PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33742523-1 2021 The protein disulphide isomerase (PDI) gene family is a large, diverse group of enzymes recognised for their roles in disulphide bond formation within the endoplasmic reticulum (ER). disulphide 12-22 prolyl 4-hydroxylase subunit beta Homo sapiens 34-37 2619767-2 1989 The process is catalysed within the lumen of the endoplasmic reticulum by the enzyme protein disulphide-isomerase (PDI), which is abundant in secretory cells and catalyses thiol: protein-disulphide interchange in vitro with very broad protein substrate specificity. disulphide 93-103 prolyl 4-hydroxylase subunit beta Homo sapiens 115-118 2619767-3 1989 The presence of PDI within microsomal vesicles is essential for efficient and rapid cotranslational disulphide bond formation during protein synthesis in vitro. disulphide 100-110 prolyl 4-hydroxylase subunit beta Homo sapiens 16-19 3173483-0 1988 Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes. disulphide 40-50 prolyl 4-hydroxylase subunit beta Homo sapiens 60-88 3173483-1 1988 The formation of disulphide bonds in mammalian secretory and cell-surface proteins occurs in the lumen of the endoplasmic reticulum and is believed to be catalysed by the enzyme protein disulphide-isomerase (PDI). disulphide 17-27 prolyl 4-hydroxylase subunit beta Homo sapiens 178-206 3173483-1 1988 The formation of disulphide bonds in mammalian secretory and cell-surface proteins occurs in the lumen of the endoplasmic reticulum and is believed to be catalysed by the enzyme protein disulphide-isomerase (PDI). disulphide 17-27 prolyl 4-hydroxylase subunit beta Homo sapiens 208-211 3173483-3 1988 A clear requirement for PDI in the correct folding or assembly of disulphide-bonded proteins during biosynthesis has not been demonstrated. disulphide 66-76 prolyl 4-hydroxylase subunit beta Homo sapiens 24-27 6615425-7 1983 The purified enzyme will also catalyse net reduction of insulin disulphide bonds by reduced glutathione (i.e. it has thiol:protein-disulphide oxidoreductase or glutathione:insulin transhydrogenase activity), but this requires considerably higher concentrations of enzyme and reduced glutathione than does the disulphide-isomerization activity. disulphide 64-74 prolyl 4-hydroxylase subunit beta Homo sapiens 160-196 33023153-11 2020 PDIA1-dependent regulation of cancer-endothelial cell interactions involves disulphide exchange and most likely integrin activation but is not mediated by the regulation of ICAM-1 expression or changes in cellular bioenergetics in breast cancer or endothelial cells. disulphide 76-86 prolyl 4-hydroxylase subunit beta Homo sapiens 0-5 33466919-6 2021 By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1. disulphide 210-220 prolyl 4-hydroxylase subunit beta Homo sapiens 42-45 33466919-6 2021 By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1. disulphide 210-220 prolyl 4-hydroxylase subunit beta Homo sapiens 138-141 33466919-6 2021 By probing the alternative orientation of PDI with respect to hVKORC1, the functionally related noncovalent complex formed by hVKORC1 and PDI was found, which is proposed to be a first precursor to probe thiol-disulphide exchange reactions between PDI and hVKORC1. disulphide 210-220 prolyl 4-hydroxylase subunit beta Homo sapiens 138-141 25520620-5 2014 Protein disulphide isomerase (PDI) is a disulphide bond-modulating ER chaperone, which can also facilitate the ER-associated degradation (ERAD) of misfolded proteins. disulphide 8-18 prolyl 4-hydroxylase subunit beta Homo sapiens 30-33 32872499-5 2020 Disulphide formation in nascent polypeptides is discussed with focus on (i) its mechanistic relationship with conformational folding, (ii) evidence for its occurrence at the co-translational stage during ER entry, and (iii) the role of protein disulphide isomerase (PDI) family members. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 236-264 32872499-5 2020 Disulphide formation in nascent polypeptides is discussed with focus on (i) its mechanistic relationship with conformational folding, (ii) evidence for its occurrence at the co-translational stage during ER entry, and (iii) the role of protein disulphide isomerase (PDI) family members. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 266-269 27786579-2 2017 PDI and ERp57 also possess disulphide interchange activity, in which protein disulphide bonds are oxidized, reduced and isomerized, to form their native conformation. disulphide 27-37 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 27786579-2 2017 PDI and ERp57 also possess disulphide interchange activity, in which protein disulphide bonds are oxidized, reduced and isomerized, to form their native conformation. disulphide 77-87 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 31069770-2 2019 PDI catalyzes the reduction, oxidation, or isomerization of disulphide bonds in its substrate proteins. disulphide 60-70 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 24697695-7 2014 This discrepancy may suggest that disulphide bonds in cargo proteins can be utilized to oxidize PDI, hence facilitating substrate detachment and degradation also in the absence of Ero1. disulphide 34-44 prolyl 4-hydroxylase subunit beta Homo sapiens 96-99 21057456-1 2010 Disulphide formation in the endoplasmic reticulum (ER) is catalysed by members of the protein disulphide isomerase (PDI) family. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 86-114 23533690-7 2013 PDI is essential for normal protein folding by oxidation and reduction of disulphide bonds, and hence any disruption to this process may have consequences for motor neurons. disulphide 74-84 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 21250820-1 2011 Protein disulphide isomerase (PDI) in the endoplasmic reticulum catalyzes the rearrangement of disulphide bridges during folding of secreted proteins. disulphide 8-18 prolyl 4-hydroxylase subunit beta Homo sapiens 30-33 21424268-1 2011 In living systems, protein disulphide isomerase (PDI, EC 5.3.4.1) regulates the formation of new disulphide bonds in proteins (oxidase activity) and catalyzes the rearrangement of non-native disulphide bonds (isomerase activity), leading proteins towards their native configuration. disulphide 27-37 prolyl 4-hydroxylase subunit beta Homo sapiens 49-52 21424268-1 2011 In living systems, protein disulphide isomerase (PDI, EC 5.3.4.1) regulates the formation of new disulphide bonds in proteins (oxidase activity) and catalyzes the rearrangement of non-native disulphide bonds (isomerase activity), leading proteins towards their native configuration. disulphide 97-107 prolyl 4-hydroxylase subunit beta Homo sapiens 19-47 21424268-1 2011 In living systems, protein disulphide isomerase (PDI, EC 5.3.4.1) regulates the formation of new disulphide bonds in proteins (oxidase activity) and catalyzes the rearrangement of non-native disulphide bonds (isomerase activity), leading proteins towards their native configuration. disulphide 97-107 prolyl 4-hydroxylase subunit beta Homo sapiens 49-52 21424268-5 2011 These reactions were thought to involve oxidation of disulphide bonds between CCCs and wool or hair cysteine residues, catalyzed by the oxidized PDI active site. disulphide 53-63 prolyl 4-hydroxylase subunit beta Homo sapiens 145-148 21424268-6 2011 On the other hand, PDI was demonstrated to enhance the migration of a disulphide bond-functionalized dye within the keratin matrix and trigger the release of RNase A from wool fibres" surface. disulphide 70-80 prolyl 4-hydroxylase subunit beta Homo sapiens 19-22 21424268-7 2011 These observations may indicate that an isomerisation reaction occurred, catalyzed by the reduced PDI active site, to achieve the thiol-disulphide exchange, i.e. the rearrangement of disulphide bonds between CCCs and keratin. disulphide 136-146 prolyl 4-hydroxylase subunit beta Homo sapiens 98-101 21424268-7 2011 These observations may indicate that an isomerisation reaction occurred, catalyzed by the reduced PDI active site, to achieve the thiol-disulphide exchange, i.e. the rearrangement of disulphide bonds between CCCs and keratin. disulphide 183-193 prolyl 4-hydroxylase subunit beta Homo sapiens 98-101 24348565-4 2013 PDI catalyzes the rearrangement and formation of disulphide bonds, thus facilitating protein folding, and in neurodegeneration may act to ameliorate the burden of protein misfolding. disulphide 49-59 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 22492663-1 2012 P5, one of the protein disulphide isomerase (PDI) family members, catalyses disulphide bond formation in proteins and exhibits molecular chaperone and calcium binding activities in vitro, whereas its physiological significance remains controversial. disulphide 23-33 prolyl 4-hydroxylase subunit beta Homo sapiens 45-48 21057456-1 2010 Disulphide formation in the endoplasmic reticulum (ER) is catalysed by members of the protein disulphide isomerase (PDI) family. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 116-119 21057456-5 2010 Here, we demonstrate that several members of the PDI family are able to directly reduce this PrxIV disulphide and in the process become oxidized. disulphide 99-109 prolyl 4-hydroxylase subunit beta Homo sapiens 49-52 21057456-7 2010 The oxidation of PDI family members by PrxIV is a highly efficient process and demonstrates how oxidation by H(2)O(2) can be coupled to disulphide formation. disulphide 136-146 prolyl 4-hydroxylase subunit beta Homo sapiens 17-20 21057456-8 2010 Oxidation of PDI by PrxIV may therefore increase efficiency of disulphide formation by Ero1 and also allows disulphide formation via alternative sources of H(2)O(2). disulphide 63-73 prolyl 4-hydroxylase subunit beta Homo sapiens 13-16 21057456-8 2010 Oxidation of PDI by PrxIV may therefore increase efficiency of disulphide formation by Ero1 and also allows disulphide formation via alternative sources of H(2)O(2). disulphide 108-118 prolyl 4-hydroxylase subunit beta Homo sapiens 13-16 20802462-4 2010 We find PDI to be the main substrate of Ero1alpha, and mixed-disulphide complexes of Ero1 primarily form with PDI, to a lesser extent with the PDI-family members ERp57 and ERp72, but are not detectable with another homologue TMX3. disulphide 61-71 prolyl 4-hydroxylase subunit beta Homo sapiens 110-113 20802462-0 2010 Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 35-38 20802462-3 2010 Both the oxidase Ero1alpha and the oxidoreductase protein disulphide isomerase (PDI) strongly contribute to the rapid recovery kinetics, but experiments in ERO1-deficient cells indicate the existence of parallel pathways for disulphide generation. disulphide 58-68 prolyl 4-hydroxylase subunit beta Homo sapiens 80-83 20802462-4 2010 We find PDI to be the main substrate of Ero1alpha, and mixed-disulphide complexes of Ero1 primarily form with PDI, to a lesser extent with the PDI-family members ERp57 and ERp72, but are not detectable with another homologue TMX3. disulphide 61-71 prolyl 4-hydroxylase subunit beta Homo sapiens 110-113 15960611-2 2005 In this paper, we present a sensitive fluorimetric assay for continuous determination of disulphide reduction activity of PDI. disulphide 89-99 prolyl 4-hydroxylase subunit beta Homo sapiens 122-125 18028487-6 2008 Finally, using purified proteins PDI had greater ability to isomerize disulphide bonds than the alphaIIbbeta3 integrin, which also has PDI-like activity. disulphide 70-80 prolyl 4-hydroxylase subunit beta Homo sapiens 33-36 16724068-4 2006 PDI catalyses thiol-disulphide exchange, thus facilitating disulphide bond formation and rearrangement reactions. disulphide 20-30 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 16724068-4 2006 PDI catalyses thiol-disulphide exchange, thus facilitating disulphide bond formation and rearrangement reactions. disulphide 59-69 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 18971943-1 2008 Formation of disulphide bonds within the mammalian endoplasmic reticulum (ER) requires the combined activities of Ero1alpha and protein disulphide isomerase (PDI). disulphide 13-23 prolyl 4-hydroxylase subunit beta Homo sapiens 128-156 18971943-1 2008 Formation of disulphide bonds within the mammalian endoplasmic reticulum (ER) requires the combined activities of Ero1alpha and protein disulphide isomerase (PDI). disulphide 13-23 prolyl 4-hydroxylase subunit beta Homo sapiens 158-161 16246124-2 2005 Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 141-144 16246124-2 2005 Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 146-174 16246124-2 2005 Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. disulphide 72-82 prolyl 4-hydroxylase subunit beta Homo sapiens 141-144 16246124-2 2005 Disulphide bonds are formed in many of these proteins through a dithiol-disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. disulphide 72-82 prolyl 4-hydroxylase subunit beta Homo sapiens 146-174 15960611-6 2005 Therefore the PDI-dependent disulphide reduction can be monitored by the increase in fluorescence accompanying the loss of proximity-quenching upon conversion of diabz-GSSG into abz-GSH. disulphide 28-38 prolyl 4-hydroxylase subunit beta Homo sapiens 14-17 22358923-5 1996 This will be especially significant in the case of antibodies as each molecule consists of 4 chains linked by disulphide bonds which require specific intracellular factors to be properly folded and processed (Heavy chain binding protein, Protein Disulfide Isomerase a.o.). disulphide 110-120 prolyl 4-hydroxylase subunit beta Homo sapiens 238-265 15643448-2 2005 Protein disulphide isomerase (PDI) is now known to catalyse all of the reactions that are involved in native disulphide bond formation, but despite more than 40 years of study, its mechanism of action is still not fully understood. disulphide 8-18 prolyl 4-hydroxylase subunit beta Homo sapiens 30-33 15493980-2 2004 Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 147-175 15493980-2 2004 Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. disulphide 0-10 prolyl 4-hydroxylase subunit beta Homo sapiens 177-180 15493980-3 2004 This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exist within the same compartment and why so many oxidoreductases exist when PDI alone can perform all three of these functions. disulphide 117-127 prolyl 4-hydroxylase subunit beta Homo sapiens 353-356 10754564-5 2000 Contributions of PDI homologues to the catalysis of oxidative folding will be discussed, as will similarities between eukaryotic and prokaryotic disulphide-bond-forming systems. disulphide 145-155 prolyl 4-hydroxylase subunit beta Homo sapiens 17-20 15171728-2 2004 PDI (protein disulphide-isomerase) has recently been found to be localized to the cell surface, where it exhibits both disulphide-exchange and denitrosation activities. disulphide 13-23 prolyl 4-hydroxylase subunit beta Homo sapiens 0-3 15171728-3 2004 The disulphide-exchange activity of PDI has been linked to aspects of platelet aggregation. disulphide 4-14 prolyl 4-hydroxylase subunit beta Homo sapiens 36-39 15171728-9 2004 Secondly, RSNOs are denitrosated at the same PDI-active site that catalyses the disulphide bond formation between integrins and their ligands, thereby attenuating irreversible aggregation. disulphide 80-90 prolyl 4-hydroxylase subunit beta Homo sapiens 45-48 10573423-2 1999 Evidence indicates that members of the protein disulphide isomerase (PDI) superfamily are part of the machinery needed for proper oxidation and isomerization of disulphide bonds. disulphide 47-57 prolyl 4-hydroxylase subunit beta Homo sapiens 69-72 10573423-7 1999 We show that the endoplasmic-reticulum-resident oxidoreductases PDI and ERp57 are directly involved in disulphide oxidation and isomerization, and, together with the lectins calnexin and calreticulin, are central in glycoprotein folding in the endoplasmic reticulum of mammalian cells. disulphide 103-113 prolyl 4-hydroxylase subunit beta Homo sapiens 64-67 9560306-1 1998 Protein disulphide isomerase (PDI) has been shown to be a multifunctional protein capable of catalysing disulphide-bond formation and isomerization, and of participating as a non-catalytic subunit of prolyl 4-hydroxylase (P4-H) and microsomal triacylglycerol transfer protein. disulphide 8-18 prolyl 4-hydroxylase subunit beta Homo sapiens 30-33 9310357-6 1997 The interaction between PDI and the bound peptide therefore is enhanced by the formation of mixed disulphide bonds. disulphide 98-108 prolyl 4-hydroxylase subunit beta Homo sapiens 24-27 1816070-1 1991 The Protein disulphide-isomerase (PDI, EC 5.3.4.1, Thiol-proteindisulphide oxidoreductase, EC 1.8.4.2) is thought to regulate the sulfhydryl status of cells and to catalyze thiol/disulphide exchange reactions involved in the post-translational processing of disulphide containing secretory proteins. disulphide 64-74 prolyl 4-hydroxylase subunit beta Homo sapiens 4-32 1522109-2 1992 The observation that these lipoprotein particles are heavily disulphide crosslinked is paradoxical since HBsAg assembly is classically believed to occur in the ER, and hence in the presence of high levels of protein disulphide isomerase (PDI) which should resolve these higher intermolecular crosslinks. disulphide 61-71 prolyl 4-hydroxylase subunit beta Homo sapiens 208-236 1522109-3 1992 Indeed, incubation of mature, highly disulphide crosslinked HBsAg with recombinant PDI causes the disassembly of HBsAg to dimers. disulphide 37-47 prolyl 4-hydroxylase subunit beta Homo sapiens 83-86 8037666-3 1994 The coincidence of the similar apparent optimum pH values of uncatalysed and PDI-catalysed reactions suggests that conditions favourable to spontaneous refolding of proteins may help PDI to catalyse thiol/disulphide interchange. disulphide 205-215 prolyl 4-hydroxylase subunit beta Homo sapiens 77-80 8037666-3 1994 The coincidence of the similar apparent optimum pH values of uncatalysed and PDI-catalysed reactions suggests that conditions favourable to spontaneous refolding of proteins may help PDI to catalyse thiol/disulphide interchange. disulphide 205-215 prolyl 4-hydroxylase subunit beta Homo sapiens 183-186 8037666-4 1994 Under the conditions described here no exogenously added dithiothreitol was required for PDI-catalysed renaturation, implying that the disulphide form of PDI was reduced to its active form by the free thiol groups in prochymosin molecules. disulphide 135-145 prolyl 4-hydroxylase subunit beta Homo sapiens 154-157 1816070-1 1991 The Protein disulphide-isomerase (PDI, EC 5.3.4.1, Thiol-proteindisulphide oxidoreductase, EC 1.8.4.2) is thought to regulate the sulfhydryl status of cells and to catalyze thiol/disulphide exchange reactions involved in the post-translational processing of disulphide containing secretory proteins. disulphide 12-22 prolyl 4-hydroxylase subunit beta Homo sapiens 34-37 1816070-1 1991 The Protein disulphide-isomerase (PDI, EC 5.3.4.1, Thiol-proteindisulphide oxidoreductase, EC 1.8.4.2) is thought to regulate the sulfhydryl status of cells and to catalyze thiol/disulphide exchange reactions involved in the post-translational processing of disulphide containing secretory proteins. disulphide 64-74 prolyl 4-hydroxylase subunit beta Homo sapiens 34-37 2025220-12 1991 The activity of PDI in thiol/disulphide interchange derives from the presence of vicinal dithiol groups in which one thiol group of each pair has an unusually low pK and high nucleophilic reactivity at physiological pH. disulphide 29-39 prolyl 4-hydroxylase subunit beta Homo sapiens 16-19 2025222-2 1991 The activities of protein disulphide-isomerase (PDI) and thioredoxin in catalysing disulphide bond isomerization in a protein substrate were compared by using the standard assay, namely the re-activation of "scrambled" RNAase. disulphide 26-36 prolyl 4-hydroxylase subunit beta Homo sapiens 48-51 34474345-1 2021 The catalysis of disulphide (SS) bonds is the most important characteristic of protein disulphide isomerase (PDI) family. disulphide 17-27 prolyl 4-hydroxylase subunit beta Homo sapiens 79-107 34474345-1 2021 The catalysis of disulphide (SS) bonds is the most important characteristic of protein disulphide isomerase (PDI) family. disulphide 17-27 prolyl 4-hydroxylase subunit beta Homo sapiens 109-112