PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32997203-6	2020	The oxidizing capacity of H2O2 was linked to improved disulfide bond formation, by expressing a fusion of two endoplasmic reticulum-resident proteins, the thiol peroxidase GPx7 and the protein disulfide isomerase, PDI.	Hydrogen Peroxide	26-30	protein disulfide isomerase family A member 2	Homo sapiens	214-217
206294-8	1978	Ki for pdCp and pTp were found to be approximately 3.10(-6) M. The investigation of the inhibition mechanism as well the determination of Ki were accomplished with the help of homogenous low molecular weight substrates--ApApA and the phosphoamide MeOPheNH(pdA)2.	phosphoamide meophenh	234-255	protein disulfide isomerase family A member 2	Homo sapiens	256-261
1272807-3	1976	The hydrolysate of the purified photoproduct, p(dA)2, isolated from irradiated p(dA)2 by DEAE chromatography also had an Rf of 0.29 as well as an absorbance maximum at 310 nm.	2-diethylaminoethanol	89-93	protein disulfide isomerase family A member 2	Homo sapiens	46-52
1272807-3	1976	The hydrolysate of the purified photoproduct, p(dA)2, isolated from irradiated p(dA)2 by DEAE chromatography also had an Rf of 0.29 as well as an absorbance maximum at 310 nm.	2-diethylaminoethanol	89-93	protein disulfide isomerase family A member 2	Homo sapiens	79-85
33447253-13	2020	Its role fits the mechanistic theory of proteostasis in which an ideal balance of PDI isoforms is required in the endoplasmic reticulum (ER) for normal exine formation in plants subjected to heat stress.	exine	152-157	protein disulfide isomerase family A member 2	Homo sapiens	82-85
605774-3	1977	Within the group of patients treated with a peripheral decarboxylase inhibitor (PDI), the combination of all the plasma levels of O-Methyldopa from patients with dyskinesias shows significantly higher values than those from patients without dyskinesias.	Methyldopa	130-142	protein disulfide isomerase family A member 2	Homo sapiens	44-78
605774-3	1977	Within the group of patients treated with a peripheral decarboxylase inhibitor (PDI), the combination of all the plasma levels of O-Methyldopa from patients with dyskinesias shows significantly higher values than those from patients without dyskinesias.	Methyldopa	130-142	protein disulfide isomerase family A member 2	Homo sapiens	80-83
878846-2	1977	In patients treated with a combination of L-dopa and a peripheral decarboxylase inhibitor (PDI), those with dyskinesias have very high plasma O-methyl-dopa levels compared with those who have no dyskinesias.	Levodopa	42-48	protein disulfide isomerase family A member 2	Homo sapiens	91-94
878846-2	1977	In patients treated with a combination of L-dopa and a peripheral decarboxylase inhibitor (PDI), those with dyskinesias have very high plasma O-methyl-dopa levels compared with those who have no dyskinesias.	Methyldopa	142-155	protein disulfide isomerase family A member 2	Homo sapiens	55-89
878846-2	1977	In patients treated with a combination of L-dopa and a peripheral decarboxylase inhibitor (PDI), those with dyskinesias have very high plasma O-methyl-dopa levels compared with those who have no dyskinesias.	Methyldopa	142-155	protein disulfide isomerase family A member 2	Homo sapiens	91-94
33448048-0	2021	Efficient Photocatalytic Overall Water Splitting Induced by the Giant Internal Electric Field of a g-C3 N4 /rGO/PDIP Z-Scheme Heterojunction.	Water	33-38	protein disulfide isomerase family A member 2	Homo sapiens	112-116
33448048-1	2021	A graphitic carbon nitride/rGO/perylene diimide polymer (g-C3 N4 /rGO/PDIP) Z-scheme heterojunction is successfully constructed to realize high-flux charge transfer and efficient photocatalytic overall water splitting.	cyanogen	12-26	protein disulfide isomerase family A member 2	Homo sapiens	70-74
33448048-1	2021	A graphitic carbon nitride/rGO/perylene diimide polymer (g-C3 N4 /rGO/PDIP) Z-scheme heterojunction is successfully constructed to realize high-flux charge transfer and efficient photocatalytic overall water splitting.	rgo/perylene diimide polymer	27-55	protein disulfide isomerase family A member 2	Homo sapiens	70-74
33448048-1	2021	A graphitic carbon nitride/rGO/perylene diimide polymer (g-C3 N4 /rGO/PDIP) Z-scheme heterojunction is successfully constructed to realize high-flux charge transfer and efficient photocatalytic overall water splitting.	Water	202-207	protein disulfide isomerase family A member 2	Homo sapiens	70-74
33448048-3	2021	Thus, g-C3 N4 /rGO/PDIP presents an efficient and stable photocatalytic overall water splitting activity with H2 and O2 evolution rate of 15.80 and 7.80 micromol h-1 , respectively,  12.1 times higher than g-C3 N4 nanosheets.	Water	80-85	protein disulfide isomerase family A member 2	Homo sapiens	19-23
33448048-3	2021	Thus, g-C3 N4 /rGO/PDIP presents an efficient and stable photocatalytic overall water splitting activity with H2 and O2 evolution rate of 15.80 and 7.80 micromol h-1 , respectively,  12.1 times higher than g-C3 N4 nanosheets.	Deuterium	110-112	protein disulfide isomerase family A member 2	Homo sapiens	19-23
33448048-3	2021	Thus, g-C3 N4 /rGO/PDIP presents an efficient and stable photocatalytic overall water splitting activity with H2 and O2 evolution rate of 15.80 and 7.80 micromol h-1 , respectively,  12.1 times higher than g-C3 N4 nanosheets.	Oxygen	117-119	protein disulfide isomerase family A member 2	Homo sapiens	19-23
33396541-0	2020	PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly.	Disulfides	14-23	protein disulfide isomerase family A member 2	Homo sapiens	0-3
33396541-7	2020	Herein, the mechanism of PDI-regulated disulfide bond formation is important for understanding not only protein folding and associated diseases, but also the formation of functional biomolecular assembly.	Disulfides	39-48	protein disulfide isomerase family A member 2	Homo sapiens	25-28
32997203-7	2020	In concert, these proteins mediate disulfide transfer from H2O2 to target proteins via PDI-Gpx7 fusions.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	87-90
32997203-7	2020	In concert, these proteins mediate disulfide transfer from H2O2 to target proteins via PDI-Gpx7 fusions.	Hydrogen Peroxide	59-63	protein disulfide isomerase family A member 2	Homo sapiens	87-90
32316996-8	2020	RESULTS: The percentage of the disulfide-bonded HA trimers increased significantly in the PDIs-overexpressed 293 T cells, and ERp57 was more valid to the stability of HA than PDI.	Disulfides	31-40	protein disulfide isomerase family A member 2	Homo sapiens	90-93
30735910-1	2019	Protein disulfide isomerases (PDI) are a family of redox chaperones that catalyze formation or isomerization of disulfide bonds in proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	30-33
31797966-3	2019	Here we describe a protein disulphide isomerase essential for malarial transmission (PDI-Trans/PBANKA_0820300) to the mosquito.	nitrophenide	27-37	protein disulfide isomerase family A member 2	Homo sapiens	85-88
31797966-4	2019	We show that PDI-Trans activity is male-specific, surface-expressed, essential for fertilization/transmission, and exhibits disulphide isomerase activity which is up-regulated post-gamete activation.	nitrophenide	124-134	protein disulfide isomerase family A member 2	Homo sapiens	13-16
31797966-5	2019	We demonstrate that PDI-Trans is a viable anti-malarial drug and vaccine target blocking malarial transmission with the use of PDI inhibitor bacitracin (98.21%/92.48% reduction in intensity/prevalence), and anti-PDI-Trans antibodies (66.22%/33.16% reduction in intensity/prevalence).	Bacitracin	141-151	protein disulfide isomerase family A member 2	Homo sapiens	20-23
31927964-1	2020	The ability of the doublet excited state of perylene diimide anion radical 2(PDI- )* to reduce aromatic electron acceptors was probed by picosecond time-resolved transient absorption (TA) spectroscopy.	perylene diimide anion radical	44-74	protein disulfide isomerase family A member 2	Homo sapiens	77-80
31794946-1	2020	Disulfide bond formation is catalyzed by the protein disulfide Isomerases (PDI) family.	Disulfides	0-9	protein disulfide isomerase family A member 2	Homo sapiens	45-73
31794946-1	2020	Disulfide bond formation is catalyzed by the protein disulfide Isomerases (PDI) family.	Disulfides	0-9	protein disulfide isomerase family A member 2	Homo sapiens	75-78
31760358-7	2020	Functional in vitro assays demonstrated that 6-OHDA inactivates protein disulfide isomerase (PDI), which is a central player in protein folding and redox homeostasis.	Oxidopamine	45-51	protein disulfide isomerase family A member 2	Homo sapiens	93-96
31760358-7	2020	Functional in vitro assays demonstrated that 6-OHDA inactivates protein disulfide isomerase (PDI), which is a central player in protein folding and redox homeostasis.	Disulfides	72-81	protein disulfide isomerase family A member 2	Homo sapiens	93-96
30735910-5	2019	Treatment with a PDI inhibitor, LOC14 inhibited PDIA3 activity in lung epithelial cells, decreased intramolecular disulfide bonds and subsequent oligomerization (maturation) of HA in both H1N1 (A/PR8/34) and H3N2 (X31, A/Aichi/68) infected lung epithelial cells.	Disulfides	114-123	protein disulfide isomerase family A member 2	Homo sapiens	17-20
30735910-5	2019	Treatment with a PDI inhibitor, LOC14 inhibited PDIA3 activity in lung epithelial cells, decreased intramolecular disulfide bonds and subsequent oligomerization (maturation) of HA in both H1N1 (A/PR8/34) and H3N2 (X31, A/Aichi/68) infected lung epithelial cells.	LOC14	32-37	protein disulfide isomerase family A member 2	Homo sapiens	17-20
29222525-3	2017	Here we show that genes encoding human PDIA1 and its two paralogs PDIA8 and PDIA2 are each flanked by genes encoding Rho guanine-dissociation inhibitors (GDI), known regulators of RhoGTPases/cytoskeleton.	Guanine	121-128	protein disulfide isomerase family A member 2	Homo sapiens	76-81
30315102-6	2018	MS analysis of these complexes helped identify the disulfide-linked PDIp targets in vivo, revealing that PDIp interacts directly with a number of pancreatic digestive enzymes.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	68-72
30315102-6	2018	MS analysis of these complexes helped identify the disulfide-linked PDIp targets in vivo, revealing that PDIp interacts directly with a number of pancreatic digestive enzymes.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	105-109
30398270-2	2019	The polyurea membrane was synthesized by molecular layer deposition using p-phenylenediisocyanate (PDI) and p-phenylenediamine (PDA) as sequential precursors.	polyurea	4-12	protein disulfide isomerase family A member 2	Homo sapiens	99-102
30775641-4	2018	Here, we present a study investigating the effect of PDI inhibition on Huh7 human hepatoma cells harboring an HCV subgenomic replicon using the abscisic acid-derived PDI inhibitor origamicin.	Abscisic Acid	144-157	protein disulfide isomerase family A member 2	Homo sapiens	53-56
30775641-4	2018	Here, we present a study investigating the effect of PDI inhibition on Huh7 human hepatoma cells harboring an HCV subgenomic replicon using the abscisic acid-derived PDI inhibitor origamicin.	Abscisic Acid	144-157	protein disulfide isomerase family A member 2	Homo sapiens	166-169
30775641-4	2018	Here, we present a study investigating the effect of PDI inhibition on Huh7 human hepatoma cells harboring an HCV subgenomic replicon using the abscisic acid-derived PDI inhibitor origamicin.	origamicin	180-190	protein disulfide isomerase family A member 2	Homo sapiens	53-56
30775641-4	2018	Here, we present a study investigating the effect of PDI inhibition on Huh7 human hepatoma cells harboring an HCV subgenomic replicon using the abscisic acid-derived PDI inhibitor origamicin.	origamicin	180-190	protein disulfide isomerase family A member 2	Homo sapiens	166-169
25475092-2	2016	Collagen trimerization is set up via disulphide bond formation, catalysed by protein disulphide isomerase (PDI).	disulphide	37-47	protein disulfide isomerase family A member 2	Homo sapiens	107-110
28949004-6	2017	Here, we show that the chaperone 78-kDa glucose-regulated protein (GRP78) protects the MPD against PDI-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.	Disulfides	113-122	protein disulfide isomerase family A member 2	Homo sapiens	99-102
29151413-13	2017	Mean Pdi max at 7 days was significantly lower than that at 3 days [cmH2O (1 cmH2O = 0.098 kPa): 20.2+-4.2 vs. 28.1+-4.4, P < 0.01].	cmh2o	77-82	protein disulfide isomerase family A member 2	Homo sapiens	5-8
29151413-14	2017	By the end of the evaluation period at 11 days of MV, mean Pdi max decreased about 38.7% to the 1 day of MV (cmH2O: 19.8+-4.7 vs. 32.3+-3.9, P < 0.01).	cmh2o	109-114	protein disulfide isomerase family A member 2	Homo sapiens	59-62
29151413-20	2017	The sensitivity of the diagnosis was 81.8% and the specificity was 100% when cut-off value of Pdi max was 23.2 cmH2O.	cmh2o	111-116	protein disulfide isomerase family A member 2	Homo sapiens	94-97
28461071-1	2017	Alphaviruses require conserved cysteine residues for proper folding and assembly of the E1 and E2 envelope glycoproteins, and likely depend on host protein disulfide isomerase-family enzymes (PDI) to aid in facilitating disulfide bond formation and isomerization in these proteins.	Disulfides	156-165	protein disulfide isomerase family A member 2	Homo sapiens	192-195
26896642-5	2016	PDI"s inhibitors bacitracin and nitroblue tetrazolium reduced the percent of infected cells and small amounts of recTgPDI proteins interfered with the invasion step.	Bacitracin	17-27	protein disulfide isomerase family A member 2	Homo sapiens	0-3
26896642-5	2016	PDI"s inhibitors bacitracin and nitroblue tetrazolium reduced the percent of infected cells and small amounts of recTgPDI proteins interfered with the invasion step.	Nitroblue Tetrazolium	32-53	protein disulfide isomerase family A member 2	Homo sapiens	0-3
26725377-6	2016	Methods and results Using click chemistry to link anti-CD61 and a C-terminal azido disulfide-linked peptide construct with a quenched reporter, we developed a fluorogenic platelet-targeting antibody (PDI-sAb) for thiol reductase activity detection in whole blood under flow conditions.	azido disulfide	77-92	protein disulfide isomerase family A member 2	Homo sapiens	200-203
26725377-7	2016	PDI-sAb was highly responsive to various exogenous reducing agents (dithiothreitol, glutathione and recombinant PDI) and detected thiol reductase activity on P-selectin/phosphatidylserine-positive platelets activated with convulxin/PAR1 agonist peptide, a signal partially blocked by PDI inhibitors and antibody.	Dithiothreitol	68-82	protein disulfide isomerase family A member 2	Homo sapiens	0-3
26725377-7	2016	PDI-sAb was highly responsive to various exogenous reducing agents (dithiothreitol, glutathione and recombinant PDI) and detected thiol reductase activity on P-selectin/phosphatidylserine-positive platelets activated with convulxin/PAR1 agonist peptide, a signal partially blocked by PDI inhibitors and antibody.	Glutathione	84-95	protein disulfide isomerase family A member 2	Homo sapiens	0-3
26725377-11	2016	Conclusion PDI-sAb is a sensitive and real-time reporter of platelet- and vascular-derived disulfide reduction that targets clots as they form under flow to reveal spatial gradients.	Disulfides	91-100	protein disulfide isomerase family A member 2	Homo sapiens	11-14
25593085-10	2015	We also demonstrated that MNS inhibited PDI activity both in a pure enzyme system and in intact cancer cells.	3,4-methylenedioxy-beta-nitrostyrene	26-29	protein disulfide isomerase family A member 2	Homo sapiens	40-43
25137134-2	2014	It functions not only to eliminate peroxide but also to promote oxidative protein folding via oxidizing protein disulfide isomerase (PDI).	Peroxides	35-43	protein disulfide isomerase family A member 2	Homo sapiens	133-136
25575667-6	2015	However, ER calcium depletion in vivo led to a selective 2.5-fold decline in PDI1A mobility, whereas the mobility of the reducing PDI family member, ERdj5 was unaffected.	Calcium	12-19	protein disulfide isomerase family A member 2	Homo sapiens	77-80
25316421-3	2015	To investigate the antioxidant activity of P-DIP, we determined the scavenging activity of hydroxyl radicals and DPPH, as well as the reducing power.	Hydroxyl Radical	91-108	protein disulfide isomerase family A member 2	Homo sapiens	43-48
25316421-5	2015	Compared with DIP, P-DIP showed a satisfactory water-solubility and significant increase in the antioxidant properties.	Water	47-52	protein disulfide isomerase family A member 2	Homo sapiens	19-24
25316421-6	2015	Moreover, P-DIP also showed more significant inhibitory effects on the growth of MCF-7 and B16 tumor cells than the water-insoluble DIP.	Water	116-121	protein disulfide isomerase family A member 2	Homo sapiens	10-15
25419565-3	2014	As the ligands and receptors each contain disulfide bonds, a regulatory role for the cell surface protein disulfide isomerase (PDI) was investigated.	Disulfides	42-51	protein disulfide isomerase family A member 2	Homo sapiens	127-130
25419565-4	2014	OBJECTIVE: We utilized complementary in vitro and in vivo models to determine the potential role of PDI in regulating the ability of the NPs to generate its second messenger, cyclic guanosine monophosphate.	Cyclic GMP	175-205	protein disulfide isomerase family A member 2	Homo sapiens	100-103
25419565-5	2014	METHODS AND RESULTS: Inhibition of PDI attenuated the ability of ANP, BNP and CNP to generate cGMP in human mesangial cells (HMCs), human umbilical vein endothelial cells (HUVECs), and human aortic smooth muscle cells (HASMCs), each of which were shown to express PDI.	Cyclic GMP	94-98	protein disulfide isomerase family A member 2	Homo sapiens	35-38
25419565-7	2014	Addition of PDI to cultured LLC-PK1 cells increased intracellular cGMP generation mediated by ANP.	Cyclic GMP	66-70	protein disulfide isomerase family A member 2	Homo sapiens	12-15
25419565-8	2014	Inhibition of PDI in vivo attenuated NP-mediated generation of cGMP by ANP.	Cyclic GMP	63-67	protein disulfide isomerase family A member 2	Homo sapiens	14-17
25419565-11	2014	CONCLUSION: These data demonstrate for the first time that cell surface PDI expression and function regulate the capacity of natriuretic peptides to generate cGMP through interaction with their receptors.	Cyclic GMP	158-162	protein disulfide isomerase family A member 2	Homo sapiens	72-75
23167757-0	2013	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).	Nitrogen	0-1	protein disulfide isomerase family A member 2	Homo sapiens	49-94
24070012-4	2013	In this article, by using in situ proteome profiling experiments in combination with in vitro PDI enzymatic inhibition assays, we have discovered a phenyl vinyl sulfonate-containing small molecule (P1; shown) as a relatively potent and specific inhibitor of endogenous human PDI in several mammalian cancer cells (e.g., GI50 ~ 4 muM).	phenyl ethenesulfonate	148-170	protein disulfide isomerase family A member 2	Homo sapiens	94-97
24070012-4	2013	In this article, by using in situ proteome profiling experiments in combination with in vitro PDI enzymatic inhibition assays, we have discovered a phenyl vinyl sulfonate-containing small molecule (P1; shown) as a relatively potent and specific inhibitor of endogenous human PDI in several mammalian cancer cells (e.g., GI50 ~ 4 muM).	phenyl ethenesulfonate	148-170	protein disulfide isomerase family A member 2	Homo sapiens	275-278
24070012-6	2013	Our results indicate P1 is indeed a novel, cell-permeable small molecule PDI inhibitor, and the electrophilic vinyl sulfonate scaffold might serve as a starting point for future development of next-generation PDI inhibitors and probes.	vinyl sulfonate	110-125	protein disulfide isomerase family A member 2	Homo sapiens	209-212
23118353-9	2013	Importantly, pharmacological inhibition of PDI or its down-regulation by short interfering RNAs prevented NOX activation in microglia and subsequent production of superoxide.	Superoxides	163-173	protein disulfide isomerase family A member 2	Homo sapiens	43-46
23167757-0	2013	N-linked glycosylation modulates dimerization of protein disulfide isomerase family A member 2 (PDIA2).	Nitrogen	0-1	protein disulfide isomerase family A member 2	Homo sapiens	96-101
23167757-4	2013	Unlike most PDI family members, PDIA2 contains three predicted N-linked glycosylation sites.	Nitrogen	63-64	protein disulfide isomerase family A member 2	Homo sapiens	32-37
23167757-5	2013	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.	Asparagine	88-91	protein disulfide isomerase family A member 2	Homo sapiens	160-165
23167757-5	2013	By site-directed mutagenesis and enzymatic deglycosylation, we show here that all three Asn residues within the potential N-linked glycosylation sites of human PDIA2 (N127, N284 and N516) are glycosylated in human cells.	Nitrogen	122-123	protein disulfide isomerase family A member 2	Homo sapiens	160-165
23167757-6	2013	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.	4-CHLORO-3-METHYLPHENYLBORONIC ACID	25-29	protein disulfide isomerase family A member 2	Homo sapiens	112-117
23167757-6	2013	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.	Glutamine	52-55	protein disulfide isomerase family A member 2	Homo sapiens	112-117
23167757-6	2013	Furthermore, mutation of N284 to glycosylation-null Gln increases formation of a highly stable disulfide-bonded PDIA2 dimer.	Disulfides	95-104	protein disulfide isomerase family A member 2	Homo sapiens	112-117
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	168-177	protein disulfide isomerase family A member 2	Homo sapiens	75-78
23949117-3	2013	Detailed analyses of oxidative folding catalyzed by the reconstituted Prx4-PDIs pathways demonstrated that, while P5 and ERp46 are dedicated to rapid, but promiscuous, disulfide introduction, PDI is an efficient proofreader of non-native disulfides.	Disulfides	238-248	protein disulfide isomerase family A member 2	Homo sapiens	75-78
23949117-4	2013	Remarkably, the Prx4-dependent formation of native disulfide bonds was accelerated when PDI was combined with ERp46 or P5, suggesting that PDIs work synergistically to increase the rate and fidelity of oxidative protein folding.	Disulfides	51-60	protein disulfide isomerase family A member 2	Homo sapiens	88-91
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	40-49	protein disulfide isomerase family A member 2	Homo sapiens	13-17
23141538-1	2012	PDI catalyzes the oxidative folding of disulfide-containing proteins.	Disulfides	39-48	protein disulfide isomerase family A member 2	Homo sapiens	0-3
23141538-5	2012	In contrast, a PDI domain favors native disulfides by catalyzing oxidation at a late stage of folding.	Disulfides	40-50	protein disulfide isomerase family A member 2	Homo sapiens	15-18
23141538-6	2012	We propose a model for cotranslational oxidative folding wherein PDI acts as a placeholder that is relieved by the pairing of cysteines caused by substrate folding.	Cysteine	126-135	protein disulfide isomerase family A member 2	Homo sapiens	65-68
21238616-0	2011	Both PDI and PDIp can attack the native disulfide bonds in thermally-unfolded RNase and form stable disulfide-linked complexes.	Disulfides	100-109	protein disulfide isomerase family A member 2	Homo sapiens	13-17
21238616-1	2011	Protein disulfide isomerase (PDI) and its pancreatic homolog (PDIp) are folding catalysts for the formation, reduction, and/or isomerization of disulfide bonds in substrate proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	62-66
21238616-2	2011	However, the question as to whether PDI and PDIp can directly attack the native disulfide bonds in substrate proteins is still not answered, which is the subject of the present study.	Disulfides	80-89	protein disulfide isomerase family A member 2	Homo sapiens	44-48
21238616-6	2011	In support of this suggestion, we show that both PDI and PDIp form stable disulfide-linked complexes only with thermally-unfolded RNase, and RNase in the complexes can be released and reactivated dependently of the redox conditions used.	Disulfides	74-83	protein disulfide isomerase family A member 2	Homo sapiens	57-61
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Sulfhydryl Compounds	50-55	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	56-65	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21238616-8	2011	These data indicate that PDI and PDIp can perform thiol-disulfide exchange reactions with native disulfide bonds in unfolded RNase via formation of stable disulfide-linked complexes, and from these complexes RNase is further released.	Disulfides	97-106	protein disulfide isomerase family A member 2	Homo sapiens	33-37
21130735-4	2011	We have recently demonstrated in vitro that polyphenolic phytochemicals, curcumin and masoprocol, can rescue S-nitroso-PDI formation by scavenging NOx.	Curcumin	73-81	protein disulfide isomerase family A member 2	Homo sapiens	119-122
21080683-0	2011	Characterization of the estradiol-binding site structure of human pancreas-specific protein disulfide isomerase: indispensable role of the hydrogen bond between His278 and the estradiol 3-hydroxyl group.	Estradiol	24-33	protein disulfide isomerase family A member 2	Homo sapiens	66-111
21080683-0	2011	Characterization of the estradiol-binding site structure of human pancreas-specific protein disulfide isomerase: indispensable role of the hydrogen bond between His278 and the estradiol 3-hydroxyl group.	Hydrogen	139-147	protein disulfide isomerase family A member 2	Homo sapiens	66-111
21080683-0	2011	Characterization of the estradiol-binding site structure of human pancreas-specific protein disulfide isomerase: indispensable role of the hydrogen bond between His278 and the estradiol 3-hydroxyl group.	Estradiol	176-185	protein disulfide isomerase family A member 2	Homo sapiens	66-111
21080683-2	2011	Human pancreas-specific protein disulfide isomerase (PDIp), a protein folding catalyst, was recently found to be able to bind E(2).	Estradiol	126-130	protein disulfide isomerase family A member 2	Homo sapiens	6-51
21080683-2	2011	Human pancreas-specific protein disulfide isomerase (PDIp), a protein folding catalyst, was recently found to be able to bind E(2).	Estradiol	126-130	protein disulfide isomerase family A member 2	Homo sapiens	53-57
21080683-4	2011	Analysis of various truncated PDIp proteins showed that the b-b" fragment contains an intact E(2)-binding site that has the same binding affinity as the full-length PDIp protein, with apparent K(d) values of approximately 170 nM.	Estradiol	93-97	protein disulfide isomerase family A member 2	Homo sapiens	30-34
21080683-4	2011	Analysis of various truncated PDIp proteins showed that the b-b" fragment contains an intact E(2)-binding site that has the same binding affinity as the full-length PDIp protein, with apparent K(d) values of approximately 170 nM.	Estradiol	93-97	protein disulfide isomerase family A member 2	Homo sapiens	165-169
21080683-6	2011	The hydrogen bond, formed between the 3-hydroxyl group of E(2) (donor) and PDIp"s His278 (acceptor), is indispensable for its binding.	Hydrogen	4-12	protein disulfide isomerase family A member 2	Homo sapiens	75-79
21130735-4	2011	We have recently demonstrated in vitro that polyphenolic phytochemicals, curcumin and masoprocol, can rescue S-nitroso-PDI formation by scavenging NOx.	Masoprocol	86-96	protein disulfide isomerase family A member 2	Homo sapiens	119-122
21130735-4	2011	We have recently demonstrated in vitro that polyphenolic phytochemicals, curcumin and masoprocol, can rescue S-nitroso-PDI formation by scavenging NOx.	s-nitroso	109-118	protein disulfide isomerase family A member 2	Homo sapiens	119-122
21130735-7	2011	Furthermore, our data also reveal that rotenone attenuates PDI expression in the same cell line, a phenomenon that can be mitigated through EF-24 intervention.	Rotenone	39-47	protein disulfide isomerase family A member 2	Homo sapiens	59-62
20951197-5	2011	Some algal PDI-Fs possess selenocysteine residues.	Selenocysteine	26-40	protein disulfide isomerase family A member 2	Homo sapiens	11-14
19091013-3	2008	PDI is capable of mediating thio-disulfide interchange reactions and could enable the reduction of gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	thio-disulfide	28-42	protein disulfide isomerase family A member 2	Homo sapiens	0-3
21283970-7	2011	Bosentan, an oral endothelin receptor antagonists (ETRA), was shown to prevent new DU, but failed to heal existing DU, while the oral phopshodiesterase inhibitor (PDI) Sildenafil reduces the occurrence of RP and might be effective in ulcer healing.	Sildenafil Citrate	168-178	protein disulfide isomerase family A member 2	Homo sapiens	134-161
21283970-7	2011	Bosentan, an oral endothelin receptor antagonists (ETRA), was shown to prevent new DU, but failed to heal existing DU, while the oral phopshodiesterase inhibitor (PDI) Sildenafil reduces the occurrence of RP and might be effective in ulcer healing.	Sildenafil Citrate	168-178	protein disulfide isomerase family A member 2	Homo sapiens	163-166
19150607-0	2009	Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond.	Disulfides	32-41	protein disulfide isomerase family A member 2	Homo sapiens	61-65
19150607-3	2009	We found that formation of an inter-subunit disulfide bond in the recombinant human PDIp can alter not only its structure, but also its functions.	Disulfides	44-53	protein disulfide isomerase family A member 2	Homo sapiens	84-88
19150607-4	2009	PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond.	Disulfides	198-207	protein disulfide isomerase family A member 2	Homo sapiens	0-4
19150607-5	2009	The oxidized PDIp (with an inter-subunit disulfide bond) appears to expose more hydrophobic patches and is more sensitive to protease digestion compared to the reduced form.	Disulfides	41-50	protein disulfide isomerase family A member 2	Homo sapiens	13-17
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	53-57
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Disulfides	35-44	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	98-106	protein disulfide isomerase family A member 2	Homo sapiens	53-57
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	98-106	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	98-106	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	116-124	protein disulfide isomerase family A member 2	Homo sapiens	53-57
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	116-124	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-7	2009	The formation of the inter-subunit disulfide bond in PDIp is mainly contributed by its non-active cysteine residue (cysteine-4), which is only present in human and primate PDIp, but not in rodent PDIp.	Cysteine	116-124	protein disulfide isomerase family A member 2	Homo sapiens	172-176
19150607-8	2009	In addition, we observed that the formation of the inter-subunit disulfide bond in PDIp is redox-dependent and is favored under oxidizing conditions, and that PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	83-87
19150607-8	2009	In addition, we observed that the formation of the inter-subunit disulfide bond in PDIp is redox-dependent and is favored under oxidizing conditions, and that PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	159-163
19150607-9	2009	In light of these observations, it is concluded that the structures and functions of human PDIp are redox-regulated through formation of an inter-subunit disulfide bond between two cysteine-4 residues.	Disulfides	154-163	protein disulfide isomerase family A member 2	Homo sapiens	91-95
19150607-9	2009	In light of these observations, it is concluded that the structures and functions of human PDIp are redox-regulated through formation of an inter-subunit disulfide bond between two cysteine-4 residues.	Cysteine	181-189	protein disulfide isomerase family A member 2	Homo sapiens	91-95
19429457-5	2009	Moreover, we found that PDIp could serve as a high-capacity intracellular E(2)-binding protein and could modulate the intracellular concentrations of E(2) in cultured mammalian cells as well as in human pancreatic tissue.	Estradiol	74-78	protein disulfide isomerase family A member 2	Homo sapiens	24-28
21145486-1	2010	Endoplasmic reticulum (ER) oxidation 1 (ERO1) transfers disulfides to protein disulfide isomerase (PDI) and is essential for oxidative protein folding in simple eukaryotes such as yeast and worms.	Disulfides	56-66	protein disulfide isomerase family A member 2	Homo sapiens	99-102
21145486-3	2010	To identify ERO1-independent pathways to disulfide bond formation, we purified PDI oxidants with a trapping mutant of PDI.	Disulfides	41-50	protein disulfide isomerase family A member 2	Homo sapiens	118-121
21145486-7	2010	In the presence of an H(2)O(2)-generating system, purified PRDX4 oxidized PDI and reconstituted oxidative folding of RNase A.	Hydrogen Peroxide	22-30	protein disulfide isomerase family A member 2	Homo sapiens	74-77
20660153-3	2010	We show that PDI plays a predominant role in oxidative folding because its depletion delayed disulfide formation in all secretory proteins tested.	Disulfides	93-102	protein disulfide isomerase family A member 2	Homo sapiens	13-16
20130085-2	2010	Our previous analyses demonstrated that the ER oxidoreductase protein disulfide isomerase (PDI) acts as a redox-dependent chaperone to unfold CTA1, a reaction postulated to initiate toxin retro-translocation.	cta1	142-146	protein disulfide isomerase family A member 2	Homo sapiens	91-94
20163832-3	2010	In this article we review PDI contribution to different models of TF decryption, namely the disulfide switch model and the phosphatidylserine dynamics, and hypothesize on PDI contribution to TF self-association and association with lipid domains.	Disulfides	92-101	protein disulfide isomerase family A member 2	Homo sapiens	26-29
20163832-4	2010	Experimental evidence debate the disulfide switch model of TF decryption and its regulation by PDI.	Disulfides	33-42	protein disulfide isomerase family A member 2	Homo sapiens	95-98
20163832-6	2010	Interestingly, PDI reductase activity could maintain TF in the reduced monomeric form, while also maintaining low exposure of PS, both states correlated with low procoagulant function.	Phosphorus	126-128	protein disulfide isomerase family A member 2	Homo sapiens	15-18
19882737-2	2010	Mammalian protein disulfide isomerase (PDI) has previously been shown to have a role in the formation of disulfide bonds in immunoglobulins.	Disulfides	18-27	protein disulfide isomerase family A member 2	Homo sapiens	39-42
19091013-3	2008	PDI is capable of mediating thio-disulfide interchange reactions and could enable the reduction of gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	33-42	protein disulfide isomerase family A member 2	Homo sapiens	0-3
19091013-4	2008	In this scenario, inhibition of HIV-1 entry can be brought about by introducing agents that can block thiol-disulfide interchange reaction of cell surface PDI.	thiol-disulfide	102-117	protein disulfide isomerase family A member 2	Homo sapiens	155-158
19091013-6	2008	This study attempts to perceive the mode of binding of dithionitrobenzoic acid (DTNB), and its structurally related compounds on PDI enzyme.	Dithionitrobenzoic Acid	55-78	protein disulfide isomerase family A member 2	Homo sapiens	129-132
19091013-6	2008	This study attempts to perceive the mode of binding of dithionitrobenzoic acid (DTNB), and its structurally related compounds on PDI enzyme.	Dithionitrobenzoic Acid	80-84	protein disulfide isomerase family A member 2	Homo sapiens	129-132
16182193-3	2005	This could enable PDI to reduce gp120 disulfide bonds, which triggers the major conformational changes in gp120 and gp41 required for virus entry.	Disulfides	38-47	protein disulfide isomerase family A member 2	Homo sapiens	18-21
16507315-1	2006	Cell-surface protein disulfide isomerase (PDI) has been proposed to promote disulfide bond rearrangements in HIV-1 envelope protein (Env) that accompany Env-mediated fusion.	Disulfides	21-30	protein disulfide isomerase family A member 2	Homo sapiens	42-45
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	Sulfhydryl Compounds	26-31	protein disulfide isomerase family A member 2	Homo sapiens	213-216
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	Sulfhydryl Compounds	26-31	protein disulfide isomerase family A member 2	Homo sapiens	273-276
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	Dithionitrobenzoic Acid	49-85	protein disulfide isomerase family A member 2	Homo sapiens	273-276
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	DTNB	87-91	protein disulfide isomerase family A member 2	Homo sapiens	213-216
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	DTNB	87-91	protein disulfide isomerase family A member 2	Homo sapiens	273-276
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	Sulfhydryl Compounds	175-180	protein disulfide isomerase family A member 2	Homo sapiens	213-216
16507315-4	2006	However, the cell-surface thiol-reactive reagent 5, 5"-dithiobis(2-nitrobenzoic acid) (DTNB) had a much stronger inhibitory effect in our system, suggesting that cell-surface thiol-containing molecules other than PDI, acting alone or in concert, have a greater effect than PDI on HIV-1 Env-mediated fusion.	Sulfhydryl Compounds	175-180	protein disulfide isomerase family A member 2	Homo sapiens	273-276
16507315-5	2006	We evaluated one such candidate, thioredoxin, a PDI family member reported to reduce a labile disulfide bond in CD4.	Disulfides	94-103	protein disulfide isomerase family A member 2	Homo sapiens	48-51
16222722-9	2005	Results of this study show that the majority of adducts form on proteins that contain reactive thiols in a CXXC motif, such as protein disulfide isomerase A(3) (ERp57), protein disulfide isomerase (PDI), and endothelial PDI.	Sulfhydryl Compounds	95-101	protein disulfide isomerase family A member 2	Homo sapiens	198-201
16222722-9	2005	Results of this study show that the majority of adducts form on proteins that contain reactive thiols in a CXXC motif, such as protein disulfide isomerase A(3) (ERp57), protein disulfide isomerase (PDI), and endothelial PDI.	Sulfhydryl Compounds	95-101	protein disulfide isomerase family A member 2	Homo sapiens	220-223
15450603-1	2004	The essential flavoenzyme Ero1p both creates de novo disulfide bonds and transfers these disulfides to the folding catalyst protein disulfide isomerase (PDI).	Disulfides	89-99	protein disulfide isomerase family A member 2	Homo sapiens	153-156
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	Tretinoin	261-274	protein disulfide isomerase family A member 2	Homo sapiens	65-103
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	Tretinoin	261-274	protein disulfide isomerase family A member 2	Homo sapiens	105-109
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	Tretinoin	276-278	protein disulfide isomerase family A member 2	Homo sapiens	65-103
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	Tretinoin	276-278	protein disulfide isomerase family A member 2	Homo sapiens	105-109
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	lactacystin	408-419	protein disulfide isomerase family A member 2	Homo sapiens	65-103
15353226-4	2004	We show that the protein disulfide isomerase (PDI) family member pancreatic protein disulfide isomerase (PDIp), previously considered exclusively expressed in pancreatic tissue, is uniquely upregulated among PDI family members within 24 h following exposure of retinoic acid (RA)-differentiated SH-SY5Y human neuroblastoma cells to either 1 mM MPP(+) or 10 microM of the highly specific proteasome inhibitor lactacystin.	lactacystin	408-419	protein disulfide isomerase family A member 2	Homo sapiens	105-109
15353226-6	2004	Collectively, these findings suggest that increased PDIp expression in dopaminergic (DA) neurons might contribute to LB formation and neurodegeneration, and that this increased PDIp expression may be the result of proteasome impairment.	lb	117-119	protein disulfide isomerase family A member 2	Homo sapiens	52-56
15644496-2	2005	The triggering of fusion requires cleavage of two of the nine disulfide bonds of gp120 by a cell-surface protein disulfide-isomerase (PDI).	Disulfides	62-71	protein disulfide isomerase family A member 2	Homo sapiens	134-137
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparin	59-66	protein disulfide isomerase family A member 2	Homo sapiens	95-98
15644496-7	2005	In vitro, and in conditions in which gp120 could bind CD4, heparin and heparan sulfate reduced PDI-mediated gp120 reduction by approximately 80%.	Heparitin Sulfate	71-86	protein disulfide isomerase family A member 2	Homo sapiens	95-98
15664856-1	2005	PDI is an enzyme that acts as a chaperone, shufflase, and oxidase during the folding of disulfide-containing proteins.	Disulfides	88-97	protein disulfide isomerase family A member 2	Homo sapiens	0-3
15664856-2	2005	The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured.	aromatic thiols	15-30	protein disulfide isomerase family A member 2	Homo sapiens	59-62
15664856-2	2005	The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured.	thiol glutathione	115-132	protein disulfide isomerase family A member 2	Homo sapiens	59-62
15664856-2	2005	The ability of aromatic thiols to increase the activity of PDI-catalyzed protein folding over that of the standard thiol glutathione (GSH) was measured.	Glutathione	134-137	protein disulfide isomerase family A member 2	Homo sapiens	59-62
15664856-3	2005	4-Mercaptobenzoic acid (ArSH) increased the activity of PDI by a factor of three.	4-mercaptobenzoate	0-22	protein disulfide isomerase family A member 2	Homo sapiens	56-59
10794419-0	2000	Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.	Tyrosine	63-71	protein disulfide isomerase family A member 2	Homo sapiens	158-203
12218051-2	2002	PDI is present at the surface of HIV-1 target cells and reduces disulfide bonds in a model peptide attached to the cell membrane.	Disulfides	64-73	protein disulfide isomerase family A member 2	Homo sapiens	0-3
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	38-47	protein disulfide isomerase family A member 2	Homo sapiens	26-29
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	protein disulfide isomerase family A member 2	Homo sapiens	26-29
12218051-3	2002	Here we show that soluble PDI cleaves disulfide bonds in recombinant envelope glycoprotein gp120 and that gp120 bound to the surface receptor CD4 undergoes a disulfide reduction that is prevented by PDI inhibitors.	Disulfides	158-167	protein disulfide isomerase family A member 2	Homo sapiens	199-202
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	protein disulfide isomerase family A member 2	Homo sapiens	18-21
12218051-8	2002	We propose that a PDI.CD4 association at the cell surface enables PDI to reach CD4-bound virus and to reduce disulfide bonds present in the domain of gp120 that binds to CD4.	Disulfides	109-118	protein disulfide isomerase family A member 2	Homo sapiens	66-69
11229362-3	2000	To investigate redox homeostasis further in AD, we analyzed protein disulfide isomerase (PDI), a multifunctional enzyme, which catalyzes the disruption and formation of disulfide bonds.	Disulfides	68-77	protein disulfide isomerase family A member 2	Homo sapiens	89-92
11229362-4	2000	PDI plays a pivotal role in both secreted and cell-surface-associated protein disulfide rearrangement.	Disulfides	78-87	protein disulfide isomerase family A member 2	Homo sapiens	0-3
12065480-4	2002	Matrix-assisted laser desorption ionization mass-spectrometry sequence analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen receptor complex which carries out thiol-disulfide exchange reactions at infected host cell surfaces.	Sulfhydryl Compounds	209-214	protein disulfide isomerase family A member 2	Homo sapiens	143-146
12065480-4	2002	Matrix-assisted laser desorption ionization mass-spectrometry sequence analysis revealed the 55-kDa protein to be protein disulfide isomerase (PDI), a member of the estrogen receptor complex which carries out thiol-disulfide exchange reactions at infected host cell surfaces.	Disulfides	122-131	protein disulfide isomerase family A member 2	Homo sapiens	143-146
12065480-5	2002	Exposure of HEC-1B cells during EB attachment (1.5 to 2 h) to three different inhibitors of PDI reductive reactions--(i) the thiol-alkylating reagent DTNB (5,5"-dithiobis[2-nitrobenzoic acid]), (ii) bacitracin, and (iii) anti-PDI antibodies--resulted in reduced chlamydial infectivity.	Dithionitrobenzoic Acid	150-154	protein disulfide isomerase family A member 2	Homo sapiens	92-95
11839698-4	2002	The isolated a and a" domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways.	Sulfhydryl Compounds	66-71	protein disulfide isomerase family A member 2	Homo sapiens	33-36
11839698-4	2002	The isolated a and a" domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways.	Disulfides	72-81	protein disulfide isomerase family A member 2	Homo sapiens	33-36
11839698-4	2002	The isolated a and a" domains of PDI are good catalysts of simple thiol-disulfide interchange reactions but require additional domains to be effective as catalysts of the rate-limiting disulfide isomerizations in protein folding pathways.	Disulfides	185-194	protein disulfide isomerase family A member 2	Homo sapiens	33-36
10893409-6	2000	BiP binds the unfolded polypeptide chains and keeps them in a conformation in which the cysteine residues are accessible for PDI.	Cysteine	88-96	protein disulfide isomerase family A member 2	Homo sapiens	125-128
10794419-0	2000	Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.	Tyrosine	63-71	protein disulfide isomerase family A member 2	Homo sapiens	204-208
10794419-0	2000	Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.	Tryptophan	76-86	protein disulfide isomerase family A member 2	Homo sapiens	158-203
10794419-0	2000	Specificity in substrate binding by protein folding catalysts: tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp.	Tryptophan	76-86	protein disulfide isomerase family A member 2	Homo sapiens	204-208
10794419-3	2000	In this study, we explore the specificity of these proteins in binding peptides and related ligands and show that tyrosine and tryptophan residues in peptides are the recognition motifs for their binding by PDIp.	Tyrosine	114-122	protein disulfide isomerase family A member 2	Homo sapiens	207-211
10794419-3	2000	In this study, we explore the specificity of these proteins in binding peptides and related ligands and show that tyrosine and tryptophan residues in peptides are the recognition motifs for their binding by PDIp.	Tryptophan	127-137	protein disulfide isomerase family A member 2	Homo sapiens	207-211
10469657-5	1999	The folding catalyst PDI increases dramatically both yields and rates of lysozyme refolding, largely by facilitating the conversion of des-[76-94] to the native state.	Diethylstilbestrol	135-138	protein disulfide isomerase family A member 2	Homo sapiens	21-24
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Sulfhydryl Compounds	127-133	protein disulfide isomerase family A member 2	Homo sapiens	29-32
10417146-6	1999	Binding of PDI-refolded full-length (P < 0.001) and cysteine-rich (P = 0.005) Hgl2 to CHO cells was galactose dependent and competitively inhibited by native hololectin (50% inhibitory concentration of 39.6 ng/ml).	Cysteine	55-63	protein disulfide isomerase family A member 2	Homo sapiens	11-14
10417146-6	1999	Binding of PDI-refolded full-length (P < 0.001) and cysteine-rich (P = 0.005) Hgl2 to CHO cells was galactose dependent and competitively inhibited by native hololectin (50% inhibitory concentration of 39.6 ng/ml).	CAV protocol	89-92	protein disulfide isomerase family A member 2	Homo sapiens	11-14
10417146-6	1999	Binding of PDI-refolded full-length (P < 0.001) and cysteine-rich (P = 0.005) Hgl2 to CHO cells was galactose dependent and competitively inhibited by native hololectin (50% inhibitory concentration of 39.6 ng/ml).	Galactose	103-112	protein disulfide isomerase family A member 2	Homo sapiens	11-14
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	29-32
9703976-1	1998	Protein disulfide isomerase (PDI), the product of the essential PDI1 gene of Saccharomyces cerevisiae catalyzes oxidization of thiols, reduction of disulfide bonds, and isomerization of disulfides.	Disulfides	186-196	protein disulfide isomerase family A member 2	Homo sapiens	29-32
9703976-6	1998	The function of these non-active site Cys of yeast PDI is poorly understood.	Cysteine	38-41	protein disulfide isomerase family A member 2	Homo sapiens	51-54
9703976-7	1998	Whereas in yeast PDI, these Cys residues are in the vicinity of the N-terminal-most active site, in mammalian PDI their position is closer to the C-terminal-most active site.	Cysteine	28-31	protein disulfide isomerase family A member 2	Homo sapiens	17-20
9703976-9	1998	As reported earlier, the N-terminal Cys of the two active sites sequences of yeast PDI were found to be required for cell viability, but mutation of the C-terminal Cys to Ser in the two active sites was not lethal.	Cysteine	36-39	protein disulfide isomerase family A member 2	Homo sapiens	83-86
9703976-9	1998	As reported earlier, the N-terminal Cys of the two active sites sequences of yeast PDI were found to be required for cell viability, but mutation of the C-terminal Cys to Ser in the two active sites was not lethal.	Cysteine	164-167	protein disulfide isomerase family A member 2	Homo sapiens	83-86
9703976-9	1998	As reported earlier, the N-terminal Cys of the two active sites sequences of yeast PDI were found to be required for cell viability, but mutation of the C-terminal Cys to Ser in the two active sites was not lethal.	Serine	171-174	protein disulfide isomerase family A member 2	Homo sapiens	83-86
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	dithiol	40-47	protein disulfide isomerase family A member 2	Homo sapiens	69-72
18642336-2	1997	PDI and PPI were successfully immobilized on cross-linked agarose beads.	Sepharose	58-65	protein disulfide isomerase family A member 2	Homo sapiens	0-3
18642336-3	1997	PDI inactivation during coupling reaction was overcome by oxidizing active site thiols with dimethylsulfoxide and led to a 64% active enzyme.	Sulfhydryl Compounds	80-86	protein disulfide isomerase family A member 2	Homo sapiens	0-3
18642336-3	1997	PDI inactivation during coupling reaction was overcome by oxidizing active site thiols with dimethylsulfoxide and led to a 64% active enzyme.	Dimethyl Sulfoxide	92-109	protein disulfide isomerase family A member 2	Homo sapiens	0-3
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Bacitracin	79-89	protein disulfide isomerase family A member 2	Homo sapiens	136-139
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	thiol-disulfide	216-231	protein disulfide isomerase family A member 2	Homo sapiens	136-139
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	thiol-disulfide	216-231	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	thiol-disulfide	216-231	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Sulfhydryl Compounds	256-262	protein disulfide isomerase family A member 2	Homo sapiens	136-139
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Sulfhydryl Compounds	256-262	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Sulfhydryl Compounds	256-262	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	136-139
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-2	1994	More recently it was found that the same membrane function can be inhibited by bacitracin, an inhibitor of protein disulfide-isomerase (PDI), and by monoclonal antibodies against PDI, suggesting that PDI catalyzes a thiol-disulfide interchange between its thiols and the disulfides of membrane-bound macromolecules.	Disulfides	271-281	protein disulfide isomerase family A member 2	Homo sapiens	179-182
8183947-3	1994	We provide evidence that the same reductive process plays a role in the penetration of membrane-bound human immunodeficiency virus (HIV) and show that HIV infection of human lymphoid cells is markedly inhibited by the membrane-impermeant sulfhydryl blocker 5,5"-dithiobis(2-nitrobenzoic acid), by bacitracin, and by anti-PDI antibodies.	5,5"-dithiobis	257-271	protein disulfide isomerase family A member 2	Homo sapiens	321-324
8183947-4	1994	The results imply that HIV and its target cell engage in a thiol-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection.	Sulfhydryl Compounds	59-64	protein disulfide isomerase family A member 2	Homo sapiens	99-102
8183947-4	1994	The results imply that HIV and its target cell engage in a thiol-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection.	Disulfides	65-74	protein disulfide isomerase family A member 2	Homo sapiens	99-102
8183947-4	1994	The results imply that HIV and its target cell engage in a thiol-disulfide interchange mediated by PDI and that the reduction of critical disulfides in viral envelope glycoproteins may be the initial event that triggers conformational changes required for HIV entry and cell infection.	Disulfides	138-148	protein disulfide isomerase family A member 2	Homo sapiens	99-102
1761235-1	1991	Protein disulfide isomerase (PDI) is an enzyme involved in the catalysis of disulfide bond formation in secretory and cell-surface proteins.	Disulfides	8-17	protein disulfide isomerase family A member 2	Homo sapiens	29-32
1761235-2	1991	Using an oligodeoxyribonucleotide designed to detect the conserved "thioredoxin-like" active site of vertebrate PDIs, we have isolated a gene encoding PDI from the lower eukaryote, Saccharomyces cerevisiae.	Oligodeoxyribonucleotides	9-33	protein disulfide isomerase family A member 2	Homo sapiens	112-115
9435226-8	1998	As predicted from the amino acid sequence homology, recombinant DiTG catalyzed the isomerization of intramolecular disulfide/sulfhydryl bonds in denatured RNase in vitro as effectively as did mammalian PDI.	ditg	64-68	protein disulfide isomerase family A member 2	Homo sapiens	202-205
9115635-6	1997	Treatment of PDIp with peptide:N-glycosidase F caused PDIp down shift in the NaDodSO4-PAGE gel, indicating that PDIp is a glycoprotein.	nadodso4	77-85	protein disulfide isomerase family A member 2	Homo sapiens	13-17
9115635-6	1997	Treatment of PDIp with peptide:N-glycosidase F caused PDIp down shift in the NaDodSO4-PAGE gel, indicating that PDIp is a glycoprotein.	nadodso4	77-85	protein disulfide isomerase family A member 2	Homo sapiens	54-58
9115635-6	1997	Treatment of PDIp with peptide:N-glycosidase F caused PDIp down shift in the NaDodSO4-PAGE gel, indicating that PDIp is a glycoprotein.	nadodso4	77-85	protein disulfide isomerase family A member 2	Homo sapiens	54-58
1720555-1	1991	The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu).	Alanine	218-221	protein disulfide isomerase family A member 2	Homo sapiens	201-204
1720555-1	1991	The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu).	Pro-Trp-Cys	222-233	protein disulfide isomerase family A member 2	Homo sapiens	201-204
1720555-1	1991	The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu).	Cysteine	230-233	protein disulfide isomerase family A member 2	Homo sapiens	201-204
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	disulphide	48-58	protein disulfide isomerase family A member 2	Homo sapiens	69-72
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	Glutathione Disulfide	135-138	protein disulfide isomerase family A member 2	Homo sapiens	69-72
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	Glutathione Disulfide	141-145	protein disulfide isomerase family A member 2	Homo sapiens	69-72
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	dithiol	170-177	protein disulfide isomerase family A member 2	Homo sapiens	69-72
2025221-2	1991	The redox properties of the active-site dithiol/disulphide groups of PDI were determined by equilibrating the enzyme with an excess of GSH + GSSG, rapidly alkylating the dithiol form of the enzyme to inactivate it irreversibly, and determining the proportion of the disulphide form by measuring the residual activity under standard conditions.	disulphide	266-276	protein disulfide isomerase family A member 2	Homo sapiens	69-72
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	dithiol	49-56	protein disulfide isomerase family A member 2	Homo sapiens	33-36
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	dithiol	49-56	protein disulfide isomerase family A member 2	Homo sapiens	139-142
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	disulphide	57-67	protein disulfide isomerase family A member 2	Homo sapiens	33-36
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	disulphide	57-67	protein disulfide isomerase family A member 2	Homo sapiens	139-142
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	Glutathione Disulfide	191-194	protein disulfide isomerase family A member 2	Homo sapiens	33-36
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	Niacinamide	196-208	protein disulfide isomerase family A member 2	Homo sapiens	33-36
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	Dithiothreitol	236-250	protein disulfide isomerase family A member 2	Homo sapiens	33-36
2025221-6	1991	The standard redox potential for PDI active-site dithiol/disulphide couples was calculated from this result and found to be -0.11 V; hence PDI is a stronger oxidant and weaker reductant than GSH, nicotinamide cofactors, thioredoxin and dithiothreitol.	Dithiothreitol	236-250	protein disulfide isomerase family A member 2	Homo sapiens	139-142
2025221-8	1991	The redox equilibrium data for PDI with the GSH/GSSG redox couple showed sigmoidal deviations from linearity.	Glutathione Disulfide	44-47	protein disulfide isomerase family A member 2	Homo sapiens	31-34
2025221-8	1991	The redox equilibrium data for PDI with the GSH/GSSG redox couple showed sigmoidal deviations from linearity.	Glutathione Disulfide	48-52	protein disulfide isomerase family A member 2	Homo sapiens	31-34
33808471-5	2021	Moreover, redox-regulated protein disulfide isomerase (PDI) chaperones have an essential role in catalyzing formation of disulfide bonds in viral proteins.	Disulfides	34-43	protein disulfide isomerase family A member 2	Homo sapiens	55-58
33808471-6	2021	This review aims at describing the role of GSH in modulating redox sensitive pathways, in particular that mediated by NF-kB, and PDI activity.	Glutathione	43-46	protein disulfide isomerase family A member 2	Homo sapiens	129-132
34379416-3	2021	Using all-atom molecular dynamics (MD) simulations and Markov state modeling (MSM), we unveil the influence of glycans on the conformational flexibility of the multidomain protein disulfide isomerase (PDI), which is a ubiquitous chaperone in the endoplasmic reticulum (ER).	Polysaccharides	111-118	protein disulfide isomerase family A member 2	Homo sapiens	201-204
34379416-4	2021	Yeast PDI (yPDI) from Saccharomyces cerevisiae is glycosylated at asparagine side chains and the knowledge of its five modified sites enables a realistic computational modeling.	Asparagine	66-76	protein disulfide isomerase family A member 2	Homo sapiens	6-9
34379416-5	2021	We compare simulations of glycosylated and unglycosylated yPDI and find that the presence of glycan-glycan and glycan-protein interactions influences the flexibility of PDI in different ways.	glycan-glycan	93-106	protein disulfide isomerase family A member 2	Homo sapiens	169-172
34379416-5	2021	We compare simulations of glycosylated and unglycosylated yPDI and find that the presence of glycan-glycan and glycan-protein interactions influences the flexibility of PDI in different ways.	Polysaccharides	111-117	protein disulfide isomerase family A member 2	Homo sapiens	169-172
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	73-82	protein disulfide isomerase family A member 2	Homo sapiens	118-123
34436011-8	2021	Network analysis showed significant difference in immune response and in disulfide bond formation, with EGR1/EGR2 and PDIA2 genes as regulators for immune response and disulfide bond formation, respectively.	Disulfides	168-177	protein disulfide isomerase family A member 2	Homo sapiens	118-123
34206252-3	2021	hPDI can interact with 17beta-estradiol (E2), an endogenous female sex hormone.	Estradiol	23-39	protein disulfide isomerase family A member 2	Homo sapiens	0-4
34206252-3	2021	hPDI can interact with 17beta-estradiol (E2), an endogenous female sex hormone.	Estradiol	41-43	protein disulfide isomerase family A member 2	Homo sapiens	0-4
34206252-8	2021	A steered molecular dynamics analysis shows that the forces required to separate the two subunits (namely, hPDI and hMTPalpha subunit) of the hMTP complex in the absence of E2 are significantly higher than the forces required to separate the complex in which its hPDI is already bound with E2.	Estradiol	173-175	protein disulfide isomerase family A member 2	Homo sapiens	107-111
34206252-8	2021	A steered molecular dynamics analysis shows that the forces required to separate the two subunits (namely, hPDI and hMTPalpha subunit) of the hMTP complex in the absence of E2 are significantly higher than the forces required to separate the complex in which its hPDI is already bound with E2.	Estradiol	290-292	protein disulfide isomerase family A member 2	Homo sapiens	263-267
34206252-9	2021	E2 makes the interface between hMTPalpha and hPDI subunits more flexible and less stable.	Estradiol	0-2	protein disulfide isomerase family A member 2	Homo sapiens	45-49
35099693-3	2022	In this paper, Pd/SBA-15 catalysts (Pd-IP/S15) were prepared by NaOH treatment of surface hydroxyl groups on SBA-15, the ion exchange of Na+ with Pd(NH3)42+, and then reduction of Pd ions via glow discharge plasma.	Palladium	15-17	protein disulfide isomerase family A member 2	Homo sapiens	36-41
35099693-3	2022	In this paper, Pd/SBA-15 catalysts (Pd-IP/S15) were prepared by NaOH treatment of surface hydroxyl groups on SBA-15, the ion exchange of Na+ with Pd(NH3)42+, and then reduction of Pd ions via glow discharge plasma.	sba	18-21	protein disulfide isomerase family A member 2	Homo sapiens	36-41
35099693-3	2022	In this paper, Pd/SBA-15 catalysts (Pd-IP/S15) were prepared by NaOH treatment of surface hydroxyl groups on SBA-15, the ion exchange of Na+ with Pd(NH3)42+, and then reduction of Pd ions via glow discharge plasma.	Sodium Hydroxide	64-68	protein disulfide isomerase family A member 2	Homo sapiens	36-41
35099693-3	2022	In this paper, Pd/SBA-15 catalysts (Pd-IP/S15) were prepared by NaOH treatment of surface hydroxyl groups on SBA-15, the ion exchange of Na+ with Pd(NH3)42+, and then reduction of Pd ions via glow discharge plasma.	sba	109-112	protein disulfide isomerase family A member 2	Homo sapiens	36-41
35099693-3	2022	In this paper, Pd/SBA-15 catalysts (Pd-IP/S15) were prepared by NaOH treatment of surface hydroxyl groups on SBA-15, the ion exchange of Na+ with Pd(NH3)42+, and then reduction of Pd ions via glow discharge plasma.	Palladium	180-182	protein disulfide isomerase family A member 2	Homo sapiens	36-41
35099693-7	2022	Pd NPs with high dispersion are obtained on SBA-15, which enhances the catalytic activity of Pd-IP/S15.	SBA-15	44-50	protein disulfide isomerase family A member 2	Homo sapiens	93-98
35099693-8	2022	The coordination of Pd NPs with O of Si-OH on SBA-15 enabled Pd-IP/S15 to exhibit excellent catalytic stability.	Silicon	37-39	protein disulfide isomerase family A member 2	Homo sapiens	61-66
35099693-8	2022	The coordination of Pd NPs with O of Si-OH on SBA-15 enabled Pd-IP/S15 to exhibit excellent catalytic stability.	SBA-15	46-52	protein disulfide isomerase family A member 2	Homo sapiens	61-66