PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16778134-8 2006 OxLDL or exogenous H2O2 oxidized GAPDH thiols, decreasing GAPDH protein half-life and increasing GAPDH sensitivity to proteasome-mediated protein degradation in vitro. Sulfhydryl Compounds 39-45 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 33-38 8327504-4 1993 Exposure of GAPDH modified by NAD in the presence of SNP to HgCl2, which acts at thiol linkages, released two products. Sulfhydryl Compounds 81-86 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 12-17 8327504-9 1993 These results demonstrate that NO-stimulated modification of GAPDH with NAD is not ADP-ribosylation as previously reported but rather is covalent binding of NAD through a NO-dependent thiol intermediate, possibly providing an example of an unexpected, altered reactivity of a nitrosylated protein. Sulfhydryl Compounds 184-189 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 61-66 8177227-1 1993 The activity lost during storage of a solution of muscle glyceraldehyde 3-phosphate dehydrogenase was rapidly restored on adding a thiol compound, but not arsenite or azide. Sulfhydryl Compounds 131-136 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 57-97 2297224-1 1990 The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status. Sulfhydryl Compounds 20-25 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 43-83 2297224-1 1990 The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status. Sulfhydryl Compounds 20-25 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 85-88 2297224-1 1990 The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status. Sulfhydryl Compounds 159-164 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 43-83 2297224-1 1990 The activity of the thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase (GPD), in vertebrate cells, was modulated by a change in the intracellular thiol:disulfide redox status. Sulfhydryl Compounds 159-164 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 85-88 2297224-3 1990 Loss of reduced protein thiols, as measured by binding of the thiol reagent iodoacetic acid to GPD, and loss of GPD enzymatic activity occurred in a dose-dependent manner. Sulfhydryl Compounds 24-30 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 95-98 2297224-3 1990 Loss of reduced protein thiols, as measured by binding of the thiol reagent iodoacetic acid to GPD, and loss of GPD enzymatic activity occurred in a dose-dependent manner. Sulfhydryl Compounds 24-29 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 95-98 2297224-5 1990 The enzymatic recovery of GPD activity was observed either without addition of thiols to the medium or by incubation of a sonicated cell mixture with 2 mM cysteine, cystine, cysteamine, or glutathione (GSH); GSSG had no effect. Sulfhydryl Compounds 79-85 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-29 2297224-8 1990 These findings indicate that the cellular thiol redox status can be important in determining GPD enzymatic activity. Sulfhydryl Compounds 42-47 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-96 6395896-3 1984 Heavy atom effects observed in the CH3Hg(II)-sulfhydryl complex of pig GAPD resemble closely those reported earlier for the analogous rabbit GAPD-CH3Hg(II) complex. Sulfhydryl Compounds 45-55 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 141-145 2716009-6 1989 We suggest that intrachondrocyte oxidant damage occurs through oxidation of the sensitive thiol (-SH) residue at the active center of G-3-PDH, with subsequent reduction in the rate of glycolytic ATP synthesis and the intracellular concentration of ATP which is required for DNA, protein, proteoglycan and hyaluronic acid synthesis. Sulfhydryl Compounds 90-95 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 134-141 3675570-0 1987 Reversible oxidation of glyceraldehyde 3-phosphate dehydrogenase thiols in human lung carcinoma cells by hydrogen peroxide. Sulfhydryl Compounds 65-71 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 24-64 3675570-6 1987 Glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) has been identified as the protein undergoing thiol/disulfide redox status and enzymic activity changes. Sulfhydryl Compounds 101-106 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-40 4287347-0 1966 Influence of substrate-induced enzymic inactivation on the sulfhydryl content of glyceraldehyde-3-phosphate dehydrogenase. Sulfhydryl Compounds 59-69 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 81-121 7158169-0 1982 Human muscle glyceraldehyde-3-phosphate dehydrogenase: reactivity of sulphydryl groups. Sulfhydryl Compounds 69-79 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 13-53 7158169-2 1982 The kinetics of the reaction of thiol groups of glyceraldehyde-3-phosphate dehydrogenase from human muscle with 5,5"-dithiobis-2-nitrobenzoate (DTNB) was studied spectrophotometrically using the conventional and stopped-flow methods. Sulfhydryl Compounds 32-37 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 48-88 684756-3 1978 The activity of glyceraldehyde-3-phosphate dehydrogenase was inhibited by blocking thiol-groups with the mercury compounds. Sulfhydryl Compounds 83-88 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 16-56 684756-7 1978 Thioltransferase, known to catalyze thiol-disulfide exchange reactions, increased the regain of glyceraldehyde-3-phosphate dehydrogenase activity to nearly the original value. Sulfhydryl Compounds 36-41 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 96-136 207651-1 1978 The yields in molecules per 100 eV for active-site and sulphydryl loss from glyceraldehyde-3-phosphate dehydrogenase have been determined in nitrous-oxide-saturated, aerated and argon-saturated solutions. Sulfhydryl Compounds 55-65 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 76-116 13084626-0 1953 Coenzyme binding and the thiol groups of glyceraldehyde-3-phosphate dehydrogenase. Sulfhydryl Compounds 25-30 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 41-81 1000490-6 1976 In addition, those enzymes that have been demonstrated to be most sensitive to established sulfhydryl inhibitors, such as glyceraldehyde-3-phosphate dehydrogenase, were also most sensitive to rhodium(II) carboxylate inactivation. Sulfhydryl Compounds 91-101 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 122-162 4975312-2 1969 The amino acid sequences around the thiol groups of glyceraldehyde 3-phosphate dehydrogenase from badger and monkey skeletal muscle were compared with the sequences around the thiol groups in the enzyme isolated from other organisms. Sulfhydryl Compounds 36-41 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-92 4975312-2 1969 The amino acid sequences around the thiol groups of glyceraldehyde 3-phosphate dehydrogenase from badger and monkey skeletal muscle were compared with the sequences around the thiol groups in the enzyme isolated from other organisms. Sulfhydryl Compounds 176-181 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-92 13714413-3 1961 The heat lability, substrate and coenzyme specificity, and sulfhydryl and phosphate dependence of the tissue component catalyzing this reaction indicate that glyceraldehyde-3-phosphate dehydrogenase activity is being demonstrated. Sulfhydryl Compounds 59-69 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 158-198 25196942-0 2015 Thiol-based regulation of glyceraldehyde-3-phosphate dehydrogenase in blood bank-stored red blood cells: a strategy to counteract oxidative stress. Sulfhydryl Compounds 0-5 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-66 33055209-6 2020 This adaptive metabolic switch is rapid, reversible, and accompanied by thiol-mediated changes in the structures and activities of key glycolytic signaling pathway proteins, including GAPDH and G6PD. Sulfhydryl Compounds 72-77 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 184-189 31760917-2 2019 The main problem of selective GAPDH inhibition is a highly conserved nature of the enzyme active site and, especially, Cys150 environment important for the catalytic action of cysteine sulfhydryl group. Sulfhydryl Compounds 176-195 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 30-35 31111667-7 2019 GAPDH, with a thiol group in its active site, is more sensitive to Ag than MDH, displaying many thiol groups but none in its active site, suggesting that thiol groups at the active site strongly determines the sensitivity of enzymes toward AgNPs. Sulfhydryl Compounds 14-19 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 31111667-7 2019 GAPDH, with a thiol group in its active site, is more sensitive to Ag than MDH, displaying many thiol groups but none in its active site, suggesting that thiol groups at the active site strongly determines the sensitivity of enzymes toward AgNPs. Sulfhydryl Compounds 96-101 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 31111667-7 2019 GAPDH, with a thiol group in its active site, is more sensitive to Ag than MDH, displaying many thiol groups but none in its active site, suggesting that thiol groups at the active site strongly determines the sensitivity of enzymes toward AgNPs. Sulfhydryl Compounds 96-101 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 27405778-2 2016 Previous studies documented metabolic reprogramming in stored red blood cells (RBCs) and oxidation of GAPDH at functional residues upon exposure to pro-oxidants diamide and H2O2 Here we hypothesize that routine storage of erythrocyte concentrates promotes metabolic modulation of stored RBCs by targeting functional thiol residues of GAPDH. Sulfhydryl Compounds 316-321 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 102-107 32536603-7 2020 In E. coli, the most significant target of IR by a wide margin was glyceraldehyde 3"-phosphate dehydrogenase (GAPDH), in which the thiol side chain of the catalytic Cys residue was oxidized to sulfonic acid. Sulfhydryl Compounds 131-136 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 110-115 26898502-5 2016 We report that multiple thiol-containing proteins involved in metabolism and glycolysis; fructose bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and creatine kinase, together with a number of chaperone, antioxidant and structural proteins, were modified in a reversible manner in macrophages treated with HOSCN. Sulfhydryl Compounds 24-29 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 148-188 26898502-5 2016 We report that multiple thiol-containing proteins involved in metabolism and glycolysis; fructose bisphosphate aldolase, triosephosphate isomerase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and creatine kinase, together with a number of chaperone, antioxidant and structural proteins, were modified in a reversible manner in macrophages treated with HOSCN. Sulfhydryl Compounds 24-29 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 190-195 26873191-2 2016 Chemical profile is characterized by reactions with thiols and thiol proteins such as aldehyde dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, caspases among others. Sulfhydryl Compounds 52-58 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 110-150 26873191-2 2016 Chemical profile is characterized by reactions with thiols and thiol proteins such as aldehyde dehydrogenase, glyceraldehyde 3-phosphate dehydrogenase, caspases among others. Sulfhydryl Compounds 52-57 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 110-150 26453916-13 2015 The current study raises significant questions about the reported ability of H2S to activate GAPDH by the sulfuration of its active site thiol, and indicates that polysulfide is a stronger protein S-sulfurating agent than sulfide. Sulfhydryl Compounds 137-142 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-98 25196942-2 2015 Accumulating evidence in other cells indicates that oxidative thiol modifications in cytosolic GAPDH drive this molecule into functional avenues that deviate from glycolysis. Sulfhydryl Compounds 62-67 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 95-100 24064205-6 2013 Disulfiram, a thiol-modifying drug, inhibits both the dehydrogenase and GTN reductase activity of GAPDH, while DTT or tris(2-carboxyethyl)phosphine reverse the GTN-induced inhibition. Sulfhydryl Compounds 14-19 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 98-103 24662796-4 2014 In this review we describe how thiol modification of Cys-152 in GAPDH re-routes metabolic pathways in the cell and converts a metabolic enzyme into a pro-apoptotic factor. Sulfhydryl Compounds 31-36 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 64-69 23360541-7 2013 Thiolated siRNA targeting glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was directly conjugated to the polymeric micelles via thiol exchange reactions with the pyridal disulfide groups present in the micelle corona. Sulfhydryl Compounds 129-134 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-66 23895568-0 2013 Direct and nitroxyl (HNO)-mediated reactions of acyloxy nitroso compounds with the thiol-containing proteins glyceraldehyde 3-phosphate dehydrogenase and alkyl hydroperoxide reductase subunit C. Nitroxyl (HNO) reacts with thiols, and this reactivity requires the use of donors with 1-nitrosocyclohexyl acetate, pivalate, and trifluoroacetate, forming a new group. Sulfhydryl Compounds 83-88 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 109-149 23895568-0 2013 Direct and nitroxyl (HNO)-mediated reactions of acyloxy nitroso compounds with the thiol-containing proteins glyceraldehyde 3-phosphate dehydrogenase and alkyl hydroperoxide reductase subunit C. Nitroxyl (HNO) reacts with thiols, and this reactivity requires the use of donors with 1-nitrosocyclohexyl acetate, pivalate, and trifluoroacetate, forming a new group. Sulfhydryl Compounds 222-228 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 109-149 23360541-7 2013 Thiolated siRNA targeting glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was directly conjugated to the polymeric micelles via thiol exchange reactions with the pyridal disulfide groups present in the micelle corona. Sulfhydryl Compounds 129-134 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 68-73 19474219-9 2009 Furthermore, the relative capacity of thiols to support AsV reduction mediated by PNP, GPa, PTA, and GAPDH apparently depended on the type of arsenylated metabolites (i.e., arsenate ester or anhydride) produced by these enzymes. Sulfhydryl Compounds 38-44 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 101-106 23009681-7 2012 Both caused a loss of thiols on GAPDH and covalent attachment of quinones derived from TD to the protein. Sulfhydryl Compounds 22-28 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 32-37 22819842-6 2012 Using a proteomics approach with the thiol-specific probe, 5-iodoacetamidofluorescein, we show that several proteins including peptidylprolyl isomerase A (cyclophilin A), protein disulfide isomerase, glyceraldehyde-3-phosphate dehydrogenase and galectin-1 are particularly sensitive to oxidation by HOCl and N-chloramines formed at inflammatory sites. Sulfhydryl Compounds 37-42 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 200-240 19478237-12 2009 In conclusion, phosphorolytic enzymes, such as PNP, GAPDH, GPa, and PTA, promote thiol-dependent AsV reduction because they convert AsV into arsenylated products reducible by thiols more readily than AsV. Sulfhydryl Compounds 81-86 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-57 19478237-12 2009 In conclusion, phosphorolytic enzymes, such as PNP, GAPDH, GPa, and PTA, promote thiol-dependent AsV reduction because they convert AsV into arsenylated products reducible by thiols more readily than AsV. Sulfhydryl Compounds 175-181 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-57 19474219-10 2009 Importantly, AsV reduction by both acetyl-arsenate-producing enzymes (i.e., PTA and GAPDH) exhibited striking similarities in responsiveness to various thiols, thus highlighting the role of arsenylated metabolite formation. Sulfhydryl Compounds 152-158 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 84-89 18771724-5 2008 To investigate the functional modulation caused by binding of EGCG, we examined the interaction between EGCG and a thiol enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Sulfhydryl Compounds 115-120 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 129-169 18771724-5 2008 To investigate the functional modulation caused by binding of EGCG, we examined the interaction between EGCG and a thiol enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Sulfhydryl Compounds 115-120 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 171-176 16229492-6 2005 Ions at M + n x 31 units were detected in the ESI mass spectra of intact HCalB (n = 1-5) and GAPDH (n = 2), indicating conversion of thiol groups on these proteins to RSONH2 (+31 units). Sulfhydryl Compounds 133-138 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-98 16682416-6 2006 GAPDH inhibition displayed an IC(50) of approximately 3 microM for both nitroalkenes, an IC(50) equivalent to the potent thiol oxidant peroxynitrite (ONOO(-)) and an IC(50) 30-fold less than H(2)O(2), indicating that nitroalkenes are potent thiol-reactive species. Sulfhydryl Compounds 121-126 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 16682416-8 2006 Liquid chromatography-mass spectrometry-based proteomic analysis of human red cells confirmed that nitroalkenes readily undergo covalent, thiol-reversible post-translational modification of nucleophilic amino acids in GSH and GAPDH in vivo. Sulfhydryl Compounds 138-143 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 226-231 16337878-6 2006 For GAPDH each chloramine oxidized two thiols. Sulfhydryl Compounds 39-45 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 4-9 16337878-8 2006 Competition studies showed that thiols of CK were 4 times more reactive with taurine chloramine than thiols of GAPDH (rate constants of 1200 and 300 M-1s-1 respectively). Sulfhydryl Compounds 101-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 111-116 11890743-9 2002 The results demonstrate that cdb3 and GAPD contain reactive thiols that can be transnitrosylated mainly by means of GSNO; these can ultimately influence GAPD translocation/activity and the glycolytic flux. Sulfhydryl Compounds 60-66 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 38-42 16139273-1 2005 Erythrocyte glyceraldehyde-3-phosphate dehydrogenase (G3PD) is a glycolytic enzyme containing critical thiol groups and whose activity is reversibly inhibited by binding to the cell membrane. Sulfhydryl Compounds 103-108 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 12-52 16139273-1 2005 Erythrocyte glyceraldehyde-3-phosphate dehydrogenase (G3PD) is a glycolytic enzyme containing critical thiol groups and whose activity is reversibly inhibited by binding to the cell membrane. Sulfhydryl Compounds 103-108 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 54-58 15950210-11 2005 Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols. Sulfhydryl Compounds 121-127 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 23-28 15950210-11 2005 Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols. Sulfhydryl Compounds 121-127 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 115-120 15950210-11 2005 Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols. Sulfhydryl Compounds 121-127 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 115-120 15950210-11 2005 Thus, 9,10-PQ inhibits GAPDH by two distinct mechanisms: through ROS generation that results in the oxidization of GAPDH thiols, and by an oxygen-independent mechanism that results in the modification of GAPDH catalytic thiols. Sulfhydryl Compounds 220-226 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 23-28 12032148-6 2002 When a sulfhydryl enzyme, glyceraldehyde-3-phosphate dehydrogenase, was incubated with acrolein-modified bovine serum albumin in sodium phosphate buffer (pH 7.2) at 37 degrees C, a significant loss of sulfhydryl groups, which was accompanied by the loss of enzyme activity and the formation of high molecular mass protein species (>200 kDa), was observed. Sulfhydryl Compounds 7-17 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 26-66 12139975-9 2002 Such an interpretation is supported by the detection of the loss of thiol groups on GAPDH and the detection of cross-linked materials on protein gels. Sulfhydryl Compounds 68-73 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 84-89 11890743-2 2002 In this study we have investigated which NO-reactive thiols might be influencing GAPD translocation and the specific role of glutathione. Sulfhydryl Compounds 53-59 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 81-85 11890743-9 2002 The results demonstrate that cdb3 and GAPD contain reactive thiols that can be transnitrosylated mainly by means of GSNO; these can ultimately influence GAPD translocation/activity and the glycolytic flux. Sulfhydryl Compounds 60-66 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 153-157 10880356-4 2000 Furthermore, we show that c-Jun, p50, glycogen phosphorylase b, glyceraldehyde-3-phosphate dehydrogenase, creatine kinase, glutaredoxin and caspase-3 can be precipitated from a mixture of purified thiol-containing proteins by the formation of a mixed-disulphide bond with GSNO-Sepharose. Sulfhydryl Compounds 197-202 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 64-104 11885270-0 2002 S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin. Sulfhydryl Compounds 73-78 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 23-63 12369901-0 2001 Protein thiol modification of glyceraldehyde-3-phosphate dehydrogenase and caspase-3 by nitric oxide. Sulfhydryl Compounds 8-13 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 30-70 12369901-5 2001 Here, we summarize current knowledge on active site thiol modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and caspase-3 by nitric oxide. Sulfhydryl Compounds 52-57 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 74-114 12369901-5 2001 Here, we summarize current knowledge on active site thiol modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and caspase-3 by nitric oxide. Sulfhydryl Compounds 52-57 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 116-121 10516189-4 1999 Of the thiol enzymes we investigated, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was particularly susceptible to inactivation, creatine kinase was moderately susceptible, and lactate dehydrogenase was unaffected by HOCl at the concentrations used. Sulfhydryl Compounds 7-12 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 38-78 10516189-4 1999 Of the thiol enzymes we investigated, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was particularly susceptible to inactivation, creatine kinase was moderately susceptible, and lactate dehydrogenase was unaffected by HOCl at the concentrations used. Sulfhydryl Compounds 7-12 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 80-85 10391884-7 1999 Lys-C digestion of GAPDH, followed by peptide isolation by high performance liquid chromatography, matrix-assisted laser desorption ionization time-of-flight analysis, and Edman sequencing, demonstrated that NADH attachment occurred at Cys-149, the active-site thiol. Sulfhydryl Compounds 261-266 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 19-24 10391884-0 1999 Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase. Sulfhydryl Compounds 0-6 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 57-97 10391884-3 1999 We now demonstrate that in contrast to NO-mediated attachment of NAD, covalent attachment of NADH to GAPDH proceeds in the presence of low molecular weight thiols, independent of NO. Sulfhydryl Compounds 156-162 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 101-106 10391884-9 1999 Thus, linkage of GAPDH to NADH, in contrast to NAD, occurs in the presence of thiol, is independent of NO, and is mediated by superoxide. Sulfhydryl Compounds 78-83 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 17-22 8912669-1 1996 Previous studies have demonstrated that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) undergoes NAD(H) linkage to an active site thiol when it comes into contact with .NO-related oxidants. Sulfhydryl Compounds 132-137 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 40-80 10403526-2 1999 There are 16 free thiols, including 4 active site thiols, in a tetramer of GAPDH molecule. Sulfhydryl Compounds 18-24 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-80 10403526-2 1999 There are 16 free thiols, including 4 active site thiols, in a tetramer of GAPDH molecule. Sulfhydryl Compounds 50-56 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-80 10403526-4 1999 After treatment for 30 min, free thiols were maximally decreased to 8-10 per GAPDH tetramer and enzyme activity was also inhibited to 5-10% of control activity. Sulfhydryl Compounds 33-39 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 77-82 10403526-6 1999 Since similar results were obtained in the case of hydrogen peroxide (H2O2) treatment, which is known to oxidize the thiols, these effects of nitric oxide donors were probably due to modification of thiol groups present in a GAPDH molecule. Sulfhydryl Compounds 117-123 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 225-230 10403526-6 1999 Since similar results were obtained in the case of hydrogen peroxide (H2O2) treatment, which is known to oxidize the thiols, these effects of nitric oxide donors were probably due to modification of thiol groups present in a GAPDH molecule. Sulfhydryl Compounds 117-122 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 225-230 10403526-12 1999 These findings suggest that nitric oxide inhibits GAPDH activity by modifications of the thiols which are essential for this activity, and that the modification includes formation of sulfenic acid, which is not restored by DTT. Sulfhydryl Compounds 89-95 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 50-55 10403526-13 1999 S-nitrosylation, which is one type of thiol modification by NO, occurred when GAPDH was treated with SNAP but not SNP. Sulfhydryl Compounds 38-43 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 78-83 10403526-15 1999 It seems that SNAP nitrosylates the active site thiols of GAPDH to prevent these thiols from oxidizing to sulfenic acid. Sulfhydryl Compounds 48-54 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 58-63 10403526-15 1999 It seems that SNAP nitrosylates the active site thiols of GAPDH to prevent these thiols from oxidizing to sulfenic acid. Sulfhydryl Compounds 81-87 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 58-63 10092623-2 1999 In this study we show that nitrosonium tetrafluoroborate (BF4NO), a NO+ donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosylation and caused enzyme inhibition. Sulfhydryl Compounds 92-97 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 108-148 10092623-2 1999 In this study we show that nitrosonium tetrafluoroborate (BF4NO), a NO+ donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by S-nitrosylation and caused enzyme inhibition. Sulfhydryl Compounds 92-97 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 150-155 10092623-4 1999 In contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S-glutathionylation of a thiol group of GAPDH both in vitro and under cellular conditions. Sulfhydryl Compounds 101-106 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 116-121 9038816-2 1997 We have previously shown that NO inhibits GAPDH by S-nitrosylation of the active site cysteine residue, which is reversed by low-molecular-weight thiols. Sulfhydryl Compounds 146-152 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 42-47 8912669-3 1996 We performed spin-trapping studies with purified apo-GAPDH to identify a putative thiol intermediate produced by AAPH as well as by .NO-related oxidants. Sulfhydryl Compounds 82-87 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 53-58 10403526-0 1999 Critical role of sulfenic acid formation of thiols in the inactivation of glyceraldehyde-3-phosphate dehydrogenase by nitric oxide. Sulfhydryl Compounds 44-50 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 74-114 10403526-1 1999 The relationship between possible modifications of the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by nitric oxide (NO) and modified enzyme activity was examined. Sulfhydryl Compounds 55-60 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 71-111 10403526-1 1999 The relationship between possible modifications of the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by nitric oxide (NO) and modified enzyme activity was examined. Sulfhydryl Compounds 55-60 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 113-118 9642155-1 1998 In this report the protein human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been examined to clarify the roles of (a) direct oxidation and (b) thiol-disulphide exchange (with glutathione disulphide) on the modification of its catalytic activity. Sulfhydryl Compounds 153-158 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 33-73 9642155-1 1998 In this report the protein human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has been examined to clarify the roles of (a) direct oxidation and (b) thiol-disulphide exchange (with glutathione disulphide) on the modification of its catalytic activity. Sulfhydryl Compounds 153-158 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-80 9706739-2 1998 It was demonstrated that submillimolar concentrations of the NO donor sodium nitroprusside (SNP) not only strongly inactivated GAPDH by S-nitrosylation of the enzyme thiols but also decreased the binding affinity of GAPDH for the RBC membrane. Sulfhydryl Compounds 166-172 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 127-132 9706739-2 1998 It was demonstrated that submillimolar concentrations of the NO donor sodium nitroprusside (SNP) not only strongly inactivated GAPDH by S-nitrosylation of the enzyme thiols but also decreased the binding affinity of GAPDH for the RBC membrane. Sulfhydryl Compounds 166-172 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 216-221 9706739-3 1998 In fact, the incubation with SNP for 60 min at 30 degrees C and at a concentration > 50 microM induced the dissociation of the native GAPDH from the white unsealed membranes (standard ghosts) in a concentration-dependent manner with a partial recovery of the enzyme activity and thiols when SNP concentrations higher of 1 mM were used. Sulfhydryl Compounds 282-288 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 137-142 9038816-5 1997 The mechanism for inhibition appears to involve reversible modification of GAPDH because addition of thiols to cell extracts restored activity. Sulfhydryl Compounds 101-107 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 75-80 8912669-1 1996 Previous studies have demonstrated that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) undergoes NAD(H) linkage to an active site thiol when it comes into contact with .NO-related oxidants. Sulfhydryl Compounds 132-137 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 82-87 8680862-9 1996 Another thiol-dependent enzyme glyceraldehyde-3-phosphate dehydrogenase was also markedly inhibited by EA in a time-dependent fashion. Sulfhydryl Compounds 8-13 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 31-71 7573405-7 1995 Consistent with this finding, GSNO-mediated GAPDH inhibition was reversible with low-molecular-weight thiols, and the reversal of inhibition correlated with the "denitrosylation" of GAPDH. Sulfhydryl Compounds 102-108 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 44-49 7673130-3 1995 The IC50 of SNAP for GPx was 2 microM at 1 h of incubation and was 20% of the IC50 for another thiol enzyme, glyceraldehyde-3-phosphate dehydrogenase, in which a specific cysteine residue is known to be nitrosylated. Sulfhydryl Compounds 95-100 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 109-149 7639707-7 1995 The NAD+ linkage to neuronal GAPDH measured in the presence of NO and superoxide probably involves sulphydryl groups, since the radiolabelling of the protein was reversed by exposure to HgCl2 and prevented by pretreatment with the alkylating agent N-ethylmaleimide. Sulfhydryl Compounds 99-109 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 29-34 7540026-19 1995 Modification of GAPDH is probably just one interesting target related to NO-redox chemistry and active-site thiol modification. Sulfhydryl Compounds 108-113 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 16-21 7929187-10 1994 The thiols covalently bound to purified S-thiolated GAPDH were removed by dithioerythritol and were identified as glutathione and cysteine; glutathione was predominant. Sulfhydryl Compounds 4-10 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 52-57 7929187-11 1994 These results indicate that during the respiratory burst in monocytes, low molecular weight thiols can bind to specific cytosolic proteins, including GAPDH. Sulfhydryl Compounds 92-98 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 150-155 7540026-0 1995 Protein thiol modification of glyceraldehyde-3-phosphate dehydrogenase as a target for nitric oxide signaling. Sulfhydryl Compounds 8-13 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 30-70 8034046-0 1994 Mechanism of covalent modification of glyceraldehyde-3-phosphate dehydrogenase at its active site thiol by nitric oxide, peroxynitrite and related nitrosating agents. Sulfhydryl Compounds 98-103 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 38-78 8034046-1 1994 Previous studies have suggested that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) undergoes covalent modification of an active site thiol by a NO.-induced [32P]NAD(+)-dependent mechanism. Sulfhydryl Compounds 136-141 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 37-77 8034046-1 1994 Previous studies have suggested that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) undergoes covalent modification of an active site thiol by a NO.-induced [32P]NAD(+)-dependent mechanism. Sulfhydryl Compounds 136-141 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 79-84 8034046-7 1994 Peroxynitrite (ONOO-) also induces GAPDH modification in the presence of thiol, consistent with the notion that this species can transfer NO+ (or NO2+) through the intermediacy of RS-NO. Sulfhydryl Compounds 73-78 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 35-40