-cyanoalanine synthase CYS-C1, catalyzing the conversion of cysteine and cyanide to hydrogen sulfide and beta-cyanoalanine. Cysteine 165-173 cysteine synthase C1 Arabidopsis thaliana 128-134 22302369-7 2012 Oral administration of cysteine to mice significantly increased NQO1 mRNA levels in the mouse intestinal mucosa. Cysteine 23-31 NAD(P)H dehydrogenase, quinone 1 Mus musculus 64-68 22704610-1 2012 Cathepsin H is a unique member of the cysteine cathepsins that acts primarily as an aminopeptidase. Cysteine 38-46 cathepsin H Homo sapiens 0-11 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). Cysteine 79-88 Fc receptor like 5 Homo sapiens 45-50 22660956-12 2012 In both patients, a novel de novo mutation of PAX2 was detected, which leads to the substitution of a highly conserved cysteine (p.C52Y). Cysteine 119-127 paired box 2 Homo sapiens 46-50 22966037-5 2012 Electrophiles and oxidants modify critical cysteine thiols of Keap1 and Nrf2 to inhibit Nrf2 ubiquitination, leading to Nrf2 activation and induction. Cysteine 43-51 kelch-like ECH-associated protein 1 Mus musculus 62-67 22824864-4 2012 PQQ inhibited protein tyrosine phosphatase 1B (PTP1B), which negatively regulates the EGFR signaling by tyrosine dephosphorylation, to oxidatively modify the catalytic cysteine through its redox cycling activity to generate H(2)O(2). Cysteine 168-176 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 47-52 22740694-2 2012 HypF catalyzes S-carbamoylation of the C-terminal cysteine of HypE via three steps using carbamoylphosphate and ATP, producing two unstable intermediates: carbamate and carbamoyladenylate. Cysteine 50-58 fibroblast growth factor 23 Homo sapiens 0-4 22740694-7 2012 The structure of HypF in complex with HypE revealed that HypF can associate with HypE without disturbing its homodimeric interaction and that the binding manner allows the C-terminal Cys-351 of HypE to access the S-carbamoylation active site in HypF, suggesting that the third step can also proceed without the release of carbamoyladenylate. Cysteine 183-186 fibroblast growth factor 23 Homo sapiens 17-21 22740694-7 2012 The structure of HypF in complex with HypE revealed that HypF can associate with HypE without disturbing its homodimeric interaction and that the binding manner allows the C-terminal Cys-351 of HypE to access the S-carbamoylation active site in HypF, suggesting that the third step can also proceed without the release of carbamoyladenylate. Cysteine 183-186 fibroblast growth factor 23 Homo sapiens 57-61 22740694-7 2012 The structure of HypF in complex with HypE revealed that HypF can associate with HypE without disturbing its homodimeric interaction and that the binding manner allows the C-terminal Cys-351 of HypE to access the S-carbamoylation active site in HypF, suggesting that the third step can also proceed without the release of carbamoyladenylate. Cysteine 183-186 fibroblast growth factor 23 Homo sapiens 57-61 22648419-4 2012 GSSG oxidizes copper-coordinating cysteines of Atox1 with the formation of an intramolecular disulfide. Cysteine 34-43 antioxidant 1 copper chaperone Homo sapiens 47-52 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. Cysteine 112-115 chondromodulin Homo sapiens 141-146 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. Cysteine 124-127 chondromodulin Homo sapiens 141-146 22429838-6 2012 A synthetic cyclic peptide corresponding to the ChM-I region between Ile(82) to Arg(100) also inhibited the migration of HUVEC, while replacing the Cys(83) and Cys(99) residues in this peptide with Ser completely negated this inhibitory activity. Cysteine 148-151 chondromodulin Homo sapiens 48-53 22429838-6 2012 A synthetic cyclic peptide corresponding to the ChM-I region between Ile(82) to Arg(100) also inhibited the migration of HUVEC, while replacing the Cys(83) and Cys(99) residues in this peptide with Ser completely negated this inhibitory activity. Cysteine 160-163 chondromodulin Homo sapiens 48-53 22547024-4 2012 We show that vacuolar targeting of CBL2 is specifically brought about by S-acylation of three cysteine residues in its N-terminus and that CBL2 S-acylation and targeting occur by a Brefeldin A-insensitive pathway. Cysteine 94-102 calcineurin B-like protein 2 Arabidopsis thaliana 35-39 22740475-6 2012 We selected two proteins, complement factor H (CFH) and apolipoprotein H (ApoH), with dye (Cy) ratios showing greater than 2.0-fold differences between the pooled samples. Cysteine 91-93 complement factor H Homo sapiens 26-45 22664871-3 2012 In this article, we report the 2.7-A crystal structure of human RANKL trimer in complex with the N-terminal fragment of human OPG containing four cysteine-rich TNFR homologous domains (OPG-CRD). Cysteine 146-154 TNF superfamily member 11 Homo sapiens 64-69 22689926-3 2012 In this research, an Affibody analog, anti-EGFR Ac-Cys-Z(EGFR:1907), was successfully site-specifically (18)F-labeled for PET of EGFR expression. Cysteine 51-54 thyroid stimulating hormone receptor Mus musculus 122-125 22689926-12 2012 CONCLUSION: (18)F-FBEM-Cys-Z(EGFR:1907) is a novel protein scaffold-based PET probe for imaging EGFR overexpression of tumors, and its ability to differentiate tumors with high and low EGFR expression in vivo holds promise for future clinical translation. Cysteine 23-26 thyroid stimulating hormone receptor Mus musculus 74-77 22605564-0 2012 Cysteine racemization during the Fmoc solid phase peptide synthesis of the Nav1.7-selective peptide--protoxin II. Cysteine 0-8 sodium voltage-gated channel alpha subunit 9 Homo sapiens 75-81 22354836-3 2012 The ability of electrophilic derivatives to interact with hASBT was evaluated by 2-aminoethyl-methanethiosulfonate (MTSEA)-biotin labeling of thiol groups in TM7 cysteine mutants. Cysteine 162-170 solute carrier family 10 member 2 Homo sapiens 58-63 22813739-2 2012 The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1"s transactivation domain are critical for coactivator function. Cysteine 126-129 regulatory protein (NPR1) Arabidopsis thaliana 32-36 22813739-2 2012 The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1"s transactivation domain are critical for coactivator function. Cysteine 126-129 regulatory protein (NPR1) Arabidopsis thaliana 163-167 22813739-2 2012 The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1"s transactivation domain are critical for coactivator function. Cysteine 139-142 regulatory protein (NPR1) Arabidopsis thaliana 32-36 22813739-2 2012 The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1"s transactivation domain are critical for coactivator function. Cysteine 139-142 regulatory protein (NPR1) Arabidopsis thaliana 163-167 22458656-2 2012 In addition to cognate proline, prolyl-tRNA synthetase (ProRS) can activate cysteine and alanine and misacylate tRNA(Pro). Cysteine 76-84 glutamyl-prolyl-tRNA synthetase 1 Homo sapiens 32-54 22458656-2 2012 In addition to cognate proline, prolyl-tRNA synthetase (ProRS) can activate cysteine and alanine and misacylate tRNA(Pro). Cysteine 76-84 glutamyl-prolyl-tRNA synthetase 1 Homo sapiens 56-61 22676268-7 2012 Among the several active cysteine-substitution mutants of LPCAT1 generated, we identified one to be resistant to treatment by sulfhydryl-alkylating and sulfhydryl-oxidizer agents. Cysteine 25-33 lysophosphatidylcholine acyltransferase 1 Homo sapiens 58-64 22860208-5 2012 Our results suggest that the hMGL cysteine mutant maintains the same overall architecture as wild-type hMGL. Cysteine 34-42 monoglyceride lipase Homo sapiens 29-33 22860208-5 2012 Our results suggest that the hMGL cysteine mutant maintains the same overall architecture as wild-type hMGL. Cysteine 34-42 monoglyceride lipase Homo sapiens 103-107 22576105-2 2012 Formylglycine generating enzyme (FGE) recognizes a pentapeptide consensus sequence, CxPxR, and it specifically oxidizes the cysteine in this sequence to an unusual aldehyde-bearing formylglyine. Cysteine 124-132 sulfatase modifying factor 1 Homo sapiens 0-31 22576105-2 2012 Formylglycine generating enzyme (FGE) recognizes a pentapeptide consensus sequence, CxPxR, and it specifically oxidizes the cysteine in this sequence to an unusual aldehyde-bearing formylglyine. Cysteine 124-132 sulfatase modifying factor 1 Homo sapiens 33-36 22576105-4 2012 The conversion of cysteine to formylglycine is accomplished by co-overexpression of FGE, either transiently or as a stable cell line, and the resulting aldehyde can be selectively reacted with alpha-nucleophiles to generate a site-selectively modified bioconjugate. Cysteine 18-26 sulfatase modifying factor 1 Homo sapiens 84-87 22414809-2 2012 In mice with liver-specific deletion of CDO expression, hepatic and plasma cysteine levels increased. Cysteine 75-83 cysteine dioxygenase 1, cytosolic Mus musculus 40-43 22414809-5 2012 This upregulation of CDO concentration and active-site cofactor formation were not associated with an increase in CDO mRNA and thus presumably were due to a decrease in CDO degradation and an increase in CDO cofactor formation in association with increased exposure of extrahepatic tissues to cysteine in mice lacking hepatic CDO. Cysteine 293-301 cysteine dioxygenase 1, cytosolic Mus musculus 21-24 22414809-6 2012 Extrahepatic tissues of liver CDO-knockout mice also had higher levels of hypotaurine, consistent with increased metabolism of cysteine by the CDO/cysteinesulfinate decarboxylase pathway. Cysteine 127-135 cysteine dioxygenase 1, cytosolic Mus musculus 30-33 22414809-6 2012 Extrahepatic tissues of liver CDO-knockout mice also had higher levels of hypotaurine, consistent with increased metabolism of cysteine by the CDO/cysteinesulfinate decarboxylase pathway. Cysteine 127-135 cysteine dioxygenase 1, cytosolic Mus musculus 143-146 22402363-10 2012 We provide evidence for one mechanism of Ox-PAPC activation of ADAM involving covalent binding of Ox-PAPC to cysteine on ADAM. Cysteine 109-117 protocadherin 8 Homo sapiens 44-48 22402363-10 2012 We provide evidence for one mechanism of Ox-PAPC activation of ADAM involving covalent binding of Ox-PAPC to cysteine on ADAM. Cysteine 109-117 protocadherin 8 Homo sapiens 101-105 22402363-11 2012 Free thiol cysteine analogs showed inhibition of IL-8 induction by Ox-PAPC, and both a cysteine analog and a cell surface thiol blocker strongly inhibited ADAM activity induction by Ox-PAPC. Cysteine 11-19 protocadherin 8 Homo sapiens 70-74 22310694-0 2012 Cysteines control the N- and C-linker-dependent gating of KCNH1 potassium channels. Cysteine 0-9 potassium voltage-gated channel subfamily H member 1 Homo sapiens 58-63 22310694-5 2012 Intracellular application of H(2)O(2) or cysteine-specific modifiers potently inhibited KCNH1 channels in two phases. Cysteine 41-49 potassium voltage-gated channel subfamily H member 1 Homo sapiens 88-93 22741101-4 2012 We initially confirmed that BACE1 is mainly palmitoylated at four C-terminal cysteine residues in stably transfected neuroblastoma cells. Cysteine 77-85 beta-secretase 1 Rattus norvegicus 28-33 22406622-4 2012 Tandem mass spectrometry analyses identified Cys(256) of serpin A1 and Cys(263) of serpin A3 as the S-glutathionylated residues. Cysteine 71-74 serpin family A member 3 Homo sapiens 83-92 22066718-4 2012 A novel heterozygous mutation in exon 2 of GCMB was identified in both affected individuals that changes cysteine at position 106 of the putative DNA-binding domain of GCMB to arginine (C106R). Cysteine 105-113 glial cells missing transcription factor 2 Homo sapiens 43-47 22066718-4 2012 A novel heterozygous mutation in exon 2 of GCMB was identified in both affected individuals that changes cysteine at position 106 of the putative DNA-binding domain of GCMB to arginine (C106R). Cysteine 105-113 glial cells missing transcription factor 2 Homo sapiens 168-172 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 113-121 calmodulin 2 Gallus gallus 45-55 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 113-121 calmodulin 2 Gallus gallus 57-60 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 123-126 calmodulin 2 Gallus gallus 45-55 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 123-126 calmodulin 2 Gallus gallus 57-60 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 184-187 calmodulin 2 Gallus gallus 45-55 22550304-3 2012 This protocol describes how to label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. Cysteine 184-187 calmodulin 2 Gallus gallus 57-60 22550304-5 2012 To confirm that the two Cys residues in the labeled CaM are actually cross-linked by BR, a sample of purified BR-CaM is digested by an endoproteinase and analyzed by mass spectrometry. Cysteine 24-27 calmodulin 2 Gallus gallus 52-55 22612783-2 2012 Contrary to the endoplasmatic reticulum ER where several chaperones of the disulfide isomerase family exist, oxidative folding in the IMS is exclusively catalyzed by the oxoreductase Mia40 that recognizes a group of proteins with characteristic cysteine motifs organized in twin CX(3)C, twin CX(9)C or CX(2)C motifs. Cysteine 245-253 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 183-188 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. Cysteine 93-101 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. Cysteine 93-101 matrix metallopeptidase 9 Homo sapiens 223-228 21928342-5 2012 Thus, we show that Wif-1 physically binds to connective tissue growth factor (CTGF/CCN2) in vitro, predominantly by interaction with the C-terminal cysteine knot domain of CTGF. Cysteine 148-156 Wnt inhibitory factor 1 Mus musculus 19-24 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. Cysteine 169-177 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 73-78 22222112-3 2012 The deduced GhAGP31 protein contains the conserved features of non-classical AGPs: a putative signal peptide, N-terminal histidine-rich stretch, middle repetitive proline-rich domain and a cysteine-containing "PAC" domain. Cysteine 189-197 non-classical arabinogalactan protein 31-like Gossypium hirsutum 12-19 22416124-2 2012 Epicutaneous sensitization with ovalbumin of WT mice but not DeltadblGATA mice, the latter of which lack eosinophils, caused skin thickening, collagen deposition, and increased mRNA expression of the cys-LT generating enzyme LTC(4) synthase (LTC(4)S). Cysteine 200-203 leukotriene C4 synthase Mus musculus 225-240 22416124-2 2012 Epicutaneous sensitization with ovalbumin of WT mice but not DeltadblGATA mice, the latter of which lack eosinophils, caused skin thickening, collagen deposition, and increased mRNA expression of the cys-LT generating enzyme LTC(4) synthase (LTC(4)S). Cysteine 200-203 leukotriene C4 synthase Mus musculus 242-249 22442077-6 2012 Consequently, a KCNB1 variant resistant to oxidation, obtained by mutating a conserved cysteine to alanine, (C73A), was neuroprotective. Cysteine 87-95 potassium voltage gated channel, Shab-related subfamily, member 1 Mus musculus 16-21 22222468-7 2012 Determination of cysteine oxidation revealed increased NOX4-mediated K(v)1.5 channel oxidation. Cysteine 17-25 NADPH oxidase 4 Rattus norvegicus 55-59 22249179-7 2012 Chromatin remodeling by TIP60 involved the sequential recruitment of acetyl-Lys-310 RelA/p65 to its target gene promoters. Cysteine 69-75 lysine acetyltransferase 5 Homo sapiens 24-29 22257021-11 2012 We therefore postulate that cysteine-mediated intermolecular reactions are suppressed by complex formation of the divalent metal ion and citrate with oxytocin, thereby inhibiting the formation of citrate adducts and reactions of the cysteine thiol group in oxytocin. Cysteine 28-36 oxytocin/neurophysin I prepropeptide Homo sapiens 150-158 22257021-11 2012 We therefore postulate that cysteine-mediated intermolecular reactions are suppressed by complex formation of the divalent metal ion and citrate with oxytocin, thereby inhibiting the formation of citrate adducts and reactions of the cysteine thiol group in oxytocin. Cysteine 28-36 oxytocin/neurophysin I prepropeptide Homo sapiens 257-265 22212194-2 2012 The V2 ligand sequence from matricellular protein CCN1 (cysteine-rich 61, CYR61) was multimerized and cloned into elastin polymer LysB10, creating LysB10.V2. Cysteine 56-64 elastin Homo sapiens 114-121 22088136-1 2012 The redox-active protein cytochrome b(562) has been engineered to introduce pairs of thiol groups in the form of cysteine residues at specified sites. Cysteine 113-121 mitochondrially encoded cytochrome b Homo sapiens 25-37 22045338-5 2012 We demonstrate that palmitoylation of cysteine residue(s) adjacent to the membrane-spanning domain promotes MAM enrichment of the transmembrane thioredoxin family protein TMX. Cysteine 38-46 thioredoxin related transmembrane protein 1 Homo sapiens 171-174 22244324-2 2012 (2012), who reveal that RelA (p65) sulfhydration, at its highly conserved cysteine 38 residue, regulates association with the coactivator RPS3, DNA binding, and antiapoptotic gene expression. Cysteine 74-82 ribosomal protein S3 Homo sapiens 138-142 22079049-6 2012 The structure of this newly characterized small cysteine-rich domain suggests potential involvement of JTB in interactions with proteins or extracellular matrix and may help to uncover the elusive biological functions of this protein. Cysteine 48-56 jumping translocation breakpoint Homo sapiens 103-106 22117067-2 2012 By transiently and stably expressing human-relevant mutants of Tamm-Horsfall protein in polarized Madin-Darby canine kidney cells, we show here that a cysteine-altering mutation in the evolutionally conserved cysteine-rich domain had more severe defects in ER exit and surface translocation and triggered more apoptosis than a cysteine-altering mutation outside the domain. Cysteine 151-159 uromodulin Homo sapiens 63-84 22117067-2 2012 By transiently and stably expressing human-relevant mutants of Tamm-Horsfall protein in polarized Madin-Darby canine kidney cells, we show here that a cysteine-altering mutation in the evolutionally conserved cysteine-rich domain had more severe defects in ER exit and surface translocation and triggered more apoptosis than a cysteine-altering mutation outside the domain. Cysteine 209-217 uromodulin Homo sapiens 63-84 22117067-2 2012 By transiently and stably expressing human-relevant mutants of Tamm-Horsfall protein in polarized Madin-Darby canine kidney cells, we show here that a cysteine-altering mutation in the evolutionally conserved cysteine-rich domain had more severe defects in ER exit and surface translocation and triggered more apoptosis than a cysteine-altering mutation outside the domain. Cysteine 209-217 uromodulin Homo sapiens 63-84 20401673-5 2012 For some proteins regulated by cysteine oxidation, the residues and molecular mechanism involved have been extensively studied and are well understood, such as the protein tyrosine phosphatase PTP1B and MAP3 kinase ASK1, as well as transcription factor complex Keap1-Nrf2. Cysteine 31-39 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 193-198 23177983-9 2012 For GLUT1, results from extensive mutagenesis, cysteine substitution and accessibility studies can be incorporated into a homology model with a barrel-like structure in which accessibility to the extracellular and intracellular medium is altered by pinching movements of some of the helices. Cysteine 47-55 solute carrier family 2 member 1 Homo sapiens 4-9 22489126-1 2012 Gamma glutamyl transpeptidase (GGT) is a transferase, which is of great importance in sustaining intracellular cysteine and glutathione levels. Cysteine 111-119 inactive glutathione hydrolase 2 Homo sapiens 0-29 22489126-1 2012 Gamma glutamyl transpeptidase (GGT) is a transferase, which is of great importance in sustaining intracellular cysteine and glutathione levels. Cysteine 111-119 inactive glutathione hydrolase 2 Homo sapiens 31-34 21374595-1 2012 Covalent adduction of a NO moiety to cysteines (S-nitrosylation or SNO) is a major route for NO to directly regulate protein functions. Cysteine 37-46 strawberry notch homolog 2 Homo sapiens 67-70 22052738-4 2012 Here, we found that Phe and Cys are important for peptide binding to IL-15Ralpha. Cysteine 28-31 interleukin 15 receptor subunit alpha Homo sapiens 69-80 22100634-2 2012 To develop peptide antagonists selectively inhibiting the function of Mac-1, we used a random constrained 6-mer (cys-6aa-cys) peptide library to map the structural features of CD11b, by determining the epitope of neutralizing monoclonal antibody mAb 44a (anti-CD11b). Cysteine 113-116 integrin subunit alpha M Homo sapiens 70-75 22100634-2 2012 To develop peptide antagonists selectively inhibiting the function of Mac-1, we used a random constrained 6-mer (cys-6aa-cys) peptide library to map the structural features of CD11b, by determining the epitope of neutralizing monoclonal antibody mAb 44a (anti-CD11b). Cysteine 121-124 integrin subunit alpha M Homo sapiens 70-75 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. Cysteine 4-7 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. Cysteine 4-7 thioredoxin 1 Mus musculus 112-115 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. Cysteine 13-16 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. Cysteine 13-16 thioredoxin 1 Mus musculus 112-115 20858066-6 2012 Two novel compounds we report (MP1 and MP2) covalently link ibuprofen and ketoprofen directly to the amide nitrogen of n-acetyl-glucosamine (NAG); the other compound (MP3) covalently links ibuprofen to the amide nitrogen, using a short chain acetyl linker. Cysteine 121-127 late endosomal/lysosomal adaptor, MAPK and MTOR activator 3 Homo sapiens 31-34 22080603-1 2012 Snakin-1 (SN1) is an antimicrobial cysteine-rich peptide isolated from potato (Solanum tuberosum) that was classified as a member of the Snakin/Gibberellic Acid Stimulated in Arabidopsis protein family. Cysteine 35-43 STSN1 Solanum tuberosum 0-8 22080603-1 2012 Snakin-1 (SN1) is an antimicrobial cysteine-rich peptide isolated from potato (Solanum tuberosum) that was classified as a member of the Snakin/Gibberellic Acid Stimulated in Arabidopsis protein family. Cysteine 35-43 STSN1 Solanum tuberosum 10-13 23226417-5 2012 Mutation of all four of ERp57"s active site cysteine residues blocked sensitivity to reducing agents, suggesting that redox-dependent conformational changes in ERp57 affect binding to RalA. Cysteine 44-52 RAS like proto-oncogene A Homo sapiens 184-188 23227172-2 2012 A fluorescent donor probe was introduced to unique and key cysteine residues on the C- and N-termini of cTnI. Cysteine 59-67 troponin I3, cardiac type Homo sapiens 104-108 23152803-6 2012 In the Tat/Env complex the cysteine-rich region of Tat engages the Env V3 loop, whereas the Tat RGD sequence remains free and directs the virus to integrins present on DCs. Cysteine 27-35 endogenous retrovirus group K member 20 Homo sapiens 11-14 23152803-6 2012 In the Tat/Env complex the cysteine-rich region of Tat engages the Env V3 loop, whereas the Tat RGD sequence remains free and directs the virus to integrins present on DCs. Cysteine 27-35 endogenous retrovirus group K member 20 Homo sapiens 67-70 23155404-10 2012 CB4856 contains a variation that affects the second exon of tac-1 causing a cysteine to tryptophan change at amino acid 94 also within the TACC domain. Cysteine 76-84 Transforming acid coiled-coil-containing protein 1 Caenorhabditis elegans 60-65 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. Cysteine 49-57 cystatin 8 (cystatin-related epididymal spermatogenic) Mus musculus 4-8 23185254-8 2012 The antibacterial and Anti-Uu activities were not impaired when the cysteine residues of CRES protein were mutated, indicating that the antimicrobial effect was not dependent on its disulfide bonds. Cysteine 68-76 cystatin 8 (cystatin-related epididymal spermatogenic) Mus musculus 89-93 23185364-4 2012 Here we show that the ezrin membrane-actin linker interacts with S endodomain through the F1 lobe of its FERM domain and that both the eight carboxy-terminal amino-acids and a membrane-proximal cysteine cluster of S endodomain are important for this interaction in vitro. Cysteine 194-202 ezrin Chlorocebus sabaeus 22-27 23071662-7 2012 In behavioral experiments, intraplantar administration of NaHS and L-cysteine evoked mechanical and cold hypersensitivities in Trpa1(+/+) but not in Trpa1(-/-) mice. Cysteine 67-77 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 127-132 23028758-1 2012 In humans and mice, the Cys(2)His(2) zinc finger protein PRDM9 binds to a DNA sequence motif enriched in hotspots of recombination, possibly modifying nucleosomes, and recruiting recombination machinery to initiate Double Strand Breaks (DSBs). Cysteine 24-27 PR domain containing 9 Mus musculus 57-62 22957097-7 2012 Comparing the protected epitopes of two stimulating TSHR-Abs we found both similarities and differences but both antibodies also contacted the hinge region and the amino terminus of the TSHR following the signal peptide and encompassing cysteine box 1 which has previously been shown to be important for TSH binding and activation. Cysteine 237-245 thyroid stimulating hormone receptor Homo sapiens 52-56 22957097-7 2012 Comparing the protected epitopes of two stimulating TSHR-Abs we found both similarities and differences but both antibodies also contacted the hinge region and the amino terminus of the TSHR following the signal peptide and encompassing cysteine box 1 which has previously been shown to be important for TSH binding and activation. Cysteine 237-245 thyroid stimulating hormone receptor Homo sapiens 186-190 22912718-3 2012 Here, we demonstrate that in cardiomyocytes, palmitoylation of beta(2)AR, the covalent acylation of cysteine residue 341, plays a critical role in shaping subcellular cAMP-PKA activities in cardiomyocytes via regulating beta(2)AR association with arrestin/PDE4D. Cysteine 100-108 adrenoceptor beta 2 Homo sapiens 63-72 22912718-3 2012 Here, we demonstrate that in cardiomyocytes, palmitoylation of beta(2)AR, the covalent acylation of cysteine residue 341, plays a critical role in shaping subcellular cAMP-PKA activities in cardiomyocytes via regulating beta(2)AR association with arrestin/PDE4D. Cysteine 100-108 adrenoceptor beta 2 Homo sapiens 220-229 22912718-3 2012 Here, we demonstrate that in cardiomyocytes, palmitoylation of beta(2)AR, the covalent acylation of cysteine residue 341, plays a critical role in shaping subcellular cAMP-PKA activities in cardiomyocytes via regulating beta(2)AR association with arrestin/PDE4D. Cysteine 100-108 phosphodiesterase 4D Homo sapiens 256-261 22912718-4 2012 Replacing cysteine 341 on beta(2)AR with alanine (C341A) leads to an impaired binding to beta arrestin 2. Cysteine 10-18 adrenoceptor beta 2 Homo sapiens 26-35 22761781-9 2012 The cellular and recombinant species of modified PRX3 were resistant to dithiothreitol and SDS and suppressed by NAC, indicating that TS covalently adducts cysteine residues in PRX3. Cysteine 156-164 X-linked Kx blood group Homo sapiens 113-116 22719858-4 2012 The results of substituted cysteine accessibility mapping studies support the novel concept that ligand-induced changes in the conformation of TM3 play a role in stabilizing GPCR. Cysteine 27-35 tropomyosin 3 Homo sapiens 143-146 21938521-0 2011 Single cysteines in the extracellular and transmembrane regions modulate pannexin 1 channel function. Cysteine 7-16 pannexin 1 L homeolog Xenopus laevis 73-83 21938521-4 2011 To further elucidate regulatory mechanisms, we substituted cysteine residues, expected key elements for channel function, in extracellular and transmembrane regions of Pannexin 1 (Panx1). Cysteine 59-67 pannexin 1 L homeolog Xenopus laevis 168-178 21938521-10 2011 From this, we conclude that cysteine residues of Panx1 reveal differential functional profiles for channel activation and drug sensitivity. Cysteine 28-36 pannexin 1 L homeolog Xenopus laevis 49-54 21813750-10 2011 We assessed the relationship of prestin oligomerization to cysteine position using fluorescence resonance energy transfer. Cysteine 59-67 solute carrier family 26 member 5 Homo sapiens 32-39 21740309-7 2011 In summary, VEGF stimulates localized formation of Cys-OH-IQGAP1 at the leading edge, thereby promoting directional EC migration, which may contribute to post-natal angiogenesis in vivo. Cysteine 51-54 vascular endothelial growth factor A Mus musculus 12-16 21763243-6 2011 Analysis of mutant forms of TRPA1 revealed that TNBS bound covalently to cysteine (and lysine) residues in the cytoplasmic N-terminus. Cysteine 73-81 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 28-33 21763243-7 2011 A stable sulfinic acid transformation of the cysteine-SH group, shown by mass spectrometry, might contribute to sustained sensitization of TRPA1. Cysteine 45-53 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 139-144 21771783-5 2011 We reveal that AKAP79 is palmitoylated via two cysteines in its N-terminal region. Cysteine 47-56 A-kinase anchoring protein 5 Homo sapiens 15-21 21771783-7 2011 Mutation of the two critical cysteines results in exclusion of AKAP79 from lipid rafts and alterations in its membrane diffusion behavior. Cysteine 29-38 A-kinase anchoring protein 5 Homo sapiens 63-69 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. Cysteine 70-73 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. Cysteine 78-81 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. Cysteine 78-81 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. Cysteine 78-81 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. Cysteine 78-81 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. Cysteine 78-81 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 50-59 21775125-0 2011 G-quadruplex DNAzyme-based Hg2+ and cysteine sensors utilizing Hg2+-mediated oligonucleotide switching. Cysteine 36-44 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 63-66 21715326-6 2011 The most selective variant (TM8) was used to generate a second library in which residues Cys(1)-Gln(9) were soft-randomized. Cysteine 89-92 tetraspanin 16 Homo sapiens 28-31 21773579-0 2011 Achieving cell penetration with distance-matching cysteine cross-linkers: a facile route to cell-permeable peptide dual inhibitors of Mdm2/Mdmx. Cysteine 50-58 MDM2 proto-oncogene Homo sapiens 134-138 21773579-2 2011 By cross-linking a peptide dual inhibitor of Mdm2/Mdmx containing cysteines at i,i+7 positions, dramatic enhancement in cell permeability was achieved, along with increased helicity and biological activity. Cysteine 66-75 MDM2 proto-oncogene Homo sapiens 45-49 22309020-2 2011 In the vascular system, H2S is synthesized from cysteine by cystathionine-gamma-lyase (CSE) in smooth muscle cells (SMC) and 3- mercaptopyruvate sulfuresterase (3MST) and CSE in the endothelial cells. Cysteine 48-56 cystathionine gamma-lyase Homo sapiens 60-85 22309020-2 2011 In the vascular system, H2S is synthesized from cysteine by cystathionine-gamma-lyase (CSE) in smooth muscle cells (SMC) and 3- mercaptopyruvate sulfuresterase (3MST) and CSE in the endothelial cells. Cysteine 48-56 cystathionine gamma-lyase Homo sapiens 87-90 21609323-7 2011 In addition, EWI2 is constitutively palmitoylated at the cytoplasmic cysteine residues located at the N-terminal of those basic residues. Cysteine 69-77 immunoglobulin superfamily member 8 Homo sapiens 13-17 21876369-2 2011 Recently, cysteine residue incorporation to HIV-1 Tat peptide increased liposomemediated transfection compared with unmodified Tat peptide. Cysteine 10-18 Tat Human immunodeficiency virus 1 50-53 21750812-0 2011 Two-photon ratiometric sensing of Hg2+ by using cysteine functionalized Ag nanoparticles. Cysteine 48-56 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 34-37 21107874-5 2011 Molecular genetic analysis identified a new missense mutation (c.608C>G) of KIF5A gene resulting in a serine to cysteine substitution, S203C, located in a highly conserved domain of the protein. Cysteine 112-120 kinesin family member 5A Homo sapiens 76-81 21385624-3 2011 Upon the exposure to electrophilic and oxidative stress, reactive cysteine residues in Keap1 are covalently modified, which abrogates the E3 ligase activity of the Cul3-Keap1 complex. Cysteine 66-74 kelch-like ECH-associated protein 1 Mus musculus 87-92 21385624-3 2011 Upon the exposure to electrophilic and oxidative stress, reactive cysteine residues in Keap1 are covalently modified, which abrogates the E3 ligase activity of the Cul3-Keap1 complex. Cysteine 66-74 kelch-like ECH-associated protein 1 Mus musculus 169-174 21507889-2 2011 Alignments of C31 integrase (Int) and its relatives indicate the presence of a conserved motif containing four cysteines resembling a zinc finger. Cysteine 111-120 inturned planar cell polarity protein Homo sapiens 29-32 21703357-7 2011 Since NO can modify the function or activity of target proteins through S-nitrosylation of cysteine, we attempted to investigate whether the cytoprotective effect of NO is mediated through Nrf2 activation by directly modifying cysteine residues of Keap1. Cysteine 227-235 Kelch-like ECH-associated protein 1 Rattus norvegicus 248-253 21636574-1 2011 Cysteine (C)-X-C motif chemokine receptor 4 (CXCR4), the primary receptor for stromal cell-derived factor-1 (SDF-1), is involved in bone morphogenic protein 2 (BMP2)-induced osteogenic differentiation of mesenchymal progenitors. Cysteine 0-8 chemokine (C-X-C motif) receptor 4 Mus musculus 45-50 21746906-0 2011 Exoplasmic cysteine Cys384 of the HDL receptor SR-BI is critical for its sensitivity to a small-molecule inhibitor and normal lipid transport activity. Cysteine 11-19 scavenger receptor class B member 1 Homo sapiens 47-52 21746906-4 2011 Here we show that BLT-1 is an irreversible inhibitor of SR-BI, raising the possibility that cysteine(s) in SR-BI interact with BLT-1. Cysteine 92-100 scavenger receptor class B member 1 Homo sapiens 56-61 21746906-4 2011 Here we show that BLT-1 is an irreversible inhibitor of SR-BI, raising the possibility that cysteine(s) in SR-BI interact with BLT-1. Cysteine 92-100 scavenger receptor class B member 1 Homo sapiens 107-112 21746906-5 2011 Mass spectrometric analysis of purified SR-BI showed two of its six exoplasmic cysteines have free thiol groups (Cys251 and Cys384). Cysteine 79-88 scavenger receptor class B member 1 Homo sapiens 40-45 21481189-2 2011 We show here that the mouse Dnmt3a DNA methyltransferase is able to transfer the methyl group from S-adenosyl-l-methionine (AdoMet) to a cysteine residue in its catalytic center. Cysteine 137-145 methionine adenosyltransferase I, alpha Mus musculus 99-122 21301863-4 2011 Here, employing voltage-clamped, inside-out patches from HEK293 cells expressing single, double and triple cysteine mutations in the BK(Ca) alpha-subunit, we test the hypothesis that CO regulation is conferred upon the channel by interactions with cysteine residues within the RCK2 domain. Cysteine 248-256 potassium calcium-activated channel subfamily M alpha 1 Homo sapiens 133-153 21384128-3 2011 To investigate if these domains interact during the NaPi-II transport cycle, we introduced novel cysteines at three functionally important sites associated with the predicted re-entrant domains of the flounder NaPi-IIb for the purpose of fluorescent labelling and cross-linking. Cysteine 97-106 solute carrier family 34 member 2 L homeolog Xenopus laevis 210-218 21256830-12 2011 As C227 has previously been identified as the reactive cysteine in CBR1, the variant CBR1 C227S was generated, which, in comparison to the wild-type protein, displayed a similar k(cat), but a 30-fold higher K(m), and did not show substrate inhibition. Cysteine 55-63 carbonyl reductase 1 Homo sapiens 67-71 21256830-12 2011 As C227 has previously been identified as the reactive cysteine in CBR1, the variant CBR1 C227S was generated, which, in comparison to the wild-type protein, displayed a similar k(cat), but a 30-fold higher K(m), and did not show substrate inhibition. Cysteine 55-63 carbonyl reductase 1 Homo sapiens 85-89 21555563-4 2011 Bacteria-mediated ROS generation induces oxidation of target cysteines in the redox-sensitive tyrosine phosphatases, LMW-PTP and SHP-2, which in turn results in increased phosphorylation of focal adhesion kinase (FAK), a key protein regulating the turnover of FAs. Cysteine 61-70 acid phosphatase 1 Homo sapiens 117-124 21555563-4 2011 Bacteria-mediated ROS generation induces oxidation of target cysteines in the redox-sensitive tyrosine phosphatases, LMW-PTP and SHP-2, which in turn results in increased phosphorylation of focal adhesion kinase (FAK), a key protein regulating the turnover of FAs. Cysteine 61-70 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 129-134 21593323-2 2011 Free cysteine is then taken up by neurons through excitatory amino acid transporter 3 [EAAT3; also termed Slc1a1 (solute carrier family 1 member 1)] to support de novo glutathione synthesis. Cysteine 5-13 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 87-92 21593323-2 2011 Free cysteine is then taken up by neurons through excitatory amino acid transporter 3 [EAAT3; also termed Slc1a1 (solute carrier family 1 member 1)] to support de novo glutathione synthesis. Cysteine 5-13 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 106-112 21593323-2 2011 Free cysteine is then taken up by neurons through excitatory amino acid transporter 3 [EAAT3; also termed Slc1a1 (solute carrier family 1 member 1)] to support de novo glutathione synthesis. Cysteine 5-13 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 114-146 20518849-10 2011 Recombinant human cardiac MLC1 was additionally nitrosylated at cysteine 67 and 76 corresponding to cysteine 81 of rat MLC1. Cysteine 64-72 modulator of VRAC current 1 Rattus norvegicus 26-30 20518849-10 2011 Recombinant human cardiac MLC1 was additionally nitrosylated at cysteine 67 and 76 corresponding to cysteine 81 of rat MLC1. Cysteine 100-108 modulator of VRAC current 1 Rattus norvegicus 26-30 21139629-2 2011 Excitatory amino-acid transporter type 3 (EAAT3) is the major neuronal EAAT and also uptakes cysteine, the rate-limiting substrate for synthesis of glutathione. Cysteine 93-101 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 0-40 21139629-2 2011 Excitatory amino-acid transporter type 3 (EAAT3) is the major neuronal EAAT and also uptakes cysteine, the rate-limiting substrate for synthesis of glutathione. Cysteine 93-101 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 42-47 21145939-0 2011 Redox state of troponin C cysteine in the D/E helix alters the C-domain affinity for the thin filament of vertebrate striated muscle. Cysteine 26-34 tenascin Oryctolagus cuniculus 15-25 21275893-2 2011 In the vasculature, cystathionine-gamma-lyase (CSE) is the main enzyme responsible for H(2)S biosynthesis starting from the substrate e.g. L-cysteine. Cysteine 139-149 cystathionine gamma-lyase Homo sapiens 20-45 21275893-2 2011 In the vasculature, cystathionine-gamma-lyase (CSE) is the main enzyme responsible for H(2)S biosynthesis starting from the substrate e.g. L-cysteine. Cysteine 139-149 cystathionine gamma-lyase Homo sapiens 47-50 21275895-3 2011 The production of H(2)S from L-cysteine is catalysed primarily by two enzymes, cystathionine gamma-lyase and cystathionine beta-synthase. Cysteine 29-39 cystathionine gamma-lyase Homo sapiens 79-104 21228277-3 2011 The C-terminal catalytic domain is similar to UfSP1 with Cys(294), Asp(418), His(420), Tyr(282), and a regulatory loop participating in catalysis. Cysteine 57-60 UFM1-specific peptidase 1 Mus musculus 46-51 21329673-0 2011 The cysteine-rich domain of human T1R3 is necessary for the interaction between human T1R2-T1R3 sweet receptors and a sweet-tasting protein, thaumatin. Cysteine 4-12 taste 1 receptor member 2 Homo sapiens 86-90 20967800-4 2011 Chemical synthesis of hBD28 rendered extremely poor yields due to inefficient cysteine oxidation. Cysteine 78-86 defensin beta 128 Homo sapiens 22-27 21354971-9 2011 Furthermore, the immediate metabolite of dimethylfumarate, monomethylfumarate, leads to direct modification of the inhibitor of nuclear factor (erythroid-derived 2)-related factor 2, Kelch-like ECH-associated protein 1, at cysteine residue 151. Cysteine 223-231 kelch-like ECH-associated protein 1 Mus musculus 144-218 21370512-19 2004 (19) prepared a Cys-tagged vector of VEGF121 by cloning two single-chain 3-112 amino acid fragments of VEGF121 joining head-to-tail to express as scVEGF, which binds to VEGFR-2. Cysteine 16-19 kinase insert domain receptor Homo sapiens 169-176 21345212-5 2011 To test the model, we created spe-42 transgenes coding for mutations in each of the 8 cysteine residues predicted to coordinate Zn++ ions in the RING finger motif. Cysteine 86-94 DC_STAMP domain-containing protein Caenorhabditis elegans 30-36 21131483-6 2011 L-cysteine, the substrate of the H2S-producing enzymes cystathionine gamma-lyase (CSE) and cystathionine beta-synthase (CBS), also dilated pial arterioles. Cysteine 0-10 cystathionine gamma-lyase Sus scrofa 55-80 21131483-6 2011 L-cysteine, the substrate of the H2S-producing enzymes cystathionine gamma-lyase (CSE) and cystathionine beta-synthase (CBS), also dilated pial arterioles. Cysteine 0-10 cystathionine gamma-lyase Sus scrofa 82-85 21131483-7 2011 The dilation to L-cysteine was blocked by the CSE inhibitor d,l-propargylglycine (PPG, 10 mM) but was unaffected by the CBS inhibitor amino-oxyacetate (AOA, 1 mM). Cysteine 16-26 cystathionine gamma-lyase Sus scrofa 46-49 20971157-0 2011 Functional and structural evaluation of cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT). Cysteine 40-48 arsenite methyltransferase Homo sapiens 71-117 20971157-0 2011 Functional and structural evaluation of cysteine residues in the human arsenic (+3 oxidation state) methyltransferase (hAS3MT). Cysteine 40-48 arsenite methyltransferase Homo sapiens 119-125 20971157-2 2011 There are fourteen cysteine residues in the human AS3MT (hAS3MT), among which twelve are absolutely conserved; Cys334 and Cys360 are unique; Cys368 and Cys369 are identified as a CysCys pair. Cysteine 19-27 arsenite methyltransferase Homo sapiens 50-55 20971157-2 2011 There are fourteen cysteine residues in the human AS3MT (hAS3MT), among which twelve are absolutely conserved; Cys334 and Cys360 are unique; Cys368 and Cys369 are identified as a CysCys pair. Cysteine 19-27 arsenite methyltransferase Homo sapiens 57-63 20971157-3 2011 The roles of several conserved cysteine residues in rat AS3MT and hAS3MT have been reported. Cysteine 31-39 arsenite methyltransferase Rattus norvegicus 56-61 20971157-3 2011 The roles of several conserved cysteine residues in rat AS3MT and hAS3MT have been reported. Cysteine 31-39 arsenite methyltransferase Homo sapiens 66-72 20971157-9 2011 Additionally, all these cysteine residues except Cys375 affect the thermotropic properties of the hAS3MT. Cysteine 24-32 arsenite methyltransferase Homo sapiens 98-104 20440617-2 2011 Dekant has proposed that gamma-glutamyl transpeptidase (GGT), aminopeptidase N (APN) and cysteine-conjugate-beta-lyase (CCBL) comprise a multi-enzyme pathway that acts on xenobiotic-glutathione conjugates converting them to nephrotoxic metabolites. Cysteine 89-97 inactive glutathione hydrolase 2 Homo sapiens 25-54 21105877-6 2011 Cysteine-scanning mutagenesis shows that as long as a single cysteine residue (out of a total of 13 per monomer) remains in TPH2, it cross-links upon oxidation and only cysteine-less mutants are resistant to this effect. Cysteine 0-8 tryptophan hydroxylase 2 Homo sapiens 124-128 21105877-6 2011 Cysteine-scanning mutagenesis shows that as long as a single cysteine residue (out of a total of 13 per monomer) remains in TPH2, it cross-links upon oxidation and only cysteine-less mutants are resistant to this effect. Cysteine 61-69 tryptophan hydroxylase 2 Homo sapiens 124-128 21105877-6 2011 Cysteine-scanning mutagenesis shows that as long as a single cysteine residue (out of a total of 13 per monomer) remains in TPH2, it cross-links upon oxidation and only cysteine-less mutants are resistant to this effect. Cysteine 169-177 tryptophan hydroxylase 2 Homo sapiens 124-128 21105877-10 2011 The propensity of TPH2 to misfold upon oxidation of its cysteine residues is responsible for its catalytic lability and may be related to loss of serotonin neuronal function in PD and the emergence of non-motor (psychiatric) symptoms. Cysteine 56-64 tryptophan hydroxylase 2 Homo sapiens 18-22 21185901-1 2011 The neuronal Na(+)-dependent glutamate transporter, excitatory amino acid carrier 1 (EAAC1, also called EAAT3), has been implicated in the control of synaptic spillover of glutamate, synaptic plasticity, and the import of cysteine for neuronal synthesis of glutathione. Cysteine 222-230 solute carrier family 1 member 1 Rattus norvegicus 52-83 21185901-1 2011 The neuronal Na(+)-dependent glutamate transporter, excitatory amino acid carrier 1 (EAAC1, also called EAAT3), has been implicated in the control of synaptic spillover of glutamate, synaptic plasticity, and the import of cysteine for neuronal synthesis of glutathione. Cysteine 222-230 solute carrier family 1 member 1 Rattus norvegicus 85-90 21185901-1 2011 The neuronal Na(+)-dependent glutamate transporter, excitatory amino acid carrier 1 (EAAC1, also called EAAT3), has been implicated in the control of synaptic spillover of glutamate, synaptic plasticity, and the import of cysteine for neuronal synthesis of glutathione. Cysteine 222-230 solute carrier family 1 member 1 Rattus norvegicus 104-109 21124317-5 2011 LMO1 encodes a cysteine-rich transcriptional regulator, and its paralogues (LMO2, LMO3 and LMO4) have each been previously implicated in cancer. Cysteine 15-23 LIM domain only 4 Homo sapiens 91-95 20518697-5 2011 As the sulfenate labeling is lost, the Cys-149 sulfinic/sulfonic acid oxidation states of GAPDH appear. Cysteine 39-42 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 90-95 20518697-8 2011 The selective GAPDH inhibitor koningic acid (which functions by forming a covalent adduct at Cys-149) fully prevented basal SOH labeling, as well as subsequent peroxide-induced hyperoxidation. Cysteine 93-96 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 14-19 21278127-4 2011 PDIL2;3 knockdown inhibited the accumulation of Cys-rich 10-kD prolamin (crP10) in the core of PB-I. Cysteine 48-51 submaxillary gland androgen regulated protein 3A Homo sapiens 95-99 22145046-7 2011 CONCLUSION/SIGNIFICANCE: These results demonstrate that VEGF induces cysteine oxidation in VEGFR-2 and c-Src in an NADPH oxidase-derived ROS-dependent manner, suggesting that VEGFR-2 and c-Src can "sense" redox levels in ECs. Cysteine 69-77 kinase insert domain receptor Homo sapiens 91-98 22145046-7 2011 CONCLUSION/SIGNIFICANCE: These results demonstrate that VEGF induces cysteine oxidation in VEGFR-2 and c-Src in an NADPH oxidase-derived ROS-dependent manner, suggesting that VEGFR-2 and c-Src can "sense" redox levels in ECs. Cysteine 69-77 kinase insert domain receptor Homo sapiens 175-182 21337007-3 2011 Molecular modeling in this review shows that IL-17s may adopt a "cysteine knot" fold commonly seen in nerve growth factor (NGF) and other neurotrophins. Cysteine 65-73 interleukin 17A Homo sapiens 45-50 20923703-13 2010 CP"s putative GSH-peroxidase activity can thus provide cytoprotection but is possibly affected by the S-nitrosation of a catalytically important cysteine residue. Cysteine 145-153 ceruloplasmin and hephaestin like 1 Bos taurus 0-2 21116635-0 2010 Melody, an ENU mutation in Caspase 3, alters the catalytic cysteine residue and causes sensorineural hearing loss in mice. Cysteine 59-67 caspase 3 Mus musculus 27-36 21131558-8 2010 Deletion of a C-terminal metallothionein-like Cys-rich domain impacted neither nutritional copper signaling nor the effect of mercuric supplementation, but rendered CRR1 insensitive to hypoxia and to nickel supplementation, which normally activate the copper deficiency regulon in wild-type cells. Cysteine 46-49 uncharacterized protein Chlamydomonas reinhardtii 165-169 20855893-5 2010 GCK inactivation and down-regulation were predominantly mediated by ethanol metabolism-generated peroxynitrite, which were suppressed by the peroxynitrite scavengers N(gamma)-monomethyl-L-arginine, uric acid, and deferoxamine but not by the S-nitrosylation inhibitor DTT, indicating that tyrosine nitration is the predominant modification associated with GCK down-regulation and inactivation rather than S-nitrosylation of cysteine. Cysteine 423-431 glucokinase Homo sapiens 0-3 20831872-4 2010 This work explores the structural basis for receptor selectivity by studying chimeric proteins developed by interchanging loops between the cysteine-rich domain of ASIP and the cysteine-rich domain of AgRP. Cysteine 140-148 agouti signaling protein Homo sapiens 164-168 20831872-4 2010 This work explores the structural basis for receptor selectivity by studying chimeric proteins developed by interchanging loops between the cysteine-rich domain of ASIP and the cysteine-rich domain of AgRP. Cysteine 177-185 agouti related neuropeptide Homo sapiens 201-205 21084597-2 2010 EAAC1 uptake of cysteine provides substrate for neuronal glutathione synthesis, which plays a key role in both antioxidant defenses and intracellular zinc binding. Cysteine 16-24 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 0-5 21084597-8 2010 These findings suggest that cysteine uptake by EAAC1 is important for zinc homeostasis and neuronal antioxidant function under ischemic conditions. Cysteine 28-36 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 47-52 21124938-6 2010 The catalytic cysteine mutant PopP2-C321A is impaired in its avirulence activity although it is still able to interact with RRS1-R. Cysteine 14-22 Disease resistance protein (TIR-NBS-LRR class) Arabidopsis thaliana 124-128 21072368-1 2010 Sulfite oxidase (SO) is a molybdenum-cofactor-dependent enzyme that catalyzes the oxidation of sulfite to sulfate, the final step in the catabolism of the sulfur-containing amino acids, cysteine and methionine. Cysteine 186-194 sulfite oxidase Homo sapiens 0-15 21072368-1 2010 Sulfite oxidase (SO) is a molybdenum-cofactor-dependent enzyme that catalyzes the oxidation of sulfite to sulfate, the final step in the catabolism of the sulfur-containing amino acids, cysteine and methionine. Cysteine 186-194 sulfite oxidase Homo sapiens 17-19 20835883-4 2010 In this study, we introduced a Cys to Tyr mutation in the transmembrane domain of ZmERS1b and ZmETR2b that is present in the etr1-1 dominant negative mutant and expressed each protein in Arabidopsis. Cysteine 31-34 Signal transduction histidine kinase, hybrid-type, ethylene sensor Arabidopsis thaliana 125-129 20801176-2 2010 The virus-specific part of the replicase complex constitutes nonstructural proteins 1-4 (nsP1-nsP4) and is bound to cytoplasmic membranes by an amphipathic helix inside of nsP1 and through the palmitoylation of cysteine residues in nsP1. Cysteine 211-219 SH2 domain containing 3A Homo sapiens 89-93 20801176-2 2010 The virus-specific part of the replicase complex constitutes nonstructural proteins 1-4 (nsP1-nsP4) and is bound to cytoplasmic membranes by an amphipathic helix inside of nsP1 and through the palmitoylation of cysteine residues in nsP1. Cysteine 211-219 SH2 domain containing 3A Homo sapiens 172-176 20801176-2 2010 The virus-specific part of the replicase complex constitutes nonstructural proteins 1-4 (nsP1-nsP4) and is bound to cytoplasmic membranes by an amphipathic helix inside of nsP1 and through the palmitoylation of cysteine residues in nsP1. Cysteine 211-219 SH2 domain containing 3A Homo sapiens 172-176 20940320-2 2010 Here we report three crystal structures of human tetherin, including the full-length ectodomain, a triple cysteine mutant and an ectodomain truncation. Cysteine 106-114 bone marrow stromal cell antigen 2 Homo sapiens 49-57 20605785-7 2010 In addition, this is the first structure of a eukaryotic zinc-containing MsrB, which highlights the structural role of this metal ion bound to four conserved Cys. Cysteine 158-161 methionine sulfoxide reductase B2 Homo sapiens 73-77 20688912-6 2010 We identified cysteine 306, a juxtamembrane residue on transmembrane domain 6 (TM6) of DAT, as the intrinsic residue exhibiting enhanced reactivity. Cysteine 14-22 solute carrier family 6 member 3 Homo sapiens 87-90 20688912-7 2010 Similar effects on DAT cysteine accessibility and radioligand binding were observed with addition of zinc, a reagent known to promote the outward facing conformation of DAT. Cysteine 23-31 solute carrier family 6 member 3 Homo sapiens 19-22 20688912-7 2010 Similar effects on DAT cysteine accessibility and radioligand binding were observed with addition of zinc, a reagent known to promote the outward facing conformation of DAT. Cysteine 23-31 solute carrier family 6 member 3 Homo sapiens 169-172 20688912-8 2010 Using substituted cysteine mutants on various positions likely to be extracellular, we identified additional residues located on TM1, TM6, TM7, and TM12 of DAT that are sensitive to alterations in the membrane cholesterol content. Cysteine 18-26 solute carrier family 6 member 3 Homo sapiens 156-159 20837014-3 2010 The phospholipase active site possesses a structurally conserved Cys-His-His catalytic triad as found in NlpC/P60 peptidases, indicating H-REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. Cysteine 65-68 phospholipase A and acyltransferase 3 Homo sapiens 137-145 20563897-1 2010 A highly conserved region of 21 amino acids flanked by cysteine residues, contained within a larger repeated domain, has been proposed to be the antibody-binding site in the ovarian cancer biomarker CA125 (MUC16). Cysteine 55-63 mucin 16, cell surface associated Homo sapiens 199-204 20563897-1 2010 A highly conserved region of 21 amino acids flanked by cysteine residues, contained within a larger repeated domain, has been proposed to be the antibody-binding site in the ovarian cancer biomarker CA125 (MUC16). Cysteine 55-63 mucin 16, cell surface associated Homo sapiens 206-211 20440442-1 2010 Endogenous hydrogen sulfide (H(2)S) is naturally synthesized in many types of mammalian cells from L-cysteine in the reactions catalyzed by cystathionine-beta-synthase and cystathionine-gamma-lyase (CSE). Cysteine 99-109 cystathionine gamma-lyase Homo sapiens 172-197 20440442-1 2010 Endogenous hydrogen sulfide (H(2)S) is naturally synthesized in many types of mammalian cells from L-cysteine in the reactions catalyzed by cystathionine-beta-synthase and cystathionine-gamma-lyase (CSE). Cysteine 99-109 cystathionine gamma-lyase Homo sapiens 199-202 20666399-3 2010 In animals, SO catalyzes the oxidation of toxic sulfite to sulfate as the final step in the catabolism of the sulfur-containing amino acids, methionine and cysteine. Cysteine 156-164 sulfite oxidase Homo sapiens 12-14 20727192-0 2010 Increased expression of cysteine cathepsins in ovarian tissue from chickens with ovarian cancer. Cysteine 24-32 cathepsin S Gallus gallus 33-43 20727192-1 2010 BACKGROUND: Cysteine cathepsins (CTSs) are involved in the degradation and remodeling of the extracellular matrix and are associated with cell transformation, differentiation, motility, and adhesion. Cysteine 12-20 cathepsin S Gallus gallus 21-31 20727192-1 2010 BACKGROUND: Cysteine cathepsins (CTSs) are involved in the degradation and remodeling of the extracellular matrix and are associated with cell transformation, differentiation, motility, and adhesion. Cysteine 12-20 cathepsin S Gallus gallus 33-37 20566639-2 2010 However, premature infants or patients with hepatic failure may require dietary cysteine due to a lack of cystathionine gamma-lyase (CTH), a key trans-sulfuration enzyme. Cysteine 80-88 cystathionine gamma-lyase Homo sapiens 106-131 20566639-2 2010 However, premature infants or patients with hepatic failure may require dietary cysteine due to a lack of cystathionine gamma-lyase (CTH), a key trans-sulfuration enzyme. Cysteine 80-88 cystathionine gamma-lyase Homo sapiens 133-136 20600126-5 2010 The mutation of residues in the human MC4R--such as Leu106 of extracellular loop 1, and Asp122, Ile125, and Asp126 of transmembrane (TM) helix 3, His264 (TM6), and Met292 (TM7)--to Cys residues produced definitive indications of proximity to the side chains of residues in the core region of the peptide ligand. Cysteine 181-184 melanocortin 4 receptor Homo sapiens 38-42 20662535-19 2010 The chemical synthesis of the SH3-domain of SHO1 succeeded in highest yields when cysteine placements at positions S23, F24, and E36 were avoided. Cysteine 82-90 osmosensor SHO1 Saccharomyces cerevisiae S288C 44-48 20715853-5 2010 A DNA binding polyacridine peptide, Cys-(Acr-Lys)(4), was prepared by solid-phase peptide synthesis using Fmoc-Lys(Acr), then conjugated to the maleimide on the N-glycan to produce a glycopeptide. Cysteine 36-39 acrosin Cricetulus griseus 41-44 20715853-5 2010 A DNA binding polyacridine peptide, Cys-(Acr-Lys)(4), was prepared by solid-phase peptide synthesis using Fmoc-Lys(Acr), then conjugated to the maleimide on the N-glycan to produce a glycopeptide. Cysteine 36-39 acrosin Cricetulus griseus 115-118 20631078-6 2010 HERC2 ubiquitinates BRCA1; this reaction depends on Cys(4762) of HERC2, the catalytic ubiquitin binding site, and the degron of BRCA1. Cysteine 52-55 BRCA1 DNA repair associated Homo sapiens 20-25 20614171-1 2010 Mitochondrial membrane carriers containing proline and cysteine, such as adenine nucleotide translocase (ANT), are potential targets of cyclophilin D (CyP-D) and potential Ca(2+)-induced permeability transition pore (PTP) components or regulators; CyP-D, a mitochondrial peptidyl-prolyl cis-trans isomerase, is the probable target of the PTP inhibitor cyclosporine A (CsA). Cysteine 55-63 peptidylprolyl isomerase D Rattus norvegicus 136-149 20614171-1 2010 Mitochondrial membrane carriers containing proline and cysteine, such as adenine nucleotide translocase (ANT), are potential targets of cyclophilin D (CyP-D) and potential Ca(2+)-induced permeability transition pore (PTP) components or regulators; CyP-D, a mitochondrial peptidyl-prolyl cis-trans isomerase, is the probable target of the PTP inhibitor cyclosporine A (CsA). Cysteine 55-63 peptidylprolyl isomerase D Rattus norvegicus 151-156 20614171-1 2010 Mitochondrial membrane carriers containing proline and cysteine, such as adenine nucleotide translocase (ANT), are potential targets of cyclophilin D (CyP-D) and potential Ca(2+)-induced permeability transition pore (PTP) components or regulators; CyP-D, a mitochondrial peptidyl-prolyl cis-trans isomerase, is the probable target of the PTP inhibitor cyclosporine A (CsA). Cysteine 55-63 peptidylprolyl isomerase D Rattus norvegicus 248-253 20464001-8 2010 In contrast, hMGL titration with NAM, which leads to cysteine alkylation, stoichiometrically decreases the population of the active-site hydrogen bonds. Cysteine 53-61 monoglyceride lipase Homo sapiens 13-17 20493880-7 2010 Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. Cysteine 6-14 zinc finger and BTB domain containing 16 Homo sapiens 52-86 20493880-7 2010 Using cysteine cross-linking, we confirmed that the promyelocytic leukemia zinc finger (PLZF) BTB dimer is strand exchanged in solution, while the FAZF BTB dimer is not. Cysteine 6-14 zinc finger and BTB domain containing 16 Homo sapiens 88-92 20516068-5 2010 Mutation of all four evolutionarily conserved cysteines abolished KCC2 transport activity. Cysteine 46-55 solute carrier family 12 member 5 Homo sapiens 66-70 20467693-3 2010 In order to build up a rational for the observed differences, DFT calculations of the metal complexes adducts with N-acetyl-l-cysteine-N"-methylamide, a mimic for the Cys residue in the cathepsin B active site, were performed to provide insights into binding thermodynamics in solution. Cysteine 167-170 cathepsin B Homo sapiens 186-197 20460109-4 2010 ADAM19 has an autolytic processing activity within its Cys domain, and the processing is necessary for its proteolytic activity. Cysteine 55-58 ADAM metallopeptidase domain 19 Homo sapiens 0-6 20460109-6 2010 Cysteine-rich protein 2 (CRIP2) showed an association with ADAM19 through its DI and Cys domains. Cysteine 0-3 cysteine rich protein 2 Homo sapiens 25-30 20460109-6 2010 Cysteine-rich protein 2 (CRIP2) showed an association with ADAM19 through its DI and Cys domains. Cysteine 0-3 ADAM metallopeptidase domain 19 Homo sapiens 59-65 20498052-4 2010 We found that NOX2 mediates the inhibition of phagosomal proteolysis in macrophages through reversible oxidative inactivation of local cysteine cathepsins. Cysteine 135-143 cytochrome b-245 beta chain Homo sapiens 14-18 20498052-6 2010 These findings indicate that NOX2 oxidatively inactivates cysteine cathepsins through sustained ablation of the reductive capacity of the phagosomal lumen. Cysteine 58-66 cytochrome b-245 beta chain Homo sapiens 29-33 20385560-6 2010 Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70. Cysteine 88-91 histone deacetylase 9 Homo sapiens 137-156 20385560-6 2010 Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70. Cysteine 88-91 histone deacetylase 9 Homo sapiens 100-104 20385560-6 2010 Covalent modification at two conserved cysteine residues, corresponding to Cys(261) and Cys(273) in HDAC1, coincided with attenuation of histone deacetylase activity, changes in histone H3 and H4 acetylation patterns, derepression of a LEF1.beta-catenin model system, and transcription of HDAC-repressed genes, e.g. heme oxygenase-1 (HO-1), Gadd45, and HSP70. Cysteine 88-91 heat shock protein family A (Hsp70) member 4 Homo sapiens 353-358 20420839-2 2010 In vitro studies demonstrated that treatment of CaMKI with diamide and glutathione results in inactivation of the enzyme, with a concomitant S-glutathionylation of CaMKI at Cys(179) detected by mass spectrometry. Cysteine 173-176 calcium/calmodulin dependent protein kinase I Homo sapiens 48-53 20420839-2 2010 In vitro studies demonstrated that treatment of CaMKI with diamide and glutathione results in inactivation of the enzyme, with a concomitant S-glutathionylation of CaMKI at Cys(179) detected by mass spectrometry. Cysteine 173-176 calcium/calmodulin dependent protein kinase I Homo sapiens 164-169 20420839-3 2010 Mutagenesis studies confirmed that S-glutathionylation of Cys(179) is both necessary and sufficient for the inhibition of CaMKI by diamide and glutathione. Cysteine 58-61 calcium/calmodulin dependent protein kinase I Homo sapiens 122-127 20420839-6 2010 Thus, our results indicate that the reversible regulation of CaMKI via its modification at Cys(179) is an important mechanism in processing calcium signal transduction in cells. Cysteine 91-94 calcium/calmodulin dependent protein kinase I Homo sapiens 61-66 19967419-0 2010 Mimetics of the disulfide bridge between the N- and C-terminal cysteines of the KLK3-stimulating peptide B-2. Cysteine 63-72 immunoglobulin kappa variable 5-2 Homo sapiens 105-108 20503371-1 2010 The six mammalian CCN genes (Cyr61, CTGF, Nov, WISP1, WISP2, WISP3) encode a family of secreted, cysteine-rich, multimodular proteins having roles in cell proliferation, adhesion, migration, and differentiation during embryogenesis, wound healing, and angiogenesis. Cysteine 97-105 cellular communication network factor 4 Homo sapiens 47-52 20211273-11 2010 These data indicate that both native MUC17 and the exogenous recombinant cysteine-rich domain of MUC17 play a role in diverse cellular mechanisms related to cell restitution, and suggest a potential role for MUC17-CRD1-L-CRD2 recombinant protein in the treatment of mucosal inflammatory diseases. Cysteine 73-81 mucin 17, cell surface associated Homo sapiens 97-102 20211273-11 2010 These data indicate that both native MUC17 and the exogenous recombinant cysteine-rich domain of MUC17 play a role in diverse cellular mechanisms related to cell restitution, and suggest a potential role for MUC17-CRD1-L-CRD2 recombinant protein in the treatment of mucosal inflammatory diseases. Cysteine 73-81 mucin 17, cell surface associated Homo sapiens 97-102 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. Cysteine 6-14 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 93-98 20439747-2 2010 The mechanism of action of sulforaphane is believed to involve modifications of critical cysteine residues of Keap1, which lead to stabilization of Nrf2 to activate the antioxidant response element of phase 2 enzymes. Cysteine 89-97 kelch-like ECH-associated protein 1 Mus musculus 110-115 20439747-7 2010 We further show in living cells that a sulfoxythiocarbamate analog can label Keap1 on several key cysteine residues as well as other cellular proteins offering new insights into the mechanism of chemoprotection. Cysteine 98-106 kelch-like ECH-associated protein 1 Mus musculus 77-82 20236928-4 2010 The transition state analog for the first catalytic step comprises a ternary complex between the catalytic cysteine of PTP1B, vanadate, and the peptide DADEYL, a fragment of a physiological substrate. Cysteine 107-115 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 119-124 20236928-5 2010 The equatorial vanadate oxygen atoms bind to the P-loop, and the apical positions are occupied by the peptide tyrosine oxygen and by the PTP1B cysteine sulfur atom. Cysteine 143-151 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 137-142 20402461-3 2010 We show here that the C2A domain of Synaptotagmin-I, which had been fluorescently labeled at a single cysteine residue introduced by site-directed mutagenesis, detected the same levels of cell death as a similarly labeled Annexin-V derivative, in drug-treated murine lymphoma and human breast cancer cell lines in vitro. Cysteine 102-110 synaptotagmin I Mus musculus 36-51 19803741-1 2010 Hydrogen sulfide (H(2)S) is an important signaling molecule produced from L-cysteine by cystathionine beta-synthetase (CBS) or cystathionine gamma-lyase (CSE). Cysteine 74-84 cystathionine gamma-lyase Homo sapiens 127-152 19803741-1 2010 Hydrogen sulfide (H(2)S) is an important signaling molecule produced from L-cysteine by cystathionine beta-synthetase (CBS) or cystathionine gamma-lyase (CSE). Cysteine 74-84 cystathionine gamma-lyase Homo sapiens 154-157 20236937-8 2010 Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction. Cysteine 185-188 methionine sulfoxide reductase B 1 Arabidopsis thaliana 118-123 20236937-8 2010 Protein electrophoresis analyses coupled to mass spectrometry revealed that CDSP32 forms a heterodimeric complex with MSRB1 via reduction of the sulfenic acid formed on MSRB1 catalytic Cys after MetSO reduction. Cysteine 185-188 methionine sulfoxide reductase B 1 Arabidopsis thaliana 169-174 20357106-7 2010 Uptake of extracellular cysteine through the glutamate/cysteine transporter EAAC1 is required for de novo synthesis of glutathione in neurons. Cysteine 24-32 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 76-81 20357106-10 2010 Enhancement of Rab11 activity by expression of a dominant-active Rab11 mutant in primary HD neurons ameliorated the deficit in cysteine uptake, increased levels of intracellular glutathione, normalized clearance of ROS, and improved neuronal survival. Cysteine 127-135 RAB11A, member RAS oncogene family Mus musculus 15-20 20357106-10 2010 Enhancement of Rab11 activity by expression of a dominant-active Rab11 mutant in primary HD neurons ameliorated the deficit in cysteine uptake, increased levels of intracellular glutathione, normalized clearance of ROS, and improved neuronal survival. Cysteine 127-135 RAB11A, member RAS oncogene family Mus musculus 65-70 20357106-11 2010 Our data support a novel mechanism for oxidative stress in HD: Rab11 dysfunction slows trafficking of EAAC1 to the cell surface and impairs cysteine uptake, thereby leading to deficient synthesis of glutathione. Cysteine 140-148 RAB11A, member RAS oncogene family Mus musculus 63-68 20354224-6 2010 The differential redox sensitivity of ORAI1 and ORAI3 channels depended mainly on an extracellularly located reactive cysteine, which is absent in ORAI3. Cysteine 118-126 ORAI calcium release-activated calcium modulator 1 Homo sapiens 38-43 20166696-3 2010 Both Atox1 and WD4 have solvent-exposed metal-binding motifs with two Cys residues that coordinate Cu(I). Cysteine 70-73 antioxidant 1 copper chaperone Homo sapiens 5-10 20166696-6 2010 Next, with an activation barrier of about 9.5 kcal/mol, a second 3-coordinated intermediate forms that involves both of the Cys residues in WD4 and Cys1 of Atox1. Cysteine 124-127 antioxidant 1 copper chaperone Homo sapiens 156-161 20089835-0 2010 Role of the second cysteine-rich domain and Pro275 in protein kinase D2 interaction with ADP-ribosylation factor 1, trans-Golgi network recruitment, and protein transport. Cysteine 19-27 ADP ribosylation factor 1 Homo sapiens 89-114 20089835-5 2010 ARF1, but not ARF6, binds directly to the second cysteine-rich domain (C1b) of PKD2, and precisely to Pro275 within this domain. Cysteine 49-57 ADP ribosylation factor 1 Homo sapiens 0-4 20048155-5 2010 Consequently, we demonstrate that WFA covalently binds soluble recombinant tetrameric human GFAP at cysteine 294. Cysteine 100-108 glial fibrillary acidic protein Homo sapiens 92-96 20641826-8 2004 (7)) and used the modified protein (cys-annexin A5) to generate HYNIC-cys-annexin A5 (3). Cysteine 36-39 annexin A5 Mus musculus 40-50 20165970-3 2010 A highly conserved cysteine in their active site is post-translationally converted into formylglycine by the formylglycine-generating enzyme encoded by SUMF1 (sulfatase modifying factor 1). Cysteine 19-27 sulfatase modifying factor 1 Homo sapiens 152-157 20165970-3 2010 A highly conserved cysteine in their active site is post-translationally converted into formylglycine by the formylglycine-generating enzyme encoded by SUMF1 (sulfatase modifying factor 1). Cysteine 19-27 sulfatase modifying factor 1 Homo sapiens 159-187 19941843-4 2010 RESULTS: The NO donor compounds nitrosocysteine, nitrosoarginine and diethylamine caused strong inhibition on normal and defective G6PD activities, while a similar inhibition was observed only at higher concentrations of the sulfhydryl blocking agents: 2-mercaptoethanol , cysteine and reduced glutathione. Cysteine 39-47 glucose-6-phosphate dehydrogenase Homo sapiens 131-135 20087392-0 2010 The cys-loop ligand-gated ion channel gene superfamily of the parasitoid wasp, Nasonia vitripennis. Cysteine 4-7 WASp Drosophila melanogaster 73-77 20016000-3 2010 Here we demonstrate that the interaction of gp55 with Sf-Stk is dependent on cysteine residues in the ecotropic domain of gp55 and the extracellular domain of Sf-Stk. Cysteine 77-85 neuroplastin Homo sapiens 44-48 20016000-3 2010 Here we demonstrate that the interaction of gp55 with Sf-Stk is dependent on cysteine residues in the ecotropic domain of gp55 and the extracellular domain of Sf-Stk. Cysteine 77-85 neuroplastin Homo sapiens 122-126 20016000-4 2010 Point mutation of these cysteine residues or deletion of these domains inhibits the ability of gp55 to interact with Sf-Stk, resulting in the inability of these proteins to promote the Epo-independent growth of erythroid progenitor cells. Cysteine 24-32 neuroplastin Homo sapiens 95-99 20016000-7 2010 These data suggest that the cysteines in the extracellular domains of Sf-Stk and Sf-Ron may also mediate the interaction of these truncated receptors with other cellular factors that regulate their ability to promote cytokine-independent growth. Cysteine 28-37 macrophage stimulating 1 receptor Homo sapiens 84-87 20110468-5 2010 Moreover, Doa10 also recognized the Nt-acetylated Ala, Val, Ser, Thr, and Cys residues. Cysteine 74-77 E3 ubiquitin-protein ligase SSM4 Saccharomyces cerevisiae S288C 10-15 20137774-4 2010 Grxcr1 encodes a 290 amino acid protein that contains a region of similarity to glutaredoxin proteins and a cysteine-rich region at its C terminus. Cysteine 108-116 glutaredoxin, cysteine rich 1 Mus musculus 0-6 19911200-9 2010 A homozygous cysteine to serine change in CCBE1 has been identified in the proband, in a residue that is conserved across species. Cysteine 13-21 collagen and calcium binding EGF domains 1 Danio rerio 42-47 20014444-5 2010 Rabbit GAPDH with a reversibly protected catalytic cysteine was nitrated in vitro with tetranitromethane, resulting in complete loss of GAPDH catalytic activity. Cysteine 51-59 glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus 7-12 20014444-5 2010 Rabbit GAPDH with a reversibly protected catalytic cysteine was nitrated in vitro with tetranitromethane, resulting in complete loss of GAPDH catalytic activity. Cysteine 51-59 glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus 136-141 19955605-0 2010 L-cysteine functionalized gold nanoparticles for the colorimetric detection of Hg2+ induced by ultraviolet light. Cysteine 0-10 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 79-82 19825391-0 2010 Identification of the reactive cysteine residues in yeast dipeptidyl peptidase III. Cysteine 31-39 dipeptidyl-peptidase III Saccharomyces cerevisiae S288C 58-82 20012955-3 2010 IgA of the Igh-2(a) allotype was found to be unique in its total lack of a covalent bond between alpha and L: -chains, formation of which apparently depends on the presence of an "extra" Cys in the hinges of all of the other five allotypes. Cysteine 187-190 immunoglobulin heavy constant alpha Mus musculus 0-3 20012955-3 2010 IgA of the Igh-2(a) allotype was found to be unique in its total lack of a covalent bond between alpha and L: -chains, formation of which apparently depends on the presence of an "extra" Cys in the hinges of all of the other five allotypes. Cysteine 187-190 immunoglobulin heavy constant alpha Mus musculus 11-16 19661234-9 2010 Molecular genetic analysis revealed a novel missense mutation of ZNF469, c.10016G>A, that was predicted to affect the fourth of the five zinc finger domains of ZNF469 by changing the first cysteine to a tyrosine (p.Cys3339Tyr). Cysteine 192-200 zinc finger protein 469 Homo sapiens 65-71 19661234-9 2010 Molecular genetic analysis revealed a novel missense mutation of ZNF469, c.10016G>A, that was predicted to affect the fourth of the five zinc finger domains of ZNF469 by changing the first cysteine to a tyrosine (p.Cys3339Tyr). Cysteine 192-200 zinc finger protein 469 Homo sapiens 163-169 19950243-5 2010 However, one peptide with a mutation at the P5 position (methionine to cysteine) resulted in a significant enhanced binding to HLA A*0201 and also an increase in cell surface expression over the wild-type peptide but was unable to engage with the CD8 TCR and trigger IFNgamma production. Cysteine 71-79 CD8a molecule Homo sapiens 247-250 19808700-0 2010 Critical cysteine residues of Kelch-like ECH-associated protein 1 in arsenic sensing and suppression of nuclear factor erythroid 2-related factor 2. Cysteine 9-17 kelch-like ECH-associated protein 1 Mus musculus 30-65 20694660-5 2010 When cells are exposed to chemopreventive agents and oxidative stress, a signal involving phosphorylation and/or redox modification of critical cysteine residues in Keap1 inhibits the enzymatic activity of the Keap1-Cul3-Rbx1 E3 ubiquitin ligase complex, resulting in decreased Nrf2 ubiquitination and degradation. Cysteine 144-152 ring-box 1 Homo sapiens 221-225 19969520-1 2010 The Arabidopsis FCLY gene encodes a specific farnesylcysteine (FC) lyase, which is responsible for the oxidative metabolism of FC to farnesal and cysteine. Cysteine 53-61 farnesylcysteine lyase Arabidopsis thaliana 16-20 20026652-0 2009 A novel intermembrane space-targeting signal docks cysteines onto Mia40 during mitochondrial oxidative folding. Cysteine 51-60 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 66-71 20026652-1 2009 Mia40 imports Cys-containing proteins into the mitochondrial intermembrane space (IMS) by ensuring their Cys-dependent oxidative folding. Cysteine 14-17 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 0-5 20026652-1 2009 Mia40 imports Cys-containing proteins into the mitochondrial intermembrane space (IMS) by ensuring their Cys-dependent oxidative folding. Cysteine 105-108 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 0-5 20026652-2 2009 In this study, we show that the specific Cys of the substrate involved in docking with Mia40 is substrate dependent, the process being guided by an IMS-targeting signal (ITS) present in Mia40 substrates. Cysteine 41-44 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 87-92 20026652-2 2009 In this study, we show that the specific Cys of the substrate involved in docking with Mia40 is substrate dependent, the process being guided by an IMS-targeting signal (ITS) present in Mia40 substrates. Cysteine 41-44 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 186-191 20026652-4 2009 We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys. Cysteine 206-209 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 36-41 20026652-4 2009 We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys. Cysteine 206-209 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 242-247 20026652-4 2009 We rationalize the dual function of Mia40 as a receptor and an oxidase in a two step-specific mechanism: an ITS-guided sliding step orients the substrate noncovalently, followed by docking of the substrate Cys now juxtaposed to pair with the Mia40 active Cys. Cysteine 255-258 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 36-41 20027226-6 2009 Thus, it is likely that dh404 inhibits the ability of Keap1-Cul3-Rbx1 E3 ligase complex to target Nrf2 for ubiquitination and degradation via modifying Cys-151 of Keap1 to change the conformation of the complex. Cysteine 152-155 ring-box 1 Homo sapiens 65-69 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. Cysteine 182-185 insulin degrading enzyme Homo sapiens 79-82 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. Cysteine 195-198 insulin degrading enzyme Homo sapiens 79-82 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. Cysteine 195-198 insulin degrading enzyme Homo sapiens 79-82 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. Cysteine 195-198 insulin degrading enzyme Homo sapiens 79-82 19808678-6 2009 Our mutational analysis of IDE and peptide mass fingerprinting of GSNO-treated IDE using Fourier transform-ion cyclotron resonance mass spectrometer reveal a surprising interplay of Cys-178 with Cys-110 and Cys-819 for catalytic activity and with Cys-789 and Cys-966 for oligomerization. Cysteine 195-198 insulin degrading enzyme Homo sapiens 79-82 19808678-8 2009 The oxidation and nitrosylation of Cys-819 allow Cys-110 to be oxidized or nitrosylated, leading to complete inactivation of IDE. Cysteine 35-38 insulin degrading enzyme Homo sapiens 125-128 19808678-8 2009 The oxidation and nitrosylation of Cys-819 allow Cys-110 to be oxidized or nitrosylated, leading to complete inactivation of IDE. Cysteine 49-52 insulin degrading enzyme Homo sapiens 125-128 19808678-9 2009 Cys-789 is spatially adjacent to Cys-966, and their nitrosylation and oxidation together trigger the oligomerization and inhibition of IDE. Cysteine 0-3 insulin degrading enzyme Homo sapiens 135-138 19808678-9 2009 Cys-789 is spatially adjacent to Cys-966, and their nitrosylation and oxidation together trigger the oligomerization and inhibition of IDE. Cysteine 33-36 insulin degrading enzyme Homo sapiens 135-138 19808678-13 2009 The structure of IDE reveals the molecular basis for the long distance interactions of these cysteines and how they regulate IDE function. Cysteine 93-102 insulin degrading enzyme Homo sapiens 17-20 19808678-13 2009 The structure of IDE reveals the molecular basis for the long distance interactions of these cysteines and how they regulate IDE function. Cysteine 93-102 insulin degrading enzyme Homo sapiens 125-128 19824037-0 2009 Convergent solid-phase and solution approaches in the synthesis of the cysteine-rich Mdm2 RING finger domain. Cysteine 71-79 MDM2 proto-oncogene Homo sapiens 85-89 19779967-1 2009 PURPOSE: We investigate radio-labeling and pharmacokinetics of a new AnnexinA5 variant (HYNIC-cys-AnxA5) and then assess its utility for the non-invasive detection of cell death in liver, spleen and prostate. Cysteine 94-97 annexin A5 Rattus norvegicus 69-78 19779967-1 2009 PURPOSE: We investigate radio-labeling and pharmacokinetics of a new AnnexinA5 variant (HYNIC-cys-AnxA5) and then assess its utility for the non-invasive detection of cell death in liver, spleen and prostate. Cysteine 94-97 annexin A5 Rattus norvegicus 98-103 19779967-3 2009 Contrary to other AnnexinA5 variants, the new cys-AnxA5 allows for site-specific conjugation of a hydrazinonicotinamide-maleimide moiety and subsequent radio-labeling with (99m)Tc at a position not involved in the AnxA5-phosphatidylserine interaction. Cysteine 46-49 annexin A5 Rattus norvegicus 18-27 19779967-3 2009 Contrary to other AnnexinA5 variants, the new cys-AnxA5 allows for site-specific conjugation of a hydrazinonicotinamide-maleimide moiety and subsequent radio-labeling with (99m)Tc at a position not involved in the AnxA5-phosphatidylserine interaction. Cysteine 46-49 annexin A5 Rattus norvegicus 50-55 19779967-3 2009 Contrary to other AnnexinA5 variants, the new cys-AnxA5 allows for site-specific conjugation of a hydrazinonicotinamide-maleimide moiety and subsequent radio-labeling with (99m)Tc at a position not involved in the AnxA5-phosphatidylserine interaction. Cysteine 46-49 annexin A5 Rattus norvegicus 214-219 19779967-6 2009 RESULTS: HYNIC-cys-AnxA5 was efficiently and reproducibly labeled with (99m)Tc. Cysteine 15-18 annexin A5 Rattus norvegicus 19-24 20193280-1 2009 OBJECTIVE: To determine the anti-inflammatory functions of different cysteine mutants of apolipoprotein A-I recombinant HDLs. Cysteine 69-77 apolipoprotein A-I Mus musculus 89-107 19886837-4 2009 Major V1 Env sequence expansion, variation by a duplication event, and cumulative addition of cysteine residues and potential N-glycosylation sites over time may contribute to escape from antibody pressure directed to Env receptor domains by changing the exposure of neutralization-sensitive epitopes. Cysteine 94-102 endogenous retrovirus group K member 20 Homo sapiens 218-221 19661247-7 2009 MEASUREMENTS AND MAIN RESULTS: In a cell-free system, acrolein, in concentrations equal to those found in COPD sputum, directly adducted cysteine 319 in the MMP14 hemopexin-like domain and activated MMP14. Cysteine 137-145 matrix metallopeptidase 14 (membrane-inserted) Mus musculus 157-162 19843789-2 2009 In addition to glutamate, EAAT3 can also uptake L-cysteine, the rate-limiting substrate for the synthesis of glutathione. Cysteine 48-58 solute carrier family 1 member 1 Rattus norvegicus 26-31 19843789-4 2009 We determined whether oxidative stress would reduce L-cysteine-induced EAAT3 activity and whether this reduction would be attenuated by volatile anesthetics. Cysteine 52-62 solute carrier family 1 member 1 Rattus norvegicus 71-76 19843789-9 2009 The volatile anesthetics isoflurane, sevoflurane, and desflurane at concentrations from 1% to 3% attenuated the tert-butyl hydroperoxide-reduced EAAT3 activity for L-glutamate and L-cysteine. Cysteine 180-190 solute carrier family 1 member 1 Rattus norvegicus 145-150 19843789-10 2009 CONCLUSIONS: Our results suggest that volatile anesthetics preserve EAAT3 function to transport L-glutamate and L-cysteine under oxidative stress, which may be a mechanism for the neuroprotective effects of volatile anesthetics. Cysteine 112-122 solute carrier family 1 member 1 Rattus norvegicus 68-73 19628032-2 2009 Although the active site cysteine of TRP14 is sufficiently nucleophilic, its redox potential is similar to that of Trx1, and it receives the electrons from Trx reductase 1 (TrxR1) as does Trx1. Cysteine 25-33 thioredoxin reductase 1 Homo sapiens 156-171 19628032-2 2009 Although the active site cysteine of TRP14 is sufficiently nucleophilic, its redox potential is similar to that of Trx1, and it receives the electrons from Trx reductase 1 (TrxR1) as does Trx1. Cysteine 25-33 thioredoxin reductase 1 Homo sapiens 173-178 19726683-0 2009 Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase. Cysteine 17-26 lymphocyte antigen 6 complex Mus musculus 38-41 19726683-0 2009 Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase. Cysteine 17-26 lipoprotein lipase Mus musculus 91-109 19726683-2 2009 GPIHBP1 contains two key structural motifs, an acidic domain and an Ly6 motif (a three-fingered domain specified by 10 cysteines). Cysteine 119-128 lymphocyte antigen 6 complex Mus musculus 68-71 19875078-4 2009 Mutational and modeling studies suggest that the two agents occupy a common hydrophobic pocket located within the putative lid domain of MGL, and each reversibly interacts with one of two adjacent cysteine residues (Cys(201) and Cys(208)) flanking such pocket. Cysteine 197-205 monoglyceride lipase Homo sapiens 137-140 19875078-4 2009 Mutational and modeling studies suggest that the two agents occupy a common hydrophobic pocket located within the putative lid domain of MGL, and each reversibly interacts with one of two adjacent cysteine residues (Cys(201) and Cys(208)) flanking such pocket. Cysteine 216-219 monoglyceride lipase Homo sapiens 137-140 19875078-4 2009 Mutational and modeling studies suggest that the two agents occupy a common hydrophobic pocket located within the putative lid domain of MGL, and each reversibly interacts with one of two adjacent cysteine residues (Cys(201) and Cys(208)) flanking such pocket. Cysteine 229-232 monoglyceride lipase Homo sapiens 137-140 19860916-1 2009 BACKGROUND: Progranulin is a secreted high molecular weight growth factor bearing seven and one half copies of the cysteine-rich granulin-epithelin motif. Cysteine 115-123 granulin Mus musculus 12-23 19683004-6 2009 A second cysteine mutation was introduced into wild-type FGF-1 at adjacent position Ala66, which is known to participate as a half-cystine with position 83 in FGF-8, FGF-19, and FGF-23. Cysteine 9-17 fibroblast growth factor 23 Homo sapiens 178-184 19708669-2 2009 To emphasize the role played by the S-S bridge in the structural features of somatostatin-14 (SST-14), newly recorded CD and Raman spectra of this cyclic peptide and its open analogue obtained by Cys-->Ser substitution are presented. Cysteine 196-199 somatostatin Homo sapiens 94-100 19645416-2 2009 Recent structural analyses revealed the close proximity of Cys-150 residues from IDH2 in adjacent heterodimers, and features of the structure for the ligand-free enzyme suggested that formation of a disulfide bond between these residues might stabilize an inactive form of the enzyme. Cysteine 59-62 isocitrate dehydrogenase (NAD(+)) IDH2 Saccharomyces cerevisiae S288C 81-85 19344898-10 2009 Cysteine-1660 appears to be a critical residue for cholesterol transport of ABCA1. Cysteine 0-8 ATP binding cassette subfamily A member 1 Homo sapiens 76-81 19500832-2 2009 Alpha-elastin was chemically crosslinked with hexamethylene diisocyanate that can react with various functional groups in elastin such as lysine, cysteine, and histidine. Cysteine 146-154 elastin Homo sapiens 6-13 19500832-2 2009 Alpha-elastin was chemically crosslinked with hexamethylene diisocyanate that can react with various functional groups in elastin such as lysine, cysteine, and histidine. Cysteine 146-154 elastin Homo sapiens 122-129 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19422376-4 2009 With respect to beta(2)-AR, the Cys-19 variant is associated with greater beta(2)-AR expression than the Arg-19 variant; Gly16-beta(2)-AR are more susceptible, whereas Glu27-beta(2)-AR are almost resistant to agonist-promoted down-regulation; Thr164-beta(2)-AR are three to four times more responsive to agonist-evoked stimulation than Ile164-beta(2)-AR. Cysteine 32-35 adrenoceptor beta 2 Homo sapiens 74-84 19488745-1 2009 This work completes previous findings and, using cysteine scanning mutagenesis (CSM) and biochemical methods, provides detailed analysis of conformational changes of the S6 domain and C-linker during gating of CNGA1 channels. Cysteine 49-57 cyclic nucleotide gated channel subunit alpha 1 Homo sapiens 210-215 19488745-2 2009 Specific residues between Phe375 and Val424 were mutated to a cysteine in the CNGA1 and CNGA1(cys-free) background and the effect of intracellular Cd(2+) or cross-linkers of different length in the open and closed state was studied. Cysteine 62-65 cyclic nucleotide gated channel subunit alpha 1 Homo sapiens 88-93 19383981-9 2009 The activity of hLPCAT1 was inhibited by N-ethylmaleimide, indicating the importance of some cysteine residue(s) for the catalysis. Cysteine 93-101 lysophosphatidylcholine acyltransferase 1 Homo sapiens 16-23 19383981-10 2009 We found a conserved cysteine (Cys(211)) in hLPCAT1 that is crucial for its activity. Cysteine 21-29 lysophosphatidylcholine acyltransferase 1 Homo sapiens 44-51 19383981-10 2009 We found a conserved cysteine (Cys(211)) in hLPCAT1 that is crucial for its activity. Cysteine 31-34 lysophosphatidylcholine acyltransferase 1 Homo sapiens 44-51 19666611-5 2009 All examined cysteine single and double mutants exhibited a reduced antenna at PSII caused by a perturbed NAB1 deactivation mechanism, with double mutations and Cys-226 single mutations causing a stronger and more distinctive phenotype compared with the Cys-181 mutation. Cysteine 13-21 uncharacterized protein Chlamydomonas reinhardtii 106-110 19666611-8 2009 NAB1 is fully active in its dithiol state and is reversibly deactivated by modification of its cysteines. Cysteine 95-104 uncharacterized protein Chlamydomonas reinhardtii 0-4 19656407-16 2009 Of the five cysteine residues, Cys82, Cys150, Cys155, Cys160, and Cys216 involved in oligomer-monomer transition in NPR1, Cys216 in GmNPR1-1 and GmNPR1-2 proteins was substituted to Ser and Leu, respectively. Cysteine 12-20 regulatory protein (NPR1) Arabidopsis thaliana 116-120 19515813-7 2009 An effectively cysteine-less MATE1 mutant (Delta13Cys) was functional and refractory to reaction with the impermeant marker of accessible cysteine residues, maleimide-PEO(2)-biotin. Cysteine 15-23 solute carrier family 47 member 1 Homo sapiens 29-34 19515813-7 2009 An effectively cysteine-less MATE1 mutant (Delta13Cys) was functional and refractory to reaction with the impermeant marker of accessible cysteine residues, maleimide-PEO(2)-biotin. Cysteine 138-146 solute carrier family 47 member 1 Homo sapiens 29-34 20103838-1 2009 Mammalian leukocyte cell-derived chemotaxin 2 (LECT2) contains six evolutionarily conserved cysteine residues. Cysteine 92-100 leukocyte cell derived chemotaxin 2 Homo sapiens 10-45 20103838-1 2009 Mammalian leukocyte cell-derived chemotaxin 2 (LECT2) contains six evolutionarily conserved cysteine residues. Cysteine 92-100 leukocyte cell derived chemotaxin 2 Homo sapiens 47-52 19299483-3 2009 Given that the reactive alpha,beta-unsaturated ketone in the cyclopentenone ring of 15d-PGJ(2) covalently modifies key Cys thiols in select proteins, we hypothesized that 15d-PGJ(2) inhibits HIV transcription and replication by targeting Cys thiols in HIV-1 Tat. Cysteine 119-122 Tat Human immunodeficiency virus 1 258-261 19556306-0 2009 Mutational analysis of Cys(88) of Toll-like receptor 4 highlights the critical role of MD-2 in cell surface receptor expression. Cysteine 23-26 lymphocyte antigen 96 Homo sapiens 87-91 19464924-0 2009 Characterization of novel oxidation products of cysteine in an active site motif peptide of PTP1B. Cysteine 48-56 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 92-97 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cysteine 106-114 cystathionine gamma-lyase Homo sapiens 0-25 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cysteine 106-114 cystathionine gamma-lyase Homo sapiens 27-30 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cysteine 182-190 cystathionine gamma-lyase Homo sapiens 0-25 19486201-1 2009 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulphuration pathway for the biosynthesis of cysteine from methionine and catalyses the hydrolysis of cystathionine into cysteine. Cysteine 182-190 cystathionine gamma-lyase Homo sapiens 27-30 19542287-8 2009 Finally, it appears that two sequence motifs, the Walker A box involved in ATP binding and an iron-sulfur-cysteine cluster, are present only in subsets of AddB proteins, suggesting the existence of mechanistically distinct classes of AddB. Cysteine 106-114 adducin 2 Homo sapiens 234-238 19648408-8 2009 Animal AOX also lacks an N-terminal cysteine residue that is known to be important for AOX enzyme regulation in plants. Cysteine 36-44 acyl-CoA oxidase 1 Homo sapiens 7-10 19648408-8 2009 Animal AOX also lacks an N-terminal cysteine residue that is known to be important for AOX enzyme regulation in plants. Cysteine 36-44 acyl-CoA oxidase 1 Homo sapiens 87-90 19592663-8 2009 Lastly, monopalmitoylation of LAT on Cys(26) (but not Cys(29)) was required and sufficient for its PM transport and function. Cysteine 37-40 linker for activation of T cells Mus musculus 30-33 19493317-1 2009 Pheomelanogenesis is a complex pathway that starts with the oxidation of tyrosine (or DOPA, 3,4-dihydroxyphenylalanine) by tyrosinase in the presence of cysteine, which results in the production of 5-S-cysteinyldopa and its isomers. Cysteine 153-161 tyrosinase Homo sapiens 123-133 19478074-5 2009 The association of TGFBI and periostin is mediated by the amino-terminal cysteine-rich EMI domains of TGFBI and periostin. Cysteine 73-81 transforming growth factor beta induced Homo sapiens 19-24 19478074-5 2009 The association of TGFBI and periostin is mediated by the amino-terminal cysteine-rich EMI domains of TGFBI and periostin. Cysteine 73-81 transforming growth factor beta induced Homo sapiens 102-107 19556522-5 2009 Indeed, ABCA1 is robustly palmitoylated at cysteines 3, -23, -1110, and -1111. Cysteine 43-52 ATP binding cassette subfamily A member 1 Homo sapiens 8-13 19556522-6 2009 Abrogation of palmitoylation of ABCA1 by mutation of the cysteines results in a reduction of ABCA1 localization at the plasma membranes and a reduction in the ability of ABCA1 to efflux lipids to apolipoprotein A-I. Cysteine 57-66 ATP binding cassette subfamily A member 1 Homo sapiens 32-37 19556522-6 2009 Abrogation of palmitoylation of ABCA1 by mutation of the cysteines results in a reduction of ABCA1 localization at the plasma membranes and a reduction in the ability of ABCA1 to efflux lipids to apolipoprotein A-I. Cysteine 57-66 ATP binding cassette subfamily A member 1 Homo sapiens 93-98 19556522-6 2009 Abrogation of palmitoylation of ABCA1 by mutation of the cysteines results in a reduction of ABCA1 localization at the plasma membranes and a reduction in the ability of ABCA1 to efflux lipids to apolipoprotein A-I. Cysteine 57-66 ATP binding cassette subfamily A member 1 Homo sapiens 93-98 19607794-5 2009 S-nitrosylation of GOSPEL at cysteine 47 enhances GAPDH-GOSPEL binding and the neuroprotective actions of GOSPEL. Cysteine 29-37 glyceraldehyde-3-phosphate dehydrogenase Mus musculus 50-55 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. Cysteine 46-54 methionine sulfoxide reductase B 2 Arabidopsis thaliana 218-223 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. Cysteine 214-217 methionine sulfoxide reductase B 2 Arabidopsis thaliana 218-223 19457862-7 2009 Regarding 1-Cys MSRB1, oxidation of the enzyme after substrate reduction leads to the formation of a stable sulfenic acid on the catalytic Cys, which is subsequently glutathionylated. Cysteine 12-15 methionine sulfoxide reductase B 1 Arabidopsis thaliana 16-21 19457862-8 2009 The deglutathionylation of MSRB1 is achieved by both mono- and dithiol glutaredoxins and involves only their N-terminal conserved catalytic Cys. Cysteine 140-143 methionine sulfoxide reductase B 1 Arabidopsis thaliana 27-32 19401403-2 2009 The objectives of this study were to clone equine thrombospondin II (THBS2) and secreted protein acidic and cysteine-rich (SPARC) cDNAs and to compare the spatiotemporal expression of mRNAs and proteins during repair of body and limb wounds. Cysteine 108-116 secreted protein acidic and cysteine rich Equus caballus 123-128 18695935-2 2009 Recently it has been proposed that NAC administration may modify the plasma levels of low molecular weight thiols (LMW) like cysteine, homocysteine and glutathione, though it has been still debated if their plasma concentration increases or decreases during the therapy. Cysteine 125-133 X-linked Kx blood group Homo sapiens 35-38 19285949-3 2009 H(2)S is a gas that can be formed by the action of two enzymes, cystathionine gamma-lyase and cystathionine beta-synthase, both involved in the metabolism of cysteine. Cysteine 158-166 cystathionine gamma-lyase Homo sapiens 64-89 19378296-9 2009 Its docked pose in the RXRalpha ligand binding domain suggests that binding is stabilized by interactions of its carboxylate group with arginine 316, its indoles with cysteines 269 and 432, and its 1-methyl groups with hydrophobic residues lining the binding pocket. Cysteine 167-176 retinoid X receptor alpha Homo sapiens 23-31 18818946-6 2009 This mutation in the SLC2A10 gene replaces a cysteine encoding codon with a stop signal. Cysteine 45-53 solute carrier family 2 member 10 Homo sapiens 21-28 19328198-0 2009 Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface. Cysteine 26-35 CD81 molecule Homo sapiens 55-59 19328198-3 2009 Mutation of at least six of the eight juxtamembrane cysteines was required to completely eliminate detectable CD81 palmitoylation, indicating that several sites can be palmitoylated. Cysteine 52-61 CD81 molecule Homo sapiens 110-114 19328198-7 2009 Taken together, these findings indicate that mutation of juxtamembrane cysteines alters the interaction of CD81 with other proteins, either because of reduced palmitoylation, structural alterations in the mutant proteins, or a combination of both factors, and this affects the CD81 microenvironment on the cell surface. Cysteine 71-80 CD81 molecule Homo sapiens 107-111 19328198-7 2009 Taken together, these findings indicate that mutation of juxtamembrane cysteines alters the interaction of CD81 with other proteins, either because of reduced palmitoylation, structural alterations in the mutant proteins, or a combination of both factors, and this affects the CD81 microenvironment on the cell surface. Cysteine 71-80 CD81 molecule Homo sapiens 277-281 19464178-7 2009 Surprisingly, a truncated form of Smo that lacks the cysteine-rich domain of the ECD localizes to the cilium but is unable to activate high-level Hh signaling. Cysteine 53-61 smoothened, frizzled class receptor Danio rerio 34-37 19536442-8 2009 Similarly, cysteine specific oxidizing agent, DTNB, also increased or decreased P(o) of BK(Ca) and DTT partially reversed the effect of DTNB. Cysteine 11-19 dystrobrevin beta Cavia porcellus 46-50 19536442-8 2009 Similarly, cysteine specific oxidizing agent, DTNB, also increased or decreased P(o) of BK(Ca) and DTT partially reversed the effect of DTNB. Cysteine 11-19 dystrobrevin beta Cavia porcellus 136-140 19536442-9 2009 It is thus suggested that H2O2 and DTNB may modulate P(o) of BK(Ca) via the oxidation of cysteine residue. Cysteine 89-97 dystrobrevin beta Cavia porcellus 35-39 19303045-1 2009 The human ZC3H14 gene encodes an evolutionarily conserved Cys(3)His zinc finger protein that binds specifically to polyadenosine RNA and is thus postulated to modulate post-transcriptional gene expression. Cysteine 58-61 zinc finger CCCH-type containing 14 Homo sapiens 10-16 19303045-14 2009 Both nuclear and cytoplasmic ZC3H14 isoforms could have distinct effects on gene expression mediated by the common Cys(3)His zinc finger polyadenosine RNA binding domain. Cysteine 115-118 zinc finger CCCH-type containing 14 Homo sapiens 29-35 19420245-10 2009 A chimeric Nogo receptor variant (NgR(OMNI)) in which Cys(309)-Cys(336) is deleted and followed by a 13 aa MAG-binding motif of the NgR2 stalk, shows superior binding of OMgp, Nogo-66, and MAG compared with wild-type NgR1 or NgR2. Cysteine 54-57 reticulon 4 receptor Homo sapiens 11-24 19420245-10 2009 A chimeric Nogo receptor variant (NgR(OMNI)) in which Cys(309)-Cys(336) is deleted and followed by a 13 aa MAG-binding motif of the NgR2 stalk, shows superior binding of OMgp, Nogo-66, and MAG compared with wild-type NgR1 or NgR2. Cysteine 63-66 reticulon 4 receptor Homo sapiens 11-24 19367685-7 2009 Integration of the data provides a snapshot consistent with a metabolic defensive strategy, regulating key enzymes by redox modification, redirecting energy toward ribulose-5-phosphate recycling for NADPH production and antioxidative defence.This generally applicable method has allowed us to discover new redox regulated proteins (DAHP and carbamoylphosphate synthases, Doa1p) and to precisely identify target cysteines in a number of known ones. Cysteine 411-420 Doa1p Saccharomyces cerevisiae S288C 371-376 19018666-1 2009 Cox17, a copper chaperone for cytochrome-c oxidase, contains six conserved Cys residues and exists in three oxidative states, linked with two thiol-based redox switches. Cysteine 75-78 cytochrome c oxidase copper chaperone COX17 Homo sapiens 0-5 19351145-2 2009 The gold nanorod-bombesin (GNR-BBN) conjugates showed extraordinary in vitro stabilities against various biomolecules including NaCl, cysteine, histidine, bovine serum albumin, human serum albumin, and dithiothreitol. Cysteine 134-142 gastrin releasing peptide Homo sapiens 17-25 19351145-2 2009 The gold nanorod-bombesin (GNR-BBN) conjugates showed extraordinary in vitro stabilities against various biomolecules including NaCl, cysteine, histidine, bovine serum albumin, human serum albumin, and dithiothreitol. Cysteine 134-142 gastrin releasing peptide Homo sapiens 31-34 19261609-2 2009 It is widely assumed that desulfhydration of cysteine is the major source of H(2)S in mammals and is catalyzed by the transsulfuration pathway enzymes, cystathionine beta-synthase and cystathionine gamma-lyase (CSE). Cysteine 45-53 cystathionine gamma-lyase Homo sapiens 184-209 19261609-2 2009 It is widely assumed that desulfhydration of cysteine is the major source of H(2)S in mammals and is catalyzed by the transsulfuration pathway enzymes, cystathionine beta-synthase and cystathionine gamma-lyase (CSE). Cysteine 45-53 cystathionine gamma-lyase Homo sapiens 211-214 19261609-3 2009 In this study, we demonstrate that the profligacy of human CSE results in a variety of reactions that generate H(2)S from cysteine and homocysteine. Cysteine 122-130 cystathionine gamma-lyase Homo sapiens 59-62 19342788-1 2009 The human seminal plasma protein PSP94 is a small protein of 94 residues that contains ten cysteines. Cysteine 91-100 microseminoprotein beta Homo sapiens 33-38 19416166-4 2009 For optimal signaling the RLF requires five L-alpha-amino acids preceding cysteine A10, whereas the B chain requires only three. Cysteine 74-82 RLF zinc finger Homo sapiens 26-29 19129187-3 2009 The cluster is coordinated by an unusual arrangement of cysteine residues that originate from both sides of the AddB nuclease, forming an "iron staple" that is required for the local structural integrity of this domain. Cysteine 56-64 adducin 2 Homo sapiens 112-116 19059456-8 2009 Treatment of NADPH-reduced TrxR1 with TFs decreased 5-(Iodoacetamido) fluorescein incorporation, a fluorescent thiol-reactive reagent, suggesting that Sec/Cys residue(s) in the active site may be involved in the binding of TFs. Cysteine 155-158 thioredoxin reductase 1 Homo sapiens 27-32 18594967-5 2009 As the disease progressed, glutathione and cysteinyl glycine were further increased in mild attacks and cysteine levels correlated with homocysteine (r = 0.8, P < 0.001) and gamma-glutamyl transpeptidase activity (r = 0.75, P < 0.001). Cysteine 104-112 inactive glutathione hydrolase 2 Homo sapiens 177-206 19035567-1 2009 The protein Cripto is the founding member of the extra-cellular EGF-CFC growth factors, which are composed of two adjacent cysteine-rich domains: the EGF-like and the CFC. Cysteine 123-131 tubulin folding cofactor C Homo sapiens 68-71 19158387-6 2009 Overexpression of Usp18 elevated EGFR levels in a manner requiring the catalytic cysteine of Usp18. Cysteine 81-89 ubiquitin specific peptidase 18 Homo sapiens 18-23 19158387-6 2009 Overexpression of Usp18 elevated EGFR levels in a manner requiring the catalytic cysteine of Usp18. Cysteine 81-89 ubiquitin specific peptidase 18 Homo sapiens 93-98 19255677-1 2009 Nanomolar concentrations of cysteine-capped CdTe quantum dots (QDs) quenched the fluorescence of tryptophan moieties in glucose oxidase (GOX), while the fluorescence of the other fluorophore in the enzyme, FAD (Flavin Adenine Dinucleotide), was not affected by the QDs. Cysteine 28-36 hydroxyacid oxidase 1 Homo sapiens 120-135 19255677-1 2009 Nanomolar concentrations of cysteine-capped CdTe quantum dots (QDs) quenched the fluorescence of tryptophan moieties in glucose oxidase (GOX), while the fluorescence of the other fluorophore in the enzyme, FAD (Flavin Adenine Dinucleotide), was not affected by the QDs. Cysteine 28-36 hydroxyacid oxidase 1 Homo sapiens 137-140 19124472-8 2009 A patch clamp experiment shows that S-nitrosylation of Cys(445) modulates the KCNQ1/KCNE1 channel function. Cysteine 55-58 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 84-89 19170606-2 2009 Like Cu chaperones from other organisms, including the human homologue Atox1, CopZ has the ferredoxin-like fold and binds Cu(I) via two Cys in a conserved M(11)X(12)C(13)X(14)X(15)C(16) motif located in a solvent-exposed loop. Cysteine 136-139 antioxidant 1 copper chaperone Homo sapiens 71-76 18704946-5 2009 Forgoing the use of experimental transport and binding data of tryptamine derivatives for construction of these models enables us to critically assess and validate their predictive power: A single 5-HT binding mode was identified that retains the amine placement observed in the LeuT(Aa) structure, matches site-directed mutagenesis and substituted cysteine accessibility method (SCAM) data, complies with support vector machine derived relations activity relations, and predicts computational binding energies for 5-HT analogs with a significant correlation coefficient (R = 0.72). Cysteine 349-357 Leucine transport, high Homo sapiens 279-283 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. Cysteine 59-67 ADAM metallopeptidase domain 17 Homo sapiens 15-21 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. Cysteine 114-122 ADAM metallopeptidase domain 17 Homo sapiens 15-21 19074140-4 2009 Here, using cysteine mutagenesis in Cx50, we demonstrate that residues at the TM1/E1 border undergo movement during loop gating. Cysteine 12-20 gap junction protein alpha 8 Homo sapiens 36-40 19146392-1 2009 Atox1 is a human copper (Cu) chaperone with the ferredoxin-like fold that binds Cu(I) via two Cys residues in a M(10)X(11)C(12)X(13)X(14)C(15) motif located in a solvent-exposed loop. Cysteine 94-97 antioxidant 1 copper chaperone Homo sapiens 0-5 19199576-4 2009 Bound to the cysteine-34 position of albumin, it was cleaved efficiently by cathepsin B releasing the free drugs. Cysteine 13-21 cathepsin B Homo sapiens 76-87 19139268-2 2009 Using a heterologous expression cloning approach, we isolated beta4GalNAcTB together with beta4GalNAcTB pilot (GABPI), a multimembrane-spanning protein related to Asp-His-His-Cys (DHHC) proteins but lacking the DHHC consensus sequence. Cysteine 175-178 beta1,4-N-acetylgalactosaminyltransferase B Drosophila melanogaster 62-75 19139268-2 2009 Using a heterologous expression cloning approach, we isolated beta4GalNAcTB together with beta4GalNAcTB pilot (GABPI), a multimembrane-spanning protein related to Asp-His-His-Cys (DHHC) proteins but lacking the DHHC consensus sequence. Cysteine 175-178 beta1,4-N-acetylgalactosaminyltransferase B Drosophila melanogaster 90-103 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). Cysteine 189-197 spectrin alpha, erythrocytic 1 Homo sapiens 111-114 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). Cysteine 189-197 tropomyosin 3 Homo sapiens 210-213 18543330-7 2009 The metal-coordinating residues in the active site of ILL2 include a conserved cysteine that clearly distinguishes this protein from previously structurally characterized members of the M20 peptidase family. Cysteine 79-87 IAA-leucine resistant (ILR)-like 2 Arabidopsis thaliana 54-58 19012295-4 2008 Helix-stabilized peptides exhibited high Bcl-x(L) binding affinity with dissociation constants of 42+/-9, 21+/-1, and 55+/-4 nM for Bak(i+ 7)(72-87), Bak i+ 11)(72-87), and Bid(i+ 4)(91-111), respectively (superscript numbers refer to the spacing between cysteine residues), and up to 20-fold enhancements in affinity in relation to their helix-destabilized forms. Cysteine 255-263 BCL2 antagonist/killer 1 Homo sapiens 132-135 18848840-7 2008 Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln. Cysteine 57-60 mutY DNA glycosylase Homo sapiens 250-254 18848840-7 2008 Compared with individuals carrying genotypes of hOGG1 326Cys/Cys and hMYH 324His/His at the same time, there was a 0.33-fold (OR(adj), 0.33; 95% CI: 0.15-0.72; P<0.05) decreased risk of CBP for those with genotypes of hOGG1 326Ser/Cys+Ser/Ser and hMYH 324His/Gln+Gln/Gln. Cysteine 61-64 mutY DNA glycosylase Homo sapiens 250-254 18840608-0 2008 Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation. Cysteine 0-8 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 34-65 18840608-4 2008 We treated PTP1B with various NO donors, including S-nitrosothiol reagents and compound-releasing NO radicals, to produce site-specific Cys S-nitrosylation identified using advanced mass spectrometry (MS) techniques. Cysteine 136-139 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 11-16 18840608-6 2008 The crystal structure of NO donor-reacted PTP1B at 2.6 A resolution revealed that the S-NO state at Cys-215 had no discernible irreversibly oxidized forms, whereas other Cys residues remained in their free thiol states. Cysteine 100-103 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 42-47 18840608-6 2008 The crystal structure of NO donor-reacted PTP1B at 2.6 A resolution revealed that the S-NO state at Cys-215 had no discernible irreversibly oxidized forms, whereas other Cys residues remained in their free thiol states. Cysteine 170-173 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 42-47 18840608-7 2008 We further demonstrated that S-nitrosylation of the Cys-215 residue protected PTP1B from subsequent H(2)O(2)-induced irreversible oxidation. Cysteine 52-55 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 78-83 18986166-0 2008 Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme. Cysteine 68-76 insulin degrading enzyme Homo sapiens 109-133 18976165-5 2008 METHODS: We introduced (i) individual Cys and (ii) consecutive cumulative Cys mutations into the starting template SHCS-TSHR, a truncated TSHR-ECD moiety previously shown to behave like the wild-type TSHR. Cysteine 74-77 thyroid stimulating hormone receptor Homo sapiens 120-124 18976165-10 2008 Only SHCS-301 TSHR bound TSH in a specific manner, and it formed the base for sequential Cys mutations. Cysteine 89-92 thyroid stimulating hormone receptor Homo sapiens 14-18 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. Cysteine 42-45 thyroid stimulating hormone receptor Homo sapiens 157-161 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. Cysteine 88-91 thyroid stimulating hormone receptor Homo sapiens 157-161 18589439-3 2008 The structure of the Vav1 DH-PH-CRD/Rac1 complex to 2.6 A resolution reveals a unique intramolecular network of contacts between the Vav1 cysteine-rich domain (CRD) and the C-terminal helix of the Vav1 Dbl homology (DH) domain. Cysteine 138-146 Rac family small GTPase 1 Homo sapiens 36-40 18621727-2 2008 IDE is inhibited irreversibly by compounds that covalently modify cysteine residues, a mechanism that could be operative in the etiology of type 2 diabetes mellitus (DM2) or Alzheimer"s disease (AD). Cysteine 66-74 insulin degrading enzyme Homo sapiens 0-3 18621727-4 2008 To address this topic, we conducted a comprehensive mutational analysis of the 13 cysteine residues within IDE. Cysteine 82-90 insulin degrading enzyme Homo sapiens 107-110 18441097-8 2008 Addition of L-Cys but not D-Cys to RSNOs or DEA NONOate increased SNO and DAF-FM signal that was inhibited by coincubation with LAT competitors. Cysteine 12-17 linker for activation of T cells Rattus norvegicus 128-131 18441097-11 2008 We conclude that RSNOs (thionitrites, S-nitrosothiols) and NO enter alveolar epithelial cells predominantly by S-nitrosation of L-Cys, which is then imported through LAT. Cysteine 128-133 linker for activation of T cells Rattus norvegicus 166-169 18515280-7 2008 These results indicate that alk(en)yl trisulfide react with sulfhydryl groups in cysteine residues of cellular proteins such as microtubule proteins. Cysteine 81-89 ALK receptor tyrosine kinase Homo sapiens 28-31 18474619-6 2008 RASSF1A associated with the TNF-R1/MOAP-1 or TRAIL-R1/MOAP-1 complex via its N-terminal cysteine-rich (C1) domain containing a potential zinc finger binding motif. Cysteine 88-96 Ras association domain family member 1 Homo sapiens 0-7 18474619-6 2008 RASSF1A associated with the TNF-R1/MOAP-1 or TRAIL-R1/MOAP-1 complex via its N-terminal cysteine-rich (C1) domain containing a potential zinc finger binding motif. Cysteine 88-96 modulator of apoptosis 1 Homo sapiens 35-41 18474619-6 2008 RASSF1A associated with the TNF-R1/MOAP-1 or TRAIL-R1/MOAP-1 complex via its N-terminal cysteine-rich (C1) domain containing a potential zinc finger binding motif. Cysteine 88-96 modulator of apoptosis 1 Homo sapiens 54-60 18413666-9 2008 These data suggest that the last three transmembrane domains of mENT1 are not necessary for transport activity, but this region does contain the cysteines responsible for the sensitivity of mENT1 to sulfhydryl reagents, and the residues important for covalent modification of the protein with NBMPR. Cysteine 145-154 solute carrier family 29 (nucleoside transporters), member 1 Mus musculus 64-69 18413666-9 2008 These data suggest that the last three transmembrane domains of mENT1 are not necessary for transport activity, but this region does contain the cysteines responsible for the sensitivity of mENT1 to sulfhydryl reagents, and the residues important for covalent modification of the protein with NBMPR. Cysteine 145-154 solute carrier family 29 (nucleoside transporters), member 1 Mus musculus 190-195 18573918-5 2008 The addition of N-linked glycan to the N terminus of the substrate is prevented by mutation of a specific cysteine residue of Sec61p, as well as a specific cysteine residue of the substrate protein. Cysteine 106-114 SEC61 translocon subunit alpha 1 Homo sapiens 126-132 18426798-5 2008 Computational probing illustrates how the interactions may determine the flexibility of the permeation pathway, and mutagenesis within the network and results from assays of transport, as well as the state-dependent accessibility of a substituted cysteine in TM3, support the role of this network in regulating access between the substrate binding site and the intracellular milieu. Cysteine 247-255 tropomyosin 3 Homo sapiens 259-262 18494476-1 2008 To provide insights into the structure-function relationships of oxidosqualene-lanosterol cyclase (ERG7) from Saccharomyces cerevisiae, the Phe699 was exchanged against hydrophilic polar uncharged residues Ser, Thr, Cys, Gln, and Tyr to characterize its product profile and functional role in ERG7 activity. Cysteine 216-219 lanosterol synthase ERG7 Saccharomyces cerevisiae S288C 99-103 18476726-1 2008 Human cystathionine-gamma-lyase (CGL) is a pyridoxal-5"-phosphate (PLP)-dependent enzyme, which functions in the transsulfuration pathway that converts homocysteine to cysteine. Cysteine 156-164 cystathionine gamma-lyase Homo sapiens 6-31 18476726-1 2008 Human cystathionine-gamma-lyase (CGL) is a pyridoxal-5"-phosphate (PLP)-dependent enzyme, which functions in the transsulfuration pathway that converts homocysteine to cysteine. Cysteine 156-164 cystathionine gamma-lyase Homo sapiens 33-36 18479111-3 2008 The first cyclization occurred between the chloroacetyl group of Cab and the sulfhydryl group in Cys in situ of translation, and the second cyclization on the side chains of Aha-Pgl via Cu(I)-catalyzed azide-alkyne cycloaddition was performed. Cysteine 97-100 neural proliferation, differentiation and control 1 Homo sapiens 65-68 18545666-7 2008 As assessed by mass spectra, MAPKs activation and efficient binding to cognate MAPKKs resulted from oxidation of conserved ERK1/2 or p38-JNK1/2 cysteine domains to sulfinic and sulfonic acids at a definite H(2)O(2) level. Cysteine 144-152 mitogen-activated protein kinase 8 Mus musculus 137-143 18193173-9 2008 Furthermore, NAC acted as a GSH precursor only at cysteine medium concentrations of 10 micromol/l or below and therefore might be described as a poor cysteine repletor for glutathione synthesis. Cysteine 50-58 X-linked Kx blood group Homo sapiens 13-16 18193173-9 2008 Furthermore, NAC acted as a GSH precursor only at cysteine medium concentrations of 10 micromol/l or below and therefore might be described as a poor cysteine repletor for glutathione synthesis. Cysteine 150-158 X-linked Kx blood group Homo sapiens 13-16 18461660-9 2008 CONCLUSION: The expression and activity of both LTC4S and mGST2 are up regulated in a rat FHF model, which are, at least, partly responsible for cys-LT hepatic accumulation. Cysteine 145-148 leukotriene C4 synthase Rattus norvegicus 48-53 18199880-0 2008 Functional and structural roles of conserved cysteine residues in the carboxyl-terminal domain of the follicle-stimulating hormone receptor in human embryonic kidney 293 cells. Cysteine 45-53 follicle stimulating hormone receptor Homo sapiens 102-139 18199880-4 2008 In the present study, a functional analysis of the FSHR carboxyl-terminal segment cysteine residues was carried out. Cysteine 82-90 follicle stimulating hormone receptor Homo sapiens 51-55 18199880-8 2008 All FSHR Cys mutants were capable of binding agonist with the same affinity as the wild-type receptor and internalizing on agonist stimulation. Cysteine 9-12 follicle stimulating hormone receptor Homo sapiens 4-8 18508541-1 2008 Bone morphogenetic protein-7 (BMP7) is a member of the BMP-subfamily of perhaps a dozen proteins within the TGFbeta-superfamily of cysteine-knot fold cytokine-growth factors. Cysteine 131-139 bone morphogenetic protein 7 Homo sapiens 0-28 18508541-1 2008 Bone morphogenetic protein-7 (BMP7) is a member of the BMP-subfamily of perhaps a dozen proteins within the TGFbeta-superfamily of cysteine-knot fold cytokine-growth factors. Cysteine 131-139 bone morphogenetic protein 7 Homo sapiens 30-34 18508541-1 2008 Bone morphogenetic protein-7 (BMP7) is a member of the BMP-subfamily of perhaps a dozen proteins within the TGFbeta-superfamily of cysteine-knot fold cytokine-growth factors. Cysteine 131-139 bone morphogenetic protein 7 Homo sapiens 30-33 18398918-5 2008 Microarray analysis of the organoid cultures identified specific up-regulation of approximately 500 target genes induced by HGF and EGF, including members of the extracellular matrix (ECM) protein family, Wnt/beta-catenin pathway, transforming growth factor beta (TGF-beta)/bone morphogenetic protein (BMP) pathway, and CXC (cysteine-any amino acid-cysteine) chemokines. Cysteine 325-333 hepatocyte growth factor Rattus norvegicus 124-127 18424739-6 2008 Enhancement of HIV by HD5 and HD6 was influenced by the structure of the peptides, as loss of the intramolecular cysteine bonds was associated with loss of the HIV-enhancing effect. Cysteine 113-121 defensin alpha 6 Homo sapiens 30-33 18283100-6 2008 The activity of ASG depends on the Cys-84 residue that is predicted to be post-translationally converted to the critical active site C(alpha)-formylglycine. Cysteine 35-38 arylsulfatase G Homo sapiens 16-19 18305113-1 2008 Formylglycine-generating enzyme (FGE) catalyzes the oxidation of a specific cysteine residue in nascent sulfatase polypeptides to formylglycine (FGly). Cysteine 76-84 sulfatase modifying factor 1 Homo sapiens 0-31 18305113-1 2008 Formylglycine-generating enzyme (FGE) catalyzes the oxidation of a specific cysteine residue in nascent sulfatase polypeptides to formylglycine (FGly). Cysteine 76-84 sulfatase modifying factor 1 Homo sapiens 33-36 18305113-8 2008 Within the FGE N-terminal extension cysteine 52 is critical for the biological activity. Cysteine 36-44 sulfatase modifying factor 1 Homo sapiens 11-14 18378904-2 2008 Here, we show that LRP6 is palmitoylated on a juxtamembranous cysteine and that palmitoylation is required for exit from the endoplasmic reticulum (ER). Cysteine 62-70 LDL receptor related protein 6 Homo sapiens 19-23 17943184-7 2008 Structural modelling based on the crystal structure of human MSRA revealed that the active site of this enzyme is significantly altered after H(2)O(2)-mediated oxidation of L-methionine, L-tryptophan, and L-cysteine residues in its active site. Cysteine 205-215 methionine sulfoxide reductase A Homo sapiens 61-65 18393249-5 2008 There was a 3.37-fold or 2.54-fold increased risk of laryngeal carcinoma for individuals carrying XRCC1-399Arg/Gln+ Gln/Gln or hOGG1-326Ser/Cys+ Cys/Cys genotypes, compared with subjects carrying XRCC1-Arg/Arg or hOGG1-Ser/Ser genotype, respectively. Cysteine 145-148 X-ray repair cross complementing 1 Homo sapiens 98-103 18393249-5 2008 There was a 3.37-fold or 2.54-fold increased risk of laryngeal carcinoma for individuals carrying XRCC1-399Arg/Gln+ Gln/Gln or hOGG1-326Ser/Cys+ Cys/Cys genotypes, compared with subjects carrying XRCC1-Arg/Arg or hOGG1-Ser/Ser genotype, respectively. Cysteine 145-148 X-ray repair cross complementing 1 Homo sapiens 98-103 18199742-7 2008 Although this cysteine residue is also present in hCNT1 and hCNT2, neither transporter was affected by PCMBS. Cysteine 14-22 solute carrier family 28 member 1 Homo sapiens 50-55 18199742-7 2008 Although this cysteine residue is also present in hCNT1 and hCNT2, neither transporter was affected by PCMBS. Cysteine 14-22 solute carrier family 28 member 2 Homo sapiens 60-65 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. Cysteine 174-177 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. Cysteine 174-177 cytochrome c oxidase copper chaperone COX17 Homo sapiens 60-65 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. Cysteine 182-185 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. Cysteine 182-185 cytochrome c oxidase copper chaperone COX17 Homo sapiens 60-65 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. Cysteine 182-185 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. Cysteine 182-185 cytochrome c oxidase copper chaperone COX17 Homo sapiens 60-65 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. Cysteine 182-185 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. Cysteine 182-185 cytochrome c oxidase copper chaperone COX17 Homo sapiens 60-65 18093982-4 2008 In human Cu(I)Cox17(2S-S) the copper(I) ion is coordinated by the sulfurs of Cys(22) and Cys(23), and this is the first example of a Cys-Cys binding motif in copper proteins. Cysteine 77-80 cytochrome c oxidase copper chaperone COX17 Homo sapiens 14-19 18093982-4 2008 In human Cu(I)Cox17(2S-S) the copper(I) ion is coordinated by the sulfurs of Cys(22) and Cys(23), and this is the first example of a Cys-Cys binding motif in copper proteins. Cysteine 89-92 cytochrome c oxidase copper chaperone COX17 Homo sapiens 14-19 18311924-1 2008 We report the involvement of transmembrane domain 4 (TM4) of hASBT in forming the putative translocation pathway, using cysteine-scanning mutagenesis in conjunction with solvent-accessibility studies using the membrane-impermeant, sulfhydryl-specific methanethiosulfonate reagents. Cysteine 120-128 solute carrier family 10 member 2 Homo sapiens 61-66 18311924-2 2008 We individually mutated each of the 21 amino acids in TM4 to cysteine on a fully functional, MTS-resistant C270A-hASBT template. Cysteine 61-69 solute carrier family 10 member 2 Homo sapiens 113-118 18206667-2 2008 Fifteen Cys residues are present in the rat EP24.15 protein, seven are solvent accessible, and two are found inside the catalytic site cleft; no intraprotein disulfide is described. Cysteine 8-11 thimet oligopeptidase 1 Rattus norvegicus 44-51 18162172-5 2008 The phosphopeptides were ligated via an N-terminal cysteine to the thioester-activated C-terminus of human aldo/keto reductase AKR1A1. Cysteine 51-59 aldo-keto reductase family 1 member A1 Homo sapiens 127-133 18178549-1 2008 Inside the endoplasmic reticulum (ER) formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sulfatases the post-translational oxidation of a specific cysteine. Cysteine 165-173 sulfatase modifying factor 1 Homo sapiens 71-74 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. Cysteine 192-200 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. Cysteine 192-200 sulfatase modifying factor 1 Homo sapiens 265-268 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. Cysteine 217-226 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. Cysteine 217-226 sulfatase modifying factor 1 Homo sapiens 265-268 18178549-7 2008 The N-terminal region of FGE harboring Cys(50) and Cys(52) is dispensible for catalytic activity in vitro but required for FGE-mediated activation of sulfatases in vivo. Cysteine 39-42 sulfatase modifying factor 1 Homo sapiens 25-28 18178549-7 2008 The N-terminal region of FGE harboring Cys(50) and Cys(52) is dispensible for catalytic activity in vitro but required for FGE-mediated activation of sulfatases in vivo. Cysteine 39-42 sulfatase modifying factor 1 Homo sapiens 123-126 18178549-7 2008 The N-terminal region of FGE harboring Cys(50) and Cys(52) is dispensible for catalytic activity in vitro but required for FGE-mediated activation of sulfatases in vivo. Cysteine 51-54 sulfatase modifying factor 1 Homo sapiens 25-28 18322093-2 2008 These exogenous compounds activate TRPA1 by covalent modification of cysteine residues. Cysteine 69-77 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 35-40 18364033-6 2008 Cysteine-reducing agents suppressed H(2)O(2)-induced TRPA1 activation, whereas cysteine-oxidizing agents activated TRPA1. Cysteine 0-8 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 53-58 18364033-6 2008 Cysteine-reducing agents suppressed H(2)O(2)-induced TRPA1 activation, whereas cysteine-oxidizing agents activated TRPA1. Cysteine 79-87 transient receptor potential cation channel, subfamily A, member 1 Mus musculus 115-120 18266766-1 2008 Formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sulfatases the oxidation of a specific cysteine residue to formylglycine, which is the catalytic residue required for sulfate ester hydrolysis. Cysteine 108-116 sulfatase modifying factor 1 Homo sapiens 0-31 18266766-1 2008 Formylglycine-generating enzyme (FGE) catalyzes in newly synthesized sulfatases the oxidation of a specific cysteine residue to formylglycine, which is the catalytic residue required for sulfate ester hydrolysis. Cysteine 108-116 sulfatase modifying factor 1 Homo sapiens 33-36 18094190-10 2008 These are the first results that demonstrate a possible role of the cysteine-rich domain 3 in the function of the Tvb receptors. Cysteine 68-76 tumor necrosis factor receptor superfamily, member 10b Gallus gallus 114-117 18205395-3 2008 The changes in KOR conformation were subequently examined via the substituted cysteine accessibility method (SCAM) in transmembrane domains 6 (TM6) and 7 (TM7) and extracellular loop 2 (EL2). Cysteine 78-86 opioid receptor kappa 1 Homo sapiens 15-18 18211101-11 2008 The pKa at pH 6.4 has been assigned to Cys-57 and Cys-490"; the thiolate on Cys-490" is the nucleophile in the reduction of Trx. Cysteine 39-42 uncharacterized protein Drosophila melanogaster 124-127 18029351-9 2008 Site-directed mutagenesis revealed that Cys-152 of cPLA(2)alpha is critical for S-nitrosylation. Cysteine 40-43 phospholipase A2 group IVA Homo sapiens 51-63 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 11-19 kelch-like ECH-associated protein 1 Mus musculus 101-106 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 11-19 kelch-like ECH-associated protein 1 Mus musculus 203-208 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 46-49 kelch-like ECH-associated protein 1 Mus musculus 101-106 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 46-49 kelch-like ECH-associated protein 1 Mus musculus 203-208 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 58-61 kelch-like ECH-associated protein 1 Mus musculus 101-106 18057000-6 2008 Similarly, cysteine residues corresponding to Cys-273 and Cys-288 in the intervening region of mouse Keap1, which are essential for the repression of Nrf2 activity in cultured cells, are conserved among Keap1 orthologs in vertebrates and invertebrates, except fish. Cysteine 58-61 kelch-like ECH-associated protein 1 Mus musculus 203-208 18057000-8 2008 To our surprise, Keap1a and Keap1b contain the cysteine residue corresponding to Cys-288 and Cys-273, respectively. Cysteine 47-55 kelch-like ECH-associated protein 1b Danio rerio 28-34 18057000-8 2008 To our surprise, Keap1a and Keap1b contain the cysteine residue corresponding to Cys-288 and Cys-273, respectively. Cysteine 81-84 kelch-like ECH-associated protein 1b Danio rerio 28-34 18057000-8 2008 To our surprise, Keap1a and Keap1b contain the cysteine residue corresponding to Cys-288 and Cys-273, respectively. Cysteine 93-96 kelch-like ECH-associated protein 1b Danio rerio 28-34 18057000-10 2008 Individual mutation of either residual cysteine residue in Keap1a and Keap1b disrupted the ability of Keap1 to repress Nrf2, indicating that the presence of either Cys-273 or Cys-288 is sufficient for fish Keap1 molecules to fully function. Cysteine 39-47 kelch-like ECH-associated protein 1 Mus musculus 59-64 18057000-11 2008 These results provide an important insight into the means by which Keap1 cysteines act as sensors of electrophiles and oxidants. Cysteine 73-82 kelch-like ECH-associated protein 1 Mus musculus 67-72 18395796-5 2008 IL-17s from the oyster, sea urchin, trout and human, contained conserved cysteine residues found in all forms of IL-17 in mammals. Cysteine 73-81 interleukin 17A Homo sapiens 0-5 18067579-3 2008 We used mass spectrometry to assess the state of oxidation of the catalytic cysteine residue of endogenous PTP1B and show that this residue underwent both reversible and irreversible oxidation to high stoichiometry in response to intrinsic reactive oxygen species production. Cysteine 76-84 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 107-112 18067579-4 2008 In addition, our data show that the oxidation of PTP1B is specific to the active site Cys, with the other Cys residues in the protein remaining in a reduced state. Cysteine 86-89 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 49-54 18067579-4 2008 In addition, our data show that the oxidation of PTP1B is specific to the active site Cys, with the other Cys residues in the protein remaining in a reduced state. Cysteine 106-109 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 49-54 18083058-4 2008 We have introduced specific mutations into a conserved motif at the mid-point of the Cys-loop of the GABA A receptor subunits alpha1, beta2 and gamma2S where the sequence reads aromatic, proline, aliphatic (ArProAl motif). Cysteine 85-88 hemoglobin, beta adult minor chain Mus musculus 134-139 17940192-1 2008 Voltage-clamp fluorometry was performed with a cysteine-deprived mutant of rat organic cation transporter 1 (rOCT1) in which Phe483 in transmembrane alpha-helix (TMH) 11 close to the extracellular surface was replaced by cysteine and labeled with tetramethylrhodamine-6-maleimide. Cysteine 47-55 solute carrier family 22 member 1 Rattus norvegicus 79-107 17940192-1 2008 Voltage-clamp fluorometry was performed with a cysteine-deprived mutant of rat organic cation transporter 1 (rOCT1) in which Phe483 in transmembrane alpha-helix (TMH) 11 close to the extracellular surface was replaced by cysteine and labeled with tetramethylrhodamine-6-maleimide. Cysteine 47-55 solute carrier family 22 member 1 Rattus norvegicus 109-114 17940192-1 2008 Voltage-clamp fluorometry was performed with a cysteine-deprived mutant of rat organic cation transporter 1 (rOCT1) in which Phe483 in transmembrane alpha-helix (TMH) 11 close to the extracellular surface was replaced by cysteine and labeled with tetramethylrhodamine-6-maleimide. Cysteine 221-229 solute carrier family 22 member 1 Rattus norvegicus 109-114 17928294-5 2007 Here, we report the solution structure of the Sec13-->Cys variant of mouse SelW determined through high resolution NMR spectroscopy. Cysteine 57-60 selenoprotein W Mus musculus 78-82 17976514-0 2007 Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions. Cysteine 31-39 DnaJ heat shock protein family (Hsp40) member B11 Homo sapiens 25-30 17976514-2 2007 However, the Cys-rich region of the endoplasmic reticulum localized HEDJ (ERdj3/ERj3p), is considerably different in sequence and arrangement. Cysteine 13-16 DnaJ heat shock protein family (Hsp40) member B11 Homo sapiens 74-79 17976514-2 2007 However, the Cys-rich region of the endoplasmic reticulum localized HEDJ (ERdj3/ERj3p), is considerably different in sequence and arrangement. Cysteine 13-16 DnaJ heat shock protein family (Hsp40) member B11 Homo sapiens 80-85 17693579-3 2007 Although MCs express CysLT(2), their responses to cys-LTs are blocked by antagonists of CysLT(1). Cysteine 50-53 Miles-Carpenter X-linked mental retardation syndrome Homo sapiens 9-12 17693579-5 2007 Cys-LT-mediated responses were absent in MCs from mice lacking CysLT(1) receptors, but enhanced by the absence of CysLT(2) receptors. Cysteine 0-3 Miles-Carpenter X-linked mental retardation syndrome Homo sapiens 41-44 17845056-0 2007 Effect of pathogenic cysteine mutations on FGFR3 transmembrane domain dimerization in detergents and lipid bilayers. Cysteine 21-29 fibroblast growth factor receptor 3 Homo sapiens 43-48 17845056-3 2007 Here we study three pathogenic Cys mutations, associated with either thanatophoric dysplasia or achondroplasia, in the TM domain of fibroblast growth factor receptors 3 (FGFR3). Cysteine 31-34 fibroblast growth factor receptor 3 Homo sapiens 132-168 17845056-3 2007 Here we study three pathogenic Cys mutations, associated with either thanatophoric dysplasia or achondroplasia, in the TM domain of fibroblast growth factor receptors 3 (FGFR3). Cysteine 31-34 fibroblast growth factor receptor 3 Homo sapiens 170-175 17575076-6 2007 A deletion study identified the cysteine-rich region (CRR) of SNAP-23 as the binding site for annexin A2. Cysteine 32-40 synaptosome associated protein 23 Homo sapiens 62-69 17653867-4 2007 This interaction is mediated by the cysteine-rich region found in the C-terminal part of the Siva-1 protein. Cysteine 36-44 SIVA1 apoptosis inducing factor Homo sapiens 93-99 17624763-10 2007 These data characterize the roles of Cys residues in 3beta-HSD and validate the predictions of our structural model. Cysteine 37-40 hydroxy-delta-5-steroid dehydrogenase, 3 beta- and steroid delta-isomerase 1 Homo sapiens 53-62 17588140-0 2007 The functional role of cysteine residues for c-Abl kinase activity. Cysteine 23-31 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 45-50 17588140-3 2007 In this study, we show that the kinase activity of the non-receptor tyrosine kinase c-Abl is inhibited by in vitro thiol modification; specifically, the cysteine residues of c-Abl are modified by S-glutathionylation and by thiol alkylating agents such as 4-acetamido-4"-maleimidylstilbene-2,2"-disulfonic acid and N-ethylmaleimide. Cysteine 153-161 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 84-89 17588140-3 2007 In this study, we show that the kinase activity of the non-receptor tyrosine kinase c-Abl is inhibited by in vitro thiol modification; specifically, the cysteine residues of c-Abl are modified by S-glutathionylation and by thiol alkylating agents such as 4-acetamido-4"-maleimidylstilbene-2,2"-disulfonic acid and N-ethylmaleimide. Cysteine 153-161 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 174-179 17588140-4 2007 Modification of cysteine residues of c-Abl tyrosine kinase using glutathione disulfide and thiol alkylating agents corresponds to a concomitant loss of kinase activity. Cysteine 16-24 ABL proto-oncogene 1, non-receptor tyrosine kinase Homo sapiens 37-42 17602574-1 2007 Mammalian cysteine dioxygenase (CDO) is a non-heme iron metalloenzyme that catalyzes the first committed step in oxidative cysteine catabolism. Cysteine 10-18 cysteine dioxygenase 1, cytosolic Mus musculus 32-35 17602574-4 2007 In these experiments, CDO exhibits an ordered binding of l-cysteine prior to NO (and presumably O2) similar to that observed for the 2H1C class of non-heme iron enzymes. Cysteine 57-67 cysteine dioxygenase 1, cytosolic Mus musculus 22-25 17602574-5 2007 Moreover, the CDO active site is essentially unreactive toward NO in the absence of substrate, suggesting an obligate ordered binding of l-cysteine prior to NO. Cysteine 137-147 cysteine dioxygenase 1, cytosolic Mus musculus 14-17 17602574-7 2007 However, upon addition of NO to CDO in the presence of substrate l-cysteine, a low-spin {FeNO}7 (S = 1/2) signal that accounts for approximately 85% of the iron within the enzyme develops. Cysteine 65-75 cysteine dioxygenase 1, cytosolic Mus musculus 32-35 17602574-10 2007 The unusual {FeNO}7 (S = 1/2) electronic configuration adopted by the substrate-bound iron-nitrosyl CDO (termed {ES-NO}7) is a result of the bidentate thiol/amine coordination of l-cysteine in the NO-bound CDO active site. Cysteine 179-189 cysteine dioxygenase 1, cytosolic Mus musculus 100-103 17602574-10 2007 The unusual {FeNO}7 (S = 1/2) electronic configuration adopted by the substrate-bound iron-nitrosyl CDO (termed {ES-NO}7) is a result of the bidentate thiol/amine coordination of l-cysteine in the NO-bound CDO active site. Cysteine 179-189 cysteine dioxygenase 1, cytosolic Mus musculus 206-209 17521670-13 2007 In beta/gamma-actin, this is the cysteine residue most reactive towards H(2)O(2) in solution, and we suggest plausible structural determinants for its reactivity. Cysteine 33-41 POTE ankyrin domain family member F Homo sapiens 3-19 17611274-3 2007 SPARC (secreted protein acidic rich in cysteine) (osteonectin) was identified as an OEC-derived matricellular protein that can indirectly enhance the ability of Schwann cells to stimulate dorsal root ganglion outgrowth in vitro. Cysteine 39-47 secreted protein acidic and cysteine rich Rattus norvegicus 0-5 17611274-3 2007 SPARC (secreted protein acidic rich in cysteine) (osteonectin) was identified as an OEC-derived matricellular protein that can indirectly enhance the ability of Schwann cells to stimulate dorsal root ganglion outgrowth in vitro. Cysteine 39-47 secreted protein acidic and cysteine rich Rattus norvegicus 50-61 17371789-6 2007 When NAC supplied 10 or 20 g/kg of Cys, chick growth performance was unaffected, but NAC supplying 30 or 40 g/kg of Cys reduced (P < 0.05) BW gain by 13 and 34%, respectively, relative to the unsupplemented control diet. Cysteine 35-38 X-linked Kx blood group Homo sapiens 5-8 17503775-3 2007 Herein, we performed extensive sequence similarity searches to define and characterize a new protein family, designated Rdx, that includes mammalian selenoproteins SelW, SelV, SelT and SelH, bacterial SelW-like proteins and cysteine-containing proteins of unknown function in all three domains of life. Cysteine 224-232 radixin Homo sapiens 120-123 17503775-7 2007 By analogy to thioredoxin, Rdx proteins can use catalytic cysteine (or Sec) to form transient mixed disulfides with substrate proteins. Cysteine 58-66 radixin Homo sapiens 27-30 17475278-6 2007 In the complex, Smt3p binds a surface distal from Ubc9"s catalytic cysteine. Cysteine 67-75 SUMO family protein SMT3 Saccharomyces cerevisiae S288C 16-21 17475278-7 2007 The structure implies that a single molecule of Smt3p cannot bind concurrently to both the non-covalent binding site and the catalytic cysteine of a single Ubc9p molecule. Cysteine 135-143 SUMO family protein SMT3 Saccharomyces cerevisiae S288C 48-53 17475278-8 2007 However, formation of higher-order complexes can occur, where a single Smt3p covalently linked to one Ubc9p"s catalytic cysteine also binds non-covalently to another molecule of Ubc9p. Cysteine 120-128 SUMO family protein SMT3 Saccharomyces cerevisiae S288C 71-76 17317215-0 2007 Expression, purification, and in vitro cysteine-10 modification of native sequence recombinant human transthyretin. Cysteine 39-47 transthyretin Homo sapiens 101-114 17439147-10 2007 Among the differences of amino acid residues found between the two genes, a Cys to Ser exchange may be responsible for the inactivation of resultant protein product of S. lycopersicon gene because the Cys is an essential amino acid residue for HPL activity. Cysteine 76-79 fatty acid hydroperoxide lyase, chloroplastic Solanum lycopersicum 244-247 17439147-10 2007 Among the differences of amino acid residues found between the two genes, a Cys to Ser exchange may be responsible for the inactivation of resultant protein product of S. lycopersicon gene because the Cys is an essential amino acid residue for HPL activity. Cysteine 201-204 fatty acid hydroperoxide lyase, chloroplastic Solanum lycopersicum 244-247 17452787-2 2007 Molecular oxygen oxidizes the cysteine precursor in eukaryotic sulfatases, a reaction that is catalysed by the formylglycine-generating enzyme FGE. Cysteine 30-38 sulfatase modifying factor 1 Homo sapiens 143-146 17350155-2 2007 NO can react with Hb in at least 3 ways: 1) formation of Hb(II)NO, 2) formation of methemoglobin, and 3) formation of S-nitrosohemoglobin, through nitrosylation of the beta93 Cys residue. Cysteine 175-178 hemoglobin subunit gamma 2 Homo sapiens 83-103 17434493-1 2007 Aminoacylase III (AAIII) plays an important role in deacetylation of acetylated amino acids and N-acetylated S-cysteine conjugates of halogenated alkenes and alkanes. Cysteine 109-119 aspartoacylase (aminoacylase) 3 Mus musculus 0-16 17434493-1 2007 Aminoacylase III (AAIII) plays an important role in deacetylation of acetylated amino acids and N-acetylated S-cysteine conjugates of halogenated alkenes and alkanes. Cysteine 109-119 aspartoacylase (aminoacylase) 3 Mus musculus 18-23 17208454-2 2007 Cox17 contains six conserved Cys residues and occurs in three different oxidative states, which display different metal-binding properties and stability. Cysteine 29-32 cytochrome c oxidase copper chaperone COX17 Homo sapiens 0-5 17275330-2 2007 Vav1 is also a unique member of the GEF family in that it contains a cysteine-rich domain (CRD) that is critical for Rac1 binding and maximal guanine nucleotide exchange activity, and thus may provide a unique protein-protein interface compared to other GEF/GTPase pairs. Cysteine 69-77 Rho/Rac guanine nucleotide exchange factor 2 Homo sapiens 36-39 17275330-2 2007 Vav1 is also a unique member of the GEF family in that it contains a cysteine-rich domain (CRD) that is critical for Rac1 binding and maximal guanine nucleotide exchange activity, and thus may provide a unique protein-protein interface compared to other GEF/GTPase pairs. Cysteine 69-77 Rac family small GTPase 1 Homo sapiens 117-121 17329245-7 2007 The elongation of Pen-2 N terminus caused a reduction in the water accessibility of the luminal side of the catalytic pore of PS1 in a similar manner to that caused by an Abeta42-raising gamma-secretase modulator, fenofibrate, as determined by substituted cysteine accessibility method. Cysteine 256-264 presenilin enhancer, gamma-secretase subunit Homo sapiens 18-23 17337453-3 2007 By sensitive sequence and structure analyses, we identified SelH as a thioredoxin fold-like protein in which a conserved CXXU motif (cysteine separated by two other residues from selenocysteine) corresponds to the CXXC motif in thioredoxins. Cysteine 133-141 selenoprotein H Homo sapiens 60-64 17337453-7 2007 We cloned wild-type and cysteine mutant forms of SelH either upstream or downstream of green fluorescent protein (GFP) and localized this fusion protein to the nucleus in transfected mammalian cells, whereas mutations in the RKRK motif resulted in the cytosolic protein. Cysteine 24-32 selenoprotein H Homo sapiens 49-53 17517190-1 2007 BACKGROUND: O(6)-methylguanine-DNA-methyltransferase (MGMT) is a specific DNA revising enzyme transferring alkylated groups from DNA to its cysteine residue to avoid the abnormal twisting of DNA. Cysteine 140-148 O-6-methylguanine-DNA methyltransferase Homo sapiens 12-52 17517190-1 2007 BACKGROUND: O(6)-methylguanine-DNA-methyltransferase (MGMT) is a specific DNA revising enzyme transferring alkylated groups from DNA to its cysteine residue to avoid the abnormal twisting of DNA. Cysteine 140-148 O-6-methylguanine-DNA methyltransferase Homo sapiens 54-58 17331978-3 2007 Pathogenic mutations lead to an odd number of cysteine residues within the NOTCH3 extracellular domain (NOTCH3(ECD)), and are associated with progressive accumulation of NOTCH3(ECD) at the SMC plasma membrane. Cysteine 46-54 notch 3 Mus musculus 75-81 17331978-3 2007 Pathogenic mutations lead to an odd number of cysteine residues within the NOTCH3 extracellular domain (NOTCH3(ECD)), and are associated with progressive accumulation of NOTCH3(ECD) at the SMC plasma membrane. Cysteine 46-54 notch 3 Mus musculus 104-110 17331978-3 2007 Pathogenic mutations lead to an odd number of cysteine residues within the NOTCH3 extracellular domain (NOTCH3(ECD)), and are associated with progressive accumulation of NOTCH3(ECD) at the SMC plasma membrane. Cysteine 46-54 notch 3 Mus musculus 104-110 17234728-11 2007 CONCLUSIONS: In cells overexpressing SERCA, the cyclic GMP-independent, redox regulation of SERCA cysteine-674 is required for the inhibition of cell migration by both exogenous and endogenously generated NO. Cysteine 98-106 5'-nucleotidase, cytosolic II Homo sapiens 55-58 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. Cysteine 41-44 vitronectin Homo sapiens 50-53 17260973-7 2007 The binding site of GGT for the Cys-Gly moiety of glutathione or for the acceptor molecules was probed by the phosphonate diesters to reveal a significant difference in the mechanism of substrate recognition between E. coli and human GGT. Cysteine 32-35 inactive glutathione hydrolase 2 Homo sapiens 20-23 17260973-7 2007 The binding site of GGT for the Cys-Gly moiety of glutathione or for the acceptor molecules was probed by the phosphonate diesters to reveal a significant difference in the mechanism of substrate recognition between E. coli and human GGT. Cysteine 32-35 inactive glutathione hydrolase 2 Homo sapiens 234-237 17009962-2 2007 Dystrophin and its autosomal homologue utrophin interact with beta-dystroglycan via their highly conserved C-terminal cysteine-rich regions, comprising the WW domain (protein-protein interaction domain containing two conserved tryptophan residues), EF hand and ZZ domains. Cysteine 118-126 utrophin Homo sapiens 39-47 17208193-6 2007 In the human SDH, mutation of this tyrosine to cysteine results in paraganglioma, tumors of the parasympathetic ganglia in the head and neck. Cysteine 47-55 succinate dehydrogenase complex iron sulfur subunit B Homo sapiens 13-16 17233604-3 2007 We observed that human MCF7 breast cancer cells that overexpress IGF1R efficiently internalized fluorescein-chelator-PNA-D(Cys-Ser-Lys-Cys) to the cytoplasm, but not with D(Cys-Ala-Ala-Cys). Cysteine 123-126 insulin like growth factor 1 receptor Homo sapiens 65-70 17233604-3 2007 We observed that human MCF7 breast cancer cells that overexpress IGF1R efficiently internalized fluorescein-chelator-PNA-D(Cys-Ser-Lys-Cys) to the cytoplasm, but not with D(Cys-Ala-Ala-Cys). Cysteine 135-138 insulin like growth factor 1 receptor Homo sapiens 65-70 17233604-3 2007 We observed that human MCF7 breast cancer cells that overexpress IGF1R efficiently internalized fluorescein-chelator-PNA-D(Cys-Ser-Lys-Cys) to the cytoplasm, but not with D(Cys-Ala-Ala-Cys). Cysteine 135-138 insulin like growth factor 1 receptor Homo sapiens 65-70 17167040-5 2007 Site-directed mutagenesis based on a modeled structure of the toad protein revealed that Cys(59) and Thr(61) residues were crucial for the PGDS activity. Cysteine 89-92 prostaglandin D2 synthase (brain) Mus musculus 139-143 17251580-3 2007 Mutational analysis of cysteine and histidine residues within the conserved N-terminal zinc-binding domain in NSP1 of bovine rotavirus strain B641 abolished IRF3 degradation in transfected cells. Cysteine 23-31 interferon regulatory factor 3 Bos taurus 157-161 17187819-4 2007 We now report robust preparation of MHC tetramers with small molecule fluorophores, using a recombinant mutant of streptavidin incorporating a carboxy-terminal cysteine in each of the four identical subunits that is conjugated to maleimide derivatives of any of several small molecule fluorophores. Cysteine 160-168 major histocompatibility complex, class I, C Homo sapiens 36-39 17223684-6 2007 Previously, Cys-304 of Esa1 was the proposed nucleophile that forms an acetyl-cysteine intermediate. Cysteine 12-15 lysine acetyltransferase 5 Homo sapiens 23-27 17223684-7 2007 Here, mutation of this cysteine (C304A) in Esa1 or within the piccolo NuA4 complex yielded an enzyme that was catalytically indistinguishable from the wild type. Cysteine 23-31 lysine acetyltransferase 5 Homo sapiens 43-47 16981855-4 2007 Epitope mapping using chimaeras of the IGF-1R and insulin receptor revealed that the mAbs bind to the CR (cysteine-rich) domain of IGF-1R. Cysteine 106-114 insulin like growth factor 1 receptor Homo sapiens 39-66 16981855-4 2007 Epitope mapping using chimaeras of the IGF-1R and insulin receptor revealed that the mAbs bind to the CR (cysteine-rich) domain of IGF-1R. Cysteine 106-114 insulin like growth factor 1 receptor Homo sapiens 39-45 17175208-9 2007 The sulfonated cysteines have two sulfite oxygens involved in intramonomer hydrogen bonds that bridge Cys10, the amino acid immediately before beta-strand A, to the amino acids immediately after the edge beta-strand D. Implications of the newly observed interactions in the inhibition of fibril formation are discussed in light of the recent structural models of TTR amyloid fibrils. Cysteine 15-24 transthyretin Homo sapiens 363-366 17498549-1 2007 Degradation of elastin, the main amorphous component of elastic fibers, by elastases belonging to the serine, metallo, or cysteine families leads to the generation of elastin fragments, designated as elastokines in keeping with their cytokine-like properties. Cysteine 122-130 elastin Homo sapiens 15-22 17498549-1 2007 Degradation of elastin, the main amorphous component of elastic fibers, by elastases belonging to the serine, metallo, or cysteine families leads to the generation of elastin fragments, designated as elastokines in keeping with their cytokine-like properties. Cysteine 122-130 elastin Homo sapiens 167-174 17202439-2 2007 Interestingly, the decreased CYP1A2, 2C11, and 3A1/2 in PCM rats returned fully or partially to control levels by oral cysteine supplementation (PCMC rats). Cysteine 119-127 cytochrome P450, family 1, subfamily a, polypeptide 2 Rattus norvegicus 29-35 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. Cysteine 107-116 uroplakin 1B Homo sapiens 49-53 17172357-0 2006 The coactivator function of Arabidopsis NPR1 requires the core of its BTB/POZ domain and the oxidation of C-terminal cysteines. Cysteine 117-126 regulatory protein (NPR1) Arabidopsis thaliana 40-44 17172357-1 2006 NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. Cysteine 195-198 regulatory protein (NPR1) Arabidopsis thaliana 45-49 17172357-1 2006 NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. Cysteine 195-198 regulatory protein (NPR1) Arabidopsis thaliana 217-221 17172357-1 2006 NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. Cysteine 206-209 regulatory protein (NPR1) Arabidopsis thaliana 45-49 17172357-1 2006 NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import. Cysteine 206-209 regulatory protein (NPR1) Arabidopsis thaliana 217-221 17172357-6 2006 However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. Cysteine 219-222 bZIP transcription factor family protein Arabidopsis thaliana 36-40 17172357-6 2006 However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. Cysteine 219-222 regulatory protein (NPR1) Arabidopsis thaliana 93-97 17172357-6 2006 However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. Cysteine 231-234 bZIP transcription factor family protein Arabidopsis thaliana 36-40 17172357-6 2006 However, after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain (residues 80 to 91) and the oxidation of NPR1 Cys-521 and Cys-529. Cysteine 231-234 regulatory protein (NPR1) Arabidopsis thaliana 93-97 17194764-1 2006 In plants, association of O-acetylserine sulfhydrylase (OASS) and Ser acetyltransferase (SAT) into the Cys synthase complex plays a regulatory role in sulfur assimilation and Cys biosynthesis. Cysteine 103-106 nuclear shuttle interacting Arabidopsis thaliana 70-87 17112441-0 2006 Cysteine 138 mutation in HIV-1 Nef from patients with delayed disease progression. Cysteine 0-8 Nef Human immunodeficiency virus 1 31-34 17112441-6 2006 However, the results demonstrate a high incidence of a single amino acid polymorphism (cysteine 138) in HIV-1 Nef. Cysteine 87-95 Nef Human immunodeficiency virus 1 110-113 17014882-2 2006 Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316. Cysteine 163-171 integrin subunit alpha 2b Homo sapiens 126-133 17014882-2 2006 Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316. Cysteine 249-257 integrin subunit alpha 2b Homo sapiens 126-133 16930563-10 2006 It preferentially inhibited the activities of the cell cycle controlling phosphatases Cdc25A and Cdc25B, by binding to their catalytic cysteines. Cysteine 135-144 cell division cycle 25A Homo sapiens 86-92 16901717-6 2006 In addition, the extreme N-terminal cysteine residue of TGF-beta2 or -beta3 was replaced by a serine residue. Cysteine 36-44 transforming growth factor beta 2 Homo sapiens 56-75 16845127-5 2006 In the present paper, three sequence characteristics of the isoenzyme (PLD2) that corresponds to the often used enzyme isolated from cabbage leaves have been probed for their importance in hydrolysis as well as transphosphatidylation activities: (i) the two HKD motifs, (ii) the C terminus and (iii) the eight cysteine residues. Cysteine 310-318 phospholipase D alpha 2 Brassica oleracea 71-75 16873361-12 2006 Because the homologous amino acid in PDE3B is Cys(792), we prepared the mutant Y807C and found that its K(m) and k(cat) were similar to the wild type. Cysteine 46-49 phosphodiesterase 3B Homo sapiens 37-42 16861740-6 2006 Interestingly, PKCiota (and PKCzeta) contains a unique cysteine residue, Cys-69, within its PB1 domain that is not present in other PB1 domain containing proteins. Cysteine 55-63 protein kinase C zeta Homo sapiens 28-35 16861740-6 2006 Interestingly, PKCiota (and PKCzeta) contains a unique cysteine residue, Cys-69, within its PB1 domain that is not present in other PB1 domain containing proteins. Cysteine 73-76 protein kinase C zeta Homo sapiens 28-35 16627576-3 2006 Overexpression of CDO in 3T3-L1 preadipocytes caused a decrease in the level of cysteine (precursor of taurine) and an increase in the level of taurine in the culture medium, suggesting that CDO is involved in biosynthesis and secretion of taurine in white adipose tissue. Cysteine 80-88 cysteine dioxygenase 1, cytosolic Mus musculus 18-21 16781459-1 2006 Hydrogen sulfide (H(2)S), a regulatory gaseous molecule that is endogenously synthesized by cystathionine gamma-lyase (CSE) and/or cystathionine beta-synthase (CBS) from L-cysteine (L-Cys) metabolism, is a putative vasodilator, and its role in nitric oxide (NO) production is unexplored. Cysteine 170-180 cystathionine gamma-lyase Homo sapiens 92-117 16781459-1 2006 Hydrogen sulfide (H(2)S), a regulatory gaseous molecule that is endogenously synthesized by cystathionine gamma-lyase (CSE) and/or cystathionine beta-synthase (CBS) from L-cysteine (L-Cys) metabolism, is a putative vasodilator, and its role in nitric oxide (NO) production is unexplored. Cysteine 170-180 cystathionine gamma-lyase Homo sapiens 119-122 16781459-1 2006 Hydrogen sulfide (H(2)S), a regulatory gaseous molecule that is endogenously synthesized by cystathionine gamma-lyase (CSE) and/or cystathionine beta-synthase (CBS) from L-cysteine (L-Cys) metabolism, is a putative vasodilator, and its role in nitric oxide (NO) production is unexplored. Cysteine 182-187 cystathionine gamma-lyase Homo sapiens 92-117 16781459-1 2006 Hydrogen sulfide (H(2)S), a regulatory gaseous molecule that is endogenously synthesized by cystathionine gamma-lyase (CSE) and/or cystathionine beta-synthase (CBS) from L-cysteine (L-Cys) metabolism, is a putative vasodilator, and its role in nitric oxide (NO) production is unexplored. Cysteine 182-187 cystathionine gamma-lyase Homo sapiens 119-122 16781459-5 2006 Moreover, NO production in LPS-stimulated macrophages that are expressing CSE mRNA was significantly reduced by the addition of L-Cys, a substrate for H(2)S, but enhanced by the selective CSE inhibitor beta-cyano-L-alanine but not by the CBS inhibitor aminooxyacetic acid. Cysteine 128-133 cystathionine gamma-lyase Homo sapiens 74-77 16782878-6 2006 Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain. Cysteine 71-79 SECIS binding protein 2 Homo sapiens 49-53 16782878-6 2006 Oxidative stress induces nuclear accumulation of SBP2 via oxidation of cysteine residues within a redox-sensitive cysteine-rich domain. Cysteine 114-122 SECIS binding protein 2 Homo sapiens 49-53 16569633-7 2006 These effects were reduced by mutation of a cysteine residue in the Mpr1 pad1 N-terminal plus motif of POH1 (Cys-120) and appeared to be selective for c-Jun, because POH1 had no effect on other proteasomal substrates. Cysteine 44-52 proteasome 26S subunit, non-ATPase 14 Homo sapiens 103-107 16569633-7 2006 These effects were reduced by mutation of a cysteine residue in the Mpr1 pad1 N-terminal plus motif of POH1 (Cys-120) and appeared to be selective for c-Jun, because POH1 had no effect on other proteasomal substrates. Cysteine 44-52 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 151-156 16569633-7 2006 These effects were reduced by mutation of a cysteine residue in the Mpr1 pad1 N-terminal plus motif of POH1 (Cys-120) and appeared to be selective for c-Jun, because POH1 had no effect on other proteasomal substrates. Cysteine 109-112 proteasome 26S subunit, non-ATPase 14 Homo sapiens 103-107 16734414-4 2006 We specifically label cysteines introduced at several positions in the R helix of ClC-ec1 with AlexaFluor 488, an environment-sensitive fluorophore, and demonstrate that the labeled mutants show H+/Cl- transport activity indistinguishable from that of the wild-type protein. Cysteine 22-31 Charcot-Leyden crystal galectin Homo sapiens 82-85 16700898-1 2006 Proton pump inhibitors inhibit the gastric H+/K+-ATPase via covalent binding to cysteine residues of the proton pump. Cysteine 80-88 ATPase H+/K+ transporting subunit alpha Homo sapiens 0-11 16700898-1 2006 Proton pump inhibitors inhibit the gastric H+/K+-ATPase via covalent binding to cysteine residues of the proton pump. Cysteine 80-88 ATPase H+/K+ transporting subunit alpha Homo sapiens 105-116 16428267-1 2006 Endogenous hydrogen sulfide (H(2)S) is naturally synthesized in various types of mammalian cells from l-cysteine in a reaction catalyzed by two enzymes, cystathionine-gamma-lyase (CSE) and/or cystathionine-beta-synthase. Cysteine 102-112 cystathionine gamma-lyase Homo sapiens 153-178 16428267-1 2006 Endogenous hydrogen sulfide (H(2)S) is naturally synthesized in various types of mammalian cells from l-cysteine in a reaction catalyzed by two enzymes, cystathionine-gamma-lyase (CSE) and/or cystathionine-beta-synthase. Cysteine 102-112 cystathionine gamma-lyase Homo sapiens 180-183 16740914-6 2006 RESULTS: A missense mutation in PQBP1 was identified which changed the conserved tyrosine residue in the WW domain at position 65 to a cysteine (p.Y65C). Cysteine 135-143 polyglutamine binding protein 1 Homo sapiens 32-37 16818510-6 2006 It competitively inhibited the activity of Cdc25 (preferentially Cdc25A) by binding to the active site, likely through the catalytic cysteine, but did not inhibit PTP1B, CD45, or MKP-1 phosphatases. Cysteine 133-141 cell division cycle 25A Homo sapiens 43-48 16818510-6 2006 It competitively inhibited the activity of Cdc25 (preferentially Cdc25A) by binding to the active site, likely through the catalytic cysteine, but did not inhibit PTP1B, CD45, or MKP-1 phosphatases. Cysteine 133-141 cell division cycle 25A Homo sapiens 65-71 16620786-1 2006 2, 3, 5, 6-Tetrachloro-1, 4-benzoquinone (TCBQ) is a metabolite of pentachlorophenol known to react with cysteines of glutathione transferases (GSTs). Cysteine 105-114 glutathione S-transferase alpha 1 Rattus norvegicus 144-148 16620786-6 2006 A single tryptic peptide labelled with TCBQ was isolated from kidney rGSTA1-2 containing Cys-17 which we identify as the site of modification. Cysteine 89-92 glutathione S-transferase alpha 1 Rattus norvegicus 69-77 16620786-9 2006 Homology modelling of rGSTA1-1 modified at Cys-17 of one subunit revealed only modest structural perturbations in the second subunit and tends to exclude global structural effects. Cysteine 43-46 glutathione S-transferase alpha 2 Rattus norvegicus 22-30 16709244-7 2006 Mutations in the Dbl homology, pleckstrin homology, or cysteine-rich domains of Vav1Y3F abolished Rac1 or ERK activation in the absence of EGF and blocked the migration-promoting activity of Vav1Y3F. Cysteine 55-63 Rac family small GTPase 1 Homo sapiens 98-102 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. Cysteine 85-93 major histocompatibility complex, class I, G Homo sapiens 67-72 16632116-2 2006 Increased GGT activity has been hypothesized to play a role in subsequent mitochondrial complex I (CI) inhibition by increasing cysteine as substrate for cellular uptake. Cysteine 128-136 inactive glutathione hydrolase 2 Homo sapiens 10-13 16756473-5 2006 Sequence analyses revealed point mutations in two different genes: the normal ACC sequence at codon 620 of the TSHR gene was replaced by ATC, changing the threonine by isoleucine (T620I); and the wild-type GGT at codon 12 of Ki-RAS mutated to TGT, replacing glycine by cysteine (G12C). Cysteine 269-277 thyroid stimulating hormone receptor Homo sapiens 111-115 16497670-8 2006 We suggest that SCF(Met30) activity or Met4 utilization as a substrate may be directly regulated by intracellular cysteine concentrations. Cysteine 114-122 ubiquitin-binding SDF ubiquitin ligase complex subunit MET30 Saccharomyces cerevisiae S288C 20-25 16516848-3 2006 Cysteine oxidation alters functional properties of Slo1 channels and has been suggested to contribute to the decrease in the channel activity following patch excision often referred to as rundown. Cysteine 0-8 potassium calcium-activated channel subfamily M alpha 1 Homo sapiens 51-55 16516848-4 2006 This study examined the biophysical mechanism of rundown and whether oxidation of cysteine residues located in the C-terminus of the human Slo1 channel (C430 and C911) plays a role. Cysteine 82-90 potassium calcium-activated channel subfamily M alpha 1 Homo sapiens 139-143 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. Cysteine 100-103 major histocompatibility complex, class I, G Homo sapiens 70-75 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. Cysteine 108-111 major histocompatibility complex, class I, G Homo sapiens 70-75 16584200-1 2006 Using cysteine mutagenesis and chemical modification by methanethiosulfonate derivatives, it was demonstrated that the external putative loop, joining transmembrane segments (TM"s) IV-V of rabbit Na+/glucose cotransporter, rSGLT1, forms part of a Na+ binding and voltage sensing domain. Cysteine 6-14 solute carrier family 5 member 1 Rattus norvegicus 223-229 16545087-8 2006 We present our structural and functional studies of a novel mouse beta-defensin-related peptide (Defr1) which contains only five cysteine residues. Cysteine 129-137 defensin beta 8 Mus musculus 97-102 16545087-9 2006 Synthetic Defr1 was more active than its six-cysteine analogue against a large panel of pathogens. Cysteine 44-53 defensin beta 8 Mus musculus 10-15 16537594-5 2006 We report here that C1-ts1-S cells proliferate more slowly, produce less virus, show reduced H2O2 levels, increase their uptake of cystine, and maintain higher levels of intracellular GSH and cysteine compared to acutely infected or uninfected C1 cells. Cysteine 192-200 Trichinella spiralis resistance 1 Mus musculus 23-26 16536551-2 2006 The molecular design made use of a genetically engineered chaperonin GroEL bearing, at both entrance parts of its cylindrical cavity, cysteine residues, which were functionalized by an azobenzene derivative to construct photoresponsive mechanical gates (azo-GroEL). Cysteine 134-142 heat shock protein family D (Hsp60) member 1 Homo sapiens 69-74 16407224-11 2006 These findings indicate a link between the redox active site cysteine-independent action of TRX2 and the level of Bcl-xL in the regulation of apoptosis. Cysteine 61-69 BCL2 like 1 Gallus gallus 114-120 16519524-1 2006 The high-affinity binding site in human vitronectin (VN) for plasminogen activator inhibitor-1 (PAI-1) has been localized to the NH(2)-terminal cysteine-rich somatomedin B (SMB) domain (residues 1-44). Cysteine 144-152 vitronectin Homo sapiens 40-51 16519524-1 2006 The high-affinity binding site in human vitronectin (VN) for plasminogen activator inhibitor-1 (PAI-1) has been localized to the NH(2)-terminal cysteine-rich somatomedin B (SMB) domain (residues 1-44). Cysteine 144-152 vitronectin Homo sapiens 53-55 16519524-1 2006 The high-affinity binding site in human vitronectin (VN) for plasminogen activator inhibitor-1 (PAI-1) has been localized to the NH(2)-terminal cysteine-rich somatomedin B (SMB) domain (residues 1-44). Cysteine 144-152 vitronectin Homo sapiens 158-171 16339885-0 2006 Redox regulation of CLIC1 by cysteine residues associated with the putative channel pore. Cysteine 29-37 chloride intracellular channel 1 Homo sapiens 20-25 16339885-5 2006 We carried out covalent functional modification and site-directed mutagenesis of this controversial ion channel to test the idea that cysteine 24 is a critical redox-sensitive residue located on the extracellular (or luminal) side of membrane CLIC1 subunits, in a cysteine-proline motif close to the putative channel pore. Cysteine 134-142 chloride intracellular channel 1 Homo sapiens 243-248 16507767-1 2006 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulfuration pathway, which uses L-cysteine to produce hydrogen sulfide (H2S). Cysteine 93-103 cystathionine gamma-lyase Homo sapiens 0-25 16507767-1 2006 Cystathionine gamma-lyase (CSE) is a key enzyme in the trans-sulfuration pathway, which uses L-cysteine to produce hydrogen sulfide (H2S). Cysteine 93-103 cystathionine gamma-lyase Homo sapiens 27-30 16530514-3 2006 METHODS: Cysteine protease-deficient amoebae were generated by antisense inhibition of EhCP5, and assayed for proteolytic activity against [(35)S]cysteine-labeled mucin from LS 174T, and HT-29F Cl.16E cells. Cysteine 146-154 cathepsin B Homo sapiens 9-26 16507685-10 2006 Further chemical modification of Cys (carboxymethylation) or positively charged residues (acetylation) of beta-LG totally abolished its immunoreactivity, confirming the conformation-dependent nature of this mAb. Cysteine 33-36 beta-lactoglobulin Bos taurus 106-113 16517958-3 2006 N-acetyl-L-cysteine (NAC) is stable in solution and safe for use in humans; therefore, NAC may be a means of supplying parenteral CYS. Cysteine 130-133 X-linked Kx blood group Homo sapiens 21-24 16517958-3 2006 N-acetyl-L-cysteine (NAC) is stable in solution and safe for use in humans; therefore, NAC may be a means of supplying parenteral CYS. Cysteine 130-133 X-linked Kx blood group Homo sapiens 87-90 16517958-14 2006 CONCLUSIONS: These data demonstrate that NAC is available as a precursor for CYS to support growth and protein (nitrogen) accretion in piglets administered a parenteral solution. Cysteine 77-80 X-linked Kx blood group Homo sapiens 41-44 16317109-9 2006 However, JC638.2alpha protected an introduced cysteine (K356C) in the Kv2.1 outer pore from permanent modification by methanethiosulfonate ethyltrimethylammonium (MTSET). Cysteine 46-54 potassium voltage-gated channel subfamily B member 1 Homo sapiens 70-75 16489470-5 2006 We were able to establish a definitive linkage to the SPG10 locus, and sequencing of the KIF5A gene revealed a heterozygous missense mutation 1,035 A>G in exon 10, resulting in tyrosine-to-cysteine substitution. Cysteine 189-197 kinesin family member 5A Homo sapiens 89-94 16325219-7 2006 The form of MA that coimmunoprecipitated with CD82 was a cysteine-linked homodimer. Cysteine 57-65 CD82 molecule Homo sapiens 46-50 16492780-1 2006 Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Cysteine 54-64 cysteine dioxygenase 1, cytosolic Mus musculus 0-20 16492780-1 2006 Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Cysteine 54-64 cysteine dioxygenase 1, cytosolic Mus musculus 22-25 16290306-5 2006 Since secretion of some glycosyltransferases is controlled by formation of dimeric molecules via disulfide bonds, one of the fucosyltransferase V constructs contained the N-terminal cysteine residue 64 for dimerization, whereas this residue was replaced in the other construct by serine. Cysteine 182-190 fucosyltransferase 5 Homo sapiens 125-145 16437155-6 2006 AtSufE overexpression induces AtSufS and AtNifS1 expression, which in turn leads to elevated cysteine desulfurization activity, chlorosis and retarded development. Cysteine 93-101 nitrogen fixation S (NIFS)-like 1 Arabidopsis thaliana 41-48 16407192-5 2006 In addition, co-transfection of plasmids expressing ISG15, Ube1L, UbcH8, and Herc5 resulted in robust ISG15 conjugation in non-IFN-treated cells, while the active-site cysteine mutant of Herc5 or a mutant lacking the RCC1 repeat region did not support ISG15 conjugation. Cysteine 168-176 ubiquitin conjugating enzyme E2 L6 Homo sapiens 66-71 16424901-3 2006 Modulation of IRP1 abundance by iron did not require assembly of the Fe-S cluster, since a mutant with all cluster-ligating cysteines mutated to serine underwent iron-induced protein degradation. Cysteine 124-133 aconitase 1 Mus musculus 14-18 16445290-3 2006 We analyzed the structural effects of l-arginine (Arg) and tetrahydrobiopterin (H(4)B) binding on several key complexes (ferric, ferrous, ferrous-CO, and ferric-NO) and characterized the bonding properties of the proximal cysteine ligand. Cysteine 222-230 H4 clustered histone 4 Homo sapiens 80-85 16448092-3 2006 The modified cysteine residue of hemoglobin was previously identified as a distorted S-nitrosothiol (RSNO) or an S-hydroxyamino radical (RSN*OH). Cysteine 13-21 CAP-Gly domain containing linker protein 1 Homo sapiens 101-104 16395252-1 2006 The chemokine (CK) receptor 5 (CCR5) is necessary for two adjacent cysteines (CC)-CKs such as Regulated upon Activation Normal T cell Expressed and Secreted, a/o Macrophage Inflammatory Protein 1alpha/beta to mediate their inflammatory properties. Cysteine 67-76 C-C motif chemokine receptor 5 Homo sapiens 4-29 16395252-1 2006 The chemokine (CK) receptor 5 (CCR5) is necessary for two adjacent cysteines (CC)-CKs such as Regulated upon Activation Normal T cell Expressed and Secreted, a/o Macrophage Inflammatory Protein 1alpha/beta to mediate their inflammatory properties. Cysteine 67-76 C-C motif chemokine receptor 5 Homo sapiens 31-35 16432212-2 2006 We report that dynamin, which interacts with NO synthase, is S-nitrosylated at a single cysteine residue (C607) after stimulation of the beta(2) adrenergic receptor. Cysteine 88-96 adrenoceptor beta 2 Homo sapiens 137-164 16272152-11 2006 An hSERT mutant with single cysteine substitutions in TM1 and TM3 resulted in formation of a high affinity cadmium metal coordination site, suggesting proximity of these domains in the tertiary structure of SERT. Cysteine 28-36 tropomyosin 3 Homo sapiens 62-65 16411679-4 2006 The Mo site of sulfite oxidase has two oxygen and three Mo-S ligands (two from cofactor dithiolene plus a cysteine). Cysteine 106-114 sulfite oxidase Homo sapiens 15-30 16343415-0 2006 Expression, purification, and characterization of cysteine-free mouse P-glycoprotein. Cysteine 50-58 phosphoglycolate phosphatase Mus musculus 70-84 16343415-1 2006 Cysteine-free mouse MDR3 P-glycoprotein (Pgp) was constructed by mutagenesis of the nine natural Cys to Ala. Cysteine 0-8 phosphoglycolate phosphatase Mus musculus 25-39 16343415-1 2006 Cysteine-free mouse MDR3 P-glycoprotein (Pgp) was constructed by mutagenesis of the nine natural Cys to Ala. Cysteine 0-8 phosphoglycolate phosphatase Mus musculus 41-44 16343415-1 2006 Cysteine-free mouse MDR3 P-glycoprotein (Pgp) was constructed by mutagenesis of the nine natural Cys to Ala. Cysteine 0-3 phosphoglycolate phosphatase Mus musculus 25-39 16343415-1 2006 Cysteine-free mouse MDR3 P-glycoprotein (Pgp) was constructed by mutagenesis of the nine natural Cys to Ala. Cysteine 0-3 phosphoglycolate phosphatase Mus musculus 41-44 16343415-4 2006 Mouse Cys-free Pgp was superior in yield and stability to Cys-free human MDR1 Pgp. Cysteine 6-9 phosphoglycolate phosphatase Mus musculus 15-18 16343415-4 2006 Mouse Cys-free Pgp was superior in yield and stability to Cys-free human MDR1 Pgp. Cysteine 58-61 phosphoglycolate phosphatase Mus musculus 78-81 16679521-0 2006 The TACE zymogen: re-examining the role of the cysteine switch. Cysteine 47-55 ADAM metallopeptidase domain 17 Homo sapiens 4-8 16679521-4 2006 We have discovered that a conserved "cysteine switch" consensus motif within TACE"s Pro domain is, contrary to expectations, not required for maintenance of the inactive precursor state or for the secretion of this metalloproteinase in its functional form. Cysteine 37-45 ADAM metallopeptidase domain 17 Homo sapiens 77-81 16472173-3 2006 H(2)S is produced endogenously in mammalian tissues from L-cysteine metabolism mainly by 3 enzymes: cystathionine beta-synthetase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptosulfurtransferase (MST). Cysteine 57-67 cystathionine gamma-lyase Homo sapiens 137-162 16472173-3 2006 H(2)S is produced endogenously in mammalian tissues from L-cysteine metabolism mainly by 3 enzymes: cystathionine beta-synthetase (CBS), cystathionine gamma-lyase (CSE) and 3-mercaptosulfurtransferase (MST). Cysteine 57-67 cystathionine gamma-lyase Homo sapiens 164-167 16918475-5 2006 The determination of the X-ray crystal structure of NAT from Salmonella typhimurium led to the identification of the catalytically essential triad of residues: Cys-His-Asp, which is present in all functional NAT enzymes. Cysteine 160-163 bromodomain containing 2 Homo sapiens 52-55 16918475-5 2006 The determination of the X-ray crystal structure of NAT from Salmonella typhimurium led to the identification of the catalytically essential triad of residues: Cys-His-Asp, which is present in all functional NAT enzymes. Cysteine 160-163 bromodomain containing 2 Homo sapiens 208-211 16363808-3 2005 Two cysteine residues (C45 and C49) in the sequence CXXXCP and a histidine (H135) approximately 90 residues toward the C-terminus are conserved in Sco from bacteria, yeast, and humans. Cysteine 4-12 DELYQ11 Homo sapiens 147-150 16375456-3 2005 A specific single-cysteine mutant of GroEL (Cys261), whose cysteine is located inside the central cavity at the apical region of the protein, was covalently labeled with synthetically prepared Nile Red maleimide (NR). Cysteine 18-26 heat shock protein family D (Hsp60) member 1 Homo sapiens 37-42 16375456-3 2005 A specific single-cysteine mutant of GroEL (Cys261), whose cysteine is located inside the central cavity at the apical region of the protein, was covalently labeled with synthetically prepared Nile Red maleimide (NR). Cysteine 59-67 heat shock protein family D (Hsp60) member 1 Homo sapiens 37-42 16251189-9 2005 Alanine scanning of cysteine residues of Gpx2 revealed that an intramolecular disulfide bond was formed between Cys37 and Cys83 in vivo. Cysteine 20-28 glutathione peroxidase GPX2 Saccharomyces cerevisiae S288C 41-45 16341092-5 2005 We show that E6AP builds up a K48-linked chain on its HECT cysteine residue, while KIAA10 builds up K48- and K29-linked chains as free entities. Cysteine 59-67 ubiquitin protein ligase E3A Homo sapiens 13-17 16364538-0 2005 Cysteine 390 mutation of the TSH receptor modulates its ectodomain as an inverse agonist on the serpentine domain with decrease in basal constitutive activity. Cysteine 0-8 thyroid stimulating hormone receptor Homo sapiens 29-41 16364538-1 2005 Mutations of individual cysteine residues at codon 301, 390, 398 and 408 of the thyrotropin receptor (TSHr) to serine resulted in cell surface expression of only C301S and C390S mutants. Cysteine 24-32 thyroid stimulating hormone receptor Homo sapiens 80-100 16364538-1 2005 Mutations of individual cysteine residues at codon 301, 390, 398 and 408 of the thyrotropin receptor (TSHr) to serine resulted in cell surface expression of only C301S and C390S mutants. Cysteine 24-32 thyroid stimulating hormone receptor Homo sapiens 102-106 16204238-8 2005 The mutation of this cysteine residue exerted no effect on trimerization but increased the dissociation rate of AviTag-4-1BBL from 4-1BB. Cysteine 21-29 TNF receptor superfamily member 9 Homo sapiens 119-124 16171463-0 2005 Role of cysteine residues in the function of human UDP glucuronosyltransferase isoform 1A1 (UGT1A1). Cysteine 8-16 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 51-90 16171463-0 2005 Role of cysteine residues in the function of human UDP glucuronosyltransferase isoform 1A1 (UGT1A1). Cysteine 8-16 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 92-98 16171463-4 2005 All 11 cysteine residues of mature human UGT1A1 are highly conserved in other human UGT isoforms and in rat, mouse and Rhesus monkey UGT1A1, suggesting their functional importance. Cysteine 7-15 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 41-47 16171463-5 2005 Expression of mutagenized UGT1A1 plasmids showed that substitution of any of the seven cysteine residues located within the endoplasmic reticulum cisternae (including those mutated in patients A and B) abolished UGT1A1 activity or markedly increased its apparent K(m) for bilirubin. Cysteine 87-95 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 26-32 16171463-5 2005 Expression of mutagenized UGT1A1 plasmids showed that substitution of any of the seven cysteine residues located within the endoplasmic reticulum cisternae (including those mutated in patients A and B) abolished UGT1A1 activity or markedly increased its apparent K(m) for bilirubin. Cysteine 87-95 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 212-218 16171463-6 2005 Substitution of the three cysteine residues within the C-terminal cytosolic tail had minimal effect on basal UGT1A1 activity, but prevented UGT1A1 activation by UDP-GlcNAc. Cysteine 26-34 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 140-146 16171463-9 2005 Together, the results suggested that free thiol groups, but not disulphide bonding, of seven cysteine residues within the intracisternal region of human UGT1A1 are important for its catalytic activity, while cysteine residues in the cytosolic domain may be involved in its physiological activation by UDP-GlcNAc. Cysteine 93-101 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 153-159 16171463-9 2005 Together, the results suggested that free thiol groups, but not disulphide bonding, of seven cysteine residues within the intracisternal region of human UGT1A1 are important for its catalytic activity, while cysteine residues in the cytosolic domain may be involved in its physiological activation by UDP-GlcNAc. Cysteine 208-216 UDP glucuronosyltransferase family 1 member A1 Homo sapiens 153-159 16091733-3 2005 Hypoxia or the counteradhesive matricellular protein SPARC/BM-40 (SPARC: secreted protein acidic rich in cysteine) overexpressed during cancer progression also commutated PAR-1 to cellular invasion through the cGMP/protein kinase G (PKG) cascade, RhoA inactivation, and Rac1-dependent or -independent signaling. Cysteine 105-113 Rac family small GTPase 1 Homo sapiens 270-274 16339532-7 2005 Intracellular l-cysteine levels were reduced with BSO treatment and restored with cotreatment with NAC or l-cysteine. Cysteine 14-24 NLR family, pyrin domain containing 1A Mus musculus 99-102 16319225-3 2005 Here, we show that inhibition of TRAIL-induced apoptosis by TR4 critically depends on its association with TR2 via the NH(2)-terminal preligand assembly domain overlapping the first partial cysteine-rich domain of both receptors. Cysteine 190-198 TNF receptor superfamily member 10d Homo sapiens 60-63 16319225-3 2005 Here, we show that inhibition of TRAIL-induced apoptosis by TR4 critically depends on its association with TR2 via the NH(2)-terminal preligand assembly domain overlapping the first partial cysteine-rich domain of both receptors. Cysteine 190-198 taste 1 receptor member 2 Homo sapiens 107-110 16054744-0 2005 Site-directed mutagenesis and homology modeling indicate an important role of cysteine 439 in the stability of betaine aldehyde dehydrogenase from Pseudomonas aeruginosa. Cysteine 78-86 aldehyde dehydrogenase 7 family member A1 Homo sapiens 111-141 16054744-1 2005 Betaine aldehyde dehydrogenase (BADH) from the human pathogen Pseudomonas aeruginosa is a tetrameric enzyme that contains a catalytic Cys286 and three additional cysteine residues, Cys353, 377, and 439, per subunit. Cysteine 162-170 aldehyde dehydrogenase 7 family member A1 Homo sapiens 0-30 16054744-1 2005 Betaine aldehyde dehydrogenase (BADH) from the human pathogen Pseudomonas aeruginosa is a tetrameric enzyme that contains a catalytic Cys286 and three additional cysteine residues, Cys353, 377, and 439, per subunit. Cysteine 162-170 aldehyde dehydrogenase 7 family member A1 Homo sapiens 32-36 16359171-5 2005 For the first time, the transportation of Hg2+ cation and Hg2+ conjugate of cysteine was observed with the help of a fluorescence microscope. Cysteine 76-84 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 42-45 16359171-5 2005 For the first time, the transportation of Hg2+ cation and Hg2+ conjugate of cysteine was observed with the help of a fluorescence microscope. Cysteine 76-84 polycystin 1, transient receptor potential channel interacting pseudogene 2 Homo sapiens 58-61 16139926-7 2005 Among K-ras mutations, the amino acid glycine was substituted by cystein in 90% and valine in 10%. Cysteine 65-72 KRAS proto-oncogene, GTPase Homo sapiens 6-11 16317828-1 2005 Geranylgeranyltransferase I (GGTase I) catalyzes the post-translational transfer of lyophilic diterpenoid geranylgeranyl to the cysteine residue of proteins terminating with a CaaX motif such as Rho1p and Cdc42p. Cysteine 128-136 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 205-211 16262444-4 2005 Among three mammalian methionine-R-sulfoxide reductases (MsrBs), MsrB1 is a Sec-containing protein, whereas MsrB2 and MsrB3 contain Cys in the active site, making these enzymes an excellent system for addressing the question of why Sec is used in biological systems. Cysteine 132-135 methionine sulfoxide reductase B2 Homo sapiens 108-113 16262444-4 2005 Among three mammalian methionine-R-sulfoxide reductases (MsrBs), MsrB1 is a Sec-containing protein, whereas MsrB2 and MsrB3 contain Cys in the active site, making these enzymes an excellent system for addressing the question of why Sec is used in biological systems. Cysteine 132-135 methionine sulfoxide reductase B3 Homo sapiens 118-123 16262444-5 2005 In this study, we found that residues, which are uniquely conserved in Cys-containing MsrBs and which are critical for enzyme activity in MsrB2 and MsrB3, were not required for MsrB1, but increased the activity of its Cys mutant. Cysteine 71-74 methionine sulfoxide reductase B2 Homo sapiens 138-143 16262444-5 2005 In this study, we found that residues, which are uniquely conserved in Cys-containing MsrBs and which are critical for enzyme activity in MsrB2 and MsrB3, were not required for MsrB1, but increased the activity of its Cys mutant. Cysteine 71-74 methionine sulfoxide reductase B3 Homo sapiens 148-153 16262444-5 2005 In this study, we found that residues, which are uniquely conserved in Cys-containing MsrBs and which are critical for enzyme activity in MsrB2 and MsrB3, were not required for MsrB1, but increased the activity of its Cys mutant. Cysteine 218-221 methionine sulfoxide reductase B2 Homo sapiens 138-143 16262444-5 2005 In this study, we found that residues, which are uniquely conserved in Cys-containing MsrBs and which are critical for enzyme activity in MsrB2 and MsrB3, were not required for MsrB1, but increased the activity of its Cys mutant. Cysteine 218-221 methionine sulfoxide reductase B3 Homo sapiens 148-153 16262444-8 2005 We prepared Sec-containing forms of MsrB2 and MsrB3 and found that they were more than 100-fold more active than the natural Cys forms. Cysteine 125-128 methionine sulfoxide reductase B2 Homo sapiens 36-41 16262444-8 2005 We prepared Sec-containing forms of MsrB2 and MsrB3 and found that they were more than 100-fold more active than the natural Cys forms. Cysteine 125-128 methionine sulfoxide reductase B3 Homo sapiens 46-51 16262444-10 2005 Yet, insertion of the resolving Cys, which was conserved in MsrB1, into the selenoprotein form of MsrB3 restored the thioredoxin-dependent activity of this enzyme. Cysteine 32-35 methionine sulfoxide reductase B3 Homo sapiens 98-103 16172126-0 2005 Cysteine-scanning mutagenesis and substituted cysteine accessibility analysis of transmembrane segment 4 of the Glut1 glucose transporter. Cysteine 0-8 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 112-117 16172126-0 2005 Cysteine-scanning mutagenesis and substituted cysteine accessibility analysis of transmembrane segment 4 of the Glut1 glucose transporter. Cysteine 46-54 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 112-117 16172126-3 2005 A functional, cysteine-less, parental Glut1 molecule was used to produce 21 Glut1 point mutants by individually changing each residue along transmembrane helix 4 to a cysteine. Cysteine 14-22 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 38-43 16172126-3 2005 A functional, cysteine-less, parental Glut1 molecule was used to produce 21 Glut1 point mutants by individually changing each residue along transmembrane helix 4 to a cysteine. Cysteine 14-22 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 76-81 16172126-3 2005 A functional, cysteine-less, parental Glut1 molecule was used to produce 21 Glut1 point mutants by individually changing each residue along transmembrane helix 4 to a cysteine. Cysteine 167-175 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 38-43 16129668-9 2005 Sequence analysis of members of the Sep15 family identified a novel N-terminal cysteine-rich domain in Sep15 that is absent in SelM. Cysteine 79-87 selenoprotein M Homo sapiens 127-131 16129668-12 2005 Conversely, if the cysteine-rich domain of Sep15 is fused to the N-terminus of SelM, the resulting chimera is capable of binding GT. Cysteine 19-27 selenoprotein M Homo sapiens 79-83 16185707-2 2005 Here, we show that the mitochondrial flavin adenine dinucleotide (FAD)-linked sulfhydryl oxidase Erv1 (essential for respiration and vegetative growth 1) plays a central role in the biogenesis of small, cysteine proteins of the IMS that are import substrates for Mia40. Cysteine 203-211 Mia40p Saccharomyces cerevisiae S288C 263-268 15978671-6 2005 RIL-15 is similar to the hIL-15 (hIL-15) in that it contains seven cysteine residues. Cysteine 67-75 interleukin 15 Homo sapiens 25-31 15978671-6 2005 RIL-15 is similar to the hIL-15 (hIL-15) in that it contains seven cysteine residues. Cysteine 67-75 interleukin 15 Homo sapiens 33-39 16097806-0 2005 Cysteine modification by lipid peroxidation products inhibits protein disulfide isomerase. Cysteine 0-8 prolyl 4-hydroxylase subunit beta Rattus norvegicus 62-89 16097806-3 2005 Further mass spectral analysis of PDI isolated from the animals revealed modification of an active site Cys residue thought to be involved in client protein binding. Cysteine 104-107 prolyl 4-hydroxylase subunit beta Rattus norvegicus 34-37 16097806-6 2005 Thiol sensitivity was confirmed through concentration-dependent inhibition of PDI by the Cys modifier N-ethylmaleimide (NEM). Cysteine 89-92 prolyl 4-hydroxylase subunit beta Rattus norvegicus 78-81 16097806-9 2005 However, because an active site Cys was found to be modified by 4-HNE on PDI in vivo, it is possible that the protective effect of GSH on the chaperone decreases under conditions of sustained oxidative stress, such as during chronic alcohol consumption, as GSH is depleted. Cysteine 32-35 prolyl 4-hydroxylase subunit beta Rattus norvegicus 73-76 15944079-8 2005 Proteins encoded by group 1 genes also shared additional sequence motifs and conserved cysteines not found in group 2 proteins. Cysteine 87-96 anon-86Ca Drosophila melanogaster 20-27 16055689-7 2005 AtDHAR1, AtGSTZ1, and to a lesser degree AtNit1 underwent spontaneous thiolation with GSSG-biotin through modification of active-site cysteines. Cysteine 134-143 dehydroascorbate reductase Arabidopsis thaliana 0-7 16029433-5 2005 The analysis identified three novel exon 3 MASP2 variants introducing amino acid substitutions at positions 84 (Arg-->Gln), 103 (Arg-->Cys) and 111 (Pro-->Leu) in the CUB1 domain. Cysteine 141-144 MBL associated serine protease 2 Homo sapiens 43-48 15982668-2 2005 Fluorophore-conjugated, single-cysteine variants of Cro have been used to investigate the equilibria and kinetics of dimer assembly. Cysteine 31-39 cro Escherichia virus Lambda 52-55 15574124-4 2005 RESULTS: We report a direct interaction between the cysteine-rich domain of FLRG and ADAM12 (a disintegrin and metalloprotease 12). Cysteine 52-60 follistatin-like 3 Mus musculus 76-80 15574124-4 2005 RESULTS: We report a direct interaction between the cysteine-rich domain of FLRG and ADAM12 (a disintegrin and metalloprotease 12). Cysteine 52-60 a disintegrin and metallopeptidase domain 12 (meltrin alpha) Mus musculus 85-91 15966899-5 2005 Rbx1 is a highly evolutionarily conserved protein; however, the eighth coordination residue in its RING finger is aspartate (D97) rather than cysteine. Cysteine 142-150 ring-box 1 Homo sapiens 0-4 15978037-0 2005 Redox-regulated affinity of the third PDZ domain in the phosphotyrosine phosphatase PTP-BL for cysteine-containing target peptides. Cysteine 95-103 protein tyrosine phosphatase non-receptor type 13 Homo sapiens 84-90 15956582-6 2005 When the Cys residues were replaced by Ala residues, all single and double mutants still retained the phenotypes of infectivity, Env incorporation, and lipid raft localization of the WT Env. Cysteine 9-12 endogenous retrovirus group K member 20 Homo sapiens 186-189 15956582-9 2005 Moreover, mutations at both Cys residues significantly reduced the level of palmitoylation of the Env. Cysteine 28-31 endogenous retrovirus group K member 20 Homo sapiens 98-101 15956600-3 2005 We found that V proteins with replacement of Cys residues of the Cys cluster were still able to bind STATs but were unable to induce their degradation. Cysteine 45-48 signal transducer and activator of transcription 2 Homo sapiens 101-106 15956600-3 2005 We found that V proteins with replacement of Cys residues of the Cys cluster were still able to bind STATs but were unable to induce their degradation. Cysteine 65-68 signal transducer and activator of transcription 2 Homo sapiens 101-106 15956600-4 2005 The hPIV2 V protein binds STATs via a W-(X)3-W-(X)9-W Trp motif located just upstream of the Cys cluster. Cysteine 93-96 signal transducer and activator of transcription 2 Homo sapiens 26-31 15904891-2 2005 Fifteen cysteine mutants between positions 565 and 664 yielded cotransport currents of similar amplitude than the wild-type SGLT1 (wtSGLT1). Cysteine 8-16 solute carrier family 5 (sodium/glucose cotransporter), member 1, gene 2 L homeolog Xenopus laevis 124-129 15966719-1 2005 Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS), was studied using a fluorescence probe, acrylodan, site-specifically attached at cysteine residue C229, near the active site. Cysteine 169-177 glutaminyl-tRNA synthetase 1 Homo sapiens 52-78 15966719-1 2005 Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS), was studied using a fluorescence probe, acrylodan, site-specifically attached at cysteine residue C229, near the active site. Cysteine 169-177 glutaminyl-tRNA synthetase 1 Homo sapiens 80-85 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. Cysteine 62-65 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. Cysteine 132-135 transthyretin Mus musculus 53-56 15840587-4 2005 Biochemical analysis showed that bacterial His-tagged p12 could be converted into a dimeric p25 in a reducing agent-dependent manner, and mutating the only cysteine residue of p12 (Cys(105) --> Ala(105)) abolished the dimerization. Cysteine 181-184 tubulin polymerization promoting protein Homo sapiens 92-95 15840587-7 2005 These data supports the possibility that p25 is a homodimeric form of p12 through the cysteine residue. Cysteine 86-94 tubulin polymerization promoting protein Homo sapiens 41-44 15894113-1 2005 Leukotactin-1 (Lkn-1), a human CC chemokine that binds to both CC chemokine receptor (CCR)1 and CCR3, is distinct from other human CC chemokines in that it has long amino acid residues preceding the first cysteine at the NH(2)-terminus. Cysteine 205-213 C-C motif chemokine ligand 15 Homo sapiens 0-13 15894113-1 2005 Leukotactin-1 (Lkn-1), a human CC chemokine that binds to both CC chemokine receptor (CCR)1 and CCR3, is distinct from other human CC chemokines in that it has long amino acid residues preceding the first cysteine at the NH(2)-terminus. Cysteine 205-213 C-C motif chemokine ligand 15 Homo sapiens 15-20 15894113-2 2005 Serial deletion studies showed that at least three amino acid residues, alanine-alanine-aspartic acid (A-A-D), preceding the first cysteine at the NH(2)-terminus are essential for the biological activity of Lkn-1. Cysteine 131-139 C-C motif chemokine ligand 15 Homo sapiens 207-212 15894113-8 2005 These results identify that alanine-aspartic acid residues preceding the first cysteine at the NH(2)-terminus are essential for the binding and biological activity of Lkn-1. Cysteine 79-87 C-C motif chemokine ligand 15 Homo sapiens 167-172 15927968-8 2005 Compared with more reduced E(h), oxidized E(h) of Cys/CySS stimulated H2O2 but not nitric oxide production, activated nuclear factor-kappaB, increased expression of adhesion molecules (intercellular adhesion molecule-1, platelet endothelial cell adhesion molecule-1, P-selectin), and stimulated monocytes binding to endothelial cells. Cysteine 50-53 intercellular adhesion molecule 1 Homo sapiens 185-218 15749738-5 2005 Here, we hypothesized that the amino terminus of the TACE prodomain might contribute to the ability of the prodomain to maintain TACE in an inactive state independently of a cysteine-switch mechanism. Cysteine 174-182 ADAM metallopeptidase domain 17 Homo sapiens 53-57 15749738-10 2005 In summary, we have identified a subdomain within the amino terminus of the TACE prodomain that attenuates TACE catalytic activity independently of a cysteine-switch mechanism, which provides new insight into the regulation of TACE enzymatic activity. Cysteine 150-158 ADAM metallopeptidase domain 17 Homo sapiens 76-80 15749738-10 2005 In summary, we have identified a subdomain within the amino terminus of the TACE prodomain that attenuates TACE catalytic activity independently of a cysteine-switch mechanism, which provides new insight into the regulation of TACE enzymatic activity. Cysteine 150-158 ADAM metallopeptidase domain 17 Homo sapiens 107-111 15749738-10 2005 In summary, we have identified a subdomain within the amino terminus of the TACE prodomain that attenuates TACE catalytic activity independently of a cysteine-switch mechanism, which provides new insight into the regulation of TACE enzymatic activity. Cysteine 150-158 ADAM metallopeptidase domain 17 Homo sapiens 107-111 15897295-0 2005 Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule. Cysteine 0-8 Charcot-Leyden crystal galectin Homo sapiens 26-29 15897295-0 2005 Cysteine accessibility in ClC-0 supports conservation of the ClC intracellular vestibule. Cysteine 0-8 Charcot-Leyden crystal galectin Homo sapiens 61-64 15897295-4 2005 In this study we used cysteine-scanning mutagenesis and modification (SCAM) to screen >50 residues in the intracellular vestibule of ClC-0. Cysteine 22-30 Charcot-Leyden crystal galectin Homo sapiens 136-139 15905556-6 2005 In this study we show by genetic linkage analysis of (NOD x NOR) x NOD backcross mice that progression to severe islet inflammation after CY treatment was controlled by the Idd4 and Idd9 loci. Cysteine 138-140 insulin dependent diabetes susceptibility 9 Mus musculus 182-186 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. Cysteine 68-76 methionine sulfoxide reductase B 1 Arabidopsis thaliana 16-21 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. Cysteine 78-81 methionine sulfoxide reductase B 1 Arabidopsis thaliana 16-21 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. Cysteine 100-103 methionine sulfoxide reductase B 1 Arabidopsis thaliana 16-21 15581423-0 2005 Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch. Cysteine 111-119 ADAM metallopeptidase domain 17 Homo sapiens 46-72 15581423-0 2005 Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch. Cysteine 111-119 ADAM metallopeptidase domain 17 Homo sapiens 74-78 15581423-5 2005 We addressed the question whether a cysteine switch consensus motif is needed for the secretion of active TACE. Cysteine 36-44 ADAM metallopeptidase domain 17 Homo sapiens 106-110 15581423-6 2005 The cysteine switch mutants [C184A (Cys184-->Ala)] of TACE resembled the wild-type functionally and in their sensitivity to inhibitors. Cysteine 4-12 ADAM metallopeptidase domain 17 Homo sapiens 57-61 15581423-10 2005 The cysteine switch of TACE is not essential for the secretion of the functional enzyme, but may prevent intracellular degradation of the TACE zymogen. Cysteine 4-12 ADAM metallopeptidase domain 17 Homo sapiens 23-27 15581423-10 2005 The cysteine switch of TACE is not essential for the secretion of the functional enzyme, but may prevent intracellular degradation of the TACE zymogen. Cysteine 4-12 ADAM metallopeptidase domain 17 Homo sapiens 138-142 15584898-3 2005 In the present study, we show that Spry4 inhibits the kinase activity of TESK1 by binding to it through the C-terminal cysteine-rich region. Cysteine 119-127 sprouty RTK signaling antagonist 4 Homo sapiens 35-40 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. Cysteine 67-70 growth hormone receptor Homo sapiens 128-131 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. Cysteine 77-80 growth hormone receptor Homo sapiens 128-131 15893662-0 2005 Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. Cysteine 58-66 cytochrome c oxidase copper chaperone COX17 Homo sapiens 19-24 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. Cysteine 44-47 cytochrome c oxidase copper chaperone COX17 Homo sapiens 131-136 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. Cysteine 52-55 cytochrome c oxidase copper chaperone COX17 Homo sapiens 131-136 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. Cysteine 52-55 cytochrome c oxidase copper chaperone COX17 Homo sapiens 131-136 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. Cysteine 52-55 cytochrome c oxidase copper chaperone COX17 Homo sapiens 131-136 15713667-8 2005 On the other hand, the results from the proteoliposome fusion assay, employing cysteine- and nitroxide-scanning mutants of Sso1p, suggested that the formation of the complete core is required for membrane fusion. Cysteine 79-87 syntaxin Saccharomyces cerevisiae S288C 123-128 15684422-9 2005 Radiation, H(2)O(2), and the Ca(2+) ionophore, ionomycin, also stimulated NOS activity, and this was associated with an enhanced S-nitrosylation of the active site Cys(453) determined by isolation of S-nitrosylated wild type but not active site Cys(453) --> Ser SHP-1 mutant by the "biotin-switch" method. Cysteine 164-167 protein tyrosine phosphatase non-receptor type 6 Homo sapiens 265-270 15708846-3 2005 RLF derivatives with six residues deleted from the N terminus of the A chain are active, whereas further truncation, up to the first A chain cysteine (A-10), yields tightly binding ligands devoid of signaling activity. Cysteine 141-149 RLF zinc finger Homo sapiens 0-3 15632113-5 2005 dMT has three Cys-X-Cys motifs in each of the N- and C-terminal domains and a 42-residue-long hinge region devoid of cysteines. Cysteine 117-126 dalmatian Drosophila melanogaster 0-3 15611132-4 2005 Charge-removing replacement of Asp(575) by either asparagine or cysteine rendered the mutant NCKX2 proteins independent of K(+), whereas the charge-conservative substitution of Asp(575) to glutamate resulted in a nonfunctional mutant NCKX2 protein, accentuating the critical nature of this residue. Cysteine 64-72 solute carrier family 24 member 2 Homo sapiens 93-98 15576449-3 2005 To investigate the molecular origin of the remaining slow component of charge immobilization we studied the human cardiac Na+ channel (hH1a) in which the outermost arginine in the S4-DIV, which contributes approximately 20% to total gating charge (Qmax), was mutated to a cysteine (R1C-DIV). Cysteine 272-280 H1.1 linker histone, cluster member Homo sapiens 135-139 15660128-3 2005 Despite the presence of Mg.ATP, the Sae1/Sae2-SUMO-1-Mg.ATP structure reveals a substrate complex insomuch as the SUMO C-terminus remains unmodified within the adenylation site and 35 A from the catalytic cysteine, suggesting that additional changes within the adenylation site may be required to facilitate chemistry prior to adenylation and thioester transfer. Cysteine 205-213 SUMO1 activating enzyme subunit 1 Homo sapiens 36-40 15660134-4 2005 Mutations in critical cysteine residues of Rli1p abolish association with Fe/S clusters and lead to loss of cell viability. Cysteine 22-30 ATP binding cassette subfamily E member 1 Homo sapiens 43-48 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. Cysteine 34-42 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. Cysteine 73-82 corticotropin releasing hormone receptor 1 Rattus norvegicus 49-53 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. Cysteine 2-10 glutathione S-transferase omega 1 Homo sapiens 88-92 16399403-3 2005 As the only enzyme of the cycle located on the outer surface of plasma membrane, gamma-glutamyl transpeptidase (GGT) plays key roles in GSH homeostasis by breaking down extracellular GSH and providing cysteine, the rate-limiting substrate, for intracellular de novo synthesis of GSH. Cysteine 201-209 inactive glutathione hydrolase 2 Homo sapiens 81-110 16399403-3 2005 As the only enzyme of the cycle located on the outer surface of plasma membrane, gamma-glutamyl transpeptidase (GGT) plays key roles in GSH homeostasis by breaking down extracellular GSH and providing cysteine, the rate-limiting substrate, for intracellular de novo synthesis of GSH. Cysteine 201-209 inactive glutathione hydrolase 2 Homo sapiens 112-115 15756939-3 2005 Here, we quantitatively measured changes in mitochondrial proteins of primary rat cortical neuron cultures exposed to 25 microM Abeta(25-35) for 16 h using isotope coded affinity tag (ICAT) labeling and 2-dimensional liquid chromatography/tandem mass spectrometry (2D-LC/MS/MS) which allows simultaneous identification and quantification of cysteine-containing proteins. Cysteine 341-349 amyloid beta precursor protein Rattus norvegicus 128-133 16127296-2 2005 The antioxidant N-acetyl L-cysteine (NAC), a membrane-permeable aminothiol, is a sulfhydryl reductant reducing oxidised glutathione, as well as being a precursor of intracellular cysteine and glutathione. Cysteine 27-35 X-linked Kx blood group Homo sapiens 37-40 15579666-4 2005 Two isoforms, Serat3;1 and Serat3;2, were characterized with respect to their enzymatic properties, feedback inhibition by L-Cys, and subcellular localization. Cysteine 123-128 serine acetyltransferase 3;2 Arabidopsis thaliana 27-35 15615519-6 2004 The Asp-Pro-Ala-Ala-Thr-Ala-Tyr-cyclo[Cys-Arg-DPhe-DPhe-Asn-Ala-Phe-Cys]-Tyr-Ala-Arg-Lys-Leu peptide resulted in a 60 nM melanocortin-1 receptor agonist that is 100-fold selective versus the mMC4R, 1000-fold selective versus the mMC3R, and ca. Cysteine 38-41 melanocortin 3 receptor Mus musculus 229-234 15596720-6 2004 As judged from the quaternary structure of bovine COX, the most profound adaptive substitutions are two contiguous cysteines absent in approximately 99.9% of databased COX I sequences from Eukaryota, Archaea, and Bacteria. Cysteine 115-124 cytochrome c oxidase subunit 7A1 Bos taurus 50-53 15596720-6 2004 As judged from the quaternary structure of bovine COX, the most profound adaptive substitutions are two contiguous cysteines absent in approximately 99.9% of databased COX I sequences from Eukaryota, Archaea, and Bacteria. Cysteine 115-124 cytochrome c oxidase subunit 7A1 Bos taurus 168-171 15465825-1 2004 Cox17 is a 69-residue cysteine-rich, copper-binding protein that has been implicated in the delivery of copper to the Cu(A) and Cu(B) centers of cytochrome c oxidase via the copper-binding proteins Sco1 and Cox11, respectively. Cysteine 22-30 Cox11p Saccharomyces cerevisiae S288C 207-212 15589826-1 2004 Present work reported a novel domain--D8C (domain with conserved eight cysteines in liver-specific ZP domain-containing protein, glycoprotein 2 (GP-2) and uromodulin (UMOD)), present in liver-specific LZP, UMOD, GP-2 and some uncharacterized proteins, most of which are membrane proteins, extracellular proteins or nuclear membrane proteins. Cysteine 71-80 uromodulin Homo sapiens 155-165 15589826-1 2004 Present work reported a novel domain--D8C (domain with conserved eight cysteines in liver-specific ZP domain-containing protein, glycoprotein 2 (GP-2) and uromodulin (UMOD)), present in liver-specific LZP, UMOD, GP-2 and some uncharacterized proteins, most of which are membrane proteins, extracellular proteins or nuclear membrane proteins. Cysteine 71-80 uromodulin Homo sapiens 167-171 15589826-1 2004 Present work reported a novel domain--D8C (domain with conserved eight cysteines in liver-specific ZP domain-containing protein, glycoprotein 2 (GP-2) and uromodulin (UMOD)), present in liver-specific LZP, UMOD, GP-2 and some uncharacterized proteins, most of which are membrane proteins, extracellular proteins or nuclear membrane proteins. Cysteine 71-80 uromodulin Homo sapiens 206-210 15604241-0 2004 Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts. Cysteine 0-8 S-adenosylmethionine decarboxylase 1 Mus musculus 69-101 15604241-9 2004 The results suggest that cysteine cathepsins are the main proteases contributing to the high invasiveness of the AdoMetDC-transformed cells and that the invasion potential is largely independent of activation of the MMPs. Cysteine 25-33 S-adenosylmethionine decarboxylase 1 Mus musculus 113-121 15675819-4 2004 The particular disulfide bonds that are important in the aggregates are uncertain, although Cys(121) of beta-lactoglobulin (beta-LG) has been implicated. Cysteine 92-95 beta-lactoglobulin Bos taurus 104-122 15675819-4 2004 The particular disulfide bonds that are important in the aggregates are uncertain, although Cys(121) of beta-lactoglobulin (beta-LG) has been implicated. Cysteine 92-95 beta-lactoglobulin Bos taurus 124-131 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). Cysteine 95-98 beta-lactoglobulin Bos taurus 134-141 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. Cysteine 61-69 carbonic anhydrase 2 Homo sapiens 110-116 15590070-3 2004 The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. Cysteine 61-69 carbonic anhydrase 2 Homo sapiens 134-140 15558519-4 2004 Most are missense mutations causing a cysteine change in uromodulin sequence. Cysteine 38-46 uromodulin Homo sapiens 57-67 15539949-3 2004 We have recently demonstrated that the depletion of Hsp70 in cancer cells results in a cysteine cathepsin-dependent death, which is preceded by lysosomal destabilization and release of lysosomal constituents to the cytosol. Cysteine 87-95 heat shock protein family A (Hsp70) member 4 Homo sapiens 52-57 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. Cysteine 75-83 5'-nucleotidase, cytosolic II Homo sapiens 58-63 15642325-11 2004 We have shown that oxidative stress of H2O2 could increase the flux of this transsulfuration pathway by committing more homocysteine to cysteine and glutathione production as H2O2 (0.1 mM) inhibited the remethylation enzyme of methionine synthase while concurrently activating the CBS enzyme. Cysteine 124-132 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 227-246 15564460-7 2004 The normal cellular function of the Tva receptor is unknown; however, the extracellular domain contains a 40-amino-acid, cysteine-rich region that is homologous to the ligand binding region of the low-density lipoprotein receptor (LDLR) proteins. Cysteine 121-129 low density lipoprotein receptor Gallus gallus 197-229 15575003-7 2004 RESULTS: The mutation p.C347G (c.1039T > G) results in a conserved cysteine to glycine amino acid substitution in the uromodulin zona pellucida (ZP) domain. Cysteine 70-78 uromodulin Homo sapiens 121-131 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. Cysteine 179-188 lactate/malate dehydrogenase family protein Arabidopsis thaliana 124-132 15554709-6 2004 These studies suggested a mechanism in which TBNS acts a pY mimetic and binds to the PTP active site to form an initial noncovalent E.I complex, followed by nucleophilic attack on the TBNS nitro group by Cys-215 of PTP1B to form a reversible, covalent adduct as the tighter E.I* complex. Cysteine 204-207 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 215-220 15515067-1 2004 Alpha-amino aldehyde 4, which is readily derived from L-cysteine through cyclization and elaboration of the carboxy group, was subjected to the Strecker reaction, which, via sodium bisulfite adduct 16, afforded alpha-amino nitrile 5 with high diastereoselectivity (syn/anti=11:1) and in high yield. Cysteine 54-64 synemin Homo sapiens 265-268 15545318-4 2004 We now show that the import mechanism for UbcM2 and two other human class III E2s (UbcH6 and UBE2E2) uniquely requires the covalent attachment of Ub to the active site cysteine of these enzymes. Cysteine 168-176 ubiquitin conjugating enzyme E2 E2 Homo sapiens 93-99 15347670-2 2004 CSE uses L-cysteine as a substrate to produce hydrogen sulfide (H2S). Cysteine 9-19 cystathionine gamma-lyase Homo sapiens 0-3 15535964-1 2004 The recombinant human serum albumin (rHSA) dimer, which was cross-linked by a thiol group of Cys-34 with 1,6-bis(maleimido)hexane, has been physicochemically characterized. Cysteine 93-96 albumin Rattus norvegicus 22-35 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). Cysteine 210-218 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). Cysteine 210-218 cysteine-rich protein 1 (intestinal) Mus musculus 160-164 15535978-4 2004 A homology search of databases revealed that the deduced amino acid sequence of CRP1 displays significant similarity to those of granulin/epithelins, a family of growth-modulating factors; all cysteine residues in CRP1 are located at the same positions as those conserved characteristically in other known granulin/epithelins. Cysteine 193-201 cysteine-rich protein 1 (intestinal) Mus musculus 80-84 15535978-4 2004 A homology search of databases revealed that the deduced amino acid sequence of CRP1 displays significant similarity to those of granulin/epithelins, a family of growth-modulating factors; all cysteine residues in CRP1 are located at the same positions as those conserved characteristically in other known granulin/epithelins. Cysteine 193-201 cysteine-rich protein 1 (intestinal) Mus musculus 214-218 15355985-0 2004 Bacteria binding by DMBT1/SAG/gp-340 is confined to the VEVLXXXXW motif in its scavenger receptor cysteine-rich domains. Cysteine 98-106 deleted in malignant brain tumors 1 Homo sapiens 20-25 15355985-0 2004 Bacteria binding by DMBT1/SAG/gp-340 is confined to the VEVLXXXXW motif in its scavenger receptor cysteine-rich domains. Cysteine 98-106 deleted in malignant brain tumors 1 Homo sapiens 30-36 15364952-3 2004 Tim40 is essential for yeast cell growth, and its function in vivo requires six conserved Cys residues but not anchoring of the protein to the inner membrane by its N-terminal hydrophobic segment. Cysteine 90-93 Mia40p Saccharomyces cerevisiae S288C 0-5 15518578-1 2004 The cDNA sequence encoding rabbit, mouse, and rat extracellular superoxide dismutase (EC-SOD) predicts that the protein contains five cysteine residues. Cysteine 134-142 superoxide dismutase 3 Rattus norvegicus 50-84 15518578-1 2004 The cDNA sequence encoding rabbit, mouse, and rat extracellular superoxide dismutase (EC-SOD) predicts that the protein contains five cysteine residues. Cysteine 134-142 superoxide dismutase 3 Rattus norvegicus 86-92 15308632-3 2004 Twenty-one Glut1 mutants were created from a fully functional, cysteine-less, parental Glut1 molecule by successively changing each residue along transmembrane helix 3 to a cysteine. Cysteine 63-71 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 11-16 15308632-3 2004 Twenty-one Glut1 mutants were created from a fully functional, cysteine-less, parental Glut1 molecule by successively changing each residue along transmembrane helix 3 to a cysteine. Cysteine 173-181 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 11-16 15367662-7 2004 In particular, the conserved cysteines were crucial: mutation of either cysteine abolishted the ability of claudin-5 to increase transepithelial resistance, and mutation of Cys(64) strikingly increased the paracellular flux of monosaccharides. Cysteine 29-38 claudin 5 (transmembrane protein deleted in velocardiofacial syndrome) Canis lupus familiaris 107-116 15367662-7 2004 In particular, the conserved cysteines were crucial: mutation of either cysteine abolishted the ability of claudin-5 to increase transepithelial resistance, and mutation of Cys(64) strikingly increased the paracellular flux of monosaccharides. Cysteine 29-37 claudin 5 (transmembrane protein deleted in velocardiofacial syndrome) Canis lupus familiaris 107-116 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 --> Ser mutation or by disulfide reduction and carboxamidomethylation. Cysteine 163-166 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. Cysteine 124-132 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. Cysteine 124-132 deleted in malignant brain tumors 1 Homo sapiens 96-102 15292166-6 2004 Non-sulfated [35S]Met/Cys-labeled Muclin showed decreased binding in the overlay assay. Cysteine 22-25 deleted in malignant brain tumors 1 Homo sapiens 34-40 15556283-0 2004 Affinity labeling of a catalytic site, cysteine(247), in rat mercaptopyruvate sulfurtransferase by chloropyruvate as an analog of a substrate. Cysteine 39-47 mercaptopyruvate sulfurtransferase Rattus norvegicus 61-95 15231707-7 2004 Critical TSHR residues that determine hormone specificity have been identified in the leucine-rich repeats, and others within the cysteine-rich C-flanking region that determines hormonal activation as well as receptor silencing. Cysteine 130-138 thyroid stimulating hormone receptor Homo sapiens 9-13 15355318-2 2004 In this report we have demonstrated that rat cultured astrocytes express the enzymes (5"-lipoxygenase and LTC(4) synthase) required for cys-LT production, and release cys-LTs in resting condition and, to a greater extent, in response to calcium ionophore A23187, 1 h combined oxygen-glucose deprivation or 2-methyl-thioATP, a selective P2Y(1)/ATP receptor agonist. Cysteine 136-139 leukotriene C4 synthase Rattus norvegicus 106-121 15497768-2 2004 Recent studies demonstrate a role of the transsulfuration enzymes, cystathionine gamma-lyase and cystathionine beta-synthase, in catalyzing the desulfhydration of cysteine in brain and smooth muscle. Cysteine 163-171 cystathionine gamma-lyase Homo sapiens 67-92 15322283-3 2004 In this report we describe the cloning, expression in Escherichia coli, isolation and membrane-targeting modification of the four short consensus repeat domains of soluble human DAF with an additional C-terminal cysteine residue to permit site-specific modification. Cysteine 212-220 CD55 molecule (Cromer blood group) Homo sapiens 178-181 15341735-3 2004 The two proteins bind to a region of CYLD that contains a Cys-box motif and the third cytoskeleton-associated protein-glycine conserved (CAP-Gly) domain. Cysteine 58-61 CYLD lysine 63 deubiquitinase Homo sapiens 37-41 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. Cysteine 186-195 vitronectin Homo sapiens 39-52 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. Cysteine 186-195 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. Cysteine 186-195 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). Cysteine 262-265 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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). Cysteine 269-272 vitronectin Homo sapiens 224-227 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. Cysteine 108-111 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. Cysteine 108-111 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. Cysteine 117-120 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. Cysteine 117-120 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. Cysteine 117-120 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. Cysteine 117-120 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. Cysteine 117-120 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. Cysteine 117-120 vitronectin Homo sapiens 66-77 15184375-3 2004 Tau and microtubule-associated protein-2 cysteine oxidation and reduction were quantitated by monitoring the incorporation of 5-iodoacetamidofluorescein, a thiol-specific labeling reagent. Cysteine 41-49 microtubule associated protein 2 Homo sapiens 8-40 15136577-0 2004 Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum. Cysteine 14-22 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 39-48 15203191-10 2004 Reduced glutathione and L-cysteine also blocked Smad2 and TIMP-3 induction by TGF-beta1, whereas a nonthiol, N-acetylalanine, did not. Cysteine 24-34 TIMP metallopeptidase inhibitor 3 Homo sapiens 58-64 15034755-0 2004 Inhibition of gamma-glutamyl transpeptidase activity decreases intracellular cysteine levels in cervical carcinoma. Cysteine 77-85 inactive glutathione hydrolase 2 Homo sapiens 14-43 15034755-1 2004 PURPOSE: To determine whether gamma-glutamyl transpeptidase (gamma-GT) is involved in the maintenance of elevated cysteine levels in cervical carcinoma. Cysteine 114-122 inactive glutathione hydrolase 2 Homo sapiens 30-59 15034755-1 2004 PURPOSE: To determine whether gamma-glutamyl transpeptidase (gamma-GT) is involved in the maintenance of elevated cysteine levels in cervical carcinoma. Cysteine 114-122 inactive glutathione hydrolase 2 Homo sapiens 61-69 15034755-3 2004 The highest and lowest gamma-GT-expressing cell lines were used in in vivo experiments to determine the effect of gamma-GT inhibition on cysteine levels. Cysteine 137-145 inactive glutathione hydrolase 2 Homo sapiens 114-122 15034755-5 2004 Cysteine depletion was evident in Me180 cells which had the greatest levels of gamma-GT activity, and had a more pronounced cysteine decrease in medium with glutathione and cysteine concentrations simulating the in vivo situation. Cysteine 0-8 inactive glutathione hydrolase 2 Homo sapiens 79-87 15034755-9 2004 CONCLUSIONS: In tumours and cell lines with elevated levels of gamma-GT activity, inhibition of this enzyme led to decreases of cysteine levels. Cysteine 128-136 inactive glutathione hydrolase 2 Homo sapiens 63-71 15253869-4 2004 In other primates as well as other mammals, apoA-II, lacking a cysteine residue, is monomeric. Cysteine 63-71 apolipoprotein A2 Equus caballus 44-51 15253869-6 2004 In this report, we extend these observations by reporting on the first complete sequence for a horse apolipoprotein and by demonstrating that horse apoA-II also contains a cysteine residue at position 6. Cysteine 172-180 apolipoprotein A2 Equus caballus 148-155 15201068-7 2004 The snake FSHR is a G protein-coupled receptor with 673 amino acids, and the aminoterminal domain with 346 amino acids consists of a nine leucine-rich repeat-containing subdomain (LRR) flanked by two cysteine-rich subdomains. Cysteine 200-208 follicle stimulating hormone receptor Homo sapiens 10-14 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. Cysteine 23-31 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. Cysteine 23-31 colicin E9 Escherichia coli 90-95 15047165-5 2004 Here we have generated a highly stable hIL-18 with replacement of cysteine by serine based on the tertiary structure and the binding mechanism, retaining the biological activity. Cysteine 66-74 interleukin 18 Homo sapiens 39-45 15071191-2 2004 c) has been made by engineering cysteines into CCP and cyt. Cysteine 32-41 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 47-50 14754885-5 2004 The transfer of one copper from Atox1 to N-WNDP results in selective protection of the metal-coordinating cysteines in MBS2 against labeling with a cysteine-directed probe. Cysteine 106-115 antioxidant 1 copper chaperone Homo sapiens 32-37 14754885-5 2004 The transfer of one copper from Atox1 to N-WNDP results in selective protection of the metal-coordinating cysteines in MBS2 against labeling with a cysteine-directed probe. Cysteine 106-114 antioxidant 1 copper chaperone Homo sapiens 32-37 15063314-0 2004 Modification of cysteine residue in transthyretin and a synthetic peptide: analyses by electrospray ionization mass spectrometry. Cysteine 16-24 transthyretin Homo sapiens 36-49 15063314-4 2004 In the present paper, we show the molecular masses of various TTR derivatives including these two, and the modification process was studied using a synthetic peptide with the same sequence as cysteine containing part of TTR, i.e., SKCPLMVK. Cysteine 192-200 transthyretin Homo sapiens 220-223 14718370-0 2004 C-Mannosylation of MUC5AC and MUC5B Cys subdomains. Cysteine 36-39 LOW QUALITY PROTEIN: mucin-5B Cricetulus griseus 30-35 14718370-10 2004 Considered together, these studies suggest that the Cys subdomains of MUC5AC and MUC5B are C-mannosylated in their respective WXXW motifs. Cysteine 52-55 LOW QUALITY PROTEIN: mucin-5B Cricetulus griseus 81-86 15070946-7 2004 This difference localizes antibody binding to a cysteine-rich region at the TSHR N terminus. Cysteine 48-56 thyroid stimulating hormone receptor Homo sapiens 76-80 15145449-0 2004 3alpha/beta,20beta-hydroxysteroid dehydrogenase (porcine testicular carbonyl reductase) also has a cysteine residue that is involved in binding of cofactor NADPH. Cysteine 99-107 dehydrogenase/reductase 9 Homo sapiens 0-47 15145449-2 2004 The three-dimensional structure of porcine 3alpha/beta,20beta-hydroxysteroid dehydrogenase, also known as porcine testicular carbonyl reductase, demonstrates the proximity of the Cys 226 side chain to the bound NADP. Cysteine 179-182 dehydrogenase/reductase 9 Homo sapiens 43-90 15646069-6 2004 Since the first cysteine loop of human CCR5 is identical in sequence to its mouse homologue, mice were immunized according to an intra-peritoneal procedure with CCR5 peptide loop, #90-103. Cysteine 16-24 C-C motif chemokine receptor 5 Homo sapiens 39-43 15139528-5 2004 The L-form, D-form, retro-inverted D-form, and selective Cys-to-Ala site-directed mutants of peptides P8 and P25 were also shown to retain binding to Caco-2 cell membranes when immobilized on the surface of a model particulate. Cysteine 57-60 tubulin polymerization promoting protein Homo sapiens 109-112 15050027-1 2004 Genes in the Leukocyte Antigen 6 (Ly-6) superfamily encode glycosyl-phosphatidylinositol (GPI) anchored glycoproteins (gp) with conserved domains of 70 to 100 amino acids and 8 to 10 cysteine residues. Cysteine 183-191 lymphocyte antigen 6 complex Mus musculus 34-38 14724195-3 2004 A slow gating process closes both protopores simultaneously, has a high Q(10), is facilitated by extracellular Zn(2+) and Cd(2+) and is abolished or markedly reduced by mutation of a cysteine conserved in ClC-0, -1 and -2. Cysteine 183-191 chloride voltage-gated channel 1 Homo sapiens 205-221 14676187-4 2004 Here we engineered a Cys-less version of connexin 43 (Cx43) and assessed its function using a Xenopus oocyte expression system. Cysteine 21-24 gap junction protein alpha 1 S homeolog Xenopus laevis 54-58 14676187-6 2004 The carboxyfluorescein permeability of Cys-less hemichannels was increased by protein kinase C inhibition, like the wild-type Cx43 hemichannels. Cysteine 39-42 gap junction protein alpha 1 S homeolog Xenopus laevis 126-130 14676187-8 2004 We conclude that Cysless Cx43 forms regulated functional hemichannels, and therefore Cys-less Cx43 is a useful tool for future structural studies. Cysteine 17-20 gap junction protein alpha 1 S homeolog Xenopus laevis 25-29 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. Cysteine 207-215 cofilin Saccharomyces cerevisiae S288C 0-7 14989655-7 2004 Interestingly, the highly covalent Mo-S(180) pi bonding interaction observed in these complexes is analogous to the well-known Cu-S(Cys) pi bond in type 1 blue copper proteins, which display electronic absorption and resonance Raman spectra that are remarkably similar to these monooxomolybdenum thiolate complexes. Cysteine 132-135 MOS proto-oncogene, serine/threonine kinase Homo sapiens 35-39 14672929-12 2004 The simulation offers insight into why Sdh4p Cys-78 may be serving as the second axial ligand for the heme instead of a histidine residue. Cysteine 45-48 succinate dehydrogenase membrane anchor subunit SDH4 Saccharomyces cerevisiae S288C 39-44 14871470-2 2004 Among them, transmembrane Trx-related protein (TMX) was recently identified as a novel protein possessing an atypical active site sequence, Cys-Pro-Ala-Cys. Cysteine 140-143 thioredoxin related transmembrane protein 1 Homo sapiens 12-45 14871470-2 2004 Among them, transmembrane Trx-related protein (TMX) was recently identified as a novel protein possessing an atypical active site sequence, Cys-Pro-Ala-Cys. Cysteine 140-143 thioredoxin related transmembrane protein 1 Homo sapiens 47-50 14993790-4 2004 We hypothesized that RS-7897-derived OTCA was converted into L-Cys by 5-OPase and supplied sulfhydryl groups in vascular smooth muscle cells, the targets of the nitrate. Cysteine 61-66 5-oxoprolinase, ATP-hydrolysing Bos taurus 70-77 14993790-7 2004 The catalytic activity of bovine 5-OPase to convert OTCA to L-Cys was confirmed, as was the case for the rat enzyme. Cysteine 60-65 5-oxoprolinase, ATP-hydrolysing Bos taurus 33-40 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. Cysteine 130-139 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. Cysteine 130-139 ATP binding cassette subfamily C member 4 Homo sapiens 33-38 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). Cysteine 122-131 protein tyrosine phosphatase non-receptor type 22 Homo sapiens 28-31 14764894-0 2004 Protection against electrophile and oxidant stress by induction of the phase 2 response: fate of cysteines of the Keap1 sensor modified by inducers. Cysteine 97-106 kelch-like ECH-associated protein 1 Mus musculus 114-119 14764894-3 2004 Under basal conditions, Nrf2 resides mainly in the cytoplasm bound to its cysteine-rich, Kelch domain-containing partner Keap1, which is itself anchored to the actin cytoskeleton and represses Nrf2 activity. Cysteine 74-82 kelch-like ECH-associated protein 1 Mus musculus 121-126 14764894-4 2004 Inducers disrupt the Keap1-Nrf2 complex by modifying two (C273 and C288) of the 25 cysteine residues of Keap1. Cysteine 83-91 kelch-like ECH-associated protein 1 Mus musculus 21-26 14764894-4 2004 Inducers disrupt the Keap1-Nrf2 complex by modifying two (C273 and C288) of the 25 cysteine residues of Keap1. Cysteine 83-91 kelch-like ECH-associated protein 1 Mus musculus 104-109 14623896-2 2004 To understand better the role of STAT1 in the interferon-gamma (IFN-gamma)-induced phenotype, we generated an active form of STAT1 (STAT1C) by substituting Cys residues for both Arg-656 and Asn-658 within the C-terminal loop of the STAT1 SH2 domain. Cysteine 156-159 signal transducer and activator of transcription 1 Homo sapiens 125-130 14623896-2 2004 To understand better the role of STAT1 in the interferon-gamma (IFN-gamma)-induced phenotype, we generated an active form of STAT1 (STAT1C) by substituting Cys residues for both Arg-656 and Asn-658 within the C-terminal loop of the STAT1 SH2 domain. Cysteine 156-159 signal transducer and activator of transcription 1 Homo sapiens 132-138 14623896-2 2004 To understand better the role of STAT1 in the interferon-gamma (IFN-gamma)-induced phenotype, we generated an active form of STAT1 (STAT1C) by substituting Cys residues for both Arg-656 and Asn-658 within the C-terminal loop of the STAT1 SH2 domain. Cysteine 156-159 signal transducer and activator of transcription 1 Homo sapiens 125-130 14687762-9 2004 Addition of the sulfhydryl compounds; glutathione (GSH), N-acetyl-L-cysteine (NAC), L-cysteine or D-penicillamine significantly enhanced the rate of CN- release. Cysteine 66-76 X-linked Kx blood group Homo sapiens 78-81 14750857-2 2004 As a demonstration, glucose oxidase (GOx) was modified at its C-terminal with a linker peptide with a cysteine residue at the end. Cysteine 102-110 hydroxyacid oxidase 1 Homo sapiens 20-35 14750857-2 2004 As a demonstration, glucose oxidase (GOx) was modified at its C-terminal with a linker peptide with a cysteine residue at the end. Cysteine 102-110 hydroxyacid oxidase 1 Homo sapiens 37-40 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. Cysteine 33-41 hydroxyacid oxidase 1 Homo sapiens 22-25 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. Cysteine 100-103 hydroxyacid oxidase 1 Homo sapiens 22-25 14583620-4 2004 Sequence analysis showed that Dub-1A encodes a 468-amino acid protein that has a molecular mass of approximately 51 kDa and that contains a putative catalytic domain (Cys, His, and Asp) conserved among DUB proteins. Cysteine 167-170 ubiquitin specific peptidase 17-like B Mus musculus 30-36 15036292-4 2004 In the case of human neuroglobin, cysteines at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. Cysteine 34-43 neuroglobin Homo sapiens 21-32 15036292-7 2004 Mutation of specific cysteines, or reduction to break the S-S bond, led to a large decrease in the observed oxygen affinity of human neuroglobin, mainly due to a decrease in the histidine dissociation rate. Cysteine 21-30 neuroglobin Homo sapiens 133-144 14985536-0 2004 Construction and characterization of a kappa opioid receptor devoid of all free cysteines. Cysteine 80-89 opioid receptor kappa 1 Homo sapiens 39-60 14985536-1 2004 We have constructed an optimized mutant of the kappa opioid receptor (KOR), which is devoid of its 10 free cysteines. Cysteine 107-116 opioid receptor kappa 1 Homo sapiens 47-68 14985536-1 2004 We have constructed an optimized mutant of the kappa opioid receptor (KOR), which is devoid of its 10 free cysteines. Cysteine 107-116 opioid receptor kappa 1 Homo sapiens 70-73 18248232-8 2004 Interestingly, and uniquely, zebrafish Fshb lacked two highly conserved cysteine residues in the "determinant loop" which is thought to contribute towards receptor binding and specificity. Cysteine 72-80 follicle stimulating hormone subunit beta Danio rerio 39-43 14532268-6 2003 Attachment of the cyclopentenone prostaglandin occurs at cysteine 269, which is located in the c-Jun DNA binding domain. Cysteine 57-65 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 95-100 14687706-2 2003 RANTES is a beta chemokine in which the cysteines are adjacent (C-C), and it attracts and activates eosinophil. Cysteine 40-49 C-C motif chemokine ligand 5 Homo sapiens 0-6 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. Cysteine 154-162 adiponectin, C1Q and collagen domain containing Rattus norvegicus 90-96 14644153-4 2003 Biochemical studies demonstrated that PSKH1 is myristoylated on glycine 2 and palmitoylated on cysteine 3. Cysteine 95-103 protein serine kinase H1 Homo sapiens 38-43 14500725-3 2003 In this report we demonstrate that HPO is a flavin-linked sulfhydryl oxidase, and the invariant CXXC (Cys-Xaa-Xaa-Cys) motif in HPO is essential for the enzyme activity of HPO but not for its dimerization nor for its binding ability with JAB1. Cysteine 102-105 COP9 signalosome subunit 5 Homo sapiens 238-242 14500725-3 2003 In this report we demonstrate that HPO is a flavin-linked sulfhydryl oxidase, and the invariant CXXC (Cys-Xaa-Xaa-Cys) motif in HPO is essential for the enzyme activity of HPO but not for its dimerization nor for its binding ability with JAB1. Cysteine 114-117 COP9 signalosome subunit 5 Homo sapiens 238-242 12893640-5 2003 We speculate, however, that the unique ability of H2O2 to reversibly oxidize the reactive site cysteine residues of protein tyrosine phosphatases may result in transient inactivation of the SHP-2 that is bound to PECAM-1 under these conditions. Cysteine 95-103 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 190-195 14559776-7 2003 Mutating the predicted catalytic cysteine in AT3 inhibits each of these ubiquitin protease activities. Cysteine 33-41 ataxin 3 Homo sapiens 45-48 14672344-11 2003 Four of the six mutations occurred in the cysteine-rich ligand-binding domain and are predicted to disrupt binding of OPG to RANKL. Cysteine 42-50 TNF superfamily member 11 Homo sapiens 125-130 14534363-9 2003 In contrast, an antagonist rhodamine-Ac-Cys-Glu-His-(d-Nal)-Arg-Trp-Gly-Cys-Pro-Pro-Lys-Asp-NH2 (HS014) bound to and colocalized with MC4R-GFP on the cell surface and did not stimulate receptor internalization. Cysteine 40-43 melanocortin 4 receptor Homo sapiens 134-138 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. Cysteine 160-168 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. Cysteine 23-31 integrin subunit alpha 2b Homo sapiens 140-145 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. Cysteine 196-199 beta-lactoglobulin Bos taurus 138-145 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. Cysteine 196-199 beta-lactoglobulin Bos taurus 268-275 14609334-3 2003 To apply this approach to the C2 domain of cytosolic phospholipase A(2) (cPLA(2)), single cysteines were introduced at all 27 positions in the three Ca(2+)-binding loops and labeled with a methanethiosulfonate spin-label. Cysteine 90-99 phospholipase A2 group IVA Homo sapiens 43-80 14505673-2 2003 Maleimide derivatives of ANP have been synthesized and conjugated to cysteine-34 of human serum albumin. Cysteine 69-77 natriuretic peptide A Rattus norvegicus 25-28 14563551-2 2003 In sulfatases, FGE posttranslationally converts a cysteine residue to FGly, which is part of the catalytic site and is essential for sulfatase activity. Cysteine 50-58 sulfatase modifying factor 1 Homo sapiens 15-18 14529283-7 2003 Four of the five cysteine residues in the soluble NTPDase6 are highly conserved among all the NTPDases, while the fifth residue is not. Cysteine 17-25 ectonucleoside triphosphate diphosphohydrolase 6 Homo sapiens 50-58 12950200-3 2003 By comparison to the data of crystalline oxidized chicken sulfite oxidase, it is shown that complex 3, whose thiolate simulates binding by the highly conserved cysteine, is an accurate structural analogue of the oxidized site of this enzyme. Cysteine 160-168 sulfite oxidase Gallus gallus 58-73 12796500-2 2003 A Cys-Xaa-Xaa-Cys (CXXC)-based thiol-protein oxidoreductase activity of MIF is associated with certain biological functions. Cysteine 2-5 thioredoxin reductase 1 Homo sapiens 45-59 12796500-2 2003 A Cys-Xaa-Xaa-Cys (CXXC)-based thiol-protein oxidoreductase activity of MIF is associated with certain biological functions. Cysteine 13-17 thioredoxin reductase 1 Homo sapiens 45-59 12824178-6 2003 Mutation of the catalytic Cys residue to Ser leads to a loss of caseinolytic activity of DEK1 domain II&III. Cysteine 26-29 calpain-type cysteine protease DEK1 Zea mays 89-93 12939163-0 2003 N-Glycosylation and conserved cysteine residues in RAMP3 play a critical role for the functional expression of CRLR/RAMP3 adrenomedullin receptor. Cysteine 30-38 calcitonin receptor like receptor L homeolog Xenopus laevis 111-115 14640032-5 2003 Free TTR as well as TTR-cysteine and TTR-cysteinylglycine adducts are clearly evident. Cysteine 24-32 transthyretin Homo sapiens 20-23 14640032-5 2003 Free TTR as well as TTR-cysteine and TTR-cysteinylglycine adducts are clearly evident. Cysteine 24-32 transthyretin Homo sapiens 20-23 12915465-4 2003 The first mutation, a T-->G transversion in codon 64, is predicted to change a conserved cysteine residue to glycine in the RING finger domain of the 1863 amino acid BRCA1 protein. Cysteine 89-97 BRCA1 DNA repair associated Homo sapiens 166-171 14629116-3 2003 A59V is located at a between-species conserved region of leptin, and R4C might have effect on the tertiary structure of the leptin protein because of the presence of an extra cystein. Cysteine 175-182 leptin Bos taurus 124-130 12953119-5 2003 Furthermore, site-directed mutagenesis of TGA1 Cys-260 and Cys-266 enables the interaction with NPR1 in yeast and Arabidopsis. Cysteine 47-50 serine/threonine protein kinase NPR1 Saccharomyces cerevisiae S288C 96-100 12953119-5 2003 Furthermore, site-directed mutagenesis of TGA1 Cys-260 and Cys-266 enables the interaction with NPR1 in yeast and Arabidopsis. Cysteine 59-62 serine/threonine protein kinase NPR1 Saccharomyces cerevisiae S288C 96-100 12953119-6 2003 Together, these results indicate that TGA1 relies on the oxidation state of Cys residues to mediate the interaction with NPR1. Cysteine 76-79 regulatory protein (NPR1) Arabidopsis thaliana 121-125 12777388-3 2003 Human MAO A and MAO B each contain 9 cysteine residues (7 in conserved sequence locations). Cysteine 37-45 monoamine oxidase B Homo sapiens 16-21 12835757-1 2003 The four members of the mannose receptor family (the mannose receptor, the M-type phospholipase A(2) receptor, DEC-205 and Endo180) share a common extracellular arrangement of an amino-terminal cysteine-rich domain followed by a fibronectin type II (FNII) domain and multiple C-type lectin-like domains (CTLDs). Cysteine 194-202 lymphocyte antigen 75 Mus musculus 111-118 12837786-5 2003 In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. Cysteine 35-43 methionine sulfoxide reductase A Homo sapiens 87-91 12837786-5 2003 In contrast to the three catalytic cysteine residues found in previously characterized MsrA structures, M. tuberculosis MsrA represents a class containing only two functional cysteine residues. Cysteine 175-183 methionine sulfoxide reductase A Homo sapiens 120-124 12684517-12 2003 Localization of SNAT1 to certain dopaminergic neurons of the substantia nigra and cholinergic motoneurons suggests that SNAT1 may play additional specialized roles, providing metabolic fuel (via alpha-ketoglutarate) or precursors (cysteine, glycine) for glutathione synthesis. Cysteine 231-239 solute carrier family 38 member 1 L homeolog Xenopus laevis 16-21 12684517-12 2003 Localization of SNAT1 to certain dopaminergic neurons of the substantia nigra and cholinergic motoneurons suggests that SNAT1 may play additional specialized roles, providing metabolic fuel (via alpha-ketoglutarate) or precursors (cysteine, glycine) for glutathione synthesis. Cysteine 231-239 solute carrier family 38 member 1 L homeolog Xenopus laevis 120-125 12805206-3 2003 Using cysteine-scanning mutagenesis and charged thiol-modifying reagents, we identified two amino acids in Kir6.2 that appear to interact directly with ATP: R50 in the N-terminus, and K185 in the C-terminus. Cysteine 6-14 potassium inwardly rectifying channel subfamily J member 11 Homo sapiens 107-113 12812753-1 2003 Tenascin-N, a novel member of the tenascin family, was identified and shown to encode characteristic structural motifs of a cysteine-rich stretch, 3.5 epidermal growth factor-like repeats, 12 fibronectin type III homologous domains, and a fibrinogen-like domain. Cysteine 124-132 tenascin C Homo sapiens 34-42 12767819-4 2003 In recombinant murine Mb, azide affinities are only slightly dependent on the Cys(E9) oxidation state. Cysteine 78-81 myoglobin Mus musculus 22-24 12767819-6 2003 Recombinant expression of M. musculus Mb might have an important role in order to investigate the eventual involvement of Cys(E9) in the new physiological roles proposed for Mb. Cysteine 122-125 myoglobin Mus musculus 38-40 12778447-7 2003 CONCLUSION: The above data indicate that the polymorphism at codon 311(Cys --> Ser)in the PON2 gene is associated with ischemic morbidity in Chinese T2DM patients and C allele might be a risk factor. Cysteine 71-74 paraoxonase 2 Homo sapiens 93-97 12767513-4 2003 Two Cx37 mutations have been implicated: a Cys-54-Gln substitution in FEQNTAQP (MUT 1) and FEQNTAQA (MUT 2); an additional Pro-59-Ala substitution has been proposed in MUT 2. Cysteine 43-46 gap junction protein, alpha 4 Mus musculus 4-8 12767513-4 2003 Two Cx37 mutations have been implicated: a Cys-54-Gln substitution in FEQNTAQP (MUT 1) and FEQNTAQA (MUT 2); an additional Pro-59-Ala substitution has been proposed in MUT 2. Cysteine 43-46 mutator 1 Mus musculus 80-85 12707936-4 2003 In addition, homozygous or hemizygous carriers of the 5-HT2C Ser allele were 12 times more likely to have major depressive illness than homozygous or hemizygous carriers of the 5-HT2C Cys allele. Cysteine 184-187 5-hydroxytryptamine receptor 2C Homo sapiens 54-60 12707936-4 2003 In addition, homozygous or hemizygous carriers of the 5-HT2C Ser allele were 12 times more likely to have major depressive illness than homozygous or hemizygous carriers of the 5-HT2C Cys allele. Cysteine 184-187 5-hydroxytryptamine receptor 2C Homo sapiens 177-183 12707953-1 2003 Homocysteine (Hcy) is converted to cysteine or is remethylated to methionine by methylenetetrahydrofolate reductase (MTHFR). Cysteine 4-12 methylenetetrahydrofolate reductase Homo sapiens 80-115 12707953-1 2003 Homocysteine (Hcy) is converted to cysteine or is remethylated to methionine by methylenetetrahydrofolate reductase (MTHFR). Cysteine 4-12 methylenetetrahydrofolate reductase Homo sapiens 117-122 12771940-7 2003 ARHI is associated at the cell membrane through its prenylation at the C-terminal cysteine residue. Cysteine 82-90 DIRAS family GTPase 3 Homo sapiens 0-4 12600995-0 2003 An inverse correlation between expression of a preprocathepsin B-related protein with cysteine-rich sequences and steroid 11beta -hydroxylase in adrenocortical cells. Cysteine 86-94 cytochrome P450, family 11, subfamily b, polypeptide 1 Mus musculus 114-141 12729891-3 2003 The predicted processed 25 amino acid hepcidin 2 peptide share 68% identity with hepcidin 1 with perfect conservation of eight cysteine residues. Cysteine 127-135 hepcidin antimicrobial peptide Mus musculus 38-46 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). Cysteine 100-103 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 100-103 corticotropin releasing hormone receptor 1 Mus musculus 86-91 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). Cysteine 108-111 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 108-111 corticotropin releasing hormone receptor 1 Mus musculus 86-91 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). Cysteine 108-111 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 108-111 corticotropin releasing hormone receptor 1 Mus musculus 86-91 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). Cysteine 108-111 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 108-111 corticotropin releasing hormone receptor 1 Mus musculus 86-91 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). Cysteine 108-111 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 108-111 corticotropin releasing hormone receptor 1 Mus musculus 86-91 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). Cysteine 108-111 corticotropin releasing hormone receptor 2 Mus musculus 9-18 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). Cysteine 108-111 corticotropin releasing hormone receptor 1 Mus musculus 86-91 12732513-4 2003 Monoiodoacetate and EDTA both inhibited the PghP activity, but Zn(2+) or Mn(2+) ions fully restored the enzyme activity inhibited by the chelator, suggesting that a cysteine residue(s) and these metal ions participate in the catalytic mechanism of the enzyme. Cysteine 165-173 poly-gamma-glutamate hydrolase of phage (PghP) Bacillus phage phiNIT1 44-48 12755587-0 2003 Selective covalent binding of acrylonitrile to Cys 186 in rat liver carbonic anhydrase III in vivo. Cysteine 47-50 carbonic anhydrase 3 Rattus norvegicus 68-90 12755587-9 2003 This tryptic fragment contains two Cys residues (Cys181 and Cys186) in the rat CAIII sequence. Cysteine 35-38 carbonic anhydrase 3 Rattus norvegicus 79-84 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 4-7 calcium voltage-gated channel subunit alpha1 A Homo sapiens 33-41 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 4-7 adrenoceptor beta 2 Homo sapiens 43-45 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 8-11 calcium voltage-gated channel subunit alpha1 A Homo sapiens 33-41 12519093-4 2003 The Cys/Cys (CC) genotype of the alpha(1A)-AR R492C polymorphism was associated with a longer ECG PR interval before and during the adrenaline infusions. Cysteine 8-11 adrenoceptor beta 2 Homo sapiens 43-45 12697676-0 2003 The cysteine-rich amino terminus of the thyrotropin receptor is the immunodominant linear antibody epitope in mice immunized using naked deoxyribonucleic acid or adenovirus vectors. Cysteine 4-12 thyroid stimulating hormone receptor Mus musculus 40-60 12697676-6 2003 However, the dominant peptide recognized in both groups was the TSHR cysteine-rich N terminus (residues 22-41). Cysteine 69-77 thyroid stimulating hormone receptor Mus musculus 64-68 12697676-9 2003 The cysteine-rich TSHR N terminus is functionally important in the action of stimulating TSHR autoantibodies in humans. Cysteine 4-12 thyroid stimulating hormone receptor Homo sapiens 18-22 12697676-9 2003 The cysteine-rich TSHR N terminus is functionally important in the action of stimulating TSHR autoantibodies in humans. Cysteine 4-12 thyroid stimulating hormone receptor Homo sapiens 89-93 12734700-0 2003 Time-resolved fluorescence anisotropy studies show domain-specific interactions of calmodulin with IQ target sequences of myosin V. Single cysteine mutants of calmodulin, Cam(S38C) and Cam(N111C), have been specifically labelled with Alexa488 maleimide to study the effects of calcium on the structural dynamics of calmodulin complexed with IQ3, IQ4 and IQ34 target peptide motifs of mouse unconventional myosin-V. Cysteine 139-147 calmodulin 2 Mus musculus 83-93 12681477-1 2003 DMBT1 (deleted in malignant brain tumor 1), which encodes a large scavenger receptor cysteine rich (SRCR) B protein, has been proposed to be a tumor suppressor gene, due to the high frequency of its homozygous deletion and the lack of expression in a variety of cancers. Cysteine 85-93 deleted in malignant brain tumors 1 Homo sapiens 0-5 12614333-0 2003 The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures. Cysteine 51-59 solute carrier family 1 (glial high affinity glutamate transporter), member 2 Mus musculus 27-32 12614333-0 2003 The glutamate transporters EAAT2 and EAAT3 mediate cysteine uptake in cortical neuron cultures. Cysteine 51-59 solute carrier family 1 (neuronal/epithelial high affinity glutamate transporter, system Xag), member 1 Mus musculus 37-42 12555076-3 2003 In 39 sporadic cerebellar medulloblastomas screeened for alterations in the AXIN1 gene, another component of the Wnt pathway, we found missense AXIN1 mutations in two tumours, CCC-->TCC at codon 255 (exon 1, Pro-->Ser) and TCT-->TGT at codon 263 (exon 1, Ser-->Cys). Cysteine 273-276 axin 1 Homo sapiens 144-149 12473460-4 2003 NaD1 features all the characteristics of the cysteine-stabilized alphabeta motif that has been described for a variety of proteins of differing functions ranging from antibacterial insect defensins and ion channel-perturbing scorpion toxins to an elicitor of the sweet taste response. Cysteine 45-53 nad1 Raphanus sativus 0-4 12505156-2 2003 As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. Cysteine 91-99 nuclear RNA export factor 1 Homo sapiens 111-114 12505156-2 2003 As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. Cysteine 168-177 nuclear RNA export factor 1 Homo sapiens 111-114 12505156-3 2003 After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine 53-61 nuclear RNA export factor 1 Homo sapiens 20-23 12527209-9 2003 Finally, we show that interaction with Krm2 is mediated by the second cysteine-rich domain of Dkks. Cysteine 70-78 kringle containing transmembrane protein 2 Homo sapiens 39-43 15098675-5 2003 Site-directed spin-labeling was achieved by cysteine residues of human cardiac troponin C (TnC). Cysteine 44-52 tenascin C Homo sapiens 91-94 12454802-9 2003 Similarly, the frequency of the PON2 codon 311 Cys/Cys genotype was significantly higher in the group with three-vessel disease than in the other groups combined (15.22% vs. 4.61%; P=.018). Cysteine 47-50 paraoxonase 2 Homo sapiens 32-36 12454802-9 2003 Similarly, the frequency of the PON2 codon 311 Cys/Cys genotype was significantly higher in the group with three-vessel disease than in the other groups combined (15.22% vs. 4.61%; P=.018). Cysteine 51-54 paraoxonase 2 Homo sapiens 32-36 12624753-1 2003 The first step of cysteine biosynthesis in bacteria and plants consists in the formation of O-acetylserine catalyzed by serine acetyltransferase (SAT). Cysteine 18-26 streptothricin acetyltransferase Escherichia coli 146-149 12624753-2 2003 SAT is highly sensitive to feedback inhibition by cysteine as part of the regulatory circuit of cysteine biosynthesis und thus hampers over-expression and fermentation of cysteine in biotechnological production processes. Cysteine 50-58 streptothricin acetyltransferase Escherichia coli 0-3 12624753-2 2003 SAT is highly sensitive to feedback inhibition by cysteine as part of the regulatory circuit of cysteine biosynthesis und thus hampers over-expression and fermentation of cysteine in biotechnological production processes. Cysteine 96-104 streptothricin acetyltransferase Escherichia coli 0-3 12624753-2 2003 SAT is highly sensitive to feedback inhibition by cysteine as part of the regulatory circuit of cysteine biosynthesis und thus hampers over-expression and fermentation of cysteine in biotechnological production processes. Cysteine 96-104 streptothricin acetyltransferase Escherichia coli 0-3 12624753-3 2003 Since plants contain multiple SAT isoforms with different cysteine feedback sensitivity, this resource was exploited to demonstrate the suitability of plant SATs for the production of cysteine in both bacteria and plants. Cysteine 184-192 streptothricin acetyltransferase Escherichia coli 30-33 12624753-5 2003 The catalytic activity of SAT4 was insensitive up to 0.6 mM cysteine. Cysteine 60-68 serine acetyltransferase 1, chloroplastic-like Nicotiana tabacum 26-30 12624753-6 2003 Expression of SAT4 in a newly constructed Escherichia coli host strain without endogenous SAT activity yielded a significant accumulation of cysteine in the culture medium compared to expression of cysteine sensitive SATs in the same strain. Cysteine 141-149 sat4 Escherichia coli 14-18 12624753-6 2003 Expression of SAT4 in a newly constructed Escherichia coli host strain without endogenous SAT activity yielded a significant accumulation of cysteine in the culture medium compared to expression of cysteine sensitive SATs in the same strain. Cysteine 141-149 streptothricin acetyltransferase Escherichia coli 14-17 12624753-6 2003 Expression of SAT4 in a newly constructed Escherichia coli host strain without endogenous SAT activity yielded a significant accumulation of cysteine in the culture medium compared to expression of cysteine sensitive SATs in the same strain. Cysteine 198-206 sat4 Escherichia coli 14-18 12624753-6 2003 Expression of SAT4 in a newly constructed Escherichia coli host strain without endogenous SAT activity yielded a significant accumulation of cysteine in the culture medium compared to expression of cysteine sensitive SATs in the same strain. Cysteine 198-206 streptothricin acetyltransferase Escherichia coli 14-17 12459913-3 2003 In some PBGS, the cysteines of the metal switch sequence DXCXCX(Y/F)X(3)G(H/Q)CG have been demonstrated to bind a catalytic zinc, and in other PBGS, the aspartic acid residues of the metal switch sequence DXALDX(Y/F)X(3)G(H/Q)DG have been postulated to bind a catalytically essential magnesium and/or potassium. Cysteine 18-27 aminolevulinate dehydratase Homo sapiens 8-12 12459913-3 2003 In some PBGS, the cysteines of the metal switch sequence DXCXCX(Y/F)X(3)G(H/Q)CG have been demonstrated to bind a catalytic zinc, and in other PBGS, the aspartic acid residues of the metal switch sequence DXALDX(Y/F)X(3)G(H/Q)DG have been postulated to bind a catalytically essential magnesium and/or potassium. Cysteine 18-27 aminolevulinate dehydratase Homo sapiens 143-147 12459913-4 2003 The current work describes chimeric proteins that contain the aspartate-rich sequences of pea PBGS and Pseudomonas aeruginosa PBGS in place of the naturally occurring cysteine-rich sequence of human PBGS. Cysteine 167-175 aminolevulinate dehydratase Homo sapiens 126-130 12459913-8 2003 The identity of a basic residue, which is Arg221 in human PBGS, strictly correlates with the presence or absence of the cysteine-rich sequence. Cysteine 120-128 aminolevulinate dehydratase Homo sapiens 58-62 12449175-2 2002 The novel C chemokine single cysteine motif (SCM)-1alpha (XCL-1) and the CC chemokine monocyte chemoattractant protein (MCP)-1 (CCL-2) are also mononuclear-cell attractants and represent alternative candidate mediators of alveolitis. Cysteine 29-37 X-C motif chemokine ligand 1 Homo sapiens 58-63 12391223-2 2002 In IgA1, Cys(133) in C(H)1 forms the disulfide bond to the L chain. Cysteine 9-12 immunoglobulin heavy constant alpha 1 Homo sapiens 3-7 12421853-1 2002 In liver, cysteine dioxygenase (CDO), cysteinesulfinate decarboxylase (CSD), and gamma-glutamylcysteine synthetase (GCS) play important regulatory roles in the metabolism of cysteine to sulfate, taurine and glutathione. Cysteine 10-18 cysteine sulfinic acid decarboxylase Rattus norvegicus 71-74 12368900-4 2002 This Cys residue is strictly conserved within the MYST members, suggesting a common mode of catalysis by this HAT subfamily. Cysteine 5-8 NuA4 histone acetyltransferase complex catalytic subunit ESA1 Saccharomyces cerevisiae S288C 50-54 12458670-8 2002 L-Cysteine was required to initiate the dissociation of 14C-NAC bound to albumin. Cysteine 0-10 X-linked Kx blood group Homo sapiens 60-63 12538912-2 2002 The three-dimensional structure of eotaxin-3 determined by nuclear magnetic resonance has revealed that the N-terminal nine residues preceding the first cysteine comprise an unstructured domain, which is also observed in other chemokine molecules. Cysteine 153-161 C-C motif chemokine ligand 26 Homo sapiens 35-44 12237426-3 2002 A series of cysteines located in the envelope protein and the most important enzymatic domains of the virus helicase/NTPase, methyltransferase and RNA-dependent RNA polymerase were found to be highly conserved. Cysteine 12-21 inosine triphosphatase Homo sapiens 117-123 12215545-6 2002 NIF-1 is a 1,342-amino-acid nuclear protein containing a number of conserved domains, including six Cys-2/His-2 zinc fingers, an N-terminal stretch of acidic amino acids, and a C-terminal leucine zipper-like motif. Cysteine 100-103 zinc finger protein 335 Homo sapiens 0-5 12397382-6 2002 The W736 residue of Na(v)1.4 was replaced by a cysteine using site-directed mutagenesis. Cysteine 47-55 sodium voltage-gated channel alpha subunit 4 Rattus norvegicus 20-28 12383086-3 2002 Both LOV1 and LOV2 undergo a self-contained photocycle, which involves the formation of a covalent adduct between the FMN chromophore and a conserved active-site cysteine residue (Cys39). Cysteine 162-170 NAC domain containing protein 35 Arabidopsis thaliana 5-9 12214272-9 2002 These results identify a novel function of the TR enzyme as a signaling factor in the regulation of AP-1 activity via a cysteine motif located in the protein. Cysteine 120-128 thioredoxin reductase 1 Homo sapiens 47-49 12193649-8 2002 The most reactive residues of Keap1 (C(257), C(273), C(288), and C(297)) were identified by mapping the dexamethasone-modified cysteines by mass spectrometry of tryptic peptides. Cysteine 127-136 kelch-like ECH-associated protein 1 Mus musculus 30-35 12198013-9 2002 The increases in the NAC group were associated with a significant effect of supplement (P < 0.03) on erythrocyte cysteine concentration. Cysteine 116-124 X-linked Kx blood group Homo sapiens 21-24 12205652-2 2002 We have now identified a missense mutation affecting a conserved cysteine residue in the extracellular region of the LGI1 protein. Cysteine 65-73 leucine rich glioma inactivated 1 Homo sapiens 117-121 12070134-3 2002 A Cys-less P-gp with cysteines in transmembrane (TM) 4 or TM5 can be cross-linked with a cysteine in TM12. Cysteine 2-5 tropomyosin 3 Homo sapiens 58-61 12070134-3 2002 A Cys-less P-gp with cysteines in transmembrane (TM) 4 or TM5 can be cross-linked with a cysteine in TM12. Cysteine 21-30 tropomyosin 3 Homo sapiens 58-61 12070134-3 2002 A Cys-less P-gp with cysteines in transmembrane (TM) 4 or TM5 can be cross-linked with a cysteine in TM12. Cysteine 21-29 tropomyosin 3 Homo sapiens 58-61 12151315-1 2002 1-cys peroxiredoxin (1-cys Prx), the only member of a Prx subfamily that contains a single conserved cysteine residue, is abundant in lung. Cysteine 101-109 periaxin Rattus norvegicus 27-30 12186742-2 2002 The first peptidomimetic (PM 1) is essentially a decapeptide in which sites of A (20-21) and B (19-26) chains of insulin are linked by the peptides bond (Cys-Gly-Glu-Arg-Gly-Phe-Phe-Tyr-Cys-Asn). Cysteine 154-157 transmembrane protein 11 Homo sapiens 26-30 12195239-6 2002 CuZn and Mn SOD activities were found to be increased in CO compared to CY group. Cysteine 72-74 superoxide dismutase 2 Rattus norvegicus 9-15 12183103-6 2002 In addition, when glutarate (4 mM), a transportable substrate for both the sodium-dependent dicarboxylate transporter and the dicarboxylate/organic anion exchanger (OAT1), was added to the basolateral compartment, there was a significant reduction in the uptake and accumulation of Hg(++) in the form of mercuric conjugates of Cys. Cysteine 327-330 solute carrier family 22 member 6 Oryctolagus cuniculus 165-169 12006572-5 2002 Metabolic labeling demonstrates that these cysteines in the KChIP2 isoforms, as well as the corresponding sites in KChIP3, are palmitoylated. Cysteine 43-52 potassium voltage-gated channel interacting protein 2 Rattus norvegicus 60-66 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). Cysteine 98-101 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). Cysteine 98-101 vitronectin Homo sapiens 71-82 12093282-1 2002 By use of site-directed mutagenesis in combination with chemical modification of mutated proteins, the role of the six Cys residues in the transport function of the rat mitochondrial carnitine carrier (CAC) was studied. Cysteine 119-122 solute carrier family 25 member 20 Rattus norvegicus 202-205 12093282-7 2002 The wild-type CAC and the mutants containing Cys-136 showed substrate protection against NEM and MTSES inhibition and against NEM labeling. Cysteine 45-48 solute carrier family 25 member 20 Rattus norvegicus 14-17 12093282-9 2002 A model of the CAC is proposed in which the matrix hydrophilic loop containing Cys-136 protrudes into the membrane between the transmembrane domains of the protein. Cysteine 79-82 solute carrier family 25 member 20 Rattus norvegicus 15-18 12097165-5 2002 The distances from Cys-60 and Cys-250 of TnT to Gln-41 of F-actin were 39.5 and 30.0 A, respectively in the absence of Ca(2+), and increased by 2.6 and 5.8 A, respectively upon binding of Ca(2+) to TnC. Cysteine 19-22 tenascin Oryctolagus cuniculus 198-201 12097165-5 2002 The distances from Cys-60 and Cys-250 of TnT to Gln-41 of F-actin were 39.5 and 30.0 A, respectively in the absence of Ca(2+), and increased by 2.6 and 5.8 A, respectively upon binding of Ca(2+) to TnC. Cysteine 30-33 tenascin Oryctolagus cuniculus 198-201 12077228-7 2002 This localization of 2B4 occurs due to a CxC cysteine motif found in the transmembrane region, as determined by mutagenesis studies. Cysteine 45-53 CD244 molecule A Mus musculus 21-24 12134072-2 2002 In spite of its ability to bind activated Ras in vitro, the Ras binding domain (RBD) of Raf-1 (Raf-1[51-131]GFP) failed to detect Ras in Ras-transformed NIH 3T3 fibroblasts and required the addition of the cysteine-rich domain (CRD) (Raf-1[51-220]GFP) to show clear localization to plasma membrane ruffles. Cysteine 206-214 v-raf-leukemia viral oncogene 1 Mus musculus 88-93 11967265-7 2002 This adhesion requires integrin activation and can be prevented by antibodies to the cysteine-rich domain of ADAM13 and beta(1) integrin. Cysteine 85-93 integrin subunit beta 1 Homo sapiens 120-136 12056887-2 2002 The cysteine-rich C-terminal domain of this protein, corresponding to AGRP(87-132), exhibits receptor binding affinity and antagonism equivalent to that of the full-length protein. Cysteine 4-12 agouti related neuropeptide Homo sapiens 70-74 12036872-0 2002 The cysteine knot of platelet glycoprotein Ib beta (GPIb beta) is critical for the interaction of GPIb beta with GPIX. Cysteine 4-12 glycoprotein Ib platelet subunit beta Homo sapiens 52-61 12036872-0 2002 The cysteine knot of platelet glycoprotein Ib beta (GPIb beta) is critical for the interaction of GPIb beta with GPIX. Cysteine 4-12 glycoprotein Ib platelet subunit beta Homo sapiens 98-107 12036872-11 2002 These results suggest that the cysteine knot region of GPIb beta in the N terminus is critical for the conformation of GPIb beta that interacts with GPIX and further suggests that a critical interaction of GPIb beta with GPIX involve residues 15 through 32 of GPIb beta Cysteine 31-39 glycoprotein Ib platelet subunit beta Homo sapiens 55-64 12036872-11 2002 These results suggest that the cysteine knot region of GPIb beta in the N terminus is critical for the conformation of GPIb beta that interacts with GPIX and further suggests that a critical interaction of GPIb beta with GPIX involve residues 15 through 32 of GPIb beta Cysteine 31-39 glycoprotein Ib platelet subunit beta Homo sapiens 119-128 12036872-11 2002 These results suggest that the cysteine knot region of GPIb beta in the N terminus is critical for the conformation of GPIb beta that interacts with GPIX and further suggests that a critical interaction of GPIb beta with GPIX involve residues 15 through 32 of GPIb beta Cysteine 31-39 glycoprotein Ib platelet subunit beta Homo sapiens 119-128 11943783-5 2002 The ability of different compounds to protect the xlHAS1(C337S) mutant enzyme from loss of activity due to treatment with N-ethylmaleimide, a cysteine-modifying reagent, yields information on the relative affinity of a variety of nucleotides and nucleotide-sugars. Cysteine 142-150 hyaluronan synthase 1 S homeolog Xenopus laevis 50-56 12119100-1 2002 Acidic epididymal glycoprotein 1 (AEG1), also called cysteine-rich secretory protein 1 (CRISP1), is a member of the CRISP protein family which is characterized by 16 conserved cysteine residues at the C-terminus. Cysteine 53-61 cysteine rich secretory protein 1 Equus caballus 88-94 11923307-9 2002 This result indicates that reduction of the aminoenethiol intermediate depends on a redox-active cysteine residue in AtHAL3a. Cysteine 97-105 HAL3-like protein A Arabidopsis thaliana 117-124 11867614-3 2002 Nmp4 isoforms contain from 5 to 8 Cys(2)His(2) zinc fingers, an SH3-binding domain that overlaps with a putative AT-hook and a polyglutamine-alanine repeat (poly(QA)). Cysteine 34-37 zinc finger protein 384 Homo sapiens 0-4 11867614-4 2002 To determine the mechanistic significance of Cys(2)His(2) zinc finger association with this unusual consensus DNA binding element, we identified the Nmp4 DNA-binding and transcriptional activation domains. Cysteine 45-48 zinc finger protein 384 Homo sapiens 149-153 12006387-2 2002 Here, we investigated the role of isoprenylcysteine carboxyl methyltransferase (ICMTase), which methylates isoprenylated CAAX (where C indicates cysteine; A, aliphatic amino acids; and X, almost any other amino acid) proteins, including Rac1, a component of superoxide-generating NAD(P)H oxidase, in the expression of VCAM-1. Cysteine 43-51 Rac family small GTPase 1 Homo sapiens 237-241 11978727-3 2002 Based on sequence analysis, Png1p was classified as a member of the "transglutaminase-like superfamily" that contains a putative catalytic triad of amino acids (cysteine, histidine, and aspartic acid). Cysteine 161-169 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase Saccharomyces cerevisiae S288C 28-33 12009017-0 2002 Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization. Cysteine 27-35 fibroblast growth factor receptor 3 Homo sapiens 60-95 12009017-0 2002 Differential activation of cysteine-substitution mutants of fibroblast growth factor receptor 3 is determined by cysteine localization. Cysteine 113-121 fibroblast growth factor receptor 3 Homo sapiens 60-95 12009017-5 2002 An adjacent cysteine substitution (G375C) leads to a less severe form of human dwarfism, achondroplasia, suggesting that the intensity of FGFR3 activation by these cross-links may be position dependent. Cysteine 12-20 fibroblast growth factor receptor 3 Homo sapiens 138-143 12009017-6 2002 To test this hypothesis, we have sequentially replaced each amino acid at positions 370-375 of FGFR3 with cysteine. Cysteine 106-114 fibroblast growth factor receptor 3 Homo sapiens 95-100 12048031-0 2002 Subtle mutations in the cysteine region of HIV-1 Vif drastically alter the viral replication phenotype. Cysteine 24-32 Vif Human immunodeficiency virus 1 49-52 12048031-4 2002 These results indicate that the cysteine region of Vif is critical for the cell-dependent replication efficiency of HIV-1. Cysteine 32-40 Vif Human immunodeficiency virus 1 51-54 12582622-2 2002 The SbPRP protein is a putative bimodular protein of 126 amino acids with a proline-rich domain and a hydrophobic cysteine-rich domain plus a signal peptide at the N terminal. Cysteine 114-122 proline-rich protein Glycine max 4-9 11832479-2 2002 Structurally, Lkn-1 is distinct from other human CC chemokines in that it has long amino acid residues preceding the first cysteine at the NH(2) terminus, and contains two extra cysteines. Cysteine 123-131 C-C motif chemokine ligand 15 Homo sapiens 14-19 11832479-2 2002 Structurally, Lkn-1 is distinct from other human CC chemokines in that it has long amino acid residues preceding the first cysteine at the NH(2) terminus, and contains two extra cysteines. Cysteine 178-187 C-C motif chemokine ligand 15 Homo sapiens 14-19 11832479-7 2002 Deletion of 29 amino acids, however, abolished the agonistic activity almost completely showing that at least 3 amino acid residues preceding the first cysteine at the NH(2) terminus are essential for the biological activity of Lkn-1. Cysteine 152-160 C-C motif chemokine ligand 15 Homo sapiens 228-233 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. Cysteine 167-170 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. Cysteine 167-170 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. Cysteine 184-187 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. Cysteine 184-187 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. Cysteine 184-187 Charcot-Leyden crystal galectin Homo sapiens 278-289 12054602-3 2002 Our data indicate that a single cysteine residue, Cys-369, located in the C-terminal domain of the yeast Tim44 is exposed to the mitochondrial intermembrane space. Cysteine 32-40 protein translocase subunit TIM44 Saccharomyces cerevisiae S288C 105-110 12054602-3 2002 Our data indicate that a single cysteine residue, Cys-369, located in the C-terminal domain of the yeast Tim44 is exposed to the mitochondrial intermembrane space. Cysteine 50-53 protein translocase subunit TIM44 Saccharomyces cerevisiae S288C 105-110 12044560-4 2002 Assay mixtures contain the gamma-glutamyl transpeptidase (GGT) inhibitor acivicin in order to prevent the degradation of gamma-glutamylcysteine and of the accumulating GSH, and dithiothreitol in order to prevent the oxidation of cysteine and gamma-glutamylcysteine. Cysteine 135-143 inactive glutathione hydrolase 2 Homo sapiens 58-61 11825910-6 2002 Site-directed mutagenesis revealed that Cys(264) of hApg3p is an authentic active-site cysteine residue essential for the formation of hApg3p small middle dothApg8p homologue intermediates. Cysteine 40-43 autophagy related 3 Homo sapiens 52-58 11825910-6 2002 Site-directed mutagenesis revealed that Cys(264) of hApg3p is an authentic active-site cysteine residue essential for the formation of hApg3p small middle dothApg8p homologue intermediates. Cysteine 40-43 autophagy related 3 Homo sapiens 135-141 11825910-6 2002 Site-directed mutagenesis revealed that Cys(264) of hApg3p is an authentic active-site cysteine residue essential for the formation of hApg3p small middle dothApg8p homologue intermediates. Cysteine 87-95 autophagy related 3 Homo sapiens 52-58 11825910-6 2002 Site-directed mutagenesis revealed that Cys(264) of hApg3p is an authentic active-site cysteine residue essential for the formation of hApg3p small middle dothApg8p homologue intermediates. Cysteine 87-95 autophagy related 3 Homo sapiens 135-141 11796730-9 2002 The three-dimensional structure of the ternary complex enzyme-NADPH-5-iodouracil supports the proposal that this compound acts as a mechanism-based inhibitor, covalently modifying the active-site residue Cys-671, resulting in S-(hexahydro-2,4-dioxo-5-pyrimidinyl)cysteine. Cysteine 204-207 2,4-dienoyl-CoA reductase 1 Homo sapiens 62-67 11812789-4 2002 Cys-191, His-218, and Asp-235 of Png1p are conserved in the sequence of factor XIIIa, where these amino acids constitute a catalytic triad. Cysteine 0-3 peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase Saccharomyces cerevisiae S288C 33-38 11796727-0 2002 Essential hydrophilic carboxyl-terminal regions including cysteine residues of the yeast stretch-activated calcium-permeable channel Mid1. Cysteine 58-66 Mid1p Saccharomyces cerevisiae S288C 133-137 11796727-8 2002 These results clearly indicate that the carboxyl-terminal domain including the cysteine residues is important for Mid1 function. Cysteine 79-87 Mid1p Saccharomyces cerevisiae S288C 114-118 11799105-3 2002 The three-dimensional structure of NAT from Salmonella typhimurium has been resolved and shown to have three distinct domains and an active site catalytic triad composed of "Cys(69)-His(107)-Asp(122)," which is typical of hydrolytic enzymes such as the cysteine proteases. Cysteine 174-177 bromodomain containing 2 Homo sapiens 35-38 11815609-4 2002 In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15. Cysteine 22-25 interleukin 15 Mus musculus 166-171 11815609-4 2002 In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15. Cysteine 31-34 interleukin 15 Mus musculus 166-171 11815609-4 2002 In addition, Tyr-103, Cys-161, Cys-210, and Cys-211, previously identified to contribute to binding IL-2 and IL-7, were also found to be involved in binding IL-4 and IL-15. Cysteine 31-34 interleukin 15 Mus musculus 166-171 11929995-2 2002 Here we report that cysteine homologs of SelR are present in all organisms except certain parasites and hyperthermophiles, and this pattern of occurrence closely matches that of only one protein, peptide methionine sulfoxide reductase (MsrA). Cysteine 20-28 methionine sulfoxide reductase A Homo sapiens 204-234 11929995-2 2002 Here we report that cysteine homologs of SelR are present in all organisms except certain parasites and hyperthermophiles, and this pattern of occurrence closely matches that of only one protein, peptide methionine sulfoxide reductase (MsrA). Cysteine 20-28 methionine sulfoxide reductase A Homo sapiens 236-240 12075625-11 2002 The findings are compatible with the notions that (i) GGT-catalyzed transpeptidation was largely responsible for the growth advantage of M22 cells at limiting cysteine concentration, and for their high GSH content via the formation of GGC from a gamma-glutamyl donor (glutamine) and cyst(e)ine, and (ii) aminopeptidase/dipeptidase activity is rate-limiting in GSH repletion when GSH or CG serve as cysteine sources. Cysteine 398-406 gamma-glutamylcyclotransferase Homo sapiens 235-238 11985581-10 2002 Purified ORF6 was able to catalyse the reversible transfer of an acetyl group from N-acetylornithine to glutamate, but not the formation of N-acetylglutamate from glutamate and acetyl-coenzyme A, nor (detectably) the hydrolysis of N-acetylornithine. Cysteine 65-71 hypothetical protein Escherichia coli 9-13 11854028-1 2002 CD163 is a highly expressed macrophage membrane protein belonging to the scavenger receptor cysteine rich (SRCR) domain family. Cysteine 92-100 CD163 molecule Homo sapiens 0-5 11463334-0 2001 Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Cysteine 0-8 synaptosome associated protein 25 Rattus norvegicus 21-28 11463334-3 2001 Whereas syntaxin 1A and VAMP are tethered to the membrane by a C-terminal transmembrane domain, SNAP-25 has been suggested to be anchored to the membrane via four palmitoylated cysteine residues. Cysteine 177-185 synaptosome associated protein 25 Rattus norvegicus 96-103 11463334-4 2001 We demonstrate that the cysteine residues of SNAP-25 are not required for membrane localization when syntaxin 1A is present. Cysteine 24-32 synaptosome associated protein 25 Rattus norvegicus 45-52 11502828-9 2001 Sequence analysis of the GH receptor gene revealed a heterozygous mutation resulting in an Arg to Cys change (R161C) in exon 6 in only 1 patient, who had normal GH receptor responsiveness. Cysteine 98-101 growth hormone receptor Homo sapiens 25-36 11502838-6 2001 The secretion of adrenomedullin by JAr cells cultured in medium containing [35S]cysteine-[35S]methionine was determined by immunoprecipitation followed by PAGE. Cysteine 80-88 adrenomedullin Homo sapiens 17-31 11358972-2 2001 Dfp proteins, LanD proteins (for example EpiD, which is involved in epidermin biosynthesis), and the salt tolerance protein AtHAL3a from Arabidopsis thaliana are homooligomeric flavin-containing Cys decarboxylases (HFCD protein family). Cysteine 195-198 HAL3-like protein A Arabidopsis thaliana 124-130 11371572-7 2001 Homocysteine, but not cysteine, attenuated NO"s inhibition of purine synthesis, providing further evidence that NO was acting through methionine synthase inhibition. Cysteine 4-12 5-methyltetrahydrofolate-homocysteine methyltransferase Homo sapiens 134-153 11356856-6 2001 Internalization of these variant receptors was dependent on the catalytic cysteine residue of Rsp5p and on ubiquitin-conjugating enzymes that bind Rsp5p. Cysteine 74-82 NEDD4 like E3 ubiquitin protein ligase Homo sapiens 94-99 11425309-3 2001 Eotaxin-3 is monomeric under the conditions in this study and consists of an unstructured N-terminus before the first two conserved cysteine residues, an irregularly structured N-loop following the second conserved cysteine, a single turn of 3(10)-helix, a three-stranded antiparallel beta-sheet, an alpha-helix, and an unstructured C-terminal tail. Cysteine 132-140 C-C motif chemokine ligand 26 Homo sapiens 0-9 11425309-3 2001 Eotaxin-3 is monomeric under the conditions in this study and consists of an unstructured N-terminus before the first two conserved cysteine residues, an irregularly structured N-loop following the second conserved cysteine, a single turn of 3(10)-helix, a three-stranded antiparallel beta-sheet, an alpha-helix, and an unstructured C-terminal tail. Cysteine 215-223 C-C motif chemokine ligand 26 Homo sapiens 0-9 11432880-4 2001 The formation of this aggregate in the presence of Cu2+ is dependent on the presence of S100A13 and is mediated by cysteine-independent interactions between S100A13 and either FGF1 or p40 Syt1. Cysteine 115-123 S100 calcium binding protein A13 Homo sapiens 157-164 11323418-11 2001 In conclusion, we found that palmitoylated cysteines play an important role in the intracellular trafficking of CCR5 and are likely necessary for efficient coupling of the receptor to part of its repertoire of signaling cascades. Cysteine 43-52 C-C motif chemokine receptor 5 Homo sapiens 112-116 11323424-1 2001 Multiple or pleiotropic drug resistance often occurs in the yeast Saccharomyces cerevisiae through genetic activation of the Cys(6)-Zn(II) transcription factors Pdr1p and Pdr3p. Cysteine 125-128 drug-responsive transcription factor PDR3 Saccharomyces cerevisiae S288C 171-176 11410600-5 2001 Surprisingly, the expression of S100A13 also results in the stress-induced release of a Cys-free FGF1 mutant, which is normally not released from NIH 3T3 cells in response to heat shock. Cysteine 88-91 S100 calcium binding protein A13 Mus musculus 32-39 11278730-1 2001 A group of 16-kDa proteins, synthesized and secreted by rat pancreatic acinar cells and composed of pancreatic stone protein (PSP/reg) and isoforms of pancreatitis-associated protein (PAP), show structural homologies, including conserved amino acid sequences, cysteine residues, and highly sensitive N-terminal trypsin cleavage sites, as well as conserved functional responses in conditions of pancreatic stress. Cysteine 260-268 regenerating family member 3 beta Rattus norvegicus 151-182 11278730-1 2001 A group of 16-kDa proteins, synthesized and secreted by rat pancreatic acinar cells and composed of pancreatic stone protein (PSP/reg) and isoforms of pancreatitis-associated protein (PAP), show structural homologies, including conserved amino acid sequences, cysteine residues, and highly sensitive N-terminal trypsin cleavage sites, as well as conserved functional responses in conditions of pancreatic stress. Cysteine 260-268 regenerating family member 3 beta Rattus norvegicus 184-187 11491651-2 2001 AP-2 contains seven cysteines, and its in vitro DNA binding activity is redox-sensitive. Cysteine 20-29 transcription factor AP-2 alpha Homo sapiens 0-4 11397717-7 2001 Addition of 200 micromol/L ascorbate or N-acetyl derivatives of cysteine or methionine completely prevented LCAT inactivation by LDL preincubated with </=200 micromol/L HOCl. Cysteine 64-72 lecithin-cholesterol acyltransferase Homo sapiens 108-112 11422390-8 2001 The positions of Cys were completely conserved in bovine ZPA and ZPB compared with counterparts of other mammalian species. Cysteine 17-20 zona pellucida glycoprotein 4, pseudogene Mus musculus 65-68 11398969-5 2001 Pig DAP10 has a conserved aspartic acid in the transmembrane domain, two cysteines in the extracellular domain, and a phophatidylinositol-3 kinase-binding site (YxxM) in the cytoplasmic region. Cysteine 73-82 hematopoietic cell signal transducer Sus scrofa 4-9 11098061-8 2001 Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains. Cysteine 86-95 Neutrophil migration (granulocyte glycoprotein) Homo sapiens 126-131 11098061-8 2001 Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains. Cysteine 133-136 Neutrophil migration (granulocyte glycoprotein) Homo sapiens 126-131 11098061-8 2001 Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains. Cysteine 140-143 Neutrophil migration (granulocyte glycoprotein) Homo sapiens 126-131 11098061-8 2001 Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains. Cysteine 140-143 Neutrophil migration (granulocyte glycoprotein) Homo sapiens 126-131 11098061-8 2001 Unlike granulocyte colony-stimulating factor receptor, the connectivities of the four cysteines in the NH2-terminal domain of gp130 (Cys(6)-Cys(32) and Cys(26)-Cys(81)) are consistent with known superfamily of Ig-like domains. Cysteine 140-143 Neutrophil migration (granulocyte glycoprotein) Homo sapiens 126-131 11428461-6 2001 Apart from a replacement 298 Cys --> Tyr, rhoB-crystallin possesses all amino acid residues thought to be required for catalytic activity of the aldose reductases. Cysteine 29-32 rho-related GTP-binding protein RhoB Ovis aries 45-49 11170581-3 2001 Free cysteine thiol groups of keratin extracted from chicken feathers were partially carboxymethylated with iodoacetic acid (25-76% cysteine modification). Cysteine 5-13 keratin Gallus gallus 30-37 11170581-3 2001 Free cysteine thiol groups of keratin extracted from chicken feathers were partially carboxymethylated with iodoacetic acid (25-76% cysteine modification). Cysteine 132-140 keratin Gallus gallus 30-37 11170581-10 2001 The influences of a higher amount of glycerol and of different storage conditions on the mechanical properties of films from keratin with a defined degree of cysteine modification were also investigated. Cysteine 158-166 keratin Gallus gallus 125-132 11136826-3 2001 After passive sensitization for 5 d with IgE in the presence of SCF, anti-IgE-stimulated hMCs elaborated minimal cys-LT (0.1 +/- 0.1 ng/10(6) hMCs) and abundant prostaglandin (PG)D(2) (16.2 +/- 10.3 ng/10(6) hMCs). Cysteine 113-116 Miles-Carpenter X-linked mental retardation syndrome Homo sapiens 89-93 11136826-4 2001 Priming of hMCs by interleukin (IL)-4 with SCF during passive sensitization enhanced their anti-IgE-dependent histamine exocytosis and increased their generation of both cys-LT (by 27-fold) and PGD(2) (by 2. Cysteine 170-173 Miles-Carpenter X-linked mental retardation syndrome Homo sapiens 11-15 11136826-4 2001 Priming of hMCs by interleukin (IL)-4 with SCF during passive sensitization enhanced their anti-IgE-dependent histamine exocytosis and increased their generation of both cys-LT (by 27-fold) and PGD(2) (by 2. Cysteine 170-173 KIT ligand Homo sapiens 43-46 11136826-6 2001 Although priming with IL-3 or IL-5 alone for 5 d with SCF minimally enhanced anti-IgE-mediated cys-LT generation, these cytokines induced further six- and fourfold increases, respectively, in IgE-dependent cys-LT generation when provided with IL-4 and SCF; this occurred without changes in PGD(2) generation or histamine exocytosis relative to hMCs primed with IL-4 alone. Cysteine 95-98 KIT ligand Homo sapiens 54-57 11865974-7 2001 Thus, the data indicate that HOCl-modified LDL inactivates cathepsin B by a chloramine-dependent mechanism, most likely via oxidation of the enzyme"s critical cysteine residue. Cysteine 159-167 cathepsin B Homo sapiens 59-70 11015194-2 2000 The affinity analogue 1alpha,25-(OH)(2)D(3)-3-bromoacetate exclusively labeled Cys-288 in the VDR-LBD. Cysteine 79-82 vitamin D receptor Homo sapiens 94-97 11024467-2 2000 The crystal structure of the S-glutathiolated CAIII from rat liver reveals covalent adducts on cysteines 183 and 188. Cysteine 95-104 carbonic anhydrase 3 Rattus norvegicus 46-51 11010904-5 2000 The assimilatory sulfate reduction pathway was redirected to overproduce cysteine, and excess cysteine was converted to sulfide by cysteine desulfhydrase. Cysteine 94-102 cystathionine gamma-lyase Homo sapiens 131-153 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. Cysteine 63-66 chorionic gonadotropin subunit beta 3 Homo sapiens 28-35 11005799-6 2000 The first three-dimensional structure of a member of the NAT family identifies a catalytic triad consisting of aspartate, histidine and cysteine proposed to form the activation mechanism. Cysteine 136-144 bromodomain containing 2 Homo sapiens 57-60 11004203-0 2000 Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels. Cysteine 0-8 Charcot-Leyden crystal galectin Homo sapiens 52-55 11004203-0 2000 Cysteine modification of a putative pore residue in ClC-0: implication for the pore stoichiometry of ClC chloride channels. Cysteine 0-8 Charcot-Leyden crystal galectin Homo sapiens 101-104 11004203-4 2000 The double-barrel model proposed for ClC-0 was recently challenged by a one-pore model partly based on experiments with ClC-1 exploiting cysteine mutagenesis followed by modification with methanethiosulfonate (MTS) reagents. Cysteine 137-145 chloride voltage-gated channel 1 Homo sapiens 120-125 11034394-5 2000 Single alanine substitutions at positions A16 (Leu), A11 (Cys), B8 (Gly), and B15 (Leu) that are predicted to alter the core structure or chain folding vary widely in their impact on Ab binding. Cysteine 58-61 selectin L Rattus norvegicus 53-56 11029694-5 2000 The ma-l and hxB genes encode highly similar proteins containing domains common to pyridoxal phosphate-dependent cysteine transulphurases, including the cofactor binding site and a conserved cysteine, which is the putative sulphur donor. Cysteine 113-121 tenascin C Homo sapiens 13-16 11029694-5 2000 The ma-l and hxB genes encode highly similar proteins containing domains common to pyridoxal phosphate-dependent cysteine transulphurases, including the cofactor binding site and a conserved cysteine, which is the putative sulphur donor. Cysteine 191-199 tenascin C Homo sapiens 13-16 11027512-0 2000 Alteration of rat dipeptidyl peptidase III by site-directed mutagenesis: cysteine(176) is a regulatory residue for the enzyme activity. Cysteine 73-81 dipeptidylpeptidase 3 Rattus norvegicus 18-42 11027512-7 2000 The results indicate that Cys(176) is essential for the regulation of DPP III activity. Cysteine 26-29 dipeptidylpeptidase 3 Rattus norvegicus 70-77 10993914-3 2000 The conserved cysteine-rich domain of the NH(2)-terminal regulatory domains of cRaf-1, as well as several select domains of the mammalian protein kinase C (PKC) isoforms alpha, delta, zeta, and mu, the Drosophila and yeast PKCs, were found to bind retinol with nanomolar affinity. Cysteine 14-22 TNF receptor associated factor 3 Homo sapiens 79-85 10874045-2 2000 This relatively low activity is accounted for the catalytic residue of cit-PHGPx, which was found to be cysteine and not the rare selenocysteine (Sec) present in animal enzymes. Cysteine 104-112 glutathione peroxidase 4 Sus scrofa 75-80 10874045-4 2000 By performing appropriate nucleotide substitutions into the gene encoding cit-PHGPx, we introduced bacterial-type SECIS elements that afforded the substitution of the catalytic Cys(41) by Sec, as established by mass spectrometry, while preserving the functional integrity of the peroxidase. Cysteine 177-180 glutathione peroxidase 4 Sus scrofa 78-83 10874045-5 2000 The recombinant enzyme, whose synthesis is selenium-dependent, displayed a 4-fold enhanced peroxidase activity as compared with the Cys-containing analog, thus confirming the higher catalytic power of Sec compared with Cys in cit-PHGPx active site. Cysteine 219-222 glutathione peroxidase 4 Sus scrofa 230-235 10893423-8 2000 These results suggest that Ser(32) in the GDSWG consensus sequence provides the catalytic nucleophile for the hydrolase activity of aiPLA(2), while Cys(47) in the PVCTTE consensus sequence is at the active site for peroxidase activity. Cysteine 148-151 peroxiredoxin 6 Bos taurus 132-140 10975851-8 2000 Uptake of cysteine or cystine, possible products of GGT activity, stayed the same or decreased during the respiratory burst. Cysteine 10-18 inactive glutathione hydrolase 2 Homo sapiens 52-55 10980553-0 2000 A heterozygous novel C253Y mutation in the highly conserved cysteine residues of ROM1 gene is the cause of retinitis pigmentosa in a Spanish family? Cysteine 60-68 retinal outer segment membrane protein 1 Homo sapiens 81-85 10942404-8 2000 Three of the point mutations, in 3 patients, resulted in FECH variants with 2 of the [2Fe-2S] cluster cysteines substituted with tyrosine, serine, and glycine (ie, C406Y, C406S, and C411G) and with undetectable enzymatic activity. Cysteine 102-111 ferrochelatase Homo sapiens 57-61 10908293-2 2000 In the beta(2)-adrenergic receptor the agonist binding site has previously been structurally and functionally exchanged with an activating metal-ion site located between AspIII:08-or a His residue introduced at this position in transmembrane domain (TM)-III-and a Cys residue substituted for AsnVII:06 in TM-VII. Cysteine 264-267 adrenoceptor beta 2 Homo sapiens 7-34 10811634-5 2000 We measured the rate of GroEL cysteine reactivity toward iodo[2-(14)C]acetic acid and found that the cysteines become more accessible during binding of a cysteine free mutant of HCA II. Cysteine 30-38 heat shock protein family D (Hsp60) member 1 Homo sapiens 24-29 10811634-5 2000 We measured the rate of GroEL cysteine reactivity toward iodo[2-(14)C]acetic acid and found that the cysteines become more accessible during binding of a cysteine free mutant of HCA II. Cysteine 101-110 heat shock protein family D (Hsp60) member 1 Homo sapiens 24-29 10811634-5 2000 We measured the rate of GroEL cysteine reactivity toward iodo[2-(14)C]acetic acid and found that the cysteines become more accessible during binding of a cysteine free mutant of HCA II. Cysteine 101-109 heat shock protein family D (Hsp60) member 1 Homo sapiens 24-29 10811634-6 2000 Spin labeling of GroEL with N-(1-oxyl-2,2,5, 5-tetramethyl-3-pyrrolidinyl)iodoacetamide revealed that this additional binding occurred because buried cysteine residues become accessible during HCA II binding. Cysteine 150-158 heat shock protein family D (Hsp60) member 1 Homo sapiens 17-22 10811634-8 2000 Furthermore, by producing cysteine-modified GroEL with the spin label N-(1-oxyl-2,2,5, 5-tetramethyl-3-pyrrolidinyl)iodoacetamide and the fluorescent label 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid, we detected increases in spin-label mobility and fluorescence intensity in GroEL upon HCA II binding. Cysteine 26-34 heat shock protein family D (Hsp60) member 1 Homo sapiens 44-49 10811634-8 2000 Furthermore, by producing cysteine-modified GroEL with the spin label N-(1-oxyl-2,2,5, 5-tetramethyl-3-pyrrolidinyl)iodoacetamide and the fluorescent label 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid, we detected increases in spin-label mobility and fluorescence intensity in GroEL upon HCA II binding. Cysteine 26-34 heat shock protein family D (Hsp60) member 1 Homo sapiens 297-302 10801823-1 2000 Ha-Ras is modified by isoprenoid on Cys(186) and by reversibly attached palmitates at Cys(181) and Cys(184). Cysteine 36-39 Harvey rat sarcoma virus oncogene Mus musculus 0-6 10801823-1 2000 Ha-Ras is modified by isoprenoid on Cys(186) and by reversibly attached palmitates at Cys(181) and Cys(184). Cysteine 86-89 Harvey rat sarcoma virus oncogene Mus musculus 0-6 10801823-1 2000 Ha-Ras is modified by isoprenoid on Cys(186) and by reversibly attached palmitates at Cys(181) and Cys(184). Cysteine 86-89 Harvey rat sarcoma virus oncogene Mus musculus 0-6 10801823-2 2000 Ha-Ras loses 90% of its transforming activity if Cys(181) and Cys(184) are changed to serines, implying that palmitates make important contributions to oncogenicity. Cysteine 49-52 Harvey rat sarcoma virus oncogene Mus musculus 0-6 10801823-2 2000 Ha-Ras loses 90% of its transforming activity if Cys(181) and Cys(184) are changed to serines, implying that palmitates make important contributions to oncogenicity. Cysteine 62-65 Harvey rat sarcoma virus oncogene Mus musculus 0-6 10859345-3 2000 The DNA-binding domain of CPP1 contains two similar Cys-rich domains with 9 and 10 Cys, respectively. Cysteine 52-55 cysteine-rich polycomb-like protein Glycine max 26-30 10859345-3 2000 The DNA-binding domain of CPP1 contains two similar Cys-rich domains with 9 and 10 Cys, respectively. Cysteine 83-86 cysteine-rich polycomb-like protein Glycine max 26-30 10859240-4 2000 Reduction and carboxymethylation of the cysteine residues abolished the inhibitor activity of both caltrin proteins. Cysteine 40-48 serine peptidase inhibitor, Kazal type 1-like Rattus norvegicus 99-106 10919356-1 2000 The contribution of mannose 6-phosphate (Man 6-P)-dependent and -independent systems to lysosomal targeting of cathepsin H, a lysosomal cysteine protease, was investigated by metabolic labeling with [32P]phosphate and [35S]methionine/cysteine in primary cultures of rat hepatocytes. Cysteine 136-144 cathepsin H Homo sapiens 111-122 11001093-0 2000 An MCD spectroscopic study of the molybdenum active site in sulfite oxidase: insight into the role of coordinated cysteine. Cysteine 114-122 sulfite oxidase Homo sapiens 60-75 10858280-10 2000 The data were best interpreted by a dinuclear mu(2)()-bridged cluster with doubly bridging cysteine ligands similar to the cluster proposed to exist in the cytochrome c oxidase chaperone COX17. Cysteine 91-99 cytochrome c oxidase copper chaperone COX17 Homo sapiens 187-192 10858295-2 2000 Human and Schizosaccharomyces pombe forms of ferrochelatase contain a [2Fe-2S] cluster with three of the four coordinating cysteine ligands located within the 30 carboxyl-terminal residues. Cysteine 123-131 ferrochelatase Homo sapiens 45-59 10779372-8 2000 A new proposal is also made for the amino acid sequence of the pyrimidine-binding domain, including Cys(671), of DPD in the human and other species. Cysteine 100-103 dihydropyrimidine dehydrogenase Homo sapiens 113-116 10849350-0 2000 Expression of a bacterial serine acetyltransferase in transgenic potato plants leads to increased levels of cysteine and glutathione. Cysteine 108-116 streptothricin acetyltransferase Escherichia coli 26-50 10849350-1 2000 The coding sequence of the wild-type, cys-sensitive, cysE gene from Escherichia coli, which encodes an enzyme of the cysteine biosynthetic pathway, namely serine acetyltransferase (SAT, EC 2.3.1. Cysteine 38-41 streptothricin acetyltransferase Escherichia coli 155-179 10849350-1 2000 The coding sequence of the wild-type, cys-sensitive, cysE gene from Escherichia coli, which encodes an enzyme of the cysteine biosynthetic pathway, namely serine acetyltransferase (SAT, EC 2.3.1. Cysteine 38-41 streptothricin acetyltransferase Escherichia coli 181-184 10849350-1 2000 The coding sequence of the wild-type, cys-sensitive, cysE gene from Escherichia coli, which encodes an enzyme of the cysteine biosynthetic pathway, namely serine acetyltransferase (SAT, EC 2.3.1. Cysteine 117-125 streptothricin acetyltransferase Escherichia coli 155-179 10849350-1 2000 The coding sequence of the wild-type, cys-sensitive, cysE gene from Escherichia coli, which encodes an enzyme of the cysteine biosynthetic pathway, namely serine acetyltransferase (SAT, EC 2.3.1. Cysteine 117-125 streptothricin acetyltransferase Escherichia coli 181-184 10849350-12 2000 In conclusion, the results presented here demonstrate the importance of SAT in plant cysteine biosynthesis and show that production of cysteine and related sulfur-containing compounds can be enhanced by metabolic engineering. Cysteine 85-93 streptothricin acetyltransferase Escherichia coli 72-75 10769129-7 2000 The A domain was found to activate and transfer to PCP1 and PCP2 not only the natural L-Cys but also S-2-aminobutyrate, L-beta-chloroalanine, and L-Ser, enabling testing of the substrate specificity of the Cy domain. Cysteine 86-91 Purkinje cell protein 2 Homo sapiens 60-64 10769129-7 2000 The A domain was found to activate and transfer to PCP1 and PCP2 not only the natural L-Cys but also S-2-aminobutyrate, L-beta-chloroalanine, and L-Ser, enabling testing of the substrate specificity of the Cy domain. Cysteine 88-90 Purkinje cell protein 2 Homo sapiens 60-64 10781813-4 2000 DroVav preserves the unique, complex structure of hVav proteins, including the "calponin homology", dbl homology, pleckstrin homology; SH2 and SH3 domains in addition to regions that are acidic rich, proline rich and cysteine rich. Cysteine 217-225 Vav guanine nucleotide exchange factor Drosophila melanogaster 0-6 10727430-1 2000 Cystathionine gamma-lyase (CGL) is the last enzyme of the trans-sulphuration pathway, which converts methionine into cysteine. Cysteine 117-125 cystathionine gamma-lyase Homo sapiens 0-25 10727430-1 2000 Cystathionine gamma-lyase (CGL) is the last enzyme of the trans-sulphuration pathway, which converts methionine into cysteine. Cysteine 117-125 cystathionine gamma-lyase Homo sapiens 27-30 10727430-5 2000 In human liver samples, CGL activity was only detected in adult tissue (68+/-9 nmol of cysteine/h per mg of protein), whereas activity in fetal, premature and full-term neonatal liver tissue was undetectable. Cysteine 87-95 cystathionine gamma-lyase Homo sapiens 24-27 10733681-0 2000 arg-cys substitution at codon 1246 of the human myosin Va gene is not associated with Griscelli syndrome. Cysteine 4-7 myosin VA Homo sapiens 48-57 10821189-4 2000 The transcription of MET14 and MET25 could not be repressed by methionine in strains in which either STR4 (which encodes cystathionine beta-synthase) or STR1 (cystathionine gamma-lyase) was disrupted, whereas the repression was independent of GSH1 (which encodes the enzyme responsible for the first step in glutathione biosynthesis from cysteine). Cysteine 338-346 adenylyl-sulfate kinase Saccharomyces cerevisiae S288C 21-26 10759156-1 2000 Serum transthyretin has several isoforms, most of which are caused by disulfide linkage with cysteine residue at position 10. Cysteine 93-101 transthyretin Homo sapiens 6-19 10722684-4 2000 Results of experiments using CRP labeled at Cys-178 with 1,5-I-AENS indicate change in conformation of the helix-turn-helix, occurring after the formation of CRP-cAMP(2) complex, i.e. after saturation of the high affinity sites. Cysteine 44-47 catabolite gene activator protein Escherichia coli 29-32 10722684-4 2000 Results of experiments using CRP labeled at Cys-178 with 1,5-I-AENS indicate change in conformation of the helix-turn-helix, occurring after the formation of CRP-cAMP(2) complex, i.e. after saturation of the high affinity sites. Cysteine 44-47 catabolite gene activator protein Escherichia coli 158-161 10700381-0 2000 Importance of cysteine residues for the stability and catalytic activity of human pancreatic beta cell glucokinase. Cysteine 14-22 glucokinase Homo sapiens 103-114 10700381-8 2000 Only the Cys 230 mutant showed kinetic characteristics comparable to those of wild-type glucokinase. Cysteine 9-12 glucokinase Homo sapiens 88-99 10700381-11 2000 Conclusively our data demonstrate the functional significance of the cysteine residues of beta cell glucokinase for both structural instability of the enzyme and catalytic function. Cysteine 69-77 glucokinase Homo sapiens 100-111 10700381-12 2000 Knowledge of sensitive cysteine targets may help to develop strategies that improve glucokinase enzyme function under conditions of oxidative stress. Cysteine 23-31 glucokinase Homo sapiens 84-95 10706739-8 2000 Epitope mapping on purified CCR5-specific Abs showed that these Abs recognize a conformational epitope in the first cysteine loop of CCR5 (aa 89-102). Cysteine 116-124 C-C motif chemokine receptor 5 Homo sapiens 28-32 10706739-8 2000 Epitope mapping on purified CCR5-specific Abs showed that these Abs recognize a conformational epitope in the first cysteine loop of CCR5 (aa 89-102). Cysteine 116-124 C-C motif chemokine receptor 5 Homo sapiens 133-137 10688911-7 2000 The NADPH-disulfide oxidoreductase activity of the purified Cys(497)/Cys(498) mutant enzyme was 6% or 11% of that of wild-type rat liver TrxR1 with 5, 5"-dithiobis(2-nitrobenzoic acid) or TrxS(2), respectively, as substrate. Cysteine 60-63 thioredoxin reductase 1 Homo sapiens 137-142 10688911-7 2000 The NADPH-disulfide oxidoreductase activity of the purified Cys(497)/Cys(498) mutant enzyme was 6% or 11% of that of wild-type rat liver TrxR1 with 5, 5"-dithiobis(2-nitrobenzoic acid) or TrxS(2), respectively, as substrate. Cysteine 69-72 thioredoxin reductase 1 Homo sapiens 137-142 10704196-0 2000 Cysteine scanning mutagenesis of helices 2 and 7 in GLUT1 identifies an exofacial cleft in both transmembrane segments. Cysteine 0-8 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 52-57 10704196-1 2000 Cysteine scanning mutagenesis in conjunction with site-directed chemical modification of sulfhydryl groups by p-chloromercuribenzenesulfonate (pCMBS) or N-ethylmaleimide (NEM) was applied to putative transmembrane segments (TM) 2 and 7 of the cysteine-less glucose transporter GLUT1. Cysteine 0-8 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 277-282 10704196-5 2000 Characteristic for helix 7, three glutamine residues (Q279, Q282, and Q283) played an important role in transport activity of Cys-less GLUT1 because an individual replacement with cysteine reduced their transport rates by about 80%. Cysteine 126-129 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 135-140 10704196-5 2000 Characteristic for helix 7, three glutamine residues (Q279, Q282, and Q283) played an important role in transport activity of Cys-less GLUT1 because an individual replacement with cysteine reduced their transport rates by about 80%. Cysteine 180-188 solute carrier family 2 (facilitated glucose transporter), member 1 L homeolog Xenopus laevis 135-140 10677561-4 2000 This mutation substitutes Tyr for 74 Cys in the NPII moiety. Cysteine 37-40 neuronal pentraxin 2 Homo sapiens 48-52 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. Cysteine 152-160 neuronal pentraxin 2 Homo sapiens 0-4 10688888-13 2000 The aggregation profiles of HGD and R14C are consistent with our homology modeling studies that reveal that R14C contains two exposed cysteine residues, whereas HGD has only one. Cysteine 134-142 homogentisate 1,2-dioxygenase Homo sapiens 28-31 10774743-3 2000 Incubation of GDH with increasing concentration of o-phthalaldehyde resulted in a progressive decrease in enzyme activity, suggesting that the o-phthalaldehyde-modified lysine or cysteine is directly involved in catalysis. Cysteine 179-187 Glu/Leu/Phe/Val dehydrogenase Saccharolobus solfataricus 14-17 10679309-1 2000 Lymphotactin is unique among chemokines in that it contains only two of four conserved cysteines and may possess a structure less constrained than other chemokines. Cysteine 87-96 X-C motif chemokine ligand 1 Homo sapiens 0-12 10686340-4 2000 As a first step, the conserved cysteine (C) and histidine (H) residues were targeted for site-directed mutagenesis as potential amino acid residues involved in the N-acetylation reaction of AA-NAT. Cysteine 31-39 aralkylamine N-acetyltransferase Homo sapiens 190-196 10671517-6 2000 ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. Cysteine 71-74 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 0-6 10671517-6 2000 ERO1-L is no longer functional when either one of the highly conserved Cys-394 or Cys-397 is mutated. Cysteine 82-85 endoplasmic reticulum oxidoreductase 1 alpha Homo sapiens 0-6 10671518-0 2000 A dynactin subunit with a highly conserved cysteine-rich motif interacts directly with Arp1. Cysteine 43-51 actin related protein 1A Homo sapiens 87-91 10675660-4 2000 After incubation with the antibody, the samples were passed through a 1000 kDa cut off centrifugal concentrator to retain the antibody, thereafter, the filtrate was analyzed by ESI-MS. Several forms of normal and variant TTR were detected in the serum samples: unconjugated TTR, cysteine and cysteine-glycine conjugated TTR. Cysteine 279-287 transthyretin Homo sapiens 221-224 10758485-7 2000 The results indicated that the interaction between Ara4 and AtGDI1 depends on the conserved C-terminal Cys-motif and Thr44 in the effector domain of Ara4. Cysteine 103-106 P-loop containing nucleoside triphosphate hydrolases superfamily protein Arabidopsis thaliana 51-55 10758485-7 2000 The results indicated that the interaction between Ara4 and AtGDI1 depends on the conserved C-terminal Cys-motif and Thr44 in the effector domain of Ara4. Cysteine 103-106 guanosine nucleotide diphosphate dissociation inhibitor 1 Arabidopsis thaliana 60-66 10631324-2 2000 The N-half of the deduced amino acid sequence of 432 amino acids of CROP contains cysteine/histidine motifs and leucine zipper-like repeats. Cysteine 82-90 LUC7 like 3 pre-mRNA splicing factor Homo sapiens 68-72 10625482-4 2000 In the troponin-tropomyosin (Tn-Tm) complex, the AEDANS labels on both Cys-96 and Cys-117 were less accessible to solvent and less flexible in the presence of Ca(2+), reflecting closer interactions with TnC under these conditions. Cysteine 71-74 tenascin C Homo sapiens 203-206 10625482-4 2000 In the troponin-tropomyosin (Tn-Tm) complex, the AEDANS labels on both Cys-96 and Cys-117 were less accessible to solvent and less flexible in the presence of Ca(2+), reflecting closer interactions with TnC under these conditions. Cysteine 82-85 tenascin C Homo sapiens 203-206 10617656-10 2000 Furthermore, tyrosine-phosphorylated STAT5 associates with the substrate-trapping mutant (Cys --> Ser) of SHP-2 but not SHP-1. Cysteine 90-93 protein tyrosine phosphatase non-receptor type 11 Homo sapiens 109-114 10625533-4 2000 Current data indicate that the cysteine-rich domain of secreted Frzb proteins can bind Wnt proteins, suggesting the possibility that Frzbs compete with membrane-bound Frizzled for Wnt binding and consequently act as competitive inhibitors of Wnt signaling. Cysteine 31-39 frizzled related protein Gallus gallus 64-68 11092735-4 2000 The X. laevis DNase I polypeptide was larger than any other known vertebrate DNase I, containing a unique Cys-rich stretch of 68 or 70 amino acid residues at the carboxyl terminus, and it had less well conserved binding sites for the Ca2+, G-actin and DNA, and two DNase I signature motifs. Cysteine 106-109 DNase I Xenopus laevis 14-21 10719747-0 2000 Augmentative effects of L-cysteine and methylmethionine sulfonium chloride on mucin secretion in rabbit gastric mucous cells. Cysteine 24-34 solute carrier family 13 member 2 Rattus norvegicus 78-83 10719747-1 2000 BACKGROUND: Our previous study showed that L-cysteine (Cys) and methylmethionine sulfonium chloride (MMSC) inhibited ethanol-induced gastric mucosal damage and increased the amount of surface mucin in rats. Cysteine 43-53 solute carrier family 13 member 2 Rattus norvegicus 192-197 10719747-1 2000 BACKGROUND: Our previous study showed that L-cysteine (Cys) and methylmethionine sulfonium chloride (MMSC) inhibited ethanol-induced gastric mucosal damage and increased the amount of surface mucin in rats. Cysteine 55-58 solute carrier family 13 member 2 Rattus norvegicus 192-197 10719747-2 2000 This study examined whether Cys and MMSC augmented mucin secretion and changed distribution of mucin vesicles ultrastructurally in mucous cells by using primary cultured mucous cells from rabbit glandular stomach. Cysteine 28-31 solute carrier family 13 member 2 Rattus norvegicus 51-56 10719747-2 2000 This study examined whether Cys and MMSC augmented mucin secretion and changed distribution of mucin vesicles ultrastructurally in mucous cells by using primary cultured mucous cells from rabbit glandular stomach. Cysteine 28-31 solute carrier family 13 member 2 Rattus norvegicus 95-100 10719747-8 2000 RESULTS: L-Cysteine and MMSC increased mucin secretion and decreased cellular mucin content. Cysteine 9-19 solute carrier family 13 member 2 Rattus norvegicus 39-44 10719747-8 2000 RESULTS: L-Cysteine and MMSC increased mucin secretion and decreased cellular mucin content. Cysteine 9-19 solute carrier family 13 member 2 Rattus norvegicus 78-83 10719747-13 2000 CONCLUSIONS: The present findings indicate that the increase in mucin secretion by Cys and MMSC was not mediated through the cAMP or Ca2+ signal transduction pathway, but might occur through non-receptor-mediated mechanisms. Cysteine 83-86 solute carrier family 13 member 2 Rattus norvegicus 64-69 10625572-1 2000 The anti-adhesive extracellular matrix protein SPARC (secreted protein and rich in cysteine; osteonectin or BM-40) has been implicated in the regulation of matrix turnover, cell migration, and proliferation. Cysteine 83-91 secreted protein acidic and cysteine rich Rattus norvegicus 47-52 10625572-1 2000 The anti-adhesive extracellular matrix protein SPARC (secreted protein and rich in cysteine; osteonectin or BM-40) has been implicated in the regulation of matrix turnover, cell migration, and proliferation. Cysteine 83-91 secreted protein acidic and cysteine rich Rattus norvegicus 93-104 10625572-1 2000 The anti-adhesive extracellular matrix protein SPARC (secreted protein and rich in cysteine; osteonectin or BM-40) has been implicated in the regulation of matrix turnover, cell migration, and proliferation. Cysteine 83-91 secreted protein acidic and cysteine rich Rattus norvegicus 108-113 11041367-11 2000 Because of the absence of TRP-1 and TRP-2 in pheomelanogenesis, it may be suggested that tyrosinase is involved in lysosomal degradation after forming dopaquinone, to which the cysteine present in the lysosomal granule binds to form cysteinyldopas that will then be auto-oxidized to become pheomelanin. Cysteine 177-185 tyrosinase Homo sapiens 89-99 10578173-1 1999 Caspase stands for cysteine-dependent aspartate specific protease, and is a term coined to define proteases related to interleukin 1beta converting enzyme and CED-3.1 Thus their enzymatic properties are governed by a dominant specificity for substrates containing Asp, and by the use of a Cys side-chain for catalyzing peptide bond cleavage. Cysteine 19-27 intraflagellar transport 43 Homo sapiens 159-164 10578173-1 1999 Caspase stands for cysteine-dependent aspartate specific protease, and is a term coined to define proteases related to interleukin 1beta converting enzyme and CED-3.1 Thus their enzymatic properties are governed by a dominant specificity for substrates containing Asp, and by the use of a Cys side-chain for catalyzing peptide bond cleavage. Cysteine 289-292 intraflagellar transport 43 Homo sapiens 159-164 10508407-1 1999 Previous studies [Yu, H., Kono, M., and Oprian, D. D. (1999) Biochemistry 38, xxxx-xxxx] using split receptors and disulfide cross-linking have shown that native cysteines 140 and 222 on the cytoplasmic side of transmembrane segments (TM) 3 and 5 of rhodopsin, respectively, can cross-link to each other upon treatment with the oxidant Cu(phen)3(2+). Cysteine 162-171 tropomyosin 3 Homo sapiens 211-246 10473612-9 1999 The cysteine-rich amino-terminal domain of TN-R expressed as a recombinant peptide, termed EGF-L, appears to be responsible for the repellent effect on beta subunit-expressing cells. Cysteine 4-12 epidermal growth factor L homeolog Xenopus laevis 91-96 10823210-2 1999 [reaction: see text] Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). Cysteine 82-90 protein farnesyltransferase Saccharomyces cerevisiae S288C 21-48 10823210-2 1999 [reaction: see text] Protein farnesyltransferase (PFTase) catalyzes alkylation of cysteine residues by farnesyl diphosphate (FPP). Cysteine 82-90 protein farnesyltransferase Saccharomyces cerevisiae S288C 50-56 10463938-1 1999 Redox control of the transcription factor c-Jun maps to a single cysteine in its DNA binding domain. Cysteine 65-73 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 42-47 10463938-5 1999 We provide evidence that S-glutathiolation, which is specifically targeted to the cysteine residue located in the DNA binding site of the protein, may account for the reversible redox regulation of c-Jun DNA binding. Cysteine 82-90 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 198-203 10463938-7 1999 Given the structural similarities between the positively charged cysteine-containing DNA binding motif of c-Jun and the DNA binding site of related oxidant-sensitive transcriptional activators, the unprecedented phenomenon of redox-triggered S-thiolation of a transcription factor described in this report suggests a novel role for protein thiolation in the redox control of transcription. Cysteine 65-73 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 106-111 10473645-4 1999 The Sir2 and Hst proteins share a core domain, which includes two diagnostic sequence motifs of unknown function as well as four cysteines of a putative zinc finger. Cysteine 129-138 sirtuin 1 Homo sapiens 4-8 10473645-4 1999 The Sir2 and Hst proteins share a core domain, which includes two diagnostic sequence motifs of unknown function as well as four cysteines of a putative zinc finger. Cysteine 129-138 sulfotransferase family 2A member 1 Homo sapiens 13-16 10455175-6 1999 The human mature sPLA(2) protein consists of 125 amino acids (M(r) = 14,500) preceded by a 20-residue prepeptide and is most similar to group IIA sPLA(2) with respect to the number and positions of cysteine residues as well as overall identity (48%). Cysteine 198-206 phospholipase A2 group IIA Homo sapiens 17-23 10466928-1 1999 Secreted protein, acidic, rich in cysteine (SPARC) is a Ca2+-binding, counter-adhesive, extracellular glycoprotein associated with major morphogenic events and tissue remodeling in vertebrates. Cysteine 34-42 secreted protein, acidic, cysteine-rich (osteonectin) L homeolog Xenopus laevis 44-49 10633885-6 1999 Type I collagen (Col I) and SPARC (secreted protein, acidic and rich in cysteine) mRNAs were expressed at the confluent stage, but decreased during the mineralization stage. Cysteine 72-80 secreted protein acidic and cysteine rich Rattus norvegicus 28-33 10431244-4 1999 The frameshift mutation 1615delG in FANCA was compensated by two additional single base-pair deletions (1637delA and 1641delT); another FANCA frameshift mutation, 3559insG, was compensated by 3580insCGCTG; and a missense mutation in FANCC(1749T-->G, Leu496Arg) was altered by 1748C-->T, creating a cysteine codon. Cysteine 304-312 FA complementation group A Homo sapiens 36-41 10431244-4 1999 The frameshift mutation 1615delG in FANCA was compensated by two additional single base-pair deletions (1637delA and 1641delT); another FANCA frameshift mutation, 3559insG, was compensated by 3580insCGCTG; and a missense mutation in FANCC(1749T-->G, Leu496Arg) was altered by 1748C-->T, creating a cysteine codon. Cysteine 304-312 FA complementation group A Homo sapiens 136-141 10400914-6 1999 In contrast, MTS-LX-BZ modification of heart and mutant rSkM1 channels, containing a pore cysteine at the equivalent location as cardiac Na+ channels (ie, Y401C), persisted after drug washout unless treated with DTT, which suggests anchoring to the pore via a disulfide bond. Cysteine 90-98 sodium voltage-gated channel alpha subunit 4 Rattus norvegicus 56-61 10383387-0 1999 Extracellular cysteines of CCR5 are required for chemokine binding, but dispensable for HIV-1 coreceptor activity. Cysteine 14-23 C-C motif chemokine receptor 5 Homo sapiens 27-31 10383387-4 1999 Using site-directed mutagenesis, we mutated the four extracellular cysteines of CCR5 singly or in combination to investigate their role in maintaining the structural conformation of the receptor, its ligand binding and signal transduction properties, and its ability to function as a viral coreceptor. Cysteine 67-76 C-C motif chemokine receptor 5 Homo sapiens 80-84 10383387-7 1999 The effects of the mutations on receptor expression and conformation were partially temperature-sensitive, with partial restoration of receptor expression and conformation achieved by incubating cells at 32 degrees C. All cysteine mutants were unable to bind detectable levels of MIP-1beta, and did not respond functionally to CCR5 agonists. Cysteine 222-230 C-C motif chemokine receptor 5 Homo sapiens 327-331 10383420-4 1999 As for mGIIA sPLA2, the novel sPLA2 is made up of 125 amino acids with 14 cysteines, is basic (pI = 8.71) and its gene has been mapped to mouse chromosome 4. Cysteine 74-83 phospholipase A2, group IIA (platelets, synovial fluid) Mus musculus 30-35 10447761-6 1999 The second hypothesis was that an additional Cys residue near the C terminus of the mu-chain is responsible for the multiple covalent structures seen in IgM of the channel catfish. Cysteine 45-48 immunoglobulin heavy constant mu Mus musculus 153-156 10364215-6 1999 These studies utilize fluorescent derivatives of cysteine variants of alpha1-antichymotrypsin at the P11 and P13 residues. Cysteine 49-57 serpin family A member 3 Homo sapiens 70-93 10424456-6 1999 We demonstrate that the normal TTR monomer exists in different forms of variable stability and/or charge due to binding of sulfhydryls from plasma to the unique cysteine at position 10 of the primary structure as well as due to modification by treatment with an oxidant. Cysteine 161-169 transthyretin Homo sapiens 31-34 10430018-0 1999 Two distinct domains in hsc70 are essential for the interaction with the synaptic vesicle cysteine string protein. Cysteine 90-98 heat shock protein family A (Hsp70) member 8 Homo sapiens 24-29 10330172-3 1999 We show here that TTP binding to the TNF-alpha ARE is dependent upon the integrity of both zinc fingers, since mutation of a single cysteine residue in either zinc finger to arginine severely attenuated the binding of TTP to the TNF-alpha ARE. Cysteine 132-140 zinc finger protein 36 Mus musculus 18-21 10330172-3 1999 We show here that TTP binding to the TNF-alpha ARE is dependent upon the integrity of both zinc fingers, since mutation of a single cysteine residue in either zinc finger to arginine severely attenuated the binding of TTP to the TNF-alpha ARE. Cysteine 132-140 zinc finger protein 36 Mus musculus 218-221 10336489-2 1999 We show that in the presence of the physiological sulfhydryl glutathione nitric oxide modifies the two cysteine residues contained in the DNA binding module of c-Jun in a selective and distinct way. Cysteine 103-111 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 160-165 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. Cysteine 90-98 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 138-143 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. Cysteine 271-279 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 138-143 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 10-18 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 91-99 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 109-112 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 117-120 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 117-120 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 117-120 KIT ligand Homo sapiens 47-50 10371217-2 1999 A surface cysteine-free mutant (abbreviated as SCF) was prepared in which the five surface cysteine residues Cys-58, Cys-85, Cys-136, Cys-148 and Cys-334 were changed to alanines. Cysteine 117-120 KIT ligand Homo sapiens 47-50 10371217-5 1999 The coupling of a redox-active label, N-ferrocenylmaleimide, to the single surface cysteine mutant SCF-K344C, and the electrochemistry of this modified mutant are also described. Cysteine 83-91 KIT ligand Homo sapiens 99-102 10329659-1 1999 The membrane topography of the yeast vacuolar proton-translocating ATPase a subunit (Vph1p) has been investigated using cysteine-scanning mutagenesis. Cysteine 120-128 H(+)-transporting V0 sector ATPase subunit a Saccharomyces cerevisiae S288C 85-90 10329659-2 1999 A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity. Cysteine 2-5 H(+)-transporting V0 sector ATPase subunit a Saccharomyces cerevisiae S288C 19-24 10329659-2 1999 A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity. Cysteine 54-63 H(+)-transporting V0 sector ATPase subunit a Saccharomyces cerevisiae S288C 19-24 10329400-3 1999 We now report that like SNAP-25, SNAP-23 is palmitoylated in vivo on one or more cysteine residues present in a central "palmitoylation domain." Cysteine 81-89 synaptosome associated protein 23 Homo sapiens 33-40 10384960-0 1999 Regulation of cathepsin B activity by cysteine and related thiols. Cysteine 38-46 cathepsin B Homo sapiens 14-25 10384960-1 1999 We studied the mode of regulation of the activity of mature cathepsin B (CB) by L-cysteine and some related thiols. Cysteine 80-90 cathepsin B Homo sapiens 60-71 10384960-1 1999 We studied the mode of regulation of the activity of mature cathepsin B (CB) by L-cysteine and some related thiols. Cysteine 80-90 cathepsin B Homo sapiens 73-75 10384960-2 1999 The activity of CB with Z-Arg-Arg-NHMec as substrate was gradually inhibited over a range of increasing concentration of Cys, Cys methyl ester (CysOMe), Cys ethyl ester (CysOEt), N-acetyl-Cys (N-AcCys) and 3-mercaptopropionic acid. Cysteine 121-124 cathepsin B Homo sapiens 16-18 10384960-3 1999 However, the inhibition of CB peaked at a definite value of [Cys], [CysOMe], [CysOEt] and [N-AcCys] and was gradually reversed over a range of higher concentrations of Cys and its esters. Cysteine 61-64 cathepsin B Homo sapiens 27-29 10384960-3 1999 However, the inhibition of CB peaked at a definite value of [Cys], [CysOMe], [CysOEt] and [N-AcCys] and was gradually reversed over a range of higher concentrations of Cys and its esters. Cysteine 68-71 cathepsin B Homo sapiens 27-29 10384960-9 1999 CB reacting in an environment of concurrently decreasing [RS-] and increasing [RSH], which was achieved by means of carboxylesterase-catalyzed deesterification of CysOEt to Cys, was progressively inhibited. Cysteine 163-166 cathepsin B Homo sapiens 0-2 10384960-10 1999 Cys and N-AcCys also inhibited the fragmentation of histone H4 by CB and their concentration-dependent inhibitory profiles were qualitatively similar to those observed with Z-Arg-Arg-NHMec. Cysteine 0-3 cathepsin B Homo sapiens 66-68 10384960-11 1999 Taken together, the results indicate that the RSH form of Cys and related thiols inhibits the activity of CB while the RS- form of these thiols counteracts or reverses the inhibitory action of the RSH form. Cysteine 58-61 cathepsin B Homo sapiens 106-108 10224164-9 1999 We, therefore, conclude that PL-OOH inhibited plasma LCAT activity by modifying the enzyme"s free cysteine and/or catalytic residues. Cysteine 98-106 lecithin-cholesterol acyltransferase Homo sapiens 53-57 9891083-0 1999 rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases. Cysteine 37-45 TXK tyrosine kinase Homo sapiens 0-3 9891083-0 1999 rlk/TXK encodes two forms of a novel cysteine string tyrosine kinase activated by Src family kinases. Cysteine 37-45 TXK tyrosine kinase Homo sapiens 4-7 9891083-2 1999 Unlike other members of this kinase family, Rlk lacks a pleckstrin homology (PH) domain near the amino terminus and instead contains a distinctive cysteine string motif. Cysteine 147-155 TXK tyrosine kinase Homo sapiens 44-47 9891083-7 1999 The cysteine string, therefore, is a critical determinant of both fatty acid modification and protein localization for the larger isoform of Rlk, suggesting that Rlk regulation is distinct from the other Btk family kinases. Cysteine 4-12 TXK tyrosine kinase Homo sapiens 141-144 9891083-7 1999 The cysteine string, therefore, is a critical determinant of both fatty acid modification and protein localization for the larger isoform of Rlk, suggesting that Rlk regulation is distinct from the other Btk family kinases. Cysteine 4-12 TXK tyrosine kinase Homo sapiens 162-165 9891083-7 1999 The cysteine string, therefore, is a critical determinant of both fatty acid modification and protein localization for the larger isoform of Rlk, suggesting that Rlk regulation is distinct from the other Btk family kinases. Cysteine 4-12 Bruton tyrosine kinase Homo sapiens 204-207 10216914-6 1999 Key features of mouse ZP3, including the number and location of cysteine and proline residues and N-linked glycosylation sites, were also conserved in the rat homologue. Cysteine 64-72 zona pellucida glycoprotein 3 Mus musculus 22-25 9886386-3 1999 Assuming that conformational changes induced by the posttranslational modifications are responsible for generation of bioactivity, we constructed cysteine mutants of human rGIF (rhGIF) in which cysteine at position 57, 60, or 81 was replaced with Ala, and the mutants were expressed in Escherichia coli. Cysteine 146-154 cobalamin binding intrinsic factor Rattus norvegicus 172-176 9892020-4 1999 Examination of the biological activity of the AGRP variants demonstrates that a truncated variant, human AGRP(87-132), a 46-amino acid variant based on the carboxyl-terminal cysteine-rich domain of AGRP, is equipotent to an 111-amino acid variant, mouse [Leu127Pro]AGRP (mature AGRP minus its signal sequence), in its ability to dose dependently inhibit alpha-MSH-generated cAMP generation at the cloned melanocortin receptors. Cysteine 174-182 agouti related neuropeptide Homo sapiens 105-109 9892020-4 1999 Examination of the biological activity of the AGRP variants demonstrates that a truncated variant, human AGRP(87-132), a 46-amino acid variant based on the carboxyl-terminal cysteine-rich domain of AGRP, is equipotent to an 111-amino acid variant, mouse [Leu127Pro]AGRP (mature AGRP minus its signal sequence), in its ability to dose dependently inhibit alpha-MSH-generated cAMP generation at the cloned melanocortin receptors. Cysteine 174-182 agouti related neuropeptide Homo sapiens 105-109 9922129-2 1998 We have located the membrane-docking surface on the Ca2+-activated C2 domain of cPLA2 by engineering a single cysteine substitution at 16 different locations widely distributed across the domain surface, in each case generating a unique attachment site for a fluorescein probe. Cysteine 110-118 phospholipase A2 group IVA Homo sapiens 80-85 9851830-9 1998 The remarkable reactivity of the critical thiol group in GAPDH (Cys-149) toward peroxynitrite, which is one order of magnitude higher than that of previously studied sulfhydryls, indicate that it may constitute a preferential intracellular target for peroxynitrite. Cysteine 64-67 glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus 57-62 9830017-0 1998 Isoform-dependent differences in feedback regulation and subcellular localization of serine acetyltransferase involved in cysteine biosynthesis from Arabidopsis thaliana. Cysteine 122-130 nuclear shuttle interacting Arabidopsis thaliana 92-109 9858711-14 1998 Moreover, like GDF-9, GDF-9B lacks the cysteine residue needed for the covalent dimerization of several TGF-b family members. Cysteine 39-47 bone morphogenetic protein 15 Mus musculus 22-28 9858730-2 1998 The predicted protein sequences, spanning 579 and 576 amino acid residues for ZFz8a and ZFz8b, respectively, were highly homologous (78%) to each other and contained an extracellular cysteine-rich domain and seven transmembrane domains that are well conserved in Fz receptor protein members. Cysteine 183-191 frizzled class receptor 8b Danio rerio 88-93 9767172-8 1998 As for glutathione reductase, the mRNA level was increased at 0.5 h, and peaked strongly at 2 h, while the enzyme activity was significantly increased at 6 h after irradiation, and continued to increase up to 24 h. The level of mRNA for thioredoxin, which contributes to GSH biosynthesis by supplying cysteine to the de novo pathway, peaked between 0.5 h and 2 h post-irradiation, and rapidly declined thereafter. Cysteine 301-309 thioredoxin 1 Mus musculus 237-248 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. Cysteine 299-306 growth hormone 2 Homo sapiens 177-182 9758748-4 1998 Refolding of RBP is carried out in the presence of vitamin A by diluting denatured and reduced RBP into a redox refolding buffer consisting of 3 mM cysteine/0.3 mM cystine at 4 degreesC. Cysteine 148-156 retinol binding protein 4 Homo sapiens 13-16 9737963-5 1998 By using Pax-5 and Pax-8 recombinant proteins, we demonstrate that the binding activity of the Prd domain is regulated through the oxidation/reduction of conserved cysteine residues. Cysteine 164-172 paired box 5 Homo sapiens 9-14 9751730-5 1998 Mutational analysis of conserved cysteines contributing to VEGF-B dimer formation suggest a structural conservation with VEGF and platelet-derived growth factor. Cysteine 33-42 vascular endothelial growth factor B Homo sapiens 59-65 9775445-1 1998 A newly isolated peptide from bovine hypothalamus with prolactin-releasing activity (prolactin-releasing peptide; PrRP) was synthesized by a combination of recombinant DNA technology and a cysteine-specific cyanylation reaction, together with rat and human homologs. Cysteine 189-197 prolactin releasing hormone Bos taurus 114-118 9733680-0 1998 Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes. Cysteine 20-28 acetyltransferase Escherichia coli 65-82 9733680-2 1998 The enzyme was protected from inactivation in the presence of its substrate acetyl coenzyme A (acetyl-CoA), suggesting the presence of an essential cysteine residue in or near the active site of the acetyltransferase domain. Cysteine 148-156 acetyltransferase Escherichia coli 199-216 9733680-7 1998 From these studies, the two cysteines Cys307 and Cys324 appeared important for acetyltransferase activity and seemed to be located in or near the active site. Cysteine 28-37 acetyltransferase Escherichia coli 79-96 9712849-2 1998 In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelatase (Crouse, B. R., Sellers, V. M., Finnegan, M. G., Dailey, H. A. Cysteine 158-167 ferrochelatase Homo sapiens 130-144 9712849-2 1998 In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelatase (Crouse, B. R., Sellers, V. M., Finnegan, M. G., Dailey, H. A. Cysteine 158-167 ferrochelatase Homo sapiens 239-253 9712849-2 1998 In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelatase (Crouse, B. R., Sellers, V. M., Finnegan, M. G., Dailey, H. A. Cysteine 200-203 ferrochelatase Homo sapiens 130-144 9712849-2 1998 In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelatase (Crouse, B. R., Sellers, V. M., Finnegan, M. G., Dailey, H. A. Cysteine 209-212 ferrochelatase Homo sapiens 130-144 9712849-2 1998 In a previous study, site-directed mutagenesis experiments identified three of the four ligands to the [2Fe-2S] cluster in animal ferrochelatase as conserved cysteines in the COOH-terminal extension, Cys-403, Cys-406, and Cys-411 in human ferrochelatase (Crouse, B. R., Sellers, V. M., Finnegan, M. G., Dailey, H. A. Cysteine 209-212 ferrochelatase Homo sapiens 130-144 9712849-6 1998 Cysteine at position 196 in human recombinant ferrochelatase when changed to a serine results in an inactive enzyme that is lacking the [2Fe-2S] cluster. Cysteine 0-8 ferrochelatase Homo sapiens 46-60 9705288-0 1998 Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity. Cysteine 34-42 Raf-1 proto-oncogene, serine/threonine kinase S homeolog Xenopus laevis 58-63 9705288-0 1998 Identification of residues in the cysteine-rich domain of Raf-1 that control Ras binding and Raf-1 activity. Cysteine 34-42 Raf-1 proto-oncogene, serine/threonine kinase S homeolog Xenopus laevis 93-98 9705288-9 1998 Missense substitutions of residues 143 and 144 in the Raf-1 cysteine-rich domain were isolated multiple times. Cysteine 60-68 Raf-1 proto-oncogene, serine/threonine kinase S homeolog Xenopus laevis 54-59 9705288-13 1998 Interestingly, all three cysteine-rich domain mutations reduced the ability of the Raf-1 N-terminal regulatory region to inhibit Xenopus oocyte germinal vesicle breakdown induced by the C-terminal catalytic region of Raf-1. Cysteine 25-33 Raf-1 proto-oncogene, serine/threonine kinase S homeolog Xenopus laevis 83-88 9705288-13 1998 Interestingly, all three cysteine-rich domain mutations reduced the ability of the Raf-1 N-terminal regulatory region to inhibit Xenopus oocyte germinal vesicle breakdown induced by the C-terminal catalytic region of Raf-1. Cysteine 25-33 Raf-1 proto-oncogene, serine/threonine kinase S homeolog Xenopus laevis 217-222 9712692-6 1998 These data suggest a mechanism by which the oxidation state of conserved cysteine residues in the AP-2 DNA binding domain may contribute to its DNA binding activity. Cysteine 73-81 transcription factor AP-2 alpha Homo sapiens 98-102 9651395-1 1998 CMMP, Xenopus XMMP, and human MMP19 have a conserved unique cysteine in the catalytic domain. Cysteine 60-68 matrix metallopeptidase 21 L homeolog Xenopus laevis 14-18 9651395-4 1998 Strikingly, a homologously inserted cysteine is also found in Xenopus XMMP and human MMP19, two recently cloned novel members of the MMP family. Cysteine 36-44 matrix metallopeptidase 21 L homeolog Xenopus laevis 70-74 9653199-3 1998 The APR1 cDNA encoding APS reductase from Arabidopsis thaliana is able to complement the cysteine auxotrophy of an Escherichia coli cysH [3"-phosphoadenosine-5"-phosphosulfate (PAPS) reductase] mutant, only if the E. coli strain produces glutathione. Cysteine 89-97 APS reductase 1 Arabidopsis thaliana 4-8 9653199-3 1998 The APR1 cDNA encoding APS reductase from Arabidopsis thaliana is able to complement the cysteine auxotrophy of an Escherichia coli cysH [3"-phosphoadenosine-5"-phosphosulfate (PAPS) reductase] mutant, only if the E. coli strain produces glutathione. Cysteine 89-97 APS reductase 1 Arabidopsis thaliana 23-36 9642191-5 1998 However, the fact that Sed1p, unlike other cell wall proteins, has six cysteines and seven putative N-glycosylation sites suggests that Sed1p belongs to a new family of cell wall proteins. Cysteine 71-80 Sed1p Saccharomyces cerevisiae S288C 23-28 9621093-4 1998 Alignment of the amino acid sequences inferred from the cDNA nucleotide sequences showed that BS-C-1 and CV-1 havcr-1 differed from GL37 havcr-1 by having two substitutions in the Cys-rich region, N48H and K108Q, and 10 to 11 additional substitutions plus the insertion of 18 to 22 amino acids in the mucin-like region. Cysteine 180-183 hepatitis A virus cellular receptor 1 Homo sapiens 110-117 9624118-3 1998 H2O2 inactivated recombinant PTP1B in vitro by oxidizing its catalytic site cysteine, most likely to sulfenic acid. Cysteine 76-84 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 29-34 9624118-5 1998 Oxidation by H2O2 prevented modification of the catalytic cysteine of PTP1B by iodoacetic acid, suggesting that it should be possible to monitor the oxidation state of PTP1B in cells by measuring the incorporation of radioactivity into the enzyme after lysis of the cells in the presence of radiolabeled iodoacetic acid. Cysteine 58-66 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 70-75 9656995-7 1998 Site-directed mutagenesis of the Cys-1151 residue (one of the catalytic dyad residues of the viral protease) and of the Gly-1300 residue (the viral protease cleavage site) abrogated protease activity and p200 precursor cleavage, respectively. Cysteine 33-36 AT-rich interaction domain 2 Homo sapiens 204-208 9637742-10 1998 Regulation at the level of translation was investigated by measuring the rate of HMG-CoA reductase protein synthesis in liver slices using [35S]methionine and [35S]cysteine. Cysteine 164-172 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 81-98 9692232-9 1998 Though resembling chicken and frog VgRs, which are also members of the LDLR family, it is twice as big, carrying two clusters of cysteine-rich complement-type (Class A) repeats (implicated in ligand-binding) instead of one like vertebrate VgRs and LDLRs. Cysteine 129-137 low density lipoprotein receptor Gallus gallus 71-75 9650071-1 1998 The murine small heat shock protein Hsp25 carries a single cysteine residue in position 141 of its amino acid sequence. Cysteine 59-67 heat shock protein 1 Mus musculus 36-41 9572267-2 1998 Neurofascin is constitutively palmitoylated at cysteine-1213 at close to a 1:1 molar stoichiometry. Cysteine 47-55 neurofascin Homo sapiens 0-11 9643018-6 1998 In all five unrelated SFD pedigrees individual TIMP3 mutations were identified introducing an additional cysteine residue into the C-terminal region of the mature protein. Cysteine 105-113 TIMP metallopeptidase inhibitor 3 Homo sapiens 22-25 9643018-6 1998 In all five unrelated SFD pedigrees individual TIMP3 mutations were identified introducing an additional cysteine residue into the C-terminal region of the mature protein. Cysteine 105-113 TIMP metallopeptidase inhibitor 3 Homo sapiens 47-52 9596642-7 1998 Site-directed mutagenesis defined two highly conserved amino acids, cysteine-265 and aspartate-234, as being essential for the phosphatase activity of the AtPTP1 protein, suggesting a common catalytic mechanism for PTPases from all eukaryotic systems. Cysteine 68-76 protein tyrosine phosphatase 1 Arabidopsis thaliana 155-161 9512496-0 1998 Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat intestinal mucin muc 2 to proteolytic cleavage. Cysteine 22-30 solute carrier family 13 member 2 Rattus norvegicus 85-90 9545435-1 1998 BACKGROUND: The peptide antibiotic microcin B17 (MccB17) contains oxazole and thiazole heterocycles formed by the post-translational modification of four cysteine and four serine residues. Cysteine 154-162 NADH:ubiquinone oxidoreductase subunit B6 Homo sapiens 44-47 9790257-7 1998 The patient was revealed to be heterozygous for a missense mutation G370C, changing codon 370 (GGC) encoding Gly to TGC encoding Cys, but his parents did not have the G370C mutation. Cysteine 129-132 gamma-glutamylcyclotransferase Homo sapiens 95-98 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. Cysteine 42-50 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. Cysteine 42-50 fibroblast growth factor receptor 3 Homo sapiens 182-187 9525683-4 1998 Replacement of alanine with all four tyrosine residues and with serine-17 and cysteine-20 decrease or abolish gp120 binding and CCR5 coreceptor activity. Cysteine 78-86 C-C motif chemokine receptor 5 Homo sapiens 128-132 9479018-1 1998 Conservative substitutions of the conserved cysteine 393 (Cys393) in S6 of the voltage-gated K+ channel Kv2.1 predictably alter the stability of the open state and the conductances for K+ and Rb+. Cysteine 44-52 potassium voltage-gated channel subfamily B member 1 Homo sapiens 104-109 9659525-6 1998 Furthermore, NAC can easily be deacetylated to cysteine, an important precursor of cellular glutathione synthesis, and thus stimulate the cellular glutathione system. Cysteine 47-55 X-linked Kx blood group Homo sapiens 13-16 9520445-4 1998 Bacterial maltose-binding proteins containing the CPV or ECT CrmD cysteine-rich region bound TNF and lymphotoxin-alpha (LTalpha) and blocked their in vitro cytolytic activity. Cysteine 66-74 lymphotoxin alpha Homo sapiens 120-127 9488680-5 1998 rMGL1 and rMGL2 were found to have high activity toward methionine (10.4 and 0.67 mumol/min/mg of protein, respectively), homocysteine (370 and 128 mumol/min/mg of protein), cysteine (6.02 and 1.06 mumol/min/mg of protein), and O-acetylserine (3.74 and 1.51 mumol/min/mg of protein), but to be inactive toward cystathionine. Cysteine 126-134 C-type lectin domain containing 10A Rattus norvegicus 0-5 9488680-6 1998 Site-directed mutagenesis of an active site cysteine (C113G for MGL1 and C116G for MGL2) reduced the activity of the recombinant enzymes toward both methionine and homocysteine by approximately 80% (rMGL1) and 90% (rMGL2). Cysteine 44-52 C-type lectin domain containing 10A Rattus norvegicus 64-68 9488680-6 1998 Site-directed mutagenesis of an active site cysteine (C113G for MGL1 and C116G for MGL2) reduced the activity of the recombinant enzymes toward both methionine and homocysteine by approximately 80% (rMGL1) and 90% (rMGL2). Cysteine 44-52 C-type lectin domain containing 10A Rattus norvegicus 199-204 9490731-3 1998 As an alternative, we used a novel application of site-directed mutagenesis in which four of the six conserved cysteines in the extracellular loops of connexin 32 were moved individually and in all possible pairwise and some quadruple combinations. Cysteine 111-120 gap junction protein beta 1 Homo sapiens 151-162 9499091-3 1998 Translation of RNAs in reticulocyte lysates showed that cleavage at the nsP3/nsP4 site occurred efficiently for all mutants except for Glu-nsP4, which was cleaved inefficiently, and Pro-nsP4, which was not detectably cleaved, and that Tyr, Cys, Leu, Arg, and Phe destabilized nsP4 but Ala, Met, Thr, Asn, Gln, and Glu stabilized nsP4 to various extents. Cysteine 240-243 SH2 domain containing 3C Homo sapiens 72-76 9495800-0 1998 Chloroethylclonidine binds irreversibly to exposed cysteines in the fifth membrane-spanning domain of the human alpha2A-adrenergic receptor. Cysteine 51-60 adrenoceptor alpha 2A Homo sapiens 112-139 9495800-6 1998 Based on a three-dimensional receptor model, we systematically mutated residues 197-201 and 204 in the fifth transmembrane domain of the human alpha2A-AR to cysteine. Cysteine 157-165 adrenoceptor alpha 2A Homo sapiens 143-153 9461574-0 1998 Cysteine oxidation in the mitogenic S100B protein leads to changes in phosphorylation by catalytic CKII-alpha subunit. Cysteine 0-8 casein kinase 2 alpha 2 Homo sapiens 99-109 9461576-2 1998 To address this issue we have analyzed the susceptibility to limited proteolysis and to alkylation of cysteine residues of mitochondrial aspartate aminotransferase (mAAT) bound to GroEL. Cysteine 102-110 heat shock protein family D (Hsp60) member 1 Homo sapiens 180-185 9466817-0 1998 The leukocyte NADPH oxidase subunit p47PHOX: the role of the cysteine residues. Cysteine 61-69 neutrophil cytosolic factor 1 Homo sapiens 36-43 9466817-2 1998 We have used site-directed mutagenesis to examine the functional role of the four cysteines in p47PHOX, one of the subunits of the oxidase. Cysteine 82-91 neutrophil cytosolic factor 1 Homo sapiens 95-102 9422786-8 1998 Sequence alignment of betac with other cytokine receptor signaling subunits in light of these data shows that Cys-86 and Cys-91 represent a motif restricted to human and mouse beta chains, suggesting a unique mechanism of activation utilized by the IL-3, GM-CSF, and IL-5 receptors. Cysteine 110-113 colony stimulating factor 2 (granulocyte-macrophage) Mus musculus 255-261 9439619-2 1998 Since DNA binding of Jun-Jun and Jun-Fos dimers is regulated in vitro by redox control involving conserved cysteines, we hypothesized that the action of NO is mediated via these residues. Cysteine 107-116 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 37-40 9439619-4 1998 Cysteine-to-serine mutants showed that the inhibition of AP-1 activity following NO treatment was dependent on the presence of Cys7272 and Cys154 in the DNA binding domain of Jun and Fos, respectively. Cysteine 0-8 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 183-186 9439619-6 1998 Our results demonstrate that NO mediates its inhibitory effect by reacting specifically with the conserved cysteine residues in Jun and Fos. Cysteine 107-115 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 136-139 9467953-1 1998 Bcr is a novel serine/threonine protein kinase that is believed to require two cysteine pairs for activity (Maru and Witte, Cell, 67, 459, 1991). Cysteine 79-87 BCR activator of RhoGEF and GTPase Homo sapiens 0-3 9551966-9 1998 The CD8alpha-derived hinge successfully performs this task in chimeric scFv-Syk receptors regardless of its cysteine content. Cysteine 108-116 CD8a molecule Homo sapiens 4-12 9585127-1 1998 The environmentally sensitive and cysteine reactive fluorescent probe, IANBD, was used to monitor ligand-induced structural changes in the beta2 adrenergic receptor (beta2AR) by fluorescent spectroscopy. Cysteine 34-42 adrenoceptor beta 2 Homo sapiens 139-164 9585127-1 1998 The environmentally sensitive and cysteine reactive fluorescent probe, IANBD, was used to monitor ligand-induced structural changes in the beta2 adrenergic receptor (beta2AR) by fluorescent spectroscopy. Cysteine 34-42 adrenoceptor beta 2 Homo sapiens 166-173 9450551-1 1997 The excimer fluorescence from two pyrenyl moieties attached to cysteines in human carbonic anhydrase II has been monitored to characterize residual structure retained under strong denaturing conditions. Cysteine 63-72 carbonic anhydrase 2 Homo sapiens 82-103 9391108-3 1997 WSC1, WSC2, and WSC3 encode predicted integral membrane proteins with a conserved cysteine motif and a WSC1-green fluorescence protein fusion protein localizes to the plasma membrane. Cysteine 82-90 Wsc2p Saccharomyces cerevisiae S288C 6-10 9426002-4 1997 Multiple sequence alignments of PTGFB and representative members of all TGF-beta subfamilies evidenced a number of conserved residues, including the seven cysteines that are almost invariant in all members of the TGF-beta superfamily. Cysteine 155-164 growth differentiation factor 15 Homo sapiens 32-37 9435489-8 1997 These results show that the NH2-terminal tail of Kv2.1 participates in transitions leading to activation through interactions involving reduced cysteine(s) that can be modulated from the cytoplasmic phase. Cysteine 144-152 potassium voltage-gated channel subfamily B member 1 Homo sapiens 49-54 9344839-0 1997 Molecular cloning of a novel brain-specific serine protease with a kringle-like structure and three scavenger receptor cysteine-rich motifs. Cysteine 119-127 complement component 1, s subcomponent 1 Mus musculus 44-59 9367182-3 1997 The switch from one type of melanin to the other appears to be regulated by the levels of tyrosinase and thiols, such as cysteine and glutathione. Cysteine 121-129 tyrosinase Homo sapiens 90-100 9367182-5 1997 We prepared pheomelanins by tyrosinase oxidation of dopa or tyrosine in the presence of cysteine. Cysteine 88-96 tyrosinase Homo sapiens 28-38 9371420-3 1997 An analog of peptide CAP37 P20-44 was synthesized in which the cysteine residues at positions 26 and 42 were replaced with serine residues (CAP37 P20-44Ser). Cysteine 63-71 azurocidin 1 Homo sapiens 21-26 9326585-0 1997 The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for modulation of Wnt signaling. Cysteine 4-12 frizzled related protein L homeolog Xenopus laevis 37-43 9326585-7 1997 Partial deletions of the Frzb-1 cysteine-rich domain maintain Wnt-1 interaction, but functional inhibition is lost. Cysteine 32-40 frizzled related protein L homeolog Xenopus laevis 25-31 9336183-2 1997 Among 17 cysteine mutants expressed in Xenopus oocytes, 7 showed significant alterations in sensitivity to mu-CTX compared to wild-type rSkM1 channel (IC50 = 17.5 +/- 2.8 nM). Cysteine 9-17 sodium voltage-gated channel alpha subunit 4 Rattus norvegicus 136-141 9207144-7 1997 Further, since the modification of cysteines introduced between D11 and D12 and at the extracellular end of D3 strongly affect ClC-1 currents, these regions are suggested to be important for ion permeation. Cysteine 35-44 chloride voltage-gated channel 1 Homo sapiens 127-132 9233564-6 1997 In contrast to previously reported truncated forms of GPIb alpha, this form contains a portion of the transmembranous domain as well as the juxtamembranous cysteines engaged in a disulphide bond with GPIb beta. Cysteine 156-165 glycoprotein Ib platelet subunit alpha Homo sapiens 200-209 9240971-3 1997 We show that H[cys] induced c-fos and c-myb and increased DNA synthesis and cell proliferation 12-fold in neural crest-derived VSMC (N-VSMC). Cysteine 15-18 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 28-33 9199449-4 1997 This soluble rDBP product contained the cysteine-rich ligand domain and most of the contiguous proline-rich hydrophilic region. Cysteine 40-48 D-box binding PAR bZIP transcription factor Rattus norvegicus 13-17 9234171-1 1997 Replacement of individual P-loop residues with cysteines in rat skeletal muscle Na+ channels (SkM1) caused an increased sensitivity to current blockade by Cd2+ thus allowing detection of residues lining the pore. Cysteine 47-56 sodium voltage-gated channel alpha subunit 4 Rattus norvegicus 94-98 9309797-5 1997 We have previously shown that mutation of Ser90, located in transmembrane helix II, to either alanine or cysteine produces a selective reduction in the affinity of the (-)-enantiomers of the catecholamines for the alpha 2a-adrenoceptor, with no effect on the (+)-enantiomers or the corresponding beta-desoxy analogs. Cysteine 105-113 adrenoceptor alpha 2A Homo sapiens 214-235 9195930-7 1997 Accordingly, mutation of cysteines 51 and 276 abolished chemokine binding to DARC transfectants. Cysteine 25-34 atypical chemokine receptor 1 (Duffy blood group) Homo sapiens 77-81 9200696-5 1997 We show here that the phosphorylation of p47phox leads to a substantial decrease in the reactivity of cysteine C378 toward N-ethylmaleimide, indicating the occurrence of a conformational change involving the C-terminal region of p47phox. Cysteine 102-110 neutrophil cytosolic factor 1 Homo sapiens 41-48 9200696-5 1997 We show here that the phosphorylation of p47phox leads to a substantial decrease in the reactivity of cysteine C378 toward N-ethylmaleimide, indicating the occurrence of a conformational change involving the C-terminal region of p47phox. Cysteine 102-110 neutrophil cytosolic factor 1 Homo sapiens 229-236 9153417-2 1997 The alkyl group is transferred without a cofactor to a specific cysteine acceptor residue of MGMT, Cys-145 in the case of human MGMT, containing 207 amino acid residues and thereby inactivates the protein. Cysteine 64-72 O-6-methylguanine-DNA methyltransferase Homo sapiens 93-97 9180269-3 1997 By analogy to previous studies with human cathepsin E, this is most likely a consequence of the presence of a unique cysteine residue near the N-terminus of the mature proteinase. Cysteine 117-125 cathepsin E Homo sapiens 42-53 9194603-4 1997 The multiple forms of the thioredoxin from pig heart mitochondria in SDS-electrophoresis might be dependent on the oxidation state of the protein cysteine residues. Cysteine 146-154 thioredoxin Sus scrofa 26-37 9152386-10 1997 These data suggest that in control mice CYP2E1 catalyzes the bulk of protein binding, whereas CYP2D catalyzes slightly more cysteine conjugation than does CYP2E1. Cysteine 124-132 cytochrome P450, 2d region Mus musculus 94-99 9167018-4 1997 Then we determined the inhibitory effect of CY 216 on thrombin generation (TG) in platelet-poor plasma (PPP) and in whole blood. Cysteine 44-46 prothrombin Oryctolagus cuniculus 54-62 9054363-3 1997 To address this problem, we bypassed the assembly step and genetically fused CGbeta subunits bearing paired cysteine mutations to a wild-type alpha (WTalpha) subunit. Cysteine 108-116 chorionic gonadotropin subunit beta 3 Homo sapiens 77-83 9060467-0 1997 Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3. Cysteine 137-145 Fyn proto-oncogene Mus musculus 53-59 9065754-0 1997 Dominant negative mutant of ionotropic glutamate receptor subunit GluR3: implications for the role of a cysteine residue for its channel activity and pharmacological properties. Cysteine 104-112 LOC100301965 Xenopus laevis 28-71 9079826-0 1997 Thy cytoplamic domain of rat NKR-P1 receptor interacts with the N-terminal domain of p56(lck) via cysteine residues. Cysteine 98-106 LCK proto-oncogene, Src family tyrosine kinase Rattus norvegicus 89-92 9042819-3 1997 When 35S-cysteine-labeled, digitonin-lysed MCF-7 cells were immunoprecipitated with platelet-specific monoclonal antibodies (mAbs) to GPIb alpha, major radioactive bands were observed. Cysteine 9-17 glycoprotein Ib platelet subunit alpha Homo sapiens 134-144 9048547-0 1997 Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111. Cysteine 109-117 glutathione S-transferase alpha 2 Rattus norvegicus 53-83 9048547-0 1997 Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111. Cysteine 125-133 glutathione S-transferase alpha 2 Rattus norvegicus 53-83 9020145-3 1997 This protein exhibits the domain structure characteristic of previously described MMPs, including a signal sequence, a prodomain with the cysteine residue essential for maintaining the latency of these enzymes, an activation locus with the zinc-binding site, and a COOH-terminal fragment with sequence similarity to hemopexin. Cysteine 138-146 matrix metallopeptidase 11 Homo sapiens 82-86 9020185-2 1997 RBTN1 and RBTN2, also frequently activated in T-ALL, encode proteins only with tandem cysteine-rich LIM domains. Cysteine 86-94 LIM domain only 2 Homo sapiens 10-15 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. Cysteine 16-25 potassium voltage-gated channel subfamily B member 1 Homo sapiens 57-61 9022123-8 1997 In addition, the PCNA-labelling indices of renal tubule cells were elevated in rats treated with captafol alone and significantly reduced in rats treated simultaneously with L-cysteine. Cysteine 174-184 proliferating cell nuclear antigen Rattus norvegicus 17-21 9078440-2 1997 Molecular cloning studies demonstrated that the extracellular segment of the plexin protein possesses three internal repeats of cysteine cluster which are homologous to the cysteine-rich domain of the c-met proto-oncogene protein product. Cysteine 128-136 MET proto-oncogene, receptor tyrosine kinase S homeolog Xenopus laevis 201-206 9078440-2 1997 Molecular cloning studies demonstrated that the extracellular segment of the plexin protein possesses three internal repeats of cysteine cluster which are homologous to the cysteine-rich domain of the c-met proto-oncogene protein product. Cysteine 173-181 MET proto-oncogene, receptor tyrosine kinase S homeolog Xenopus laevis 201-206 9022000-0 1997 The cytoplasmic domain of rat NKR-P1 receptor interacts with the N-terminal domain of p56(lck) via cysteine residues. Cysteine 99-107 LCK proto-oncogene, Src family tyrosine kinase Rattus norvegicus 90-93 9022000-2 1997 The cytoplasmic domains of the CD4, CD8 and 4-1BB receptors contain the sequence Cys-X-Cys-Pro which is directly involved in coupling to another pair of cysteines in the N-terminal domain of the src family tyrosine kinase p56(lck). Cysteine 153-162 Cd4 molecule Rattus norvegicus 31-34 9022000-2 1997 The cytoplasmic domains of the CD4, CD8 and 4-1BB receptors contain the sequence Cys-X-Cys-Pro which is directly involved in coupling to another pair of cysteines in the N-terminal domain of the src family tyrosine kinase p56(lck). Cysteine 153-162 LCK proto-oncogene, Src family tyrosine kinase Rattus norvegicus 226-229 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. Cysteine 79-87 K2 Human gammaherpesvirus 8 31-36 9473776-13 1997 Moreover, increasing Cys concentrations had a modulatory effect on the basal activity of CB from SQCLC and the lung which was featured by Cys-induced inhibition of CB activity and by subsequent Cys-effected recovery of CB activity from its previous inhibition by Cys. Cysteine 21-24 cathepsin B Homo sapiens 89-91 9473776-13 1997 Moreover, increasing Cys concentrations had a modulatory effect on the basal activity of CB from SQCLC and the lung which was featured by Cys-induced inhibition of CB activity and by subsequent Cys-effected recovery of CB activity from its previous inhibition by Cys. Cysteine 138-141 cathepsin B Homo sapiens 89-91 9473776-13 1997 Moreover, increasing Cys concentrations had a modulatory effect on the basal activity of CB from SQCLC and the lung which was featured by Cys-induced inhibition of CB activity and by subsequent Cys-effected recovery of CB activity from its previous inhibition by Cys. Cysteine 138-141 cathepsin B Homo sapiens 89-91 9473776-13 1997 Moreover, increasing Cys concentrations had a modulatory effect on the basal activity of CB from SQCLC and the lung which was featured by Cys-induced inhibition of CB activity and by subsequent Cys-effected recovery of CB activity from its previous inhibition by Cys. Cysteine 138-141 cathepsin B Homo sapiens 89-91 9064653-5 1997 These findings suggest that hClC-1 contains cysteine residues near the extracellular face that may directly influence ion conduction. Cysteine 44-52 chloride voltage-gated channel 1 Homo sapiens 28-34 9352585-1 1997 O6-Methylguanine-DNA methyltransferase (MGMT) is a DNA repair protein that transfers methyl and alkyl lesions from the O6 position of guanine to a cysteine in its structure. Cysteine 147-155 O-6-methylguanine-DNA methyltransferase Homo sapiens 0-38 9352585-1 1997 O6-Methylguanine-DNA methyltransferase (MGMT) is a DNA repair protein that transfers methyl and alkyl lesions from the O6 position of guanine to a cysteine in its structure. Cysteine 147-155 O-6-methylguanine-DNA methyltransferase Homo sapiens 40-44 9027958-0 1997 The Ly-1.1 and Ly-1.2 epitopes of murine CD5 map to the membrane distal scavenger receptor cysteine-rich domain. Cysteine 91-99 lymphocyte antigen 11 Mus musculus 4-10 9027958-0 1997 The Ly-1.1 and Ly-1.2 epitopes of murine CD5 map to the membrane distal scavenger receptor cysteine-rich domain. Cysteine 91-99 CD5 antigen Mus musculus 15-21 9027958-0 1997 The Ly-1.1 and Ly-1.2 epitopes of murine CD5 map to the membrane distal scavenger receptor cysteine-rich domain. Cysteine 91-99 CD5 antigen Mus musculus 41-44 8977329-1 1996 Lymphotactin (Lptn) is a new protein belonging to the C or gamma subfamily of chemokines with only two of the four cysteine residues. Cysteine 115-123 X-C motif chemokine ligand 1 Homo sapiens 0-12 8977329-1 1996 Lymphotactin (Lptn) is a new protein belonging to the C or gamma subfamily of chemokines with only two of the four cysteine residues. Cysteine 115-123 X-C motif chemokine ligand 1 Homo sapiens 14-18 8946957-1 1996 A photoactivatable derivative of the inactivating peptide of the Shaker B potassium channel (ShB peptide) has been synthesized from ShB peptide containing an added cysteine residue at the peptide carboxy-terminus and 1-(p-azidosalicylamido)-4-(iodoacetamido)butane. Cysteine 164-172 SH2 domain containing adaptor protein B Homo sapiens 93-96 8910522-7 1996 The interaction of this antibody with LR8 showed binding characteristics exactly as those demonstrated for the physiological ligands of this receptor, in that binding of the antibody: (i) is Ca2+-dependent; (ii) is abolished by unfolding of the cysteine-rich binding domain by reduction; and (iii) interferes with the binding of very low density lipoprotein and vitellogenin. Cysteine 245-253 transmembrane protein 176B Homo sapiens 38-41 8941650-8 1996 We now purify this protein, which was named hensin, to near homogeneity and find that it belongs to the macrophage scavenger receptor cysteine rich (SRCR) family. Cysteine 134-142 deleted in malignant brain tumors 1 protein Oryctolagus cuniculus 44-50 8939750-2 1996 Two TNF receptors that belong to the cysteine-rich low affinity nerve growth factor receptor family (TNF-R1 and TNF-R2) are the sole mediators of TNF signalling. Cysteine 37-45 TNF receptor superfamily member 1B Homo sapiens 112-118 8910486-5 1996 Palmitate could be released from Nsp1 with neutral hydroxylamine, indicating a thioester linkage to a cysteine residue. Cysteine 102-110 SH2 domain containing 3A Homo sapiens 33-37 8910486-6 1996 Therefore we mutated the conserved cysteine residues of Nsp1 to alanine. Cysteine 35-43 SH2 domain containing 3A Homo sapiens 56-60 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. Cysteine 212-220 Nef Human immunodeficiency virus 1 47-50 8895321-2 1996 Immunoprecipitation of TSHR in whole cells precursor-labeled with [35S]methionine and [35S]cysteine revealed an approximately 10-fold increase in TSHR expression in cells stabilized in 10,000 nM methotrexate (TSHR-10,000 cells) compared to cells with the same gene not subjected to amplification (TSHR-0 cells). Cysteine 91-99 thyroid stimulating hormone receptor Homo sapiens 23-27 8895321-2 1996 Immunoprecipitation of TSHR in whole cells precursor-labeled with [35S]methionine and [35S]cysteine revealed an approximately 10-fold increase in TSHR expression in cells stabilized in 10,000 nM methotrexate (TSHR-10,000 cells) compared to cells with the same gene not subjected to amplification (TSHR-0 cells). Cysteine 91-99 thyroid stimulating hormone receptor Homo sapiens 146-150 8895321-2 1996 Immunoprecipitation of TSHR in whole cells precursor-labeled with [35S]methionine and [35S]cysteine revealed an approximately 10-fold increase in TSHR expression in cells stabilized in 10,000 nM methotrexate (TSHR-10,000 cells) compared to cells with the same gene not subjected to amplification (TSHR-0 cells). Cysteine 91-99 thyroid stimulating hormone receptor Homo sapiens 146-150 8895321-2 1996 Immunoprecipitation of TSHR in whole cells precursor-labeled with [35S]methionine and [35S]cysteine revealed an approximately 10-fold increase in TSHR expression in cells stabilized in 10,000 nM methotrexate (TSHR-10,000 cells) compared to cells with the same gene not subjected to amplification (TSHR-0 cells). Cysteine 91-99 thyroid stimulating hormone receptor Homo sapiens 146-150 8910378-1 1996 GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1-->6fucosyltransferase (alpha1-6FucT; EC 2.4.1.68), which catalyzes the transfer of fucose from GDP-Fuc to N-linked type complex glycopeptides, was purified from a Triton X-100 extract of porcine brain microsomes. Cysteine 11-18 fucosyltransferase 8 Rattus norvegicus 40-71 8910378-1 1996 GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1-->6fucosyltransferase (alpha1-6FucT; EC 2.4.1.68), which catalyzes the transfer of fucose from GDP-Fuc to N-linked type complex glycopeptides, was purified from a Triton X-100 extract of porcine brain microsomes. Cysteine 11-18 fucosyltransferase 8 Rattus norvegicus 73-85 8756556-5 1996 PLP-D contains one putative N-glycosylation site and six cysteine residues that are highly conserved in the placental PRL family. Cysteine 57-65 prolactin family 8, subfamily A, member 7 Rattus norvegicus 0-5 8702464-2 1996 Classical and novel protein kinase C (PKC) isozymes contain two, so-called cysteine-rich zinc finger domains that represent the binding sites for phorbol esters and the diacylglycerols. Cysteine 75-83 protein kinase C, delta Mus musculus 38-41 8889803-4 1996 The interruption of the structural conformation as a result in dsFv-HMT may be explained by the interactions between the cysteines engineered in dsFv domains and the cysteines in the HMT region. Cysteine 121-130 histamine N-methyltransferase Homo sapiens 68-71 8889803-4 1996 The interruption of the structural conformation as a result in dsFv-HMT may be explained by the interactions between the cysteines engineered in dsFv domains and the cysteines in the HMT region. Cysteine 121-130 histamine N-methyltransferase Homo sapiens 183-186 8889803-4 1996 The interruption of the structural conformation as a result in dsFv-HMT may be explained by the interactions between the cysteines engineered in dsFv domains and the cysteines in the HMT region. Cysteine 166-175 histamine N-methyltransferase Homo sapiens 68-71 8889803-4 1996 The interruption of the structural conformation as a result in dsFv-HMT may be explained by the interactions between the cysteines engineered in dsFv domains and the cysteines in the HMT region. Cysteine 166-175 histamine N-methyltransferase Homo sapiens 183-186 8663387-4 1996 beta3 is a polymorphic variant at ADH2 that differs from beta1 by a single amino acid substitution of Arg-369 --> Cys. Cysteine 117-120 alcohol dehydrogenase 1B (class I), beta polypeptide Homo sapiens 34-38 8663387-7 1996 The three-dimensional structures of beta3 and beta1 are virtually identical, with the exception that Cys-369 and two water molecules in beta3 occupy the position of Arg-369 in beta1. Cysteine 101-104 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 Homo sapiens 46-51 8809301-3 1996 Gel-filtration chromatography of crude tissue extracts yielded cathepsin B and tryptase fractions sensitive to cysteine and serine proteinase inhibitors, respectively. Cysteine 111-119 cathepsin B Homo sapiens 63-74 8645155-2 1996 We have examined the functional importance of the cysteine residues of rat liver S-adenosylmethionine synthetase. Cysteine 50-58 methionine adenosyltransferase 1A Rattus norvegicus 81-112 8645155-12 1996 Comparison of dimer/tetramer ratios indicates the importance of cysteine-69 (dimer/tetramer protein ratio of 88 versus 10.2 in the wild type) in maintaining the oligomeric state of rat liver S-adenosylmethionine synthetase. Cysteine 64-72 methionine adenosyltransferase 1A Rattus norvegicus 191-222 8642309-0 1996 A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid. Cysteine 2-10 CD44 molecule (Indian blood group) Homo sapiens 58-62 8642309-0 1996 A cysteine residue located in the transmembrane domain of CD44 is important in binding of CD44 to hyaluronic acid. Cysteine 2-10 CD44 molecule (Indian blood group) Homo sapiens 90-94 8642309-1 1996 In the transmembrane domain and cytoplasmic domain of human CD44 protein there are two cysteine residues. Cysteine 87-95 CD44 molecule (Indian blood group) Homo sapiens 60-64 8642309-2 1996 These two cysteines are conserved in all known mammalian CD44 proteins. Cysteine 10-19 CD44 molecule (Indian blood group) Homo sapiens 57-61 8642309-4 1996 Site-specific mutagenesis was used to create CD44 mutant proteins lacking either one or both of these cysteine residues. Cysteine 102-110 CD44 molecule (Indian blood group) Homo sapiens 45-49 8642309-6 1996 These transfectants were used to study whether these two cysteine residues are important in the binding of CD44(H) to fluorescein-conjugated hyaluronic acid (F-HA). Cysteine 57-65 CD44 molecule (Indian blood group) Homo sapiens 107-111 8642309-12 1996 These results provide evidence that the transmembrane domain of CD44, more specifically the cysteine residue in the transmembrane domain, is important for both activation-induced and anti-CD44 antibody-induced binding of soluble HA. Cysteine 92-100 CD44 molecule (Indian blood group) Homo sapiens 64-68 8642309-12 1996 These results provide evidence that the transmembrane domain of CD44, more specifically the cysteine residue in the transmembrane domain, is important for both activation-induced and anti-CD44 antibody-induced binding of soluble HA. Cysteine 92-100 CD44 molecule (Indian blood group) Homo sapiens 188-192 8627808-2 1996 The mRNA of the SFA-1 gene is approximately 1.6 kb in size and encodes a protein of 253 amino acids, containing four putative transmembrane domains, a number of cysteine residues, and one potential N-glycosylation site in a major hydrophilic region between the third and fourth transmembrane domains. Cysteine 161-169 CD151 molecule (Raph blood group) Homo sapiens 16-21 8641983-6 1996 Mutational types of K-ras at codon 12 in PC were aspartic acid (Asp) in nine cases, both Asp and cysteine in one case, and arginine in one case. Cysteine 97-105 KRAS proto-oncogene, GTPase Homo sapiens 20-25 8630013-0 1996 Cysteine-699, a possible palmitoylation site of the thyrotropin receptor, is not crucial for cAMP or phosphoinositide signaling but is necessary for full surface expression. Cysteine 0-8 thyroid stimulating hormone receptor Homo sapiens 52-72 8664274-1 1996 Engineered cysteine residues in yeast cytochrome c peroxidase (CCP) and yeast iso-1-cytochrome c have been used to generate site specifically cross-linked peroxidase-cytochrome c complexes for the purpose of probing interaction domains and the intramolecular electron transfer reaction. Cysteine 11-19 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 38-61 8664274-1 1996 Engineered cysteine residues in yeast cytochrome c peroxidase (CCP) and yeast iso-1-cytochrome c have been used to generate site specifically cross-linked peroxidase-cytochrome c complexes for the purpose of probing interaction domains and the intramolecular electron transfer reaction. Cysteine 11-19 cytochrome-c peroxidase Saccharomyces cerevisiae S288C 63-66 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 143-151 acetylcholinesterase Bos taurus 16-20 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 143-151 acetylcholinesterase Bos taurus 124-128 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 240-248 acetylcholinesterase Bos taurus 16-20 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 240-248 acetylcholinesterase Bos taurus 124-128 8605149-1 1996 Human cytosolic phospholipase A2 contains two cysteines, cyS324 and cyS331, chemical modification of which using thiol modifying reagents abolishes the activity of the enzyme [Li et al. Cysteine 46-55 phospholipase A2 group IVA Homo sapiens 6-32 8565766-5 1996 MMSC and Cys increased surface mucin content but lessened that of deep mucin. Cysteine 9-12 solute carrier family 13 member 2 Rattus norvegicus 31-36 8565766-5 1996 MMSC and Cys increased surface mucin content but lessened that of deep mucin. Cysteine 9-12 solute carrier family 13 member 2 Rattus norvegicus 71-76 9079362-1 1996 BACKGROUND: Hepatitis C Virus (HCV) non-structural protein 3 (NS3) encodes a trypsin-like serine protease that catalyzes the cleavages at the NS3/NS4A, NS4A/NS4B, NS4B/NS5A and NS5A/NS5B junctions in the viral polyprotein and that shows a preference for a cysteine as the P1 residue. Cysteine 256-264 polyprotein;protein F Hepatitis C virus genotype 1 157-161 9079362-1 1996 BACKGROUND: Hepatitis C Virus (HCV) non-structural protein 3 (NS3) encodes a trypsin-like serine protease that catalyzes the cleavages at the NS3/NS4A, NS4A/NS4B, NS4B/NS5A and NS5A/NS5B junctions in the viral polyprotein and that shows a preference for a cysteine as the P1 residue. Cysteine 256-264 polyprotein;protein F Hepatitis C virus genotype 1 163-167 9078466-3 1996 The 41-residue substrates, 5A/5B and 4A/4B, were processed efficiently in trans by wild-type NS3 but not by a catalytically inactive mutant protease; radiolabel sequencing confirmed that NS3-mediated cleavage occurred at the correct cysteine/serine sites, thereby authenticating this system. Cysteine 233-241 KRAS proto-oncogene, GTPase Homo sapiens 187-190 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). Cysteine 196-204 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). Cysteine 196-204 cathepsin E Homo sapiens 13-15 8698744-2 1996 The prevailing type of single-base substitution at codon 201 (71.4%) corresponded to the replacement of the wild-type sequence CGT (Arg) with TGT (Cys). Cysteine 147-150 UDP glycosyltransferase 8 Homo sapiens 127-130 8698744-4 1996 Sequencing of the corresponding region has confirmed preliminary data indicating that the single-base changes CGT (Arg) to TGT (Cys) or CGT to CAT (His) occurred. Cysteine 128-131 UDP glycosyltransferase 8 Homo sapiens 110-113 8632694-1 1996 O6-Alkylguanine derivatives sensitize tumor cells to chloroethylnitrosourea (CENU) chemotherapy by inactivation of O6-methylguanine-DNA methyltransferase (MGMT), which repairs CENU-induced O6-alkylguanines in DNA by accepting the alkyl group at a cysteine moiety. Cysteine 247-255 O-6-methylguanine-DNA methyltransferase Homo sapiens 115-153 8632694-1 1996 O6-Alkylguanine derivatives sensitize tumor cells to chloroethylnitrosourea (CENU) chemotherapy by inactivation of O6-methylguanine-DNA methyltransferase (MGMT), which repairs CENU-induced O6-alkylguanines in DNA by accepting the alkyl group at a cysteine moiety. Cysteine 247-255 O-6-methylguanine-DNA methyltransferase Homo sapiens 155-159 8569696-1 1996 A cysteine-to-phenylalanine mutation in the third transmembrane domain of the alpha 1B-adrenergic receptor constitutively activates the receptor, resulting in G protein coupling in the absence of agonist and activation of only a single effector pathway (phospholipase C but not phospholipase A2). Cysteine 2-10 adrenoceptor alpha 1B Homo sapiens 78-106 7494274-0 1995 The phenotype in vitro and in infected cells of herpes simplex virus 1 alpha trans-inducing factor (VP16) carrying temperature-sensitive mutations introduced by substitution of cysteines. Cysteine 177-186 host cell factor C1 Homo sapiens 100-104 7565304-7 1995 In addition, one of 15 PNETs retained heterozygosity but demonstrated a somatic CGT to TGT transition (arg to cys) at codon 273. Cysteine 110-113 UDP glycosyltransferase 8 Homo sapiens 80-83 7492538-7 1995 CR bound to organomercurial-agarose Cys 101 and 266 did not form cystine. Cysteine 36-39 calbindin 2 Rattus norvegicus 0-2 7492538-8 1995 The fluorescence intensities of cysteine-linked fluorescent probes 5-iodoacetamidofluorescein and N-(1-pyreneiodoacetamide) were increased approximately 1.3-fold upon calcium binding by CR. Cysteine 32-40 calbindin 2 Rattus norvegicus 186-188 7479910-1 1995 Ras CAAX (C = cysteine, A = aliphatic amino acid, and X = any amino acid) peptidomimetic inhibitors of farnesyl protein transferase suppress Ras-dependent cell transformation by preventing farnesylation of the Ras oncoprotein. Cysteine 14-22 Microsomal glutathione S-transferase-like Drosophila melanogaster 120-131 7495834-14 1995 Comparison of the labeled tryptic peptides with NPM-reacted synthetic SH1 and SH2 tryptic peptides and analysis of the treated fiber bundles" ATPase activity suggested that the sites for NPM reaction on myosin heavy chain when it locks crossbridges in a weakly-binding state are Cys-697 (SH2) and Cys-707 (SH1). Cysteine 279-282 PBV1SPCR2 Oryctolagus cuniculus 203-221 7495834-14 1995 Comparison of the labeled tryptic peptides with NPM-reacted synthetic SH1 and SH2 tryptic peptides and analysis of the treated fiber bundles" ATPase activity suggested that the sites for NPM reaction on myosin heavy chain when it locks crossbridges in a weakly-binding state are Cys-697 (SH2) and Cys-707 (SH1). Cysteine 297-300 PBV1SPCR2 Oryctolagus cuniculus 203-221 7499324-3 1995 Purified human beta 2 adrenergic receptor was covalently labeled with the cysteine-reactive, fluorescent probe N,N"-dimethyl-N-(iodoacetyl)-N"-(7-nitrobenz-2-oxa-1,3-diazol-4- yl)ethylenediamine (IANBD). Cysteine 74-82 adrenoceptor beta 2 Homo sapiens 15-41 7498471-0 1995 Interaction of glyceraldehyde-3-phosphate dehydrogenase with SH-containing compounds: evidence for the binding of L-cysteine and for the dependence of the binding on the functional state of the enzyme. Cysteine 114-124 glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus 15-55 7498471-1 1995 Incorporation of L-[35S]cysteine into rabbit muscle glyceraldehyde-3-phosphate dehydrogenase was detected following incubation of the enzyme in a mixture containing glyceraldehyde-3-phosphate, NAD+ and the labeled cysteine. Cysteine 24-32 glyceraldehyde-3-phosphate dehydrogenase Oryctolagus cuniculus 52-92 8573394-2 1995 Tat of HIV-1 (Tat-1) displays modular function with independent activation function localized to the amino-terminal, cysteine-rich, and core regions and independent RNA-binding function localized to a basic region. Cysteine 117-125 solute carrier family 16 member 10 Homo sapiens 14-19 8557170-2 1995 The human and rat CRF-BP cDNAs encode proteins of 322 amino acids with one putative signal sequence, one N-glycosylation site, and 10 conserved cysteines. Cysteine 144-153 corticotropin releasing hormone binding protein Rattus norvegicus 18-24 8553893-1 1995 Utrophin, a protein encoded by chromosome 6 is highly homologous to the cysteine-rich domain and most of the C-terminal domain of dystrophin. Cysteine 72-80 utrophin Homo sapiens 0-8 7547961-4 1995 The cysteine-rich sequences of dystrophin predominantly bound adhalin (gp50) and to full length dystrophin suggesting that these sequences may also be important to dystrophin dimerization. Cysteine 4-12 sarcoglycan, alpha (dystrophin-associated glycoprotein) Mus musculus 62-69 7673190-5 1995 The observation that in quiescent myoblasts Ang-II increase of AP1 binding and induction of DNA synthesis and, in differentiated myotubes, Ang-II stimulation of protein synthesis are abolished by the cysteine-derivative and glutathione precursor N-acetyl-L-cysteine strongly suggests a role for reactive oxygen intermediates in the intracellular transduction of Ang-II signals for immediate early gene induction, cell proliferation, and hypertrophic responses. Cysteine 200-208 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 63-66 7673217-9 1995 A systematic analysis of the region between the sixth cysteine residue and Leu-47 showed that the low affinity of hEGF for the chicken EGF receptor is mainly due to the presence of Arg-45. Cysteine 54-62 epidermal growth factor Gallus gallus 115-118 7657637-10 1995 Our results provide direct biochemical evidence that the binding site for the agonist BK in the bovine B2 receptor is adjacent to a cysteine and is differentiated from the binding site(s) for the antagonists NPC17731 and HOE140. Cysteine 132-140 kininogen 1 Bos taurus 86-88 7543525-0 1995 The antirheumatic drug disodium aurothiomalate inhibits CD4+ T cell recognition of peptides containing two or more cysteine residues. Cysteine 115-123 CD4 antigen Mus musculus 56-59 7602097-2 1995 Human Ltn shows similarity to some members of the C-C chemokine family but has lost the first and third cysteine residues that are characteristic of the C-C and C-X-C chemokines. Cysteine 104-112 X-C motif chemokine ligand 1 Homo sapiens 6-9 7476206-0 1995 The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins. Cysteine 12-20 putative mercuric transport protein MerT Escherichia coli 77-81 7476206-2 1995 Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in MerP all reduced transport and resistance. Cysteine 0-3 putative mercuric transport protein MerT Escherichia coli 55-59 7476206-2 1995 Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in MerP all reduced transport and resistance. Cysteine 0-3 putative mercuric transport protein MerT Escherichia coli 194-198 7476206-2 1995 Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in MerP all reduced transport and resistance. Cysteine 11-14 putative mercuric transport protein MerT Escherichia coli 55-59 7476206-2 1995 Cys-24 and Cys-25 in the first transmembrane region of MerT were essential for transport of mercuric ions through the cytoplasmic membrane, and mutations Cys-76-Ser, Cys-82-Ser or Gly-38-Asp in MerT or Cys-36-Ser in MerP all reduced transport and resistance. Cysteine 11-14 putative mercuric transport protein MerT Escherichia coli 194-198 7589781-2 1995 Here we report that an hCG beta-subunit analog, lacking residues 2-8, combined with the alpha-subunit more efficiently when positively charged residues between beta-subunit cysteines 10 and 11 were replaced with negatively charged residues found in the corresponding portion of follitropin. Cysteine 173-182 chorionic gonadotropin subunit beta 3 Homo sapiens 23-31 17173560-10 1995 As seen with in situ hybridization, a similar temporal pattern of expression of messenger RNAs corresponding to type I procollagen and Secreted Protein, Acidic and Rich in Cysteine (osteonectin), known to be prevalent in healing wounds, was observed in both young and aged rats. Cysteine 172-180 secreted protein acidic and cysteine rich Rattus norvegicus 182-193 7767940-10 1995 Compounds containing a free sulfhydryl group (cysteine, N-acetylcysteine, GSH or 3,4-dichlorobenzenethiol) decreased the amount of covalent binding to various degrees, suggesting the involvement of the sulfhydryl group in adduct formation with TNT following bioactivation. Cysteine 46-54 troponin T3, fast skeletal type Rattus norvegicus 244-247 7797592-3 1995 Both were highly homologous to human ICE (52% identical) and CED-3 (25% identical) and both contained the absolutely conserved pentapeptide sequence Gln-Ala-Cys-Arg-Asp containing the catalytic cysteine residue. Cysteine 157-160 intraflagellar transport 43 Homo sapiens 61-66 7797592-3 1995 Both were highly homologous to human ICE (52% identical) and CED-3 (25% identical) and both contained the absolutely conserved pentapeptide sequence Gln-Ala-Cys-Arg-Asp containing the catalytic cysteine residue. Cysteine 194-202 intraflagellar transport 43 Homo sapiens 61-66 7540771-1 1995 The crystal structures of a cysteine-215-->serine mutant of protein tyrosine phosphatase 1B complexed with high-affinity peptide substrates corresponding to an autophosphorylation site of the epidermal growth factor receptor were determined. Cysteine 28-36 protein tyrosine phosphatase non-receptor type 1 Homo sapiens 63-94 7599189-2 1995 Comparison of three sulfite oxidase sequences to several plant and fungal nitrate reductase sequences reveals a single conserved cysteine with highly conserved flanking sequences. Cysteine 129-137 sulfite oxidase Homo sapiens 20-35 7599189-3 1995 The conserved cysteine is postulated to be a ligand of molybdenum in sulfite oxidase and nitrate reductase. Cysteine 14-22 sulfite oxidase Homo sapiens 69-84 7540214-1 1995 The disulphide folding pathway of bovine pancreatic trypsin inhibitor (BPTI), especially at the two-disulphide stage, has been dissected by replacing one or two particular cysteine residues by serine. Cysteine 172-180 spleen trypsin inhibitor I Bos taurus 71-75 7758971-4 1995 Cys residues critical to the immunoglobulin (Ig) fold structure and four sites of N-linked glycosylation are absolutely conserved in ICAM-1 from all species. Cysteine 0-3 intercellular adhesion molecule 1 Canis lupus familiaris 133-139 7721766-1 1995 A heterozygous single base change in exon 49 of COL1A1, which converted the codon for pro alpha 1(I) carboxyl-terminal propeptide residue 94 from tryptophan (TGG) to cysteine (TGT) was identified in a baby with lethal osteogenesis imperfecta (OI64). Cysteine 166-174 collagen type I alpha 1 chain Homo sapiens 48-54 7713918-7 1995 Analysis of the distribution of Cys residues in aligned sequences of cloned human alpha 1-->3fucosyltransferases indicated one site, Cys143 of FucT-III and Cys156 of FucT-V, corresponded to the highly conservative replacement of Ser178 in FucT-IV, an enzyme insensitive to N-ethylmaleimide. Cysteine 32-35 fucosyltransferase 5 Homo sapiens 169-175 7723029-2 1995 Com contains six cysteine and five histidine residues that have the potential to form several alternative zinc-finger-like motifs. Cysteine 17-25 Com family DNA-binding transcriptional regulator Escherichia phage Mu 0-3 7723029-4 1995 We observed that mutation of any one of the four N-terminal cysteine residues (Cys-6, 9, 26 or 29) resulted in loss of Com activity. Cysteine 60-68 Com family DNA-binding transcriptional regulator Escherichia phage Mu 119-122 7723029-4 1995 We observed that mutation of any one of the four N-terminal cysteine residues (Cys-6, 9, 26 or 29) resulted in loss of Com activity. Cysteine 79-82 Com family DNA-binding transcriptional regulator Escherichia phage Mu 119-122 7723029-10 1995 These studies indicate that the metal coordination, site of Com is a four-cysteine complex, involving residues 6, 9, 26 and 29. Cysteine 74-82 Com family DNA-binding transcriptional regulator Escherichia phage Mu 60-63 7884906-6 1995 The cysteines previously found to be essential for vif protein function were conserved in all clones. Cysteine 4-13 Vif Human immunodeficiency virus 1 51-54 7702578-7 1995 The present study investigated the role of the six cytoplasmic cysteines of the beta-subunit of the hIR using a mutagenic approach in which insulin receptors, mutated at each cytoplasmic cysteine (to alanine) in turn, were transfected into Chinese hamster ovary (CHO) cells. Cysteine 63-71 potassium inwardly rectifying channel subfamily J member 4 Homo sapiens 100-103 7702578-12 1995 The beta-subunits of each of the hIR cytoplasmic cysteine mutant cell lines could be alkylated specifically with N-[3H]ethylmaleimide. Cysteine 49-57 potassium inwardly rectifying channel subfamily J member 4 Homo sapiens 33-36 7702578-14 1995 We conclude that the cytoplasmic cysteines of the hIR have a predominantly passive role in hIR activity although Cys-981 and Cys-1245 do affect mitogenic and glucose-transport responses of the receptor. Cysteine 33-42 potassium inwardly rectifying channel subfamily J member 4 Homo sapiens 50-53 7702578-14 1995 We conclude that the cytoplasmic cysteines of the hIR have a predominantly passive role in hIR activity although Cys-981 and Cys-1245 do affect mitogenic and glucose-transport responses of the receptor. Cysteine 33-42 potassium inwardly rectifying channel subfamily J member 4 Homo sapiens 91-94 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. Cysteine 100-108 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. Cysteine 100-108 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. Cysteine 100-108 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. Cysteine 100-108 POTE ankyrin domain family member F Homo sapiens 125-135 7877994-6 1995 c-Raf-1 and c-Jun directly interact in vitro as shown by various immobilized glutathione S-transferase-Raf fusion proteins which specify the cysteine-rich region of c-Mil/Raf as the major N-terminal binding site. Cysteine 141-149 TNF receptor associated factor 3 Homo sapiens 0-7 7852406-1 1995 The heavy chain of human glycosylasparaginase (N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26)) has five cysteinyl residues (Cys-61, Cys-64, Cys-69, Cys-163, and Cys-179). Cysteine 145-148 aspartylglucosaminidase Homo sapiens 47-92 7852406-1 1995 The heavy chain of human glycosylasparaginase (N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26)) has five cysteinyl residues (Cys-61, Cys-64, Cys-69, Cys-163, and Cys-179). Cysteine 145-148 aspartylglucosaminidase Homo sapiens 25-45 7852406-1 1995 The heavy chain of human glycosylasparaginase (N4-(beta-N-acetylglucosaminyl)-L-asparaginase (EC 3.5.1.26)) has five cysteinyl residues (Cys-61, Cys-64, Cys-69, Cys-163, and Cys-179). Cysteine 145-148 aspartylglucosaminidase Homo sapiens 47-92 7857973-1 1995 Canine pulmonary surfactant protein C (SP-C) is a small hydrophobic peptide which has one palmitoylated cysteine residue. Cysteine 104-112 surfactant protein C Canis lupus familiaris 17-37 7857973-1 1995 Canine pulmonary surfactant protein C (SP-C) is a small hydrophobic peptide which has one palmitoylated cysteine residue. Cysteine 104-112 surfactant protein C Canis lupus familiaris 39-43 7841202-3 1995 The deduced amino acid sequence of edg-2 contains a putative nuclear translocation sequence, an N-terminal acidic domain and a cysteine-rich C-terminal domain containing a putative Zinc-finger structure. Cysteine 127-135 BUD31 homolog Homo sapiens 35-40 7800044-6 1995 The cysteine residue of E6-AP responsible for ubiquitin thioester formation was mapped to a region that is highly conserved among several proteins of unknown function, suggesting that these proteins share the ability to form thioesters with ubiquitin. Cysteine 4-12 ubiquitin protein ligase E3A Homo sapiens 24-29 8839228-9 1995 In the presence of L-cysteine, ITF 296 stimulated semipurified rat lung guanylate cyclase at higher concentrations than those of NTG or ISDN, probably because of its lower rate of nitric oxide (NO) release. Cysteine 19-29 trefoil factor 3 Rattus norvegicus 31-34 21043697-5 1995 There were frequent homologies to known autoantibody-binding epitopes in the cysteine-rich and intracytoplasmic regions of GP IIb/IIIa, but also with the RGD-binding and calcium-binding regions, and with the nascent GP signal peptide which is not expressed in the functional glycoprotein. Cysteine 77-85 integrin subunit alpha 2b Homo sapiens 123-129 7798211-1 1994 Cysteine 518 of the molecular chaperonin cpn60 (groEL) has been replaced with serine (C518S) by site-directed mutagenesis. Cysteine 0-8 heat shock protein family D (Hsp60) member 1 Homo sapiens 48-53 8084002-2 1994 Interactions with the retinoblastoma tumor suppressor, pRb, and related proteins p107 and p130 rely somewhat on CR1 but largely on CR2, which contains a core binding sequence Leu-122-X-Cys-X-Glu. Cysteine 185-188 RB transcriptional corepressor 1 Rattus norvegicus 55-58 8083230-4 1994 Although chemical inactivation of cPLA2 by the sulfhydryl reagent N-ethylmaleimide made it appear that cysteine(s) may be essential for catalysis, all 9 cysteine residues of cPLA2 proved dispensable, allowing near-normal enzyme activity when substituted by alanine. Cysteine 103-111 phospholipase A2 group IVA Homo sapiens 34-39 8083230-4 1994 Although chemical inactivation of cPLA2 by the sulfhydryl reagent N-ethylmaleimide made it appear that cysteine(s) may be essential for catalysis, all 9 cysteine residues of cPLA2 proved dispensable, allowing near-normal enzyme activity when substituted by alanine. Cysteine 153-161 phospholipase A2 group IVA Homo sapiens 34-39 8083230-4 1994 Although chemical inactivation of cPLA2 by the sulfhydryl reagent N-ethylmaleimide made it appear that cysteine(s) may be essential for catalysis, all 9 cysteine residues of cPLA2 proved dispensable, allowing near-normal enzyme activity when substituted by alanine. Cysteine 153-161 phospholipase A2 group IVA Homo sapiens 174-179 8083230-7 1994 Replacement of Ser-228 by alanine (or threonine or cysteine) yielded catalytically inactive cPLA2, even though the native conformation was maintained as determined by CD spectroscopy. Cysteine 51-59 phospholipase A2 group IVA Homo sapiens 92-97 8062268-7 1994 administration of TGF alpha-delta Cys-PE40 via an osmotic minipump at a dose of 0.4 microgram/g/day over 7 days inhibited MDA-468, MA-231, and BT-20 but not MCF-7 tumor growth in female athymic mice. Cysteine 34-37 immunoglobulin kappa variable 17-121 Mus musculus 143-148 8065332-10 1994 The affinity of transcription factors for the AP-1 binding site depends on the redox state of a cysteine residue located close to the DNA-binding region of both Fos and Jun. Cysteine 96-104 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 161-164 8078477-6 1994 The use of LexA-PDR3 fusions revealed that the protein contains two activation domains, one localised near the N-terminal, cysteine-rich domain and the other localised at the C-terminus. Cysteine 123-131 drug-responsive transcription factor PDR3 Saccharomyces cerevisiae S288C 16-20 8076694-3 1994 Chemical modification of cysteine by iodoacetic acid, and histidine by diethylpyrocarbonate, resulted in a near complete inhibition of 65Zn-binding to TP2. Cysteine 25-33 transition protein 2 Rattus norvegicus 151-154 8078925-2 1994 PKD contains membrane localization signals and a cysteine-rich repeat sequence homologous to that seen in the regulatory domain of protein kinase C (PKC). Cysteine 49-57 protein kinase D1 Homo sapiens 0-3 8037455-5 1994 (b) Composition analysis revealed that the RI was rich in leucine and cysteine residues and included no amino sugars. Cysteine 70-78 ribonuclease/angiogenin inhibitor 1 Homo sapiens 43-45 8050585-4 1994 The reported three-dimensional parvalbumin structures suggest that the side chain of cysteine-72 should be solvent-accessible. Cysteine 85-93 parvalbumin Gallus gallus 31-42 8035800-4 1994 The iap genes encode a C3HC4 (or RING) finger motif found in a number of transcriptional regulatory proteins, as well as two additional Cys/His motifs (baculovirus iap repeats). Cysteine 136-139 magnesium transporter 1 Homo sapiens 4-7 8052270-7 1994 Position 116 is tyrosine in UV5 and cysteine in AA8, and the corresponding positions of XPD, RAD3, and rad15 are cysteine. Cysteine 113-121 TFIIH/NER complex ATP-dependent 5'-3' DNA helicase subunit RAD3 Saccharomyces cerevisiae S288C 93-97 7972490-2 1994 The cDNA library was made from poly(A)+ RNA from leaves challenged with mercuric chloride for 2 d. The two clones, pCh2 and pCh11, appear to encode class I chitinase isoforms with cysteine-rich domains (not found in pCh11 due to the incomplete sequence) and proline-/glycine-rich or proline-rich hinge domains, respectively. Cysteine 180-188 LOW QUALITY PROTEIN: basic endochitinase A Zea mays 124-129 7831664-2 1994 The anti-factor Xa/antithrombin ratio of these compounds determined in a rabbit plasma system were 2.5 and 1.2 for CY 216 and ACLM respectively while BCLM was devoid of anti-thrombin effect. Cysteine 115-117 prothrombin Oryctolagus cuniculus 23-31 8031794-0 1994 Inactivation of a cytosolic phospholipase A2 by thiol-modifying reagents: cysteine residues as potential targets of phospholipase A2. Cysteine 74-82 phospholipase A2 group IVA Homo sapiens 18-44 8031794-1 1994 The cytosolic phospholipase A2 (cPLA2) from the human monocytic cell line U937 contains nine cysteine residues and is subject to oxidation. Cysteine 93-101 phospholipase A2 group IVA Homo sapiens 4-30 8031794-1 1994 The cytosolic phospholipase A2 (cPLA2) from the human monocytic cell line U937 contains nine cysteine residues and is subject to oxidation. Cysteine 93-101 phospholipase A2 group IVA Homo sapiens 32-37 8041795-4 1994 Fos-(118-211) and Jun-(225-334) polypeptides were labeled with either 5-iodoacetamidofluorescein or rhodamine X iodoacetamide on unique cysteine residues located in their DNA binding domains. Cysteine 136-144 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 0-3 8033092-1 1994 Cells resist the major mutagenic effects of alkylating agents by the action of O6-methylguanine-DNA methyltransferase (MGMT), which transfers the alkyl (R) group of O6-alkylguanine, produced in DNA by these chemicals, to a cysteine residue in its active site (formation of R-MGMT). Cysteine 223-231 O-6-methylguanine-DNA methyltransferase Homo sapiens 79-117 8033092-1 1994 Cells resist the major mutagenic effects of alkylating agents by the action of O6-methylguanine-DNA methyltransferase (MGMT), which transfers the alkyl (R) group of O6-alkylguanine, produced in DNA by these chemicals, to a cysteine residue in its active site (formation of R-MGMT). Cysteine 223-231 O-6-methylguanine-DNA methyltransferase Homo sapiens 119-123 8033092-1 1994 Cells resist the major mutagenic effects of alkylating agents by the action of O6-methylguanine-DNA methyltransferase (MGMT), which transfers the alkyl (R) group of O6-alkylguanine, produced in DNA by these chemicals, to a cysteine residue in its active site (formation of R-MGMT). Cysteine 223-231 O-6-methylguanine-DNA methyltransferase Homo sapiens 275-279 8042980-6 1994 (3) Biosynthetic labelling of neurons with [35S]methionine and [35S]cysteine showed GLUT3 to be 6-10-fold more abundant than GLUT1. Cysteine 68-76 solute carrier family 2 member 3 Rattus norvegicus 84-89 8206391-2 1994 The human TRP-2 protein has 83% identity/90% similarity to the mouse sequence and has all the structural characteristics of the tyrosinase protein family, including a signal peptide, 15 conserved cysteine residues, two copper-binding domains and a C-terminal membrane-spanning region. Cysteine 196-204 dopachrome tautomerase Homo sapiens 10-15 7522033-1 1994 The whey acidic protein (WAP) is a milk protein that contains a cysteine-rich motif. Cysteine 64-72 whey acidic protein Mus musculus 25-28 7514405-3 1994 In this investigation, we explored the role of Cys-949 in the binding of transforming growth factor-beta 1 (TGF-beta 1) and TGF-beta 2 to alpha 2M-methylamine. Cysteine 47-50 transforming growth factor beta 2 Homo sapiens 124-134 8175784-4 1994 Cys-170, Cys-242, and Cys-217, implicated by bromoacetoxysteroid affinity-labeling agents as points of contact for the C-3, C-11, and C-17 positions of steroid ligands, were mutated to alanines. Cysteine 0-3 complement C3 Rattus norvegicus 119-122 8175784-4 1994 Cys-170, Cys-242, and Cys-217, implicated by bromoacetoxysteroid affinity-labeling agents as points of contact for the C-3, C-11, and C-17 positions of steroid ligands, were mutated to alanines. Cysteine 9-12 complement C3 Rattus norvegicus 119-122 8175784-4 1994 Cys-170, Cys-242, and Cys-217, implicated by bromoacetoxysteroid affinity-labeling agents as points of contact for the C-3, C-11, and C-17 positions of steroid ligands, were mutated to alanines. Cysteine 9-12 complement C3 Rattus norvegicus 119-122 8075381-2 1994 We have developed a method to measure the adducts of Cl4BQ with cysteine residues of hemoglobin (Hb) and albumin (Alb). Cysteine 64-72 albumin Rattus norvegicus 114-117 7961586-0 1994 Ligand regulation of bovine protein kinase C alpha response via either cysteine-rich repeat of conserved region C1. Cysteine 71-79 protein kinase C alpha Bos taurus 28-50 7961586-1 1994 Based on the finding by others that the conserved region C1 of conventional protein kinase C isoforms carries two independent, cysteine-rich phorbol ester binding sites, we have mapped the structural elements of the C1 region for their role in the phorbol ester- and phospholipid regulation of PKC alpha responses. Cysteine 127-135 protein kinase C alpha Bos taurus 294-303 7961586-6 1994 Our findings indicate that after partial PKC activation by deletion mutagenesis, the presence of either Cys-repeat in C1 still allows phospholipid- and phorbol ester regulation of protein kinase C alpha responses. Cysteine 104-107 protein kinase C alpha Bos taurus 180-202 8178437-5 1994 Excluding the predicted N-terminal signal sequences, 8 of 9 potential N-linked glycosylation sites and all 10 cysteine residues in gB-1 are conserved in both gB-2 and gB-3. Cysteine 110-118 gamma-aminobutyric acid type B receptor subunit 1 Homo sapiens 131-135 8172595-4 1994 These short transcripts have many features common to the deduced primary structure of dystrophin, especially in the cysteine-rich specific C-terminal domains. Cysteine 116-124 LOC100297621 Bos taurus 86-96 7512729-2 1994 Arp stimulates in vitro DNA-binding activity of the human transcription factor Jun and Fos by the reduction of a cysteine residue located in the DNA-binding domain. Cysteine 113-121 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 87-90 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. Cysteine 93-101 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. Cysteine 143-151 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. Cysteine 143-151 uroplakin 1A Bos taurus 163-167 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. Cysteine 231-240 ACE1 Drosophila melanogaster 58-63 8132599-6 1994 Subsequent binding competition studies of NIH-3T3 cells transfected with the chicken EGF receptor showed that chimeras carrying TGF-alpha sequences COOH-terminal of the sixth cysteine have a high affinity for this receptor, similar to hTGF-alpha. Cysteine 175-183 transforming growth factor alpha Gallus gallus 128-137 8132533-7 1994 Gas-phase sequencing of the tryptic peptides purified from inactive GMPS-BDB or AMPS-BDB-modified enzyme gave the cysteine-labeled peptides: C151DENILWLDYK161, and N162IC164K165 as the two major peptide products, with a smaller amount of N43TGIIC48TIGPASR55. Cysteine 114-122 GMP synthase [glutamine-hydrolyzing] Oryctolagus cuniculus 68-72 7508987-2 1994 A recombinant model of the reduced state of BPTI, called [R]Ala, in which all six Cys residues are replaced with Ala, has been expressed in Escherichia coli. Cysteine 82-85 spleen trypsin inhibitor I Bos taurus 44-48 7507494-1 1994 Our previous studies showed that the alpha 5 beta 1 integrin selects cysteine pair-containing RGD peptides from a phage display library based on a random hexapeptide. Cysteine 69-77 integrin subunit beta 1 Homo sapiens 45-60 8170472-8 1994 These results indicate that hVDR residues between cysteine-403 and serine-427 are required for very high affinity 1,25-(OH)2D3 ligand binding and transcriptional activation, but are not involved in heterodimerization. Cysteine 50-58 vitamin D receptor Homo sapiens 28-32 8289834-6 1994 Two alternative forms of Atr-I have been identified that differ in an ectodomain region encompassing the cysteine box motif characteristic of receptors in this family. Cysteine 105-113 baboon Drosophila melanogaster 25-30 8003961-5 1994 The dissociation constant for the RNase A-RI complex increased from 74 fM (RNase A) to 4.5 pM (Lys-1, Cys-7-methyl RNase), corresponding to a decrease in binding energy of 10 kJ mol-1. Cysteine 102-105 saccharopine dehydrogenase (NAD+, L-lysine-forming) Saccharomyces cerevisiae S288C 95-100 8170929-2 1994 Wild-type BLG has two disulfide bonds, C106-C119 and C66-C160, with a free cysteine at position 121. Cysteine 75-83 beta-lactoglobulin Bos taurus 10-13 8306995-4 1994 The deduced human ETF-QO sequence predicts a protein containing 617 amino acids (67 kDa), two domains associated with the binding of the AMP moiety of the FAD prosthetic group, two membrane helices and a motif containing four cysteine residues that is frequently associated with the liganding of ferredoxin-like iron-sulfur clusters. Cysteine 226-234 electron transfer flavoprotein dehydrogenase Homo sapiens 18-24 8305478-12 1994 The exact role of the cysteines in the reaction catalyzed by serine hydroxymethyltransferase remains to be elucidated. Cysteine 22-31 serine hydroxymethyltransferase, cytosolic Ovis aries 61-92 7506414-2 1994 Redox regulation is mediated by a conserved cysteine residue in the DNA-binding domain of Fos and Jun. Cysteine 44-52 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 90-93 7506414-3 1994 Previously, we demonstrated that a DNA repair protein, Ref-1, could stimulate the DNA binding activity of Fos-Jun dimers by reducing this cysteine residue. Cysteine 138-146 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 106-109 7903969-0 1994 Direct demonstration that ATP is in contact with Cys-137 in chaperonin GroEL. Cysteine 49-52 heat shock protein family D (Hsp60) member 1 Homo sapiens 71-76 7903969-2 1994 By replacing with serine each of 3 cysteine residues in GroEL, it is shown that ATP gamma S specifically cross-links to Cys-137. Cysteine 35-43 heat shock protein family D (Hsp60) member 1 Homo sapiens 56-61 7903969-2 1994 By replacing with serine each of 3 cysteine residues in GroEL, it is shown that ATP gamma S specifically cross-links to Cys-137. Cysteine 120-123 heat shock protein family D (Hsp60) member 1 Homo sapiens 56-61 7903969-3 1994 It is thus demonstrated that the ATP bound to GroEL is in direct contact with Cys-137. Cysteine 78-81 heat shock protein family D (Hsp60) member 1 Homo sapiens 46-51 8304415-8 1994 Cardiomyocyte pyruvate dehydrogenase was also inhibited by H2O2 overload, but to a lesser degree than GAPDH such that entry of hexose-derived acetyl units into the tricarboxylic acid cycle was not as restrictive as GAPDH inactivation to glycolytic ATP production. Cysteine 142-148 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 102-107 8304415-8 1994 Cardiomyocyte pyruvate dehydrogenase was also inhibited by H2O2 overload, but to a lesser degree than GAPDH such that entry of hexose-derived acetyl units into the tricarboxylic acid cycle was not as restrictive as GAPDH inactivation to glycolytic ATP production. Cysteine 142-148 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 215-220 8088708-6 1994 The high-affinity IGF binding by the IGF-I receptor is determined by its cysteine-rich domain. Cysteine 73-81 insulin like growth factor 1 receptor Homo sapiens 37-51 8138354-4 1994 Upon direct sequence analysis of intact bovine insulin, the PTH derivatives of cystine from both Cys-A7 and Cys-B7 were significantly released after Edman cycle 7 and gave approximately 20% recovery of common PTH amino acids. Cysteine 97-100 parathyroid hormone Bos taurus 60-63 8138354-4 1994 Upon direct sequence analysis of intact bovine insulin, the PTH derivatives of cystine from both Cys-A7 and Cys-B7 were significantly released after Edman cycle 7 and gave approximately 20% recovery of common PTH amino acids. Cysteine 108-111 parathyroid hormone Bos taurus 60-63 8138354-4 1994 Upon direct sequence analysis of intact bovine insulin, the PTH derivatives of cystine from both Cys-A7 and Cys-B7 were significantly released after Edman cycle 7 and gave approximately 20% recovery of common PTH amino acids. Cysteine 108-111 parathyroid hormone Bos taurus 209-212 8182597-6 1994 The positions of five cysteine residues were the same for porcine ZP4 and mouse ZP2. Cysteine 22-30 zona pellucida glycoprotein 4, pseudogene Mus musculus 66-69 18476286-0 1994 Transcriptional regulation by gold(i) thiolates involving interaction with conserved cysteine residues in the photo-oncogene products jun and fos. Cysteine 85-93 Fos proto-oncogene, AP-1 transcription factor subunit Homo sapiens 142-145 8008630-2 1994 The C-terminal of canine motilin was extended by the addition of a cysteine residue, and then biotinylated. Cysteine 67-75 motilin Canis lupus familiaris 25-32 8262944-0 1993 rBAT, related to L-cysteine transport, is localized to the microvilli of proximal straight tubules, and its expression is regulated in kidney by development. Cysteine 17-27 bile acid CoA:amino acid N-acyltransferase Rattus norvegicus 0-4 8262944-15 1993 The postnatal expression of rBAT and its specific location in the microvilli of epithelial cells from the S3 segment of the proximal tubule coincide with postnatal maturation of cystine resorption and with the site of high affinity resorption of cysteine in kidney. Cysteine 246-254 bile acid CoA:amino acid N-acyltransferase Rattus norvegicus 28-32 8262944-16 1993 This is consistent with the involvement of rBAT in a b(o,+)-like high-affinity resorption system for cysteine in the proximal straight tubule of the nephron. Cysteine 101-109 bile acid CoA:amino acid N-acyltransferase Rattus norvegicus 43-47 7903528-2 1993 The understanding of the unique specificity of endo-oligopeptidase A was useful for the synthesis of affinity labeling compounds containing as a thiol reactive group the Cys-(3-nitro-2-pyridinesulfenyl) group into dynorphin-derived peptides which are among the best substrates and competitive inhibitor of endopeptidase 22.19. Cysteine 170-173 nudE neurodevelopment protein 1 like 1 Homo sapiens 47-68 8253208-0 1993 Characterisation of a novel cysteine/histidine-rich metal binding domain from Xenopus nuclear factor XNF7. Cysteine 28-36 Nuclear factor 7 L homeolog Xenopus laevis 101-105 8230432-5 1993 N-terminal sequencing of the resulting p14-related proteins revealed that cleavage occurs between Cys-168 and Ser-169. Cysteine 98-101 ribonuclease P/MRP subunit p14 Homo sapiens 39-42 8167411-7 1993 In addition, Cdc42p from a cdc42C188S mutant strain (that has an alteration at the prenylation consensus site) was almost exclusively in the soluble fraction, suggesting that membrane localization is dependent on geranylgeranyl modification at Cys-188. Cysteine 244-247 Rho family GTPase CDC42 Saccharomyces cerevisiae S288C 13-19 8142620-5 1993 RBTN1/Ttg-1 and RBTN2/Ttg-2 encode related proteins consisting of two cysteine-rich regions called LIM domains. Cysteine 70-78 LIM domain only 2 Homo sapiens 16-21 8142620-5 1993 RBTN1/Ttg-1 and RBTN2/Ttg-2 encode related proteins consisting of two cysteine-rich regions called LIM domains. Cysteine 70-78 LIM domain only 2 Homo sapiens 22-27 8242750-5 1993 In vitro, Cdi1 removes phosphate from tyrosine residues in model substrates, but a mutant protein that bears a lesion in the putative active site cysteine does not. Cysteine 146-154 cyclin dependent kinase inhibitor 3 Homo sapiens 10-14 8226978-9 1993 Further similarities between PKC zeta and PKC iota included a highly conserved pseudosubstrate sequence, the absence of an apparent Ca(2+)-binding region, and the presence of only one cysteine-rich, zinc finger-like domain. Cysteine 184-192 protein kinase C zeta Homo sapiens 29-37 8254340-6 1993 The addition of thiols such as cysteine, which are rapidly oxidized by Cu(II), to methemoglobin formed by incubation with Cu(II) also resulted in reduction of methemoglobin, but the period of reversal was much shorter than that seen with glutathione and other less reactive thiols. Cysteine 31-39 hemoglobin subunit gamma 2 Homo sapiens 82-95 8254340-6 1993 The addition of thiols such as cysteine, which are rapidly oxidized by Cu(II), to methemoglobin formed by incubation with Cu(II) also resulted in reduction of methemoglobin, but the period of reversal was much shorter than that seen with glutathione and other less reactive thiols. Cysteine 31-39 hemoglobin subunit gamma 2 Homo sapiens 159-172 8254340-7 1993 When cysteine and glutathione were added together to Cu(II)-induced methemoglobin, the rate of reduction and reoxidation was intermediate to that seen when either was added separately. Cysteine 5-13 hemoglobin subunit gamma 2 Homo sapiens 68-81 7902568-8 1993 The mutation at position 723, which changes the amino acid sequence from Arg to Cys at residue 220, showed complete association with the PGM1 2/1 protein polymorphism: DNA from individuals showing the PGM1 1 isozyme carried the Arg codon CGT, whereas individuals showing the PGM1 2 isozyme carried the Cys codon TGT. Cysteine 80-83 UDP glycosyltransferase 8 Homo sapiens 238-241 10779281-2 1993 The clone HD6 contained DNA encoding a 215 residue protein which contained a predicted 17 amino acid residue leader sequence, no cysteines and a single N-glycosylation site. Cysteine 129-138 defensin alpha 6 Homo sapiens 10-13 7685018-3 1993 We have now tested this hypothesis employing Chinese hamster ovary cells transfected with mutated hCG-beta genes in which the Cys residues required for the formation of the final four (of six total) S-S bonds were replaced by Ala. Cysteine 126-129 chorionic gonadotropin subunit beta 3 Homo sapiens 98-106 7685018-4 1993 When the Cys residues required for the third hCG-beta S-S linkage to form (bond 9-90) were substituted, folding did not proceed beyond the earliest detectable folding intermediate (p beta 1-early). Cysteine 9-12 chorionic gonadotropin subunit beta 3 Homo sapiens 45-53 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. Cysteine 101-109 Stubble Drosophila melanogaster 50-56 8479739-5 1993 However, transactivation by c-Jun-Cys-252 is fully restored upon mutation of Ser-226. Cysteine 34-37 Jun proto-oncogene, AP-1 transcription factor subunit Homo sapiens 28-33 8317145-3 1993 Eighteen cysteine residues were identified in the sequenced region, all of which were conserved between the gp55/gp53 sequences. Cysteine 9-17 neuroplastin Homo sapiens 108-112 8463316-1 1993 Wheat calmodulin (CaM) was labeled at Cys-27 with the sulfhydryl-specific fluorescent probe 2-(4"-maleimidoanilino)-naphthalene-6-sulfonic acid (MIANS), to form MIANS.CaM. Cysteine 38-41 CaM5 Triticum aestivum 6-16 8463316-1 1993 Wheat calmodulin (CaM) was labeled at Cys-27 with the sulfhydryl-specific fluorescent probe 2-(4"-maleimidoanilino)-naphthalene-6-sulfonic acid (MIANS), to form MIANS.CaM. Cysteine 38-41 CaM5 Triticum aestivum 18-21 8484715-1 1993 Activity of the cysteine adducts of the cysteine proteinases papain and thaumatopain can be recovered by treatment with thioredoxin, thioredoxin reductase and NADPH. Cysteine 16-24 2,4-dienoyl-CoA reductase 1 Homo sapiens 159-164 8477687-8 1993 However, the ascidian homologue lacked the thread-like domain, and the rod-like domain differed from that of mouse entactin in composition, consisting of two kinds of cysteine-rich motifs, that is, the EGF-like motif and the thyroglobulin-like motif. Cysteine 167-175 nidogen 1 Mus musculus 115-123 8477687-9 1993 These results suggest that entactin/nidogen have evolved by modifying the domains, especially by shuffling the two kinds of cysteine-rich motifs. Cysteine 124-132 nidogen 1 Mus musculus 27-35 8448127-0 1993 Role of cysteines in the activation and inactivation of brewers" yeast pyruvate decarboxylase investigated with a PDC1-PDC6 fusion protein. Cysteine 8-17 indolepyruvate decarboxylase 6 Saccharomyces cerevisiae S288C 119-123 8095049-4 1993 We have determined that groEL binds to a unique peptide sequence near the amino terminus of nascent eosinophil cationic protein that includes the first of eight cysteine residues. Cysteine 161-169 heat shock protein family D (Hsp60) member 1 Homo sapiens 24-29 8095049-4 1993 We have determined that groEL binds to a unique peptide sequence near the amino terminus of nascent eosinophil cationic protein that includes the first of eight cysteine residues. Cysteine 161-169 ribonuclease A family member 3 Homo sapiens 100-127 8462280-11 1993 A cysteine important for the activity of murine CEH appears not to be in the active site as judged by N-phenylmaleimide inhibition in the presence and absence of either (2S,3S)-2,3-epoxy-3-(4-nitrophenyl)glycidol, a competitive inhibitor, or trans-stilbene oxide, a substrate. Cysteine 2-10 epoxide hydrolase 2, cytoplasmic Mus musculus 48-51 8095018-7 1993 This cysteine seemed to be involved in an interchain disulfide bridge both between intact TTR molecules and between small fragments. Cysteine 5-13 transthyretin Homo sapiens 90-93 8468318-3 1993 It exhibited striking sequence similarity to PACE4 and contained similar protein domains, such as the COOH-terminal Cys-rich region. Cysteine 116-119 proprotein convertase subtilisin/kexin type 6 Homo sapiens 45-50 8433009-2 1993 Tyrosinase activity was determined by measuring the quantity of 5-S-L-cysteinyl-L-dopa (5-S-CD) formed in the presence of D,L-dopa and L-cysteine. Cysteine 135-145 tyrosinase Homo sapiens 0-10 8419635-5 1993 UC1mc is unlike any other HIV-2 or SIVmac/sm strain in that it lacks a cysteine residue at the proposed signal peptide cleavage site in Env. Cysteine 71-79 envelope protein Simian immunodeficiency virus 136-139 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. Cysteine 332-340 annexin A1 Homo sapiens 139-151 8416944-3 1993 MBP has a cysteine-rich amino-terminal region, a collagen-like region, and a carboxyl-terminal carbohydrate-recognition domain. Cysteine 10-18 myelin basic protein Rattus norvegicus 0-3 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. Cysteine 18-21 tenascin C Homo sapiens 58-61 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. Cysteine 121-124 tenascin C Homo sapiens 58-61 8109324-8 1993 Evidence for movement of helical segments upon Ca(2+)-binding to TnC was obtained by measurements of excimer fluorescence and of resonance energy transfer with probes attached to Cys residues introduced by site-directed mutagenesis at suitable locations. Cysteine 179-182 tenascin C Homo sapiens 65-68 8381352-4 1993 Here we report that substitution of the palmitoylated cysteine by a glycine (Gly341 beta 2 AR) using site directed mutagenesis leads to a receptor being highly phosphorylated and largely uncoupled from Gs. Cysteine 54-62 adrenoceptor beta 2 Homo sapiens 84-93 8095557-5 1993 Murine T-cell hybridoma lines expressing mutant forms of CD4 were used to demonstrate that the 31 carboxyterminal aminoacids of its cytoplasmic domain, in particular cysteine-420 and cysteine-422, are crucial for the formation of CD4:p56lck complexes in vivo. Cysteine 166-174 CD4 antigen Mus musculus 57-60 8095557-5 1993 Murine T-cell hybridoma lines expressing mutant forms of CD4 were used to demonstrate that the 31 carboxyterminal aminoacids of its cytoplasmic domain, in particular cysteine-420 and cysteine-422, are crucial for the formation of CD4:p56lck complexes in vivo. Cysteine 166-174 CD4 antigen Mus musculus 230-233 8095557-5 1993 Murine T-cell hybridoma lines expressing mutant forms of CD4 were used to demonstrate that the 31 carboxyterminal aminoacids of its cytoplasmic domain, in particular cysteine-420 and cysteine-422, are crucial for the formation of CD4:p56lck complexes in vivo. Cysteine 183-191 CD4 antigen Mus musculus 57-60 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. Cysteine 279-282 chorionic gonadotropin subunit beta 3 Homo sapiens 46-54 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. Cysteine 290-293 chorionic gonadotropin subunit beta 3 Homo sapiens 46-54 8419930-0 1993 Nitrilase in biosynthesis of the plant hormone indole-3-acetic acid from indole-3-acetonitrile: cloning of the Alcaligenes gene and site-directed mutagenesis of cysteine residues. Cysteine 161-169 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 0-9 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 11-19 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 30-33 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 38-41 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 38-41 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 38-41 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 38-41 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-6 1993 Among five cysteine residues (Cys-40, Cys-115, Cys-162, Cys-163, and Cys-218) in the Alcaligenes nitrilase, only Cys-163 was conserved at the corresponding position in the Klebsiella nitrilase. Cysteine 38-41 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 97-106 8419930-8 1993 A 35% increase of the specific activity and a large reduction of the Km for thiophene-2-acetonitrile (which was used as a standard substrate for the nitrilase) were observed in the Cys-162-->Asn mutant enzyme. Cysteine 181-184 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 149-158 8419930-9 1993 The Cys-163-->Ala mutation resulted in complete loss of nitrilase activity, clearly indicating that Cys-163 is crucial for the activity and Cys-162 could not provide the catalytic function of Cys-163. Cysteine 4-7 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 59-68 8419930-9 1993 The Cys-163-->Ala mutation resulted in complete loss of nitrilase activity, clearly indicating that Cys-163 is crucial for the activity and Cys-162 could not provide the catalytic function of Cys-163. Cysteine 103-106 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 59-68 8419930-9 1993 The Cys-163-->Ala mutation resulted in complete loss of nitrilase activity, clearly indicating that Cys-163 is crucial for the activity and Cys-162 could not provide the catalytic function of Cys-163. Cysteine 103-106 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 59-68 8419930-9 1993 The Cys-163-->Ala mutation resulted in complete loss of nitrilase activity, clearly indicating that Cys-163 is crucial for the activity and Cys-162 could not provide the catalytic function of Cys-163. Cysteine 103-106 carbon-nitrogen hydrolase family protein Alcaligenes faecalis 59-68 8081722-3 1993 The models are further characterized by the presence of two disulphide bonds: one between TM3 and TM4 and a second linking the Cys residue before TM3 with the Cys residue in the loop between TM4 and TM5. Cysteine 127-130 tropomyosin 3 Homo sapiens 199-202 8081722-3 1993 The models are further characterized by the presence of two disulphide bonds: one between TM3 and TM4 and a second linking the Cys residue before TM3 with the Cys residue in the loop between TM4 and TM5. Cysteine 159-162 tropomyosin 3 Homo sapiens 146-149 8081722-3 1993 The models are further characterized by the presence of two disulphide bonds: one between TM3 and TM4 and a second linking the Cys residue before TM3 with the Cys residue in the loop between TM4 and TM5. Cysteine 159-162 tropomyosin 3 Homo sapiens 199-202 1336379-0 1992 Role of cysteine residues in the extracellular domain and exoplasmic loops of the transmembrane domain of the TSH receptor: effect of mutation to serine on TSH receptor activity and response to thyroid stimulating autoantibodies. Cysteine 8-16 thyroid stimulating hormone receptor Homo sapiens 110-122 1336379-2 1992 Cysteines 494 or 569 in the 1st and 2nd exoplasmic loops, respectively, of the transmembrane domain of the TSH receptor are important in this process or in coupling ligand binding to signal generation. Cysteine 0-9 thyroid stimulating hormone receptor Homo sapiens 107-119 1464587-2 1992 rac1 and rac2 p21s have a Cys-A-A-Leu (A = aliphatic amino acid) structure in their C-terminal region which may undergo post-translational processing including prenylation, proteolysis, and carboxyl methylation. Cysteine 26-29 Rac family small GTPase 1 Homo sapiens 0-4 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. Cysteine 110-118 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. Cysteine 110-118 proteolipid protein 1 Homo sapiens 21-24 1281423-1 1992 Proteolipid protein (PLP), the major integral membrane protein of central nervous system myelin, contains 14 cysteine residues within its 276-residue polypeptide chain. Cysteine 109-117 proteolipid protein 1 Homo sapiens 0-19 1281423-1 1992 Proteolipid protein (PLP), the major integral membrane protein of central nervous system myelin, contains 14 cysteine residues within its 276-residue polypeptide chain. Cysteine 109-117 proteolipid protein 1 Homo sapiens 21-24 1459239-5 1992 The recombinant calcyclin mutated serine at the third position to cysteine was expressed in E. coli and made dimer formation under non-reduced conditions on SDS-PAGE. Cysteine 66-74 protein S100-A6 Oryctolagus cuniculus 16-25 1447182-2 1992 The cytotoxicity of nephrotoxic cysteine conjugates (NCC) in the renal epithelial cell line, LLC-PK1, is due to the covalent binding of a reactive electrophilic metabolite produced from NCC metabolism by cysteine conjugate beta-lyase. Cysteine 32-40 prokineticin 1 Homo sapiens 97-100 1362222-5 1992 It is hypothesised that the TTR molecules which have no cysteine have a unique structure in heterozygous TTR polymers and are responsible for amyloid fibril formation. Cysteine 56-64 transthyretin Homo sapiens 28-31 1512259-0 1992 Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif. Cysteine 147-155 Furin 2 Drosophila melanogaster 37-44 1512259-6 1992 Dfurin2 contains similar protein domains as mammalian furin, however, it has an extended amino-terminal region and its cysteine-rich region is much larger than that of mammalian furin. Cysteine 119-127 Furin 2 Drosophila melanogaster 0-7 1512259-7 1992 Because of this latter phenomenon, we were able to identify a particular cysteine motif that was repeated multiple times in Dfurin2 but present only twice in mammalian furin. Cysteine 73-81 Furin 2 Drosophila melanogaster 124-131 1323841-0 1992 Conserved cysteine residue in the DNA-binding domain of the bovine papillomavirus type 1 E2 protein confers redox regulation of the DNA-binding activity in vitro. Cysteine 10-18 ubiquitin conjugating enzyme E2 B Homo sapiens 89-99 1379226-6 1992 Evidence is presented that cysteine functions as the naturally occurring reduced sulfhydryl compound in lysosomes being equipotent to 2-mercaptoethanol as an activator of folylpolyglutamate hydrolase. Cysteine 27-35 gamma-glutamyl hydrolase Mus musculus 171-199 1379744-5 1992 An unusual restriction site in the CLC-1 locus in two GM families identified a mutation associated with that disease, a phenylalanine-to-cysteine substitution in putative transmembrane domain D8. Cysteine 137-145 chloride voltage-gated channel 1 Homo sapiens 35-40 1629719-1 1992 Mammalian nerve growth factor (NGF) and brain-derived neurotrophic factor (BDNF) are members of a protein family with perfectly conserved domains arranged around the cysteine residues thought to stabilize an invariant three-dimensional scaffold in addition to distinct sequence motifs that convey different neuronal functions. Cysteine 166-174 brain derived neurotrophic factor Homo sapiens 40-73 1629719-1 1992 Mammalian nerve growth factor (NGF) and brain-derived neurotrophic factor (BDNF) are members of a protein family with perfectly conserved domains arranged around the cysteine residues thought to stabilize an invariant three-dimensional scaffold in addition to distinct sequence motifs that convey different neuronal functions. Cysteine 166-174 brain derived neurotrophic factor Homo sapiens 75-79 1321219-6 1992 Comparison of MCMV gH with that of HCMV indicates that there are 12 conserved cysteine residues and three conserved potential N-linked glycosylation sites. Cysteine 78-86 Glycoprotein H Murid betaherpesvirus 1 19-21 1313901-6 1992 The putative protein, named p135, contained a cysteine-rich zinc finger domain near the N terminus with homology to ICP0 of herpes simplex virus type 1, to protein 61 of varicella-zoster virus, to early protein 0 of pseudorabies virus, and to other viral and cellular proteins. Cysteine 46-54 dynactin subunit 1 Homo sapiens 28-32 1525953-8 1992 In contrast, the inhibition of acid CEH activity by modified albumins, such as acetyl albumin, succinyl albumin and glycine methyl ester albumin, was much lower than that of albumin, and no stimulatory effect of heat treatment on the albumins was observed. Cysteine 79-85 epoxide hydrolase 2 Rattus norvegicus 36-39 1555571-4 1992 12 cysteine residues are conserved in the bullfrog and mammalian LH beta subunit. Cysteine 3-11 luteinizing hormone subunit beta Homo sapiens 65-72 1313769-3 1992 The minimal region of Raf-1 that displays this dominant-negative phenotype (Raf-C4) contains a cysteine finger motif. Cysteine 95-103 v-raf-leukemia viral oncogene 1 Mus musculus 22-27 1313769-5 1992 In addition, we show that Raf-1 and Ras cooperate in trans-activation through the oncogene-responsive element and that the cysteine-rich region is necessary for this effect. Cysteine 123-131 v-raf-leukemia viral oncogene 1 Mus musculus 26-31 1548059-5 1992 A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis. Cysteine 44-52 protein D Escherichia coli 22-31 1578187-4 1992 In the absence of detailed structural data, the optimal placement of cysteines was determined by sequence comparison with other species of IFN-beta. Cysteine 69-78 interferon beta 1, fibroblast Mus musculus 139-147 1544906-15 1992 The amino acid residue designated by X was identified as a cysteine from previous work with DHPDHase inactivated with 5-iodouracil. Cysteine 59-67 dihydropyrimidine dehydrogenase Homo sapiens 92-100 1346974-11 1992 5-CLA-PBGS is shown to be modified at cysteine-223 on half of the subunits. Cysteine 38-46 aminolevulinate dehydratase Homo sapiens 6-10 1740159-6 1992 The apparent participation of six conserved cysteines in the formation of disulphide bridges, as in human RBP, and the similarity (about 60%) of the amino acid sequence of trout and mammalian RBPs, indicate the existence of a similar overall structure organization in evolutionary distant RBPs. Cysteine 44-53 retinol binding protein 4 Homo sapiens 106-109 1531535-2 1992 The C-terminal regions of GP-2 (Asp54-Phe530) and THP (Asp175-His644) from rat show 53% identity, 86% similarity, and 26 conserved cysteine residues including one epidermal growth factor motif. Cysteine 131-139 glycoprotein 2 Rattus norvegicus 26-30 1540183-5 1992 ACAMP-81 bound to the cysteine specific cleaved 51 kDa fragment derived from middle/tail region of synapsin I. Cysteine 22-30 synapsin I Homo sapiens 99-109 1480041-4 1992 The amino acid sequence of CSC-21K demonstrates that this protein shares significant homology with human TIMP (tissue inhibitor of metalloproteinase), including conservation of the positions of the twelve cysteine residues and three of four tryptophan residues. Cysteine 205-213 TIMP metallopeptidase inhibitor 2 Homo sapiens 27-34 1945883-2 1991 We have constructed mutations in LEU3 that affect either one of the conserved cysteines (Cys47) or one of several amino acids located within a variable subregion of the DNA binding motif. Cysteine 78-87 leucine-responsive transcriptional regulator LEU3 Saccharomyces cerevisiae S288C 33-37 1657398-4 1991 A region containing paired cysteine residues within the 426 amino acids encoded by the first exon of BCR is essential for its novel phosphotransferase activity, which overlaps with the strong SH2-binding regions. Cysteine 27-35 BCR activator of RhoGEF and GTPase Homo sapiens 101-104 1658708-9 1991 This region contains a putative C2H2 metal-binding finger, and single amino acid substitutions of the cysteine residues severely decreased CREB2 activity. Cysteine 102-110 activating transcription factor 2 Homo sapiens 139-144 1856208-2 1991 In the present study, we investigated the sites of interaction between the N-terminal regulatory domain of TnC and the inhibitory region (residues 96-116) of TnI, using a mutant rabbit skeletal TnC (designated as TnC57) that contains a single Cys at residue 57 in the C-helix. Cysteine 243-246 tenascin Oryctolagus cuniculus 107-110 1770111-3 1991 Previous mechanistic studies by us demonstrated that phenylarsenoxide derivatives, which are highly specific for vicinal thiols, could inhibit LCAT via a covalent interaction with the sulphydryl groups of the two catalytic cysteine residues and that this inhibition could be rapidly and completely reversed upon addition of 2,3-dimercaptopropanesulphonic acid. Cysteine 223-231 lecithin-cholesterol acyltransferase Homo sapiens 143-147 1719383-9 1991 The missing cysteines in IGFBP-6 resulted in the absence of the invariant Gly-Cys-Gly-Cys-Cys sequence in the amino-terminal region of the molecule. Cysteine 12-21 insulin like growth factor binding protein 6 Homo sapiens 25-32 1943708-1 1991 Oligonucleotide-directed mutagenesis of ctxB was used to produce mutants of cholera toxin B subunit (CT-B) altered at residues Cys-9, Gly-33, Lys-34, Arg-35, Cys-86 and Trp-88. Cysteine 127-130 phosphate cytidylyltransferase 1B, choline Homo sapiens 76-99 1943708-1 1991 Oligonucleotide-directed mutagenesis of ctxB was used to produce mutants of cholera toxin B subunit (CT-B) altered at residues Cys-9, Gly-33, Lys-34, Arg-35, Cys-86 and Trp-88. Cysteine 127-130 phosphate cytidylyltransferase 1B, choline Homo sapiens 101-105 1911554-9 1991 Cys-rich domains with either distant or close homology with epidermal growth factor are repeated manifold in rod-like regions of a number of ECM proteins including laminin, tenascin and thrombospondin. Cysteine 0-3 tenascin C Homo sapiens 173-181 1903399-8 1991 Site-directed mutagenesis established that the isoprenylated cysteines in the rac1, rac2, and ralA proteins were located in the fourth position from the carboxyl terminus. Cysteine 61-70 Rac family small GTPase 1 Homo sapiens 78-82 1903399-8 1991 Site-directed mutagenesis established that the isoprenylated cysteines in the rac1, rac2, and ralA proteins were located in the fourth position from the carboxyl terminus. Cysteine 61-70 RAS like proto-oncogene A Homo sapiens 94-98 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 Rac family small GTPase 1 Homo sapiens 22-26 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 RAS like proto-oncogene A Homo sapiens 35-39 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 Rac family small GTPase 1 Homo sapiens 78-82 1903399-10 1991 The isoprenylation of rac1 (CSLL), ralA (CCIL), and the site-directed mutants rac1 (CRLL) and ralA (CSIL), demonstrates that the amino acid adjacent to the cysteine need not be aliphatic. Cysteine 156-164 RAS like proto-oncogene A Homo sapiens 94-98 2034689-3 1991 The alanine substitutions that were most disruptive to hormone binding are located predominantly in four segments of a cysteine-rich domain in the hGHbp, and collectively they form a patch when mapped upon a structural model proposed for cytokine receptors. Cysteine 119-127 growth hormone receptor Homo sapiens 147-152 1850747-3 1991 Herein, we demonstrate that terminal cysteine residues in the rab1B, rab2, and rab5 proteins undergo thioether modification by isoprenyl groups when these proteins are translated in vitro in the presence of a radiolabeled isoprenoid precursor, [3H]mevalonate. Cysteine 37-45 RAB2A, member RAS oncogene family Homo sapiens 69-73 1985934-1 1991 O6-Methylguanine-DNA methyltransferase, a ubiquitous and unusual DNA repair protein, eliminates mutagenic and cytotoxic O6-alkylguanine from DNA by transferring the alkyl group to one of its cysteine residues in a second-order suicide reaction. Cysteine 191-199 O-6-methylguanine-DNA methyltransferase Homo sapiens 0-38 1985934-6 1991 A unique cysteine residue at position 145 was identified as the methyl acceptor site by autoradiographic analysis of peptides and sequence analysis of 3H-methylated O6-methylguanine-DNA methyltransferase. Cysteine 9-17 O-6-methylguanine-DNA methyltransferase Homo sapiens 165-203 16296004-2 1991 Palmitoylation of cysteine residues within the hypervariable region (amino acids 165-185) is also required for membrane localization of mammalian H-, N-, and K-ras(A). Cysteine 18-26 KRAS proto-oncogene, GTPase Homo sapiens 158-163 1702703-4 1991 The cultures incorporated [35S]cysteine into immunoprecipitable ANP. Cysteine 31-39 natriuretic peptide A Rattus norvegicus 64-67 1703489-4 1991 The polypeptide chain deduced from the AGA cDNA consists of 346 amino acids, has two potential N-glycosylation sites and 11 cysteine residues. Cysteine 124-132 aspartylglucosaminidase Homo sapiens 39-42 1828780-2 1991 Purified GFAP was stoichiometrically labeled at a single cysteine residue with fluorescein-maleimide. Cysteine 57-65 glial fibrillary acidic protein Homo sapiens 9-13 1986373-4 1991 Cys-194 lies within a region of identity to active-site Cys-88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function of this protein. Cysteine 0-3 ubiquitin conjugating enzyme E2 E2 Homo sapiens 70-98 1986373-4 1991 Cys-194 lies within a region of identity to active-site Cys-88 of the ubiquitin carrier protein E2, suggesting a potential role for this region in enzymatic function of this protein. Cysteine 56-59 ubiquitin conjugating enzyme E2 E2 Homo sapiens 70-98 2266135-2 1990 nPKC eta contains a characteristic cysteine-rich repeat sequence (C1 region) and a protein kinase domain sequence (C3 region), both of which are conserved among PKC family members. Cysteine 35-43 protein kinase C, eta Mus musculus 0-8 2376583-10 1990 However, Met-909 (progestin receptor) and Cys-754 (glucocorticoid receptor) do not occur within equivalent segments of the two proteins. Cysteine 42-45 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 51-74 2115521-9 1990 The anisotropy decay of synapsin I labeled with the long-living chromophore pyrene on Cys-223 was also analyzed. Cysteine 86-89 synapsin I Homo sapiens 24-34 2351676-7 1990 The deduced CRS1C and CRS4C polypeptides are apparent precursors of secreted, cationic, proline- and cysteine-rich peptides that contain Cys-Pro-X repeats. Cysteine 137-140 defensin, alpha, 29 Mus musculus 12-17 2183224-2 1990 Palmitic acid and an isoprenoid (farnesol) intermediate in cholesterol biosynthesis are attached to separate cysteine residues near the C termini of H-ras, N-ras, and Kirsten-ras (K-ras) exon 4A-encoded proteins. Cysteine 109-117 NRAS proto-oncogene, GTPase Homo sapiens 156-161 2183224-2 1990 Palmitic acid and an isoprenoid (farnesol) intermediate in cholesterol biosynthesis are attached to separate cysteine residues near the C termini of H-ras, N-ras, and Kirsten-ras (K-ras) exon 4A-encoded proteins. Cysteine 109-117 KRAS proto-oncogene, GTPase Homo sapiens 167-178 2183224-2 1990 Palmitic acid and an isoprenoid (farnesol) intermediate in cholesterol biosynthesis are attached to separate cysteine residues near the C termini of H-ras, N-ras, and Kirsten-ras (K-ras) exon 4A-encoded proteins. Cysteine 109-117 KRAS proto-oncogene, GTPase Homo sapiens 180-185 2320569-3 1990 Each of the protein in this family, which range from 47 to 83 residues, contains an Arg-Gly-Asp amino acid sequence found in protein ligands that binds to GPIIb-IIIa, a high (17 +/- 1%) cysteine content conserved in the primary sequence, and a homologous N-terminal region absent only in the echistatin isoforms. Cysteine 186-194 integrin subunit alpha 2b Homo sapiens 155-160 2159799-0 1990 Role of extracellular disulfide-bonded cysteines in the ligand binding function of the beta 2-adrenergic receptor. Cysteine 39-48 adrenoceptor beta 2 Homo sapiens 87-113 2159799-4 1990 Through site-directed mutagenesis, we indeed were able to identify four cysteines which are critical for normal ligand binding affinities and for the proper expression of functional beta AR at the cell surface. Cysteine 72-81 adrenoceptor beta 2 Homo sapiens 182-189 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. Cysteine 135-138 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. Cysteine 146-149 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. Cysteine 146-149 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. Cysteine 146-149 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. Cysteine 146-149 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. Cysteine 146-149 Cd4 molecule Rattus norvegicus 35-39 1968467-4 1990 Superactive octapeptide analogs of somatostatin-containing hexapeptide sequences Cys-Phe-D-Trp-Lys-Thr-Cys or Cys-Tyr-D-Trp-Lys-Val-Cys showed significant binding affinities to SS-14 receptors. Cysteine 81-84 somatostatin Homo sapiens 35-47 1968467-4 1990 Superactive octapeptide analogs of somatostatin-containing hexapeptide sequences Cys-Phe-D-Trp-Lys-Thr-Cys or Cys-Tyr-D-Trp-Lys-Val-Cys showed significant binding affinities to SS-14 receptors. Cysteine 103-106 somatostatin Homo sapiens 35-47 1968467-4 1990 Superactive octapeptide analogs of somatostatin-containing hexapeptide sequences Cys-Phe-D-Trp-Lys-Thr-Cys or Cys-Tyr-D-Trp-Lys-Val-Cys showed significant binding affinities to SS-14 receptors. Cysteine 103-106 somatostatin Homo sapiens 35-47 1968467-4 1990 Superactive octapeptide analogs of somatostatin-containing hexapeptide sequences Cys-Phe-D-Trp-Lys-Thr-Cys or Cys-Tyr-D-Trp-Lys-Val-Cys showed significant binding affinities to SS-14 receptors. Cysteine 103-106 somatostatin Homo sapiens 35-47 2107541-4 1990 1H-113Cd heteronuclear multiple-quantum NMR spectroscopy and phase-sensitive double-quantum filtered 1H correlation spectroscopy of the 112Cd(II)- and 113Cd(II)-substituted GAL4(62*) derivatives provide direct evidence that the two bound 113Cd(II) ions are coordinated only by the six cysteine residues, two of which form bridging ligands between the two 113Cd(II) ions. Cysteine 285-293 galectin 4 Homo sapiens 173-177 2107541-6 1990 Thus a binuclear metal ion cluster rather than a "zinc finger" is formed by the six cysteine residues of the GAL4 DNA-binding domain. Cysteine 84-92 galectin 4 Homo sapiens 109-113 2107543-4 1990 The main features of the predicted trx protein are several cysteine-rich regions which can be folded into zinc finger-like domains. Cysteine 59-67 trithorax Drosophila melanogaster 35-38 2107543-5 1990 Cysteine-rich portions expressed from trx cDNAs in Escherichia coli are capable of zinc binding in vitro, suggesting a possible function for the trx product as a metal-dependent DNA-binding protein. Cysteine 0-8 trithorax Drosophila melanogaster 38-41 2107543-5 1990 Cysteine-rich portions expressed from trx cDNAs in Escherichia coli are capable of zinc binding in vitro, suggesting a possible function for the trx product as a metal-dependent DNA-binding protein. Cysteine 0-8 trithorax Drosophila melanogaster 145-148 2177310-7 1990 The antagonism of SCD-induced neuromuscular blockade by cysteine (400 mg/kg, iv) was less effective and of shorter duration than that by DMPS and DMS. Cysteine 56-64 stearoyl-Coenzyme A desaturase 1 Mus musculus 18-21 2345548-6 1990 One difference was also observed between HEL and megakaryocyte GPIIb at position 633 where a cysteine in the megakaryocyte GPIIb, is replaced by a serine in the HEL sequence. Cysteine 93-101 integrin subunit alpha 2b Homo sapiens 63-68 2345548-6 1990 One difference was also observed between HEL and megakaryocyte GPIIb at position 633 where a cysteine in the megakaryocyte GPIIb, is replaced by a serine in the HEL sequence. Cysteine 93-101 integrin subunit alpha 2b Homo sapiens 123-128 1689063-10 1990 Sequence alignment of P4.2 with these two transglutaminases, however, revealed that P4.2 lacks the critical cysteine residue required for the enzymatic crosslinking of substrates. Cysteine 108-116 erythrocyte membrane protein band 4.2 Homo sapiens 84-88 1689664-5 1990 Comparison of the CD59 protein sequence with those of the Ly-6E and Ly-6C antigens discloses a similarity in overall structure, including the alignment of abundant cysteine residues, hydrophobic carboxy termini and conservation of amino acids surrounding the proposed phosphatidylinositol-glycan modification site for Ly-6 molecules. Cysteine 164-172 CD59a antigen Mus musculus 18-22 2154400-4 1990 Each contains a reading frame encoding an amino acid sequence typical of the known Ly6 molecules: a 26aa leader (except in clone RK6 which has only two of its leader codons), followed by a sequence of 108 or 109aa containing 10 cysteines in excellent alignment with those of Ly6A. Cysteine 228-237 lymphocyte antigen 6 complex Mus musculus 83-86 33798843-8 2021 Furthermore, our research confirmed that the degradation products of unirradiated ADC, Cys-1a, were relatively less toxic, thus potentially reducing the off-target toxicity caused by nonspecific uptake of ADCs. Cysteine 87-90 glutamate decarboxylase like 1 Homo sapiens 82-85 33778205-5 2021 L-Cys-AuNPs also significantly increased the expression of alkaline phosphatase, collagen type 1, osteocalcin, runt-related transcription factor 2, and microtubule-associated protein light chain 3 II and decreased the expression of sequestosome 1 in hPDLCs compared to the expression levels in the hPDLCs treated by D-Cys-AuNPs. Cysteine 0-5 sequestosome 1 Homo sapiens 232-246 27996375-0 2017 Trimeric gp120-specific bovine monoclonal antibodies require cysteine and aromatic residues in CDRH3 for high affinity binding to HIV Env. Cysteine 61-69 endogenous retrovirus group K member 20 Homo sapiens 134-137 24750035-12 2015 This novel molecular mechanism operating in the vasculature, corroborated by higher H2S levels in males, suggests that the L-cysteine/CSE/H2S pathway may be preferentially activated in males leading to gender-specific H2S biosynthesis. Cysteine 123-133 cystathionine gamma-lyase Homo sapiens 134-137 15967461-7 2005 We generated an Hsp26 variant, in which a serine residue of the N-terminal domain was replaced by cysteine. Cysteine 98-106 chaperone protein HSP26 Saccharomyces cerevisiae S288C 16-21 34662684-6 2022 Each predicted TLR was shown to possess the typical the leucine-rich repeat extracellular and TIR intracellular domains and both single cysteine clusters and multiple cysteine clusters TLRs were identified in both lymnaeid species. Cysteine 136-144 protein toll-like Biomphalaria glabrata 15-18 34662684-6 2022 Each predicted TLR was shown to possess the typical the leucine-rich repeat extracellular and TIR intracellular domains and both single cysteine clusters and multiple cysteine clusters TLRs were identified in both lymnaeid species. Cysteine 167-175 protein toll-like Biomphalaria glabrata 15-18 34896750-1 2022 Irreversible Bruton"s tyrosine kinase (BTK) inhibitor drugs are designed to bind covalently to a free-thiol cysteine in the BTK protein active site. Cysteine 108-116 Bruton tyrosine kinase Homo sapiens 13-37 34896750-1 2022 Irreversible Bruton"s tyrosine kinase (BTK) inhibitor drugs are designed to bind covalently to a free-thiol cysteine in the BTK protein active site. Cysteine 108-116 Bruton tyrosine kinase Homo sapiens 39-42 34896750-1 2022 Irreversible Bruton"s tyrosine kinase (BTK) inhibitor drugs are designed to bind covalently to a free-thiol cysteine in the BTK protein active site. Cysteine 108-116 Bruton tyrosine kinase Homo sapiens 124-127 34327571-3 2022 The current objective was to examine for associations between the intake of total SAA, including methionine (Met) and cysteine (Cys), and all-cause and disease-specific mortality US adults. Cysteine 118-126 serum amyloid A1 cluster Homo sapiens 82-85 34327571-3 2022 The current objective was to examine for associations between the intake of total SAA, including methionine (Met) and cysteine (Cys), and all-cause and disease-specific mortality US adults. Cysteine 128-131 serum amyloid A1 cluster Homo sapiens 82-85 34413458-4 2022 In participants without prevalent myeloid neoplasms, eGFR.cys was associated with myeloid mCA (n = 148, beta = -3.36, P = 0.01) and somatic driver mutations (n = 3241, beta = -1.08, P = 6.25 x 10-5) associated with myeloid neoplasia (myeloid CH), specifically mutations in CBL, TET2, JAK2, PPM1D and GNB1 but not DNMT3A or ASXL1. Cysteine 58-61 protein phosphatase, Mg2+/Mn2+ dependent 1D Homo sapiens 290-295 34413458-4 2022 In participants without prevalent myeloid neoplasms, eGFR.cys was associated with myeloid mCA (n = 148, beta = -3.36, P = 0.01) and somatic driver mutations (n = 3241, beta = -1.08, P = 6.25 x 10-5) associated with myeloid neoplasia (myeloid CH), specifically mutations in CBL, TET2, JAK2, PPM1D and GNB1 but not DNMT3A or ASXL1. Cysteine 58-61 G protein subunit beta 1 Homo sapiens 300-304 34157791-3 2021 Initiating somatic BRCA testing on a CyS allows the BRCA status to be determined sooner, and this affects clinical management. Cysteine 37-40 BRCA1 DNA repair associated Homo sapiens 19-23 34725089-2 2021 In this issue of Cancer Discovery, Zhang and colleagues identify that IL1 receptor accessory protein suppresses anoikis in Ewing sarcoma by promoting both the activity of the system Xc - cystine/glutamate antiporter and cystathionine gamma-lyase (CTH) transcription to sustain cysteine levels for reactive oxygen species detoxification.See related article by Zhang et al., p. 2884. Cysteine 277-285 cystathionine gamma-lyase Homo sapiens 220-245 34725089-2 2021 In this issue of Cancer Discovery, Zhang and colleagues identify that IL1 receptor accessory protein suppresses anoikis in Ewing sarcoma by promoting both the activity of the system Xc - cystine/glutamate antiporter and cystathionine gamma-lyase (CTH) transcription to sustain cysteine levels for reactive oxygen species detoxification.See related article by Zhang et al., p. 2884. Cysteine 277-285 cystathionine gamma-lyase Homo sapiens 247-250 34597669-6 2021 Global transcriptomic, biochemical, and cellular analyses indicated that GCN2 is necessary for maintenance of intracellular free amino acids, particularly cysteine, as well as coordination of RAC1-GTP-driven reactive oxygen species (ROS) generation, lamellipodia formation, and focal adhesion dynamics following keratinocyte wounding. Cysteine 155-163 eukaryotic translation initiation factor 2 alpha kinase 4 Homo sapiens 73-77 34542554-9 2021 The highly conserved C-terminal cysteines appear to be involved in inter-subunit communications, affecting the affinity of the cofactor binding site in RDH10 homo-oligomers as well as in the ROC. Cysteine 32-41 retinol dehydrogenase 10 Homo sapiens 152-157 34274480-9 2021 The deduced CBLN1 protein contains a putative signal sequence of 21 residues, two conserved cysteine residues, and gC1q domain. Cysteine 92-100 cerebellin 1 precursor Homo sapiens 12-17 34675960-9 2021 The distribution of pathogenic missense variants along TMEM67 gene mainly clustered in the extracellular cysteine rich region, extracellular area with unknown structure, and the transmembrane regions. Cysteine 105-113 transmembrane protein 67 Homo sapiens 55-61 34402302-5 2021 The observed reactivity of cyclometalated gold(III) enables the rational design of a cysteine-targeted covalent inhibitor of mutant KRAS. Cysteine 85-93 KRAS proto-oncogene, GTPase Homo sapiens 132-136 34409610-5 2021 Glutathione (GSH) and GSH synthesis precursor l-cysteine are decreased in Ggct-/- RBCs. Cysteine 46-56 gamma-glutamyl cyclotransferase Mus musculus 74-78 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. Cysteine 43-51 Aim32p Saccharomyces cerevisiae S288C 96-101 34390831-6 2021 HTT is palmitoylated at cysteine 214 by the huntingtin-interacting protein 14 (HIP14 or ZDHHC17) and 14-like (HIP14L or ZDHHC13) acyltransferases. Cysteine 24-32 zinc finger, DHHC domain containing 17 Mus musculus 44-77 34390831-6 2021 HTT is palmitoylated at cysteine 214 by the huntingtin-interacting protein 14 (HIP14 or ZDHHC17) and 14-like (HIP14L or ZDHHC13) acyltransferases. Cysteine 24-32 zinc finger, DHHC domain containing 17 Mus musculus 79-84 34082042-8 2021 Biochemical assay, FTIR and enzyme kinetics studies revealed that rHC-CS used O-acetyl serine as substrate to produce cysteine using de novo pathway and CS activity was also confirmed with the homogenate of H.contortus. Cysteine 118-126 holocytochrome c synthase Rattus norvegicus 66-72 34513311-0 2021 5"-tiRNA-Cys-GCA regulates VSMC proliferation and phenotypic transition by targeting STAT4 in aortic dissection. Cysteine 9-12 signal transducer and activator of transcription 4 Mus musculus 85-90 34776648-0 2021 Spin Labeling of Surface Cysteines Using a Bromoacrylaldehyde Spin Label. Cysteine 25-34 spindlin 1 Homo sapiens 0-4 34776648-0 2021 Spin Labeling of Surface Cysteines Using a Bromoacrylaldehyde Spin Label. Cysteine 25-34 spindlin 1 Homo sapiens 62-66 34776648-1 2021 Structural investigations of proteins and their biological complexes are now frequently complemented by distance constraints between spin labeled cysteines generated using double electron-electron resonance (DEER) spectroscopy, via site directed spin labeling (SDSL). Cysteine 146-155 spindlin 1 Homo sapiens 133-137 34776648-3 2021 In this article we introduce the use of bromoacrylaldehyde spin label (BASL) as a cysteine spin label, demonstrating an advantage over MTSSL due to its increased selectivity for surface cysteines, eliminating the need to "knock out" superfluous cysteine residues. Cysteine 82-90 spindlin 1 Homo sapiens 59-63 34776648-3 2021 In this article we introduce the use of bromoacrylaldehyde spin label (BASL) as a cysteine spin label, demonstrating an advantage over MTSSL due to its increased selectivity for surface cysteines, eliminating the need to "knock out" superfluous cysteine residues. Cysteine 82-90 spindlin 1 Homo sapiens 91-95 35501630-3 2022 Heterozygous patients with an arginine to cysteine mutation in MPZ (MPZR98C) develop a severe infantile form of CMT1B which is modelled by MpzR98C/ + mice that also show ER stress and an activated UPR. Cysteine 42-50 myelin protein zero Homo sapiens 112-117 35588739-5 2022 Sensing by Cysteine 151 of the NRF2 chaperone, Kelch-like ECH-associated protein 1 (KEAP1) was required for NSAID activation of NRF2 and subsequent anti-inflammatory effects both in vitro and in vivo. Cysteine 11-19 kelch-like ECH-associated protein 1 Mus musculus 47-82 35588739-5 2022 Sensing by Cysteine 151 of the NRF2 chaperone, Kelch-like ECH-associated protein 1 (KEAP1) was required for NSAID activation of NRF2 and subsequent anti-inflammatory effects both in vitro and in vivo. Cysteine 11-19 kelch-like ECH-associated protein 1 Mus musculus 84-89 35314814-1 2022 Current small-molecule inhibitors of KRAS(G12C) bind irreversibly in the switch-II pocket (SII-P), exploiting the strong nucleophilicity of the acquired cysteine as well as the preponderance of the GDP-bound form of this mutant. Cysteine 153-161 KRAS proto-oncogene, GTPase Homo sapiens 37-41 35587148-5 2022 Using the scaffold of the Bruton"s tyrosine kinase (BTK) inhibitor Ibrutinib for our proof-of-concept, we reasoned that increasing the steric bulk of fumarate-based electrophiles on Ibrutinib should improve selectivity via the steric exclusion of off-targets but retain rates of cysteine reactivity comparable to that of an acrylamide. Cysteine 279-287 Bruton tyrosine kinase Homo sapiens 26-50 35587148-5 2022 Using the scaffold of the Bruton"s tyrosine kinase (BTK) inhibitor Ibrutinib for our proof-of-concept, we reasoned that increasing the steric bulk of fumarate-based electrophiles on Ibrutinib should improve selectivity via the steric exclusion of off-targets but retain rates of cysteine reactivity comparable to that of an acrylamide. Cysteine 279-287 Bruton tyrosine kinase Homo sapiens 52-55 35490028-0 2022 Manipulating electron-spin polarization using cysteine-DNA chiral conjugates. Cysteine 46-54 spindlin 1 Homo sapiens 22-26 35490028-2 2022 We report a controlled spin-selective transmission of electrons through self-assembled monolayers of 15 base-paired double-stranded deoxyribonucleic acid functionalized with two enantiomeric cysteine molecules on gold explored through the quantum mechanical tunneling effect. Cysteine 191-199 spindlin 1 Homo sapiens 23-27 35358180-7 2022 Cysteine depalmitoylation sites in transmembrane PPT1 substrates frequently participate in disulfide bonds in the mature protein. Cysteine 0-8 palmitoyl-protein thioesterase 1 Mus musculus 49-53 34999260-2 2022 A reliable biomimetic strategy for the targeting and separation of bacterial pathogens in bloodstream infections involves the use of the broad-spectrum binding motif of human GP-340, a pattern-recognition receptor of the scavenger receptor cysteine rich (SRCR) superfamily that is expressed on epithelial surfaces but not found in blood. Cysteine 240-248 deleted in malignant brain tumors 1 Homo sapiens 175-181 35267628-7 2022 The mutated cysteine resides next to a pocket (P2) of the switch II region, and P2 is present only in the inactive GDP-bound KRAS. Cysteine 12-20 KRAS proto-oncogene, GTPase Homo sapiens 125-129 35120924-4 2022 To address whether one subunit in a SOX dimer is sufficient for catalysis, we produced heterodimeric SOX variants with abolished sulfite oxidation by replacing the molybdenum-coordinating and essential cysteine in the active site. Cysteine 202-210 sulfite oxidase Homo sapiens 101-104 35300425-12 2022 The Arabidopsis PEX4-PEX22 structure also revealed that the residue altered in pex4-1 (P123L), a mutant previously isolated via a forward-genetic screen for peroxisomal dysfunction, is near the active site cysteine of PEX4. Cysteine 206-214 peroxin 22 Arabidopsis thaliana 21-26 35051687-6 2022 Using the high-resolution structure data and models of the taste receptors T1R2 and T1R3 in the AlphaFold Protein Structure Database, we performed a docking calculation on the receptors and report that brazzein is bound between the two cysteine rich domains (CRDs) of the heterodimer protein complex. Cysteine 236-244 taste 1 receptor member 2 Homo sapiens 75-79 35222471-6 2022 This post-translational modification targets the catalytic cysteine C265 and could protect the AtPTP1 protein from its irreversible oxidation by H2O2. Cysteine 59-67 protein tyrosine phosphatase 1 Arabidopsis thaliana 95-101 34994556-3 2022 Here, we have discovered a cysteine-reactive covalent ligand, EN106, that targets FEM1B, an E3 ligase recently discovered as the critical component of the cellular response to reductive stress. Cysteine 27-35 fem-1 homolog B Homo sapiens 82-87 35020600-2 2022 To solve this problem, we prepared a hGPx1 mutant (GPx1M) with high activity in an Escherichia coli BL21(DE3)cys auxotrophic strain using a single protein production (SPP) system. Cysteine 109-112 glutathione peroxidase 1 Homo sapiens 37-42 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. Cysteine 131-140 ATPase copper transporting beta Homo sapiens 31-34 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. Cysteine 131-140 CD163 molecule Homo sapiens 36-41 35574260-6 2022 Based on a site-specific cysteine engineering and anchoring method, we first characterized the stability and unfolding pathways of apo-NGAL. Cysteine 25-33 lipocalin 2 Homo sapiens 135-139 35574260-9 2022 Here, NGAL is stretched from the designed cysteine close to the cationic residues for a maximum unfolding effect. Cysteine 42-50 lipocalin 2 Homo sapiens 6-10 35308027-8 2022 However, taking advantage of two cysteine residues, C123 and C188, that flank the WF pocket and are unique to Rab27A and Rab27B among the >60 Rab family proteins, we used the quantitative Irreversible Tethering (qIT) assay to identify the first covalent ligands for native Rab27A. Cysteine 33-41 RAB27A, member RAS oncogene family Homo sapiens 110-116 35308027-8 2022 However, taking advantage of two cysteine residues, C123 and C188, that flank the WF pocket and are unique to Rab27A and Rab27B among the >60 Rab family proteins, we used the quantitative Irreversible Tethering (qIT) assay to identify the first covalent ligands for native Rab27A. Cysteine 33-41 RAB27B, member RAS oncogene family Homo sapiens 121-127 2479987-5 1989 However, all eight of the cysteines in PDGF-B were found to be conserved in human VPF, an indication that the folding of the two proteins is probably similar. Cysteine 26-35 platelet derived growth factor subunit B Homo sapiens 39-45 2576856-3 1989 The binding of calcium and the activation are modified by treatment with NBD-Cl and with PLP suggesting the presence of cysteine and lysine residues at the high affinity binding sites. Cysteine 120-128 proteolipid protein 1 Homo sapiens 89-92 2592414-0 1989 Neurite extension and neuronal survival activities of recombinant S100 beta proteins that differ in the content and position of cysteine residues. Cysteine 128-136 S100 calcium binding protein B Bos taurus 66-75 2592414-7 1989 When either of the two cysteines in S100 beta are altered by site-directed mutagenesis, the resultant proteins maintain the overall biochemical properties of S100 beta, but lose both the neurite extension and neuronal survival activities. Cysteine 23-32 S100 calcium binding protein B Bos taurus 36-45 2592414-7 1989 When either of the two cysteines in S100 beta are altered by site-directed mutagenesis, the resultant proteins maintain the overall biochemical properties of S100 beta, but lose both the neurite extension and neuronal survival activities. Cysteine 23-32 S100 calcium binding protein B Bos taurus 158-167 2592414-8 1989 However, another S100 beta mutant, in which the relative position of one of the two cysteines was changed, had neurotrophic activity similar to that of the unmodified protein. Cysteine 84-93 S100 calcium binding protein B Bos taurus 17-26 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. Cysteine 292-301 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. Cysteine 292-301 S100 calcium binding protein B Bos taurus 203-212 2556707-2 1989 By chromatographic analyses of the 3H-methyl amino acid generated by exhaustive proteolysis of purified PDE, followed by performic acid oxidation of the digest, we have shown that this modification occurs at a C-terminal cysteine residue of the alpha subunit of this enzyme. Cysteine 221-229 aldehyde dehydrogenase 7 family member A1 Homo sapiens 104-107 2556707-5 1989 Based on the C-terminal amino acid sequence of Cys-Cys-Val-Gln predicted from the alpha cDNA sequence, we conclude that PDE undergoes posttranslational modifications, including the proteolytic removal of two or three terminal amino acids, and methyl esterification of the alpha-carboxyl group of the terminal cysteine residue. Cysteine 309-317 aldehyde dehydrogenase 7 family member A1 Homo sapiens 120-123 2556136-0 1989 Substitution of an extracellular cysteine in the beta 2-adrenergic receptor enhances agonist-promoted phosphorylation and receptor desensitization. Cysteine 33-41 adrenoceptor beta 2 Homo sapiens 49-75 2611226-8 1989 Quantitation of the total free thiols of modified PEPCK shows that 2 mol of cysteine is lost per mole of inactivated enzyme. Cysteine 76-84 phosphoenolpyruvate carboxykinase 1 Rattus norvegicus 50-55 2507878-4 1989 Plasma levels of NAT and NAC increased rapidly, accompanied by a 25% increase in tyrosine levels and a 35% decrease in total cysteine. Cysteine 125-133 bromodomain containing 2 Homo sapiens 17-20 2507878-4 1989 Plasma levels of NAT and NAC increased rapidly, accompanied by a 25% increase in tyrosine levels and a 35% decrease in total cysteine. Cysteine 125-133 X-linked Kx blood group Homo sapiens 25-28 2583128-4 1989 We conclude that ORF1 (which contains a characteristic cysteine residue) functions as a condensing enzyme, possibly as part of a heterodimeric protein including the product of ORF2. Cysteine 55-63 hypothetical protein Escherichia coli 176-180 2764900-4 1989 The purified mucin was fractionated according to buoyant density and chemically radiolabelled on tyrosine or cysteine residues and digested with specific proteinases. Cysteine 109-117 solute carrier family 13 member 2 Rattus norvegicus 13-18 2737278-2 1989 Rat and murine IFN-alpha subspecies carry a fifth Cys (Cys-86) which is not conserved in bovine and human IFN-alpha subspecies except for human IFN-alpha 1. Cysteine 50-53 interferon alpha Mus musculus 15-24 2737278-2 1989 Rat and murine IFN-alpha subspecies carry a fifth Cys (Cys-86) which is not conserved in bovine and human IFN-alpha subspecies except for human IFN-alpha 1. Cysteine 55-58 interferon alpha Mus musculus 15-24 2737278-5 1989 This suggests that in contrast to human and bovine IFN-alpha, Cys-86 in rodent IFN-alpha plays a crucial role in receptor binding. Cysteine 62-65 interferon alpha-A Bos taurus 79-88 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. Cysteine 96-104 CD8a molecule Homo sapiens 131-140 2523737-3 1989 De novo synthesis of Lp(a) by cultured hepatocytes was demonstrated by incorporation of [35S]cysteine. Cysteine 93-101 apolipoprotein(a) Papio anubis 21-26 2540197-2 1989 We report that a cysteine residue in the human beta 2-adrenergic receptor (beta 2AR) is covalently modified by thioesterification with palmitic acid. Cysteine 17-25 adrenoceptor beta 2 Homo sapiens 47-73 2540197-2 1989 We report that a cysteine residue in the human beta 2-adrenergic receptor (beta 2AR) is covalently modified by thioesterification with palmitic acid. Cysteine 17-25 adrenoceptor beta 2 Homo sapiens 75-83 2497104-0 1989 Characterization of synapsin I fragments produced by cysteine-specific cleavage: a study of their interactions with F-actin. Cysteine 53-61 synapsin I Homo sapiens 20-30 2497105-9 1989 A study of synapsin I fragments obtained by cysteine-specific cleavage showed that the collagenase-resistant head domain actively bound to phospholipid vesicles; in contrast, the collagenase-sensitive tail domain, though strongly basic, did not significantly interact. Cysteine 44-52 synapsin I Homo sapiens 11-21 2497106-6 1989 Hydrophobic photolabeling followed by cysteine-specific cleavage of synapsin I demonstrated that the head domain of synapsin I penetrates into the hydrophobic core of the bilayer. Cysteine 38-46 synapsin I Homo sapiens 68-78 2497106-6 1989 Hydrophobic photolabeling followed by cysteine-specific cleavage of synapsin I demonstrated that the head domain of synapsin I penetrates into the hydrophobic core of the bilayer. Cysteine 38-46 synapsin I Homo sapiens 116-126 2703489-4 1989 Two cysteine residues that correspond to cysteins 128 and 142 of the Torpedo nAChR alpha subunit are present in beta 3. Cysteine 4-12 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 77-82 2703489-4 1989 Two cysteine residues that correspond to cysteins 128 and 142 of the Torpedo nAChR alpha subunit are present in beta 3. Cysteine 41-49 cholinergic receptor nicotinic alpha 2 subunit Rattus norvegicus 77-82 2468158-2 1989 In addition, two specific cysteine-rich segments common to the amino-terminal regions of C7, C8 alpha, C8 beta, and C9 also occur in their expected positions in C6, suggesting functional significance. Cysteine 26-34 complement C7 Homo sapiens 89-110 2918319-2 1989 The deduced amino acid sequence possesses characteristics expected of a nAChR subunit that does not bind acetylcholine, in addition to distinctive features such as unique cysteine residues and N-linked glycosylation sites. Cysteine 171-179 cholinergic receptor nicotinic beta 1 subunit Rattus norvegicus 72-77 2464704-5 1989 The cleavage site between the signal peptide and the external env glycoprotein resides between the cysteine residue at position 21 and the threonine residue at position 22, starting from the first residue after the env gene initiator methionine. Cysteine 99-107 endogenous retrovirus group K member 20 Homo sapiens 62-65 2464704-5 1989 The cleavage site between the signal peptide and the external env glycoprotein resides between the cysteine residue at position 21 and the threonine residue at position 22, starting from the first residue after the env gene initiator methionine. Cysteine 99-107 endogenous retrovirus group K member 20 Homo sapiens 215-218 2721538-6 1989 In contrast, the administration of 2 g NAC together with paracetamol resulted in an increase in the AUC of cysteine (+29.2 nmol.ml-1.h) and glutathione (+4.6 nmol.ml-1.h). Cysteine 107-115 X-linked Kx blood group Homo sapiens 39-42 2721538-7 1989 The data show that NAC leads to a marked increase in circulating cysteine, in part by reacting with cystine and thereby forming mixed disulphides with cysteine and releasing free cysteine as shown in vitro. Cysteine 65-73 X-linked Kx blood group Homo sapiens 19-22 2721538-7 1989 The data show that NAC leads to a marked increase in circulating cysteine, in part by reacting with cystine and thereby forming mixed disulphides with cysteine and releasing free cysteine as shown in vitro. Cysteine 151-159 X-linked Kx blood group Homo sapiens 19-22 2721538-7 1989 The data show that NAC leads to a marked increase in circulating cysteine, in part by reacting with cystine and thereby forming mixed disulphides with cysteine and releasing free cysteine as shown in vitro. Cysteine 151-159 X-linked Kx blood group Homo sapiens 19-22 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. Cysteine 180-188 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 117-134 2918254-14 1989 The results indicate that reactive cysteine(s) are localized in the catalytic site of HMG-CoA reductase. Cysteine 35-43 3-hydroxy-3-methylglutaryl-CoA reductase Rattus norvegicus 86-103 3233215-8 1988 U.S.A. 76, 4966-4970] suggested that the two thiols cross-linked were SH1 (Cys-707) and SH2 (Cys-697) from the myosin heavy chain. Cysteine 75-78 PBV1SPCR2 Oryctolagus cuniculus 111-129 3233215-8 1988 U.S.A. 76, 4966-4970] suggested that the two thiols cross-linked were SH1 (Cys-707) and SH2 (Cys-697) from the myosin heavy chain. Cysteine 93-96 PBV1SPCR2 Oryctolagus cuniculus 111-129 3192520-9 1988 Tryptic digestion and amino acid sequencing of Gt alpha indicated that both Cys-347 near the carboxyl terminus and Cys-210 between the second and third consensus sequences forming the GTP-binding site were derivatized by 125I-ACTP in a ratio of approximately 70 and 30%, respectively. Cysteine 76-79 integrin subunit alpha 2b Homo sapiens 47-55 3192520-9 1988 Tryptic digestion and amino acid sequencing of Gt alpha indicated that both Cys-347 near the carboxyl terminus and Cys-210 between the second and third consensus sequences forming the GTP-binding site were derivatized by 125I-ACTP in a ratio of approximately 70 and 30%, respectively. Cysteine 115-118 integrin subunit alpha 2b Homo sapiens 47-55 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 37-40 integrin subunit alpha 2b Homo sapiens 18-26 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 48-51 integrin subunit alpha 2b Homo sapiens 18-26 3192520-13 1988 Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin. Cysteine 48-51 integrin subunit alpha 2b Homo sapiens 18-26 3264556-8 1988 Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. Cysteine 31-39 nidogen 1 Mus musculus 0-8 3264556-8 1988 Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. Cysteine 76-84 nidogen 1 Mus musculus 0-8 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. Cysteine 167-170 cathepsin D Bos taurus 116-127 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. Cysteine 241-244 cathepsin D Bos taurus 116-127 2841469-3 1988 In the present study, using metabolic labeling of viral proteins with [35S]cysteine, radioimmunoprecipitation, and carbohydrate structure analysis, we have identified a higher-molecular-weight endo-H-resistant env gene-encoded polyprotein designated gPr115env in addition to the endo-H-sensitive gPr77env. Cysteine 75-83 endogenous retrovirus group K member 20 Homo sapiens 210-213 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. Cysteine 67-76 amphiregulin Homo sapiens 0-2 2849255-4 1988 The encoded NS1 proteins had a very high molar ratio of cysteine residues. Cysteine 56-64 influenza virus NS1A binding protein Homo sapiens 12-15 3182770-4 1988 IAANS binds to Cys-133 of TnI and DANZ to Met-25 in the low affinity Ca2+-binding sites of TnC. Cysteine 15-18 tenascin C Homo sapiens 91-94 3167041-5 1988 The organization of the molecule is very similar to that of the mouse laminin B1 chain, and significant sequence homology between the B1 and B2 chains was found in their two cysteine-rich domains and in their amino-terminal globular domains. Cysteine 174-182 B.burgdorferi-associated arthritis 2 Mus musculus 134-143 3162238-7 1988 In contrast, the synthesis of SPARC (secreted protein acidic rich in cysteine/osteonectin was stimulated approximately two-fold by TGF-beta, but only in fibroblastic populations. Cysteine 69-77 secreted protein acidic and cysteine rich Rattus norvegicus 30-35 2835654-2 1988 There are eight conserved Cys residues between PDGF-B and the v-sis protein. Cysteine 26-29 platelet derived growth factor subunit B Homo sapiens 47-53 3242443-2 1988 Metabolism of HCBD involves conjugation with glutathione followed by formation of the cysteine conjugate S-(pentachloro-1,3-butadienyl) cysteine (PCBD-CYS) and then the mercapturic acid N-acetyl-S-pentachloro-1,3-butadienyl-cysteine (PCBD-NAC). Cysteine 86-94 pterin-4 alpha-carbinolamine dehydratase 1 Rattus norvegicus 146-150 3242443-2 1988 Metabolism of HCBD involves conjugation with glutathione followed by formation of the cysteine conjugate S-(pentachloro-1,3-butadienyl) cysteine (PCBD-CYS) and then the mercapturic acid N-acetyl-S-pentachloro-1,3-butadienyl-cysteine (PCBD-NAC). Cysteine 86-94 pterin-4 alpha-carbinolamine dehydratase 1 Rattus norvegicus 234-238 2966343-1 1988 We have identified a metalloendoprotease from rat kidney cortex that cleaves the cysteine-phenylalanine bond (Cys7-Phe8) within the 17 amino acid ring structure of atrial natriuretic factor (ANF). Cysteine 81-89 natriuretic peptide A Rattus norvegicus 164-189 2966343-1 1988 We have identified a metalloendoprotease from rat kidney cortex that cleaves the cysteine-phenylalanine bond (Cys7-Phe8) within the 17 amino acid ring structure of atrial natriuretic factor (ANF). Cysteine 81-89 natriuretic peptide A Rattus norvegicus 191-194 3676320-3 1987 Under approximately physiological ionic conditions (0.1 M NaCl) addition of two HMG2 molecules per nucleosome, labeled by N-(3-pyrene)maleimide at the sulfhydryl groups of Cys-110 of histones H3, resulted in a decrease of the pyrene excimer fluorescence corresponding to the slight movement of the sulfhydryl groups of the two histone H3 molecules apart. Cysteine 172-175 high mobility group protein B2 Bos taurus 80-84 2828773-3 1987 The present work is based on our previous findings that the locus of the age-related modifications in GPDH is in the nicotinamide-binding site, where the catalytically active Cys-149 residue is located, and that an increase in oxidation potential occurs in old animal tissues which may enable various oxidizing agents to play a significant role in the inactivation of certain enzymes. Cysteine 175-178 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 102-106 2828773-4 1987 Thus it has been suggested that the loss of specific activity observed in old GPDH may be due to subtle and irreversible conformational changes caused by reaction of Cys-149 with these agents. Cysteine 166-169 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 78-82 2828773-5 1987 The circularly polarized luminescence (CPL) spectrum emitted by the fluorescent sulfhydryl reagent I-AEDANS covalently bound to GPDH through Cys-149 at the nicotinamide binding site, revealed a significant difference in conformation between these sites in young and old GPDH forms. Cysteine 141-144 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 128-132 2828773-5 1987 The circularly polarized luminescence (CPL) spectrum emitted by the fluorescent sulfhydryl reagent I-AEDANS covalently bound to GPDH through Cys-149 at the nicotinamide binding site, revealed a significant difference in conformation between these sites in young and old GPDH forms. Cysteine 141-144 glyceraldehyde-3-phosphate dehydrogenase Rattus norvegicus 270-274 3676297-2 1987 This was accomplished by using TnC fluorescently modified at Cys-98 with N-(iodoacetyl)-N"-(5-sulfo-1-naphthyl)ethylenediamine for the first complex and TnI labeled at Cys-133 with the same probe for the other complex. Cysteine 61-64 tenascin C Homo sapiens 31-34 3676297-2 1987 This was accomplished by using TnC fluorescently modified at Cys-98 with N-(iodoacetyl)-N"-(5-sulfo-1-naphthyl)ethylenediamine for the first complex and TnI labeled at Cys-133 with the same probe for the other complex. Cysteine 168-171 tenascin C Homo sapiens 31-34 3659572-7 1987 Following CAF coadministration with ACM, the K" values for the sulfate-, mercapturate-, cysteine-, and methylthio metabolites were decreased approximately 35%, 56%, 42%, and 47%, respectively. Cysteine 88-96 caffeine susceptibility Mus musculus 10-13 3112579-8 1987 All four mutations that altered invariant cysteine or histidine residues led to an adr1 null phenotype. Cysteine 42-50 DNA-binding transcription factor ADR1 Saccharomyces cerevisiae S288C 83-87 3597435-1 1987 Recent results using proteases suggest that dexamethasone 21-mesylate (Dex-Mes) labeling of the rat hepatoma tissue culture (HTC) cell glucocorticoid receptor occurs at one or a few closely grouped cysteine residues (Simons, S.S., Jr. (1987) J. Biol. Cysteine 198-206 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 135-158 3597435-12 1987 We, therefore, conclude that the single Dex-Mes-labeled site of the HTC cell glucocorticoid receptor has been identified as Cys-656. Cysteine 124-127 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 77-100 3597435-13 1987 Since several lines of evidence indicate that [3H]Dex-Mes labeling of the receptor occurs in the steroid binding site, Cys-656 is the first amino acid which can be directly associated with a particular property of the glucocorticoid receptor. Cysteine 119-122 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 218-241 3040038-4 1987 Via the incorporated anchor group the undecapeptide was linked selectively at its N-terminus to the cysteine residue 107 of iso-1-cytochrome c to yield a well characterized conjugate of 1:1 stoichiometry for immunization experiments. Cysteine 100-108 cytochrome c, somatic Canis lupus familiaris 130-142 3608085-3 1987 Binding of [14C]CCl4 to histones and NHCP was also determined in the presence of 5 mM L-cysteine. Cysteine 86-96 chemokine (C-C motif) ligand 4 Mus musculus 16-20 3608085-4 1987 The results show that the activated intermediate of CCl4 bound more to histones than to NHCP in a dose- and time-dependent manner, and that 5 mM L-cysteine inhibited the binding of the activated intermediate of CCl4 to histones by 59%, without affecting the binding to NHCP. Cysteine 145-155 chemokine (C-C motif) ligand 4 Mus musculus 52-56 3608085-4 1987 The results show that the activated intermediate of CCl4 bound more to histones than to NHCP in a dose- and time-dependent manner, and that 5 mM L-cysteine inhibited the binding of the activated intermediate of CCl4 to histones by 59%, without affecting the binding to NHCP. Cysteine 145-155 chemokine (C-C motif) ligand 4 Mus musculus 211-215 3608085-5 1987 These data suggest different extents of alkylation or acylation between histones and NHCP by metabolically activated CCl4 under aerobic in vitro conditions, and differential inhibition of CCl4-alkylation-acylation by cysteine. Cysteine 217-225 chemokine (C-C motif) ligand 4 Mus musculus 188-192 3567362-1 1987 Erythropoietin (EPO) biosynthetically labelled with [35S]cysteine was produced from Chinese hamster ovary (CHO) cells containing amplified copies of human EPO cDNA. Cysteine 57-65 erythropoietin Cricetulus griseus 0-14 3567362-1 1987 Erythropoietin (EPO) biosynthetically labelled with [35S]cysteine was produced from Chinese hamster ovary (CHO) cells containing amplified copies of human EPO cDNA. Cysteine 57-65 erythropoietin Cricetulus griseus 16-19 2956090-7 1987 In addition to the variable amino-terminal region, the external domain of human T200 glycoprotein consists of a second cysteine-rich region of about 400 amino acids, a single transmembrane-spanning region and a large cytoplasmic domain of 707 amino acids shared by all of the structural variants and highly conserved between species. Cysteine 119-127 protein tyrosine phosphatase receptor type C Homo sapiens 80-97 3815338-3 1987 Transport of melphalan by BALB/c 3T3 fibroblasts was mediated by the two amino acid transport systems, the DL-beta-2-aminobicyclo(2,2,1)heptane-2-carboxylic acid-sensitive sodium-independent system preferring leucine as substrate and the sodium-dependent system preferring alanine, serine, and cysteine as substrates. Cysteine 294-302 hemoglobin, beta adult minor chain Mus musculus 110-116 2438872-6 1987 The ratio between 2-S-cysteinyldopa and 5-S-cysteinyldopa when incubating dopa and cysteine with tyrosinase was identical with the ratio between the analogically synthetised isomers of glutathionyldopa. Cysteine 83-91 tyrosinase Homo sapiens 97-107 2959500-11 1987 The Cd1Zn2(cys)9 cluster is homologous with a 12 atom fragment of the Cd4(cys)11 cluster. Cysteine 11-14 Cd4 molecule Rattus norvegicus 70-73 2959500-11 1987 The Cd1Zn2(cys)9 cluster is homologous with a 12 atom fragment of the Cd4(cys)11 cluster. Cysteine 74-77 Cd4 molecule Rattus norvegicus 70-73 3027247-0 1987 Analysis of the role of the cysteine 171 residue in the activity of herpes simplex virus type 1 thymidine kinase by oligonucleotide-directed mutagenesis. Cysteine 28-36 involved in nucleotide metabolism Human alphaherpesvirus 1 96-112 3028776-4 1986 Sequence analysis of the cDNA clone revealed that the Ly-6E.1 protein consists of a 26-amino acid leader followed by a 108-residue, cysteine-rich, core protein with no N-linked glycosylation sites. Cysteine 132-140 lymphocyte antigen 6 complex, locus A Mus musculus 54-61 3801403-4 1986 Spectroscopic studies on the intrinsic absorption and fluorescence properties of S100 alpha alpha and S100b proteins chemically modified on cysteines-85 alpha and -84 beta with iodoacetamide completed this study. Cysteine 140-149 S100 calcium binding protein B Bos taurus 102-107 3023062-6 1986 The GTP binding regions of p21 ras and a C-terminal cysteine involved in membrane anchoring are also present in ral; this strongly suggests that ral is a GTP binding protein with membrane localization. Cysteine 52-60 RAS like proto-oncogene A Homo sapiens 112-115 3023062-6 1986 The GTP binding regions of p21 ras and a C-terminal cysteine involved in membrane anchoring are also present in ral; this strongly suggests that ral is a GTP binding protein with membrane localization. Cysteine 52-60 RAS like proto-oncogene A Homo sapiens 145-148 3096851-7 1986 Of these four inhibitors and three thiol compounds also tested, PEAA was the least and cysteine the most effective against tyrosinase. Cysteine 87-95 tyrosinase Homo sapiens 123-133 2424021-0 1986 Antigenic crossreactivity of the alpha subunit of complement component C8 with the cysteine-rich domain shared by complement component C9 and low density lipoprotein receptor. Cysteine 83-91 complement C9 Homo sapiens 114-137 2424021-1 1986 Complement component C9 contains two distinct cysteine-rich domains exhibiting high sequence resemblance to a domain present in the low density lipoprotein (LDL) receptor and epidermal growth factor precursor, respectively. Cysteine 46-54 complement C9 Homo sapiens 0-23 3941095-12 1986 We have studied Ca2+-induced changes in the region C89-100 by monitoring the fluorescence of troponin C (TnC) labeled at Cys-98 with 5-(iodoacetamidoethyl)aminonaphthalene-1-sulfonic acid. Cysteine 121-124 tenascin C Homo sapiens 93-103 3941095-12 1986 We have studied Ca2+-induced changes in the region C89-100 by monitoring the fluorescence of troponin C (TnC) labeled at Cys-98 with 5-(iodoacetamidoethyl)aminonaphthalene-1-sulfonic acid. Cysteine 121-124 tenascin C Homo sapiens 105-108 3002791-4 1986 When TnC is labelled at Cys-98 with a maleimide spin probe (MSL), the spin signal is sensitive to Ca2+ binding to both the high and the low-affinity sites of TnC in the presence of either or both of the other two troponin subunits. Cysteine 24-27 tenascin C Homo sapiens 5-8 3002791-4 1986 When TnC is labelled at Cys-98 with a maleimide spin probe (MSL), the spin signal is sensitive to Ca2+ binding to both the high and the low-affinity sites of TnC in the presence of either or both of the other two troponin subunits. Cysteine 24-27 tenascin C Homo sapiens 158-161 3002791-5 1986 Since Cys-98 is located in the vicinity of one of the high-affinity sites, these results are indicative of a long-range interaction between the two halves of the TnC molecule. Cysteine 6-9 tenascin C Homo sapiens 162-165 3092198-7 1986 The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. Cysteine 52-55 secretin Rattus norvegicus 13-21 3092198-7 1986 The smallest secretin activity was observed with [1-Cys,6-Cys]secretin in the oxidized form. Cysteine 52-55 secretin Rattus norvegicus 62-70 2867670-3 1985 Cysteinylglycine, the first metabolite in the glutathione breakdown by gamma-glutamyltranspeptidase, showed a rapid and equimolar reactivity to acetaldehyde and such was comparable to the reaction seen with L-cysteine or D-penicillamine. Cysteine 207-217 inactive glutathione hydrolase 2 Homo sapiens 71-99 2994062-7 1985 In contrast to the human cardiac muscle actin gene, the aorta-type smooth muscle actin gene, and the stomach-type smooth muscle actin gene, the beta-actin gene lacks the codon for cysteine between the ATG initiation codon and the codon for the NH2-terminal amino acid of the mature protein. Cysteine 180-188 POTE ankyrin domain family member F Homo sapiens 144-154 2859127-2 1985 The inhibitory effects of cysteine (Cys), GSH and D-alpha-tocopherol on ODC induction were proportional to their abilities to decrease the incidence of skin tumors in the initiation-promotion protocol. Cysteine 26-34 ornithine decarboxylase, structural 1 Mus musculus 72-75 2859127-2 1985 The inhibitory effects of cysteine (Cys), GSH and D-alpha-tocopherol on ODC induction were proportional to their abilities to decrease the incidence of skin tumors in the initiation-promotion protocol. Cysteine 36-39 ornithine decarboxylase, structural 1 Mus musculus 72-75 2859127-5 1985 Since the inhibitory effects of Cys on both the decrease in the ratio of GSH/GSSG and the induction of ODC activity by TPA were greatly reduced by the inhibitors of gamma-glutamyl transpeptidase and gamma-glutamylcysteine synthetase, it is suggested that some of the inhibitory effects of Glu, Cys and Gly on tumor promotion could result from their interference with the metabolism of the tripeptide GSH, a natural antioxidant which inhibits chemical carcinogenesis. Cysteine 32-35 ornithine decarboxylase, structural 1 Mus musculus 103-106 2859127-5 1985 Since the inhibitory effects of Cys on both the decrease in the ratio of GSH/GSSG and the induction of ODC activity by TPA were greatly reduced by the inhibitors of gamma-glutamyl transpeptidase and gamma-glutamylcysteine synthetase, it is suggested that some of the inhibitory effects of Glu, Cys and Gly on tumor promotion could result from their interference with the metabolism of the tripeptide GSH, a natural antioxidant which inhibits chemical carcinogenesis. Cysteine 294-297 ornithine decarboxylase, structural 1 Mus musculus 103-106 3871661-4 1985 Injection of MBL-2 tumor-bearing mice with MVE-2, at 3 days after Cy treatment, caused a decrease in tumor burden and a significant increase in median survival time as compared to treatment with CY alone. Cysteine 66-68 mannose-binding lectin (protein C) 2 Mus musculus 13-18 3840106-1 1985 We utilized a cDNA encoding the cysteine-rich, tyrosine-containing mouse protamine, mouse protamine 1 (MP1), to detect the presence of several classes of differentiating germ cells in testicular extracts from wild-type and male sterile mutant mice. Cysteine 32-40 protamine 1 Mus musculus 90-101 3836241-2 1985 Oxidation of hemoglobin to methemoglobin under aerobic conditions is induced by nitrite, catalyzed by methemoglobin in the presence of hydrogen peroxide, and inhibited by chemical reagents ranging from cysteine and ascorbic acid to sulfite. Cysteine 202-210 hemoglobin subunit gamma 2 Homo sapiens 27-40 6501297-2 1984 The resonance Raman spectrum of CH3OC(=O)-Phe-NHCH2C(=S)S-cathepsin B, where the thiol S is from the active-site cysteine residue, is compared to that of the corresponding papain acyl-enzyme. Cysteine 113-121 cathepsin B Homo sapiens 58-69 6094532-8 1984 The C3 alpha chain contains 24 cysteine residues, 10 of these clustered in the C-terminal 175 amino acids of the alpha chain. Cysteine 31-39 complement C3 Homo sapiens 4-12 6501279-3 1984 The inhibitor with pI 5.0 (TPI-2) was inactive in the absence of reducing agents but was converted to an active inhibitor on addition of reducing agents such as dithiothreitol, GSH, cysteine, or 2-mercaptoethanol. Cysteine 182-190 triosephosphate isomerase 1 Rattus norvegicus 27-30 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. Cysteine 5-8 triosephosphate isomerase 1 Rattus norvegicus 79-82 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. Cysteine 19-27 triosephosphate isomerase 1 Rattus norvegicus 79-82 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. Cysteine 150-158 triosephosphate isomerase 1 Rattus norvegicus 79-82 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. Cysteine 168-171 triosephosphate isomerase 1 Rattus norvegicus 79-82 6238407-3 1984 For example, papain has been converted into a highly effective oxidoreductase by covalent modification of the sulfhydryl group of the active site cysteine residue (Cys25) with flavins such as 8-bromoacetyl-10-methylisoalloxazine. Cysteine 146-154 thioredoxin reductase 1 Homo sapiens 63-77 6235126-4 1984 The activation by Cd2+ of MLCK was inhibited by anticalmodulins (e.g., R-24571), whereas the inhibition by a higher Cd2+ concentration of MLCK and PL-Ca-PK was reversed by thiol agents (e.g., cysteine). Cysteine 192-200 Cd2 molecule Rattus norvegicus 18-21 6707022-3 1984 Cleavage of protein 4.1 at cysteine residues by 2-nitro-5-thiocyanobenzoic acid produces a series of doublets which differ by approximately 2,000 daltons and have identical peptide maps. Cysteine 27-35 erythrocyte membrane protein band 4.1 Homo sapiens 12-23 6421651-2 1984 Following a treatment with 0.5 mM Cd2+ for short periods (1, 5 min), the tension to high-K+ returned to a greater extent after washing with disodium edetate (EDTA) or cysteine, compared to normal medium. Cysteine 167-175 T-cell surface antigen CD2 Cavia porcellus 34-37 6323385-3 1983 The cysteine residue of this calmodulin is located at the 27th position from the NH2-terminal (Yazawa, M. et al. Cysteine 4-12 CaM5 Triticum aestivum 29-39 6323385-8 1983 According to the quantitative analysis of the reaction of 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB) with Cys 27, the calmodulin which binds 3 Ca2+ showed the minimum reactivity with DTNB. Cysteine 106-109 CaM5 Triticum aestivum 118-128 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. Cysteine 140-148 BOC cell adhesion associated, oncogene regulated Homo sapiens 64-67 786982-3 1976 The two samples of cysteine formed in this reaction were analyzed for their configuration at C-3. Cysteine 19-27 complement C3 Homo sapiens 93-96 1261042-9 1976 Therefore gamma-glutamyl-cysteine is produced in excessive amounts and it is subsequently converted to 5-oxoproline (and cysteine) by gamma-glutamyl cyclotransferase. Cysteine 25-33 gamma-glutamylcyclotransferase Homo sapiens 134-165 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. Cysteine 57-64 LOC105613195 Ovis aries 180-187 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. Cysteine 58-61 glyceraldehyde-3-phosphate dehydrogenase Sus scrofa 81-121 4214552-0 1974 Stereospecific irreversible inhibition of histidine ammonia-lyase by L-cysteine. Cysteine 69-79 histidine ammonia-lyase Homo sapiens 42-65 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). Cysteine 87-90 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 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). Cysteine 95-98 arginine vasopressin Bos taurus 57-71 4386590-0 1968 [Cystine and cysteine content of the green coffee bean protein]. Cysteine 13-21 brain expressed associated with NEDD4 1 Homo sapiens 50-54 33827045-5 2021 Laccase, tyrosinase, and protein disulfide isomerase form cross-links between tyrosine and cysteine residues by generating radicals. Cysteine 91-99 tyrosinase Homo sapiens 9-19 33909912-5 2021 Syk inhibition upregulates glycine level and downstream transsulfuration cysteine biosynthesis, promoting cysteine metabolism and cellular hydrogen sulfide (H2 S) production. Cysteine 73-81 spleen tyrosine kinase Mus musculus 0-3 33909912-5 2021 Syk inhibition upregulates glycine level and downstream transsulfuration cysteine biosynthesis, promoting cysteine metabolism and cellular hydrogen sulfide (H2 S) production. Cysteine 106-114 spleen tyrosine kinase Mus musculus 0-3 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. Cysteine 23-31 thioredoxin 1 Mus musculus 85-96 33964134-2 2021 Here, we have developed a novel human serum albumin-adrenomedullin (HSA-AM) conjugate, which was synthesized by the covalent attachment of a maleimide derivative of adrenomedullin to the 34th cysteine residue of human serum albumin via a linker. Cysteine 192-200 adrenomedullin Homo sapiens 52-66 33964134-2 2021 Here, we have developed a novel human serum albumin-adrenomedullin (HSA-AM) conjugate, which was synthesized by the covalent attachment of a maleimide derivative of adrenomedullin to the 34th cysteine residue of human serum albumin via a linker. Cysteine 192-200 adrenomedullin Homo sapiens 165-179 33938042-5 2021 More importantly, a sensitive L -Cys colorimetric detection is developed with the sensitivity of 0.023 muM -1 and the detection limit at least 0.018 muM in the linear range of 1-20 muM, which is by far the best enzyme-mimetic performances, to the best our knowledge. Cysteine 30-36 PWWP domain containing 3A, DNA repair factor Homo sapiens 103-109 33774492-0 2021 Discovery of novel quinazoline-based covalent inhibitors of KRAS G12C with various cysteine-targeting warheads as potential anticancer agents. Cysteine 83-91 KRAS proto-oncogene, GTPase Homo sapiens 60-64 33432415-6 2021 NGAL and RBP-4 were present in above 85% of the population, with mean concentrations of 78.5 +- 143.9 and 139.4 +- 131.7 ng/g creatinine, respectively, OPN (64%) with a mean concentration of 642.6 +- 723.3 ng/g g creatinine, and Cys-C with a mean concentration of 33.72 +- 44.96 ng/g creatinine. Cysteine 229-232 lipocalin 2 Homo sapiens 0-4 33930333-2 2021 In aerobic conditions, a cysteine residue bound to two metal ions in its ancient, catalytic subunit RTCB could make the tRNA-LC susceptible to oxidative inactivation. Cysteine 25-33 RNA 2',3'-cyclic phosphate and 5'-OH ligase Homo sapiens 100-104 33835773-8 2021 This method was qualified for the measurement of naked monoclonal antibody (mAb), a site-specific cysteine-conjugated ADC with drug to antibody ratio ~2 (DAR2) and a site-nonspecific cysteine-conjugated ADC (DAR8) in rat plasma. Cysteine 98-106 antizyme inhibitor 2 Rattus norvegicus 118-121 33378104-3 2021 We identified the cysteine residues, the hydrophobic core tetrapeptide, as well as the C-terminal negative charge as key factors for HIV-1 inhibitory activity of P6-2. Cysteine 18-26 sequestosome 1 Homo sapiens 162-166 33848522-0 2021 Inactivation of cysteine 674 in the sarcoplasmic/endoplasmic reticulum calcium ATPase 2 causes retinopathy in the mouse. Cysteine 16-24 ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 Mus musculus 36-87 33848522-2 2021 The irreversible oxidation of cysteine 674 (C674) in the sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) was increased in the type 1 diabetic retinal vasculature. Cysteine 30-38 ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 Mus musculus 57-108 33848522-2 2021 The irreversible oxidation of cysteine 674 (C674) in the sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) was increased in the type 1 diabetic retinal vasculature. Cysteine 30-38 ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 Mus musculus 110-116 33921425-7 2021 The key component of this pathway is Mia40 (called CHCHD4 in human cells), which itself contains cysteine motifs and is subject to redox regulation. Cysteine 97-105 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 37-42 33921425-7 2021 The key component of this pathway is Mia40 (called CHCHD4 in human cells), which itself contains cysteine motifs and is subject to redox regulation. Cysteine 97-105 coiled-coil-helix-coiled-coil-helix domain containing 4 Homo sapiens 51-57 33787949-0 2021 Are cysteine residues of human phospholipid scramblase 1 essential for Pb2+ and Hg2+ binding-induced scrambling of phospholipids? Cysteine 4-12 phospholipid scramblase 1 Homo sapiens 31-56 33724210-3 2021 The cysteine knot motif of TGF-beta can stabilize the structure of MSTN protein and plays an important regulatory role in the biological function of MSTN. Cysteine 4-12 transforming growth factor alpha Sus scrofa 27-35 33389794-7 2021 In addition, we found that USP21 regulated cell proliferation via cysteine 221, the catalytic site of USP21. Cysteine 66-74 ubiquitin specific peptidase 21 Homo sapiens 27-32 33389794-7 2021 In addition, we found that USP21 regulated cell proliferation via cysteine 221, the catalytic site of USP21. Cysteine 66-74 ubiquitin specific peptidase 21 Homo sapiens 102-107 33627626-8 2021 Mechanistically, both the DOC and HECT domains of HECTD3 directly interacted with TRAF3, and the catalytic Cys (C832) in the HECT domain promoted the K63-linked polyubiquitination of TRAF3 at Lys138. Cysteine 107-110 Tnf receptor-associated factor 3 Rattus norvegicus 183-188 33574344-10 2021 Individuals with a cysteine substitution in the UMOD gene appeared to have a better prognosis than individuals with other amino acid substitutions (p = 0.015). Cysteine 19-27 uromodulin Homo sapiens 48-52 33522955-9 2021 RESULTS: Here, we reported that FOXC1 could inhibit the cysteine metabolism and increase reactive oxygen species (ROS) levels by regulating cysteine metabolism-related genes, cystathionine gamma-lyase (CTH). Cysteine 56-64 cystathionine gamma-lyase Homo sapiens 175-200 33434156-7 2021 Further, the palmitoylation status of cysteine residues at the 12th and 15th sites of the protein molecule could significantly affect cellular localization of GLB1L4 protein. Cysteine 38-46 beta-galactosidase-like protein Rattus norvegicus 159-165 33584650-1 2020 CD5, a member of the scavenger receptor cysteine-rich superfamily, is a marker for T cells and a subset of B cells (B1a). Cysteine 40-48 CD5 antigen Mus musculus 0-3 33475084-6 2021 PARP-13 is preferentially MARylated on cysteine residues in its RNA binding zinc finger domain. Cysteine 39-47 zinc finger CCCH-type containing, antiviral 1 Homo sapiens 0-7 33466952-12 2021 It has been proved that the present Rotaphone-CY model is a reliable instrument for measuring short-period seismic rotations of the amplitudes as small as 10-7 rad/s. Cysteine 46-48 RRAD, Ras related glycolysis inhibitor and calcium channel regulator Homo sapiens 160-163 33977473-2 2021 KRAS4b is processed at both the N- and C-terminus, resulting in an acetylation of the N-terminus (at Thr, after aminopeptidase removal of the original N-term Met) and farnesylation/carboxymethylation of the C-terminal Cys (after proteolytic cleavage of the original C-terminal three amino acids, Val-Iso-Met). Cysteine 218-221 KRAS proto-oncogene, GTPase Homo sapiens 0-6 33271457-2 2021 Sulfite oxidase is catalyzing the terminal reaction of cellular cysteine catabolism, the oxidation of sulfite to sulfate. Cysteine 64-72 sulfite oxidase Homo sapiens 0-15 33403257-1 2020 Serine/threonine phosphatase (Stp1) is known to be involved in the regulation of cysteine phosphorylation levels in many different pathways, such as virulence factor regulation in methicillin-resistant Staphylococcus aureus (MRSA). Cysteine 81-89 AT695_RS12880 Staphylococcus aureus 17-28 32181977-4 2020 We revealed CD9 lipidation at its three most frequent lipidated sites suffices for EWI-F binding, while cysteine to alanine CD9 mutations markedly reduced binding of EWI-F. Cysteine 104-112 CD9 molecule Homo sapiens 124-127 33022283-5 2020 Mechanistically, BAM co-inhibited inhibitor of nuclear factor kappaBalpha (IkappaBalpha) kinase subunit beta (IKKbeta) and exportin-1 (XPO-1; chromosome region maintenance 1, CRM1), which are two dysregulated onco-related proteins in TNBC cells, by covalently modifying key functional cysteine residues (Cys179 of IKKbeta, Cys528 of XPO-1). Cysteine 285-293 component of inhibitor of nuclear factor kappa B kinase complex Homo sapiens 110-117 33168755-3 2020 This was achieved by the generation of a library of Cys mutations in Env glycoprotein on the viral surface, covalent labeling of the Cys residues using a Cys-reactive label that masks epitope residues, followed by infection of the labeled mutant virions in mammalian cells in the presence of NAbs. Cysteine 52-55 endogenous retrovirus group K member 20 Homo sapiens 69-72 33330413-5 2020 Moreover, we have demonstrated that PEGylation of the cysteine variant of huG-CSF with higher molecular weight PEGs, such as 30 kDa PEG and 40 kDa PEG, leads to significantly prolonged leukocyte proliferation activity compared to the variant conjugated with 20 kDa PEG. Cysteine 54-62 hugger Mus musculus 74-77 32703050-4 2020 A depression of ALB FSR was observed 195 min after LPS challenge, independent of feeding group or LPS application route, which was not paralleled by a down-regulated ALB mRNA expression but by a reduced availability of free cysteine. Cysteine 224-232 albumin Sus scrofa 16-19 33112237-6 2020 We then transposed the cysteine mutation to the native receptor, to demonstrate with high pharmacological specificity that metabotropic glutamate receptor signaling triggers opening of GluD2. Cysteine 23-31 glutamate dehydrogenase 2 Homo sapiens 185-190 33169578-5 2020 We found that Sec-to-Cys mutation at residue of 498 significantly enhanced the efficiency of TrxR1-mediated menadione reduction, though the Sec498 is capable to catalyze the menadione reduction, indicating that TrxR1-mediated menadione reduction is dominantly in a Se-independent manner. Cysteine 21-24 thioredoxin reductase 1 Homo sapiens 93-98 33169578-5 2020 We found that Sec-to-Cys mutation at residue of 498 significantly enhanced the efficiency of TrxR1-mediated menadione reduction, though the Sec498 is capable to catalyze the menadione reduction, indicating that TrxR1-mediated menadione reduction is dominantly in a Se-independent manner. Cysteine 21-24 thioredoxin reductase 1 Homo sapiens 211-216 33028983-6 2021 Molecule docking analysis showed that the epoxy group of the UA metabolite reacted with Cys-163 of CASP3, forming a covalent bond with CASP3. Cysteine 88-91 caspase 3 Mus musculus 99-104 33028983-6 2021 Molecule docking analysis showed that the epoxy group of the UA metabolite reacted with Cys-163 of CASP3, forming a covalent bond with CASP3. Cysteine 88-91 caspase 3 Mus musculus 135-140 32470580-10 2020 In-silico molecular docking study of cobra CRISP with TLR4-MD2 receptor complex reveals Nk-CRISP engages cysteine-rich domain (CRD) to interact with complex. Cysteine 105-113 lymphocyte antigen 96 Homo sapiens 59-62 31961005-7 2020 As detected by fluorescence in situ hybridization analysis and subcellular fractionation assay, SNHG8 was primarily expressed in the nucleus and exerted suppressive role on reversion inducing cysteine-rich protein with kazal motifs (RECK) expression, which implied a potential transcriptional regulation of SNHG8 on RECK level. Cysteine 192-200 small nucleolar RNA host gene 8 Homo sapiens 96-101 32747794-6 2020 We show that MTAP loss upregulates polyamine metabolism which, concurrently with cysteine withdrawal, promotes elevated reactive oxygen species and prevents cell survival. Cysteine 81-89 methylthioadenosine phosphorylase Homo sapiens 13-17 33011677-7 2020 As a result, there is a decrease of cell oxidant levels and ADAM17 sheddase activity and an increase in the reduced cysteine-containing peptides in intracellular proteins in ADAM17cyto overexpressing cells. Cysteine 116-124 ADAM metallopeptidase domain 17 Homo sapiens 174-180 32820045-4 2020 Using a general reactivity probe, we generated a data set of proteomic cysteine residues sensitive to the reduction in fumarate levels caused by genetic reintroduction of active FH into HLRCC cell lines. Cysteine 71-79 fumarate hydratase Homo sapiens 178-180 32999931-2 2020 Herein we show that the enzyme tyrosinase is capable of oxidizing exposed tyrosine residues into o-quinones that react rapidly with cysteine residues on target proteins. Cysteine 132-140 tyrosinase Homo sapiens 31-41 32962355-4 2020 As a cysteine protease, PLpro is rich in cysteines and histidines, and their protonation/deprotonation modulates catalysis and conformational plasticity. Cysteine 41-50 cathepsin B Homo sapiens 5-22 32951003-8 2020 We further revealed that (+)-CLA specifically reacted with the Cys-151 residue of Keap1, which blocked Nrf2 ubiquitylation and resulted in an increased Nrf2 stability, thereby leading to the activation of the Keap1-Nrf2 pathway to prevent drug-induced hepatocyte ferroptosis. Cysteine 63-66 kelch-like ECH-associated protein 1 Mus musculus 82-87 32951003-8 2020 We further revealed that (+)-CLA specifically reacted with the Cys-151 residue of Keap1, which blocked Nrf2 ubiquitylation and resulted in an increased Nrf2 stability, thereby leading to the activation of the Keap1-Nrf2 pathway to prevent drug-induced hepatocyte ferroptosis. Cysteine 63-66 kelch-like ECH-associated protein 1 Mus musculus 209-214 32943614-1 2020 Four-octyl itaconate (4-OI) is the cell-permeable derivative of itaconate that can activate Nrf2 signaling by alkylating Keap1"s cysteine residues. Cysteine 129-137 kelch-like ECH-associated protein 1 Mus musculus 121-126 32805914-4 2020 To enhance the anti-diabetic effect of GLP1, we designed a human cysteine modified IgG1-Fc antibody-mediated oral gene delivery vehicle, which prolongs the half-life of GLP1, protect from acidic and enzymatic degradation in the gastrointestinal tract (GI), uptakes and transports through neonatal Fc receptor (FcRn), and helps to release the GLP1 gene in the intestine. Cysteine 65-73 LOC105243590 Mus musculus 83-87 32891325-6 2020 RESULTS: The remarkable difference of PTMs was that FNTA which means prenylated cysteine as regulator was significantly decreased in eCCA than that of control. Cysteine 80-88 farnesyltransferase, CAAX box, alpha Homo sapiens 52-56 32615144-6 2020 There are other Tsa2 structures in distinct redox states in public databases and all of them are decamers, with the peroxidatic cysteine very accessible to reductants, convenient features to investigate kinetics. Cysteine 128-136 radial spoke head component 1 Homo sapiens 16-20 32571875-8 2020 We show levels of PRL cysteine phosphorylation vary in response to culture conditions and in different tissues. Cysteine 22-30 prolactin Mus musculus 18-21 32818073-5 2020 Excitatory amino acid carrier 1 (EAAC1) is an excitatory amino acid transporter expressed specifically by neurons and is the route for the neuronal uptake of glutamate/aspartate/cysteine. Cysteine 178-186 solute carrier family 1 member 1 Rattus norvegicus 0-31 32818073-5 2020 Excitatory amino acid carrier 1 (EAAC1) is an excitatory amino acid transporter expressed specifically by neurons and is the route for the neuronal uptake of glutamate/aspartate/cysteine. Cysteine 178-186 solute carrier family 1 member 1 Rattus norvegicus 33-38 32632184-5 2020 We combine synthetic thiol-reactive nucleotide derivatives with recombinantly produced Fic enzymes containing strategically placed cysteines in their active sites to yield reactive binary probes for covalent substrate capture. Cysteine 131-140 C-C motif chemokine ligand 7 Homo sapiens 87-90 32571843-0 2020 Impact of Cysteine Residues on MHC Binding Predictions and Recognition by Tumor-Reactive T Cells. Cysteine 10-18 major histocompatibility complex, class I, C Homo sapiens 31-34 32571843-2 2020 Nevertheless, prediction algorithms appear to function poorly for epitopes containing cysteine (Cys) residues, which can oxidize and form disulfide bonds with other Cys residues under oxidizing conditions, thus potentially interfering with their ability to bind to MHC molecules. Cysteine 86-94 major histocompatibility complex, class I, C Homo sapiens 265-268 32571843-2 2020 Nevertheless, prediction algorithms appear to function poorly for epitopes containing cysteine (Cys) residues, which can oxidize and form disulfide bonds with other Cys residues under oxidizing conditions, thus potentially interfering with their ability to bind to MHC molecules. Cysteine 96-99 major histocompatibility complex, class I, C Homo sapiens 265-268 32571843-5 2020 Substitutions of AABA for Cys at putative MHC anchor positions often significantly enhanced T cell recognition, whereas substitutions at non-MHC anchor positions were neutral, except for one epitope where this modification abolished T cell recognition. Cysteine 26-29 major histocompatibility complex, class I, C Homo sapiens 42-45 32250617-2 2020 As previously reported, the tetrahydropyridopyrimidines were identified as irreversible covalent inhibitors of KRASG12C that bind in the switch-II pocket of KRAS and make a covalent bond to cysteine 12. Cysteine 190-198 KRAS proto-oncogene, GTPase Homo sapiens 111-115 32502343-2 2020 Here, we report the development of MFH290, a novel cysteine (Cys)-directed covalent inhibitor of CDK12/13. Cysteine 51-59 cyclin dependent kinase 12 Homo sapiens 97-105 32502343-2 2020 Here, we report the development of MFH290, a novel cysteine (Cys)-directed covalent inhibitor of CDK12/13. Cysteine 61-64 cyclin dependent kinase 12 Homo sapiens 97-105 32502343-3 2020 MFH290 forms a covalent bond with Cys-1039 of CDK12, exhibits excellent kinome selectivity, inhibits the phosphorylation of serine-2 in the C-terminal domain (CTD) of RNA-polymerase II (Pol II) and reduces the expression of key DNA damage repair genes. Cysteine 34-37 cyclin dependent kinase 12 Homo sapiens 46-51 32502343-4 2020 Importantly, these effects were demonstrated to be CDK12-dependent as mutation of Cys-1039 rendered the kinase refractory to MFH290 and restored Pol II CTD phosphorylation and DNA damage repair gene expression. Cysteine 82-85 cyclin dependent kinase 12 Homo sapiens 51-56 32637952-4 2020 As a cysteine protease, PLpro is rich in cysteines and histidines and their protonation/deprotonation modulates catalysis and conformational plasticity. Cysteine 41-50 cathepsin B Homo sapiens 5-22 32173650-4 2020 RESULTS: Both Cy/GVAX plus degarelix and degarelix alone led to significant increases in intratumoral CD8+ T cell infiltration and PD-L1 expression as compared to a cohort of untreated, matched controls. Cysteine 14-16 CD8a molecule Homo sapiens 102-105 32529484-1 2020 Snakin-1 (SN1) from potato is a cysteine-rich antimicrobial peptide with high evolutionary conservation. Cysteine 32-40 STSN1 Solanum tuberosum 0-8 32529484-1 2020 Snakin-1 (SN1) from potato is a cysteine-rich antimicrobial peptide with high evolutionary conservation. Cysteine 32-40 STSN1 Solanum tuberosum 10-13 32647651-9 2020 15d-PGJ2-induced inactivation of IKKbeta was also attributable to its covalent thiol modification at the cysteine 179 residue of IKKbeta. Cysteine 105-113 component of inhibitor of nuclear factor kappa B kinase complex Homo sapiens 33-40 32647651-9 2020 15d-PGJ2-induced inactivation of IKKbeta was also attributable to its covalent thiol modification at the cysteine 179 residue of IKKbeta. Cysteine 105-113 component of inhibitor of nuclear factor kappa B kinase complex Homo sapiens 129-136 32576932-4 2020 Here, we demonstrate that the nitric oxide (NO) donor nitrosoglutathione (GSNO) thermodynamically stabilizes the STIM2 Ca2+ sensing region in a Cys-specific manner. Cysteine 144-147 stromal interaction molecule 2 Homo sapiens 113-118 32576932-5 2020 We uncovered a remarkable synergism in this stabilization involving the three luminal Cys of STIM2, which is unique to this paralog. Cysteine 86-89 stromal interaction molecule 2 Homo sapiens 93-98 32576932-7 2020 In HEK293T cells, enhanced free basal cytosolic Ca2+ and SOCE mediated by STIM2 overexpression could be attenuated by GSNO or mutation of the modifiable Cys located in the luminal domain. Cysteine 153-156 stromal interaction molecule 2 Homo sapiens 74-79 32576932-8 2020 Collectively, we identify the Cys residues within the N-terminal region of STIM2 as modifiable targets during nitrosative stress that can profoundly and cooperatively affect basal Ca2+ and SOCE regulation. Cysteine 30-33 stromal interaction molecule 2 Homo sapiens 75-80 32371394-5 2020 We show that the primarily nuclear sirtuins Sirt1 and Sirt6, as well as the primarily cytosolic sirtuin Sirt2, are modified and inhibited by cysteine S-nitrosation in response to exposure to both free nitric oxide and nitrosothiols (k inact/K I >= 5 M-1s-1), which is the first report of Sirt2 and Sirt6 inhibition by S-nitrosation. Cysteine 141-149 sirtuin 1 Homo sapiens 44-49 32396355-6 2020 We propose that the flexibility of Atox1 occurs owing to protonation of one or more of the cysteine residues, and that Cys15 is an important residue for Atox1 dimerization, while Cys12 is a critical residue for Cu(I) binding. Cysteine 91-99 antioxidant 1 copper chaperone Homo sapiens 35-40 32302104-5 2020 Targeting a cysteine distal to the active site, this molecule attenuates the enzymatic activity of ADA and inhibits proliferation of lymphocytic cells. Cysteine 12-20 adenosine deaminase Homo sapiens 99-102 32380971-11 2020 RESULTS: Among the target sequencing results of 527 patients, two novel mutations (Mut1: c.821A > G p.G274D, the adenine(A) was mutated to guanine(G) at position 821 of the SRF gene coding sequences (CDS), lead to the Glycine(G) mutated to Asparticacid(D) at position 274 of the SRF protein amino acid sequences; Mut2: c.880G > T p.G294C, the guanine(G) was mutated to thymine (T) at position 880 of the SRF CDS, lead to the Glycine(G) mutated to Cysteine (C) at position 294 of the SRF protein amino acid sequences.) Cysteine 447-455 serum response factor Homo sapiens 279-282 32132240-16 2020 This research, therefore, gives new insight into the functional role of palmitoylated cysteines in nsP1 for the assembly of functional alphavirus replication complexes in their mammalian host. Cysteine 86-95 SH2 domain containing 3A Homo sapiens 99-103 32165494-8 2020 These activities also occurred with a CYP24A1 isoform 2 lacking the catalytic cysteine (Cys-462), suggesting that CYP24A1"s oncogenic potential is independent of its catalytic activity. Cysteine 78-86 cytochrome P450, family 24, subfamily a, polypeptide 1 Mus musculus 38-45 32165494-8 2020 These activities also occurred with a CYP24A1 isoform 2 lacking the catalytic cysteine (Cys-462), suggesting that CYP24A1"s oncogenic potential is independent of its catalytic activity. Cysteine 78-86 cytochrome P450, family 24, subfamily a, polypeptide 1 Mus musculus 114-121 32165494-8 2020 These activities also occurred with a CYP24A1 isoform 2 lacking the catalytic cysteine (Cys-462), suggesting that CYP24A1"s oncogenic potential is independent of its catalytic activity. Cysteine 88-91 cytochrome P450, family 24, subfamily a, polypeptide 1 Mus musculus 114-121 32188693-3 2020 Using recombinant protein expression in HEK293 cells, patch clamp electrophysiology, site-directed mutagenesis, and homology modeling, we report here that modulation of Cav3.2 by redox agents and zinc is mediated by a unique extracellular module containing a high-affinity metal-binding site formed by the extracellular IS1-IS2 and IS3-IS4 loops of domain I and a cluster of extracellular cysteines in the IS1-IS2 loop. Cysteine 389-398 IS1 Homo sapiens 406-409 32188693-7 2020 Removal of extracellular cysteines from the IS1-IS2 loop of Cav3.2 reduced its sensitivity to MTSES and SP. Cysteine 25-34 IS1 Homo sapiens 44-47 32188693-8 2020 We hypothesize that oxidative modification of IS1-IS2 loop cysteines induces allosteric changes in the zinc-binding site of Cav3.2 so that it becomes sensitive to ambient zinc. Cysteine 59-68 IS1 Homo sapiens 46-49 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. Cysteine 265-268 nicotinic Acetylcholine Receptor alpha1 Drosophila melanogaster 42-47 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. Cysteine 306-315 nicotinic Acetylcholine Receptor alpha1 Drosophila melanogaster 42-47