PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2709339-2 1989 The intracellular thiol-disulfide ratio is also identical to that of mammalian tissues, due to the activity of glutathione reductase. Disulfides 24-33 glutathione-disulfide reductase Homo sapiens 111-132 2499573-3 1989 Spirulina glutathione reductase was covalently bound to Thiopropyl-Sepharose 6B in the presence of 8M urea through thiol-disulfide exchange. Disulfides 121-130 glutathione-disulfide reductase Homo sapiens 10-31 3167026-5 1988 We have identified the active site peptide containing the redox-active disulfide, a peptide corresponding to the histidine-467 region of human erythrocyte glutathione reductase, as well as the flavin binding domain that is highly conserved in all disulfide-containing flavoprotein reductase enzymes. Disulfides 71-80 glutathione-disulfide reductase Homo sapiens 155-176 6810885-0 1982 Copper inhibition of glutathione reductase and its reversal with gold thiolates, thiol, and disulfide compounds. Disulfides 92-101 glutathione-disulfide reductase Homo sapiens 21-42 3277886-6 1988 MerA, mercuric ion reductase, is an FAD-containing and redox-active disulfide-containing enzyme with homology to glutathione reductase. Disulfides 68-77 glutathione-disulfide reductase Homo sapiens 113-134 3549299-8 1987 Trypanothione reductase, the parasite enzyme, and glutathione reductase, the host enzyme, exhibit mutually exclusive specificities for their respective disulfide substrates. Disulfides 152-161 glutathione-disulfide reductase Homo sapiens 50-71 3947091-4 1986 Thus, in 8-mercapto-FAD-glutathione reductase, the oxidation-reduction state of the active center disulfide can be monitored. Disulfides 98-107 glutathione-disulfide reductase Homo sapiens 24-45 7032915-20 1981 In view of the interchain disulfide bridge glutathione reductase should be regarded as a monomeric protein. Disulfides 26-35 glutathione-disulfide reductase Homo sapiens 43-64 30221761-3 2019 In the cytosol, two NADPH-dependent enzymes, glutathione reductase and thioredoxin reductase, as well as a recently identified NADPH-independent system that uses catabolism of methionine to maintain pools of reduced glutathione, supply disulfide reducing power. Disulfides 236-245 glutathione-disulfide reductase Homo sapiens 45-66 33827045-6 2021 Thioredoxin reductase and glutathione reductase create new inter disulfide bonds. Disulfides 65-74 glutathione-disulfide reductase Homo sapiens 26-47 6893275-6 1980 The sign reversal is also present in a closely related disulfide enzyme, glutathione reductase, but absent in glucose oxidase. Disulfides 55-64 glutathione-disulfide reductase Homo sapiens 73-94 6106190-5 1980 In the course of this work it was found that the mixed disulfide between glutathione and gamma-glutamylcysteine is a good substrate of glutathione reductase. Disulfides 55-64 glutathione-disulfide reductase Homo sapiens 135-156 4148072-0 1973 Cleavage of lens protein-GSH mixed disulfide by glutathione reductase. Disulfides 35-44 glutathione-disulfide reductase Homo sapiens 48-69 24062305-8 2013 Our results also showed that physiological concentrations of glutathione, NADPH, and glutathione reductase reduced the non-active site disulfide in vitro. Disulfides 135-144 glutathione-disulfide reductase Homo sapiens 85-106 25645953-8 2015 N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters. Disulfides 170-179 glutathione-disulfide reductase Homo sapiens 69-90 25645953-8 2015 N-ethylmaleimide, a potent thiol modifier, completely inhibits human glutathione reductase from reducing the mitoNEET [2Fe-2S] clusters, indicating that the redox-active disulfide in the catalytic center of human glutathione reductase may be directly involved in reducing the mitoNEET [2Fe-2S] clusters. Disulfides 170-179 glutathione-disulfide reductase Homo sapiens 213-234 30545068-5 2018 Disulfide can be easily reversed by different enzymatic systems such as the thioredoxin/thioredoxin reductase and the glutaredoxin/glutathione/glutathione reductase systems. Disulfides 0-9 glutathione-disulfide reductase Homo sapiens 143-164 22247548-6 2012 The role of thioltransferase and glutathione reductase in the cellular reduction of disulfides and other oxidized forms of thiols was clarified. Disulfides 84-94 glutathione-disulfide reductase Homo sapiens 33-54 22154292-1 2012 For the quantitative assessment of the glutathione reductase (GR) activity with a (19)F NMR spectroscopy, we developed the heavy metal-free probes based on silica nanoparticles modified with water-soluble perfluorinated dendrimers via the disulfide linkers. Disulfides 239-248 glutathione-disulfide reductase Homo sapiens 39-60 22154292-1 2012 For the quantitative assessment of the glutathione reductase (GR) activity with a (19)F NMR spectroscopy, we developed the heavy metal-free probes based on silica nanoparticles modified with water-soluble perfluorinated dendrimers via the disulfide linkers. Disulfides 239-248 glutathione-disulfide reductase Homo sapiens 62-64 22154292-3 2012 By the reductive cleavage of the disulfide linkers with the reduced glutathione-mediated enzymatic reaction of GR, perfluorinated dendrimers can be released from the surfaces of the nanoparticles. Disulfides 33-42 glutathione-disulfide reductase Homo sapiens 111-113 19958171-6 2010 Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin/glutathione/glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and methionine sulfoxide reductase that reverses methionine sulfoxide back to methionine within proteins, are present in the mitochondrial matrix. Disulfides 143-152 glutathione-disulfide reductase Homo sapiens 95-116 18638483-5 2008 The new structures extend earlier observations to reveal that the redox-active disulfide loop in GR is an extreme case of sequential peptide bonds systematically deviating from planarity--a net deviation of 53 degrees across five residues. Disulfides 79-88 glutathione-disulfide reductase Homo sapiens 97-99 19697117-5 2009 Wild type and both mutants containing N-terminal cysteines catalyzed the reduction of disulfides in a coupled system with GSH, NADPH, and glutathione reductase. Disulfides 86-96 glutathione-disulfide reductase Homo sapiens 138-159 19336037-6 2009 We propose that Vanabin2 forms a possible electron transfer cascade from the electron donor, NADPH, via glutathione reductase, glutathione, and Vanabin2 to the acceptor, and vanadium ions conjugated through thiol-disulfide exchange reactions. Disulfides 213-222 glutathione-disulfide reductase Homo sapiens 104-125 18035847-1 2008 Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is similar in structure and mechanism to glutathione reductase except for a C-terminal 16-amino acid extension containing a rare vicinal selenylsulfide bond. Disulfides 81-90 glutathione-disulfide reductase Homo sapiens 162-183 17514531-14 2007 These results indicate that both disulfide bond formation and protein unfolding are responsible for GR inactivation. Disulfides 33-42 glutathione-disulfide reductase Homo sapiens 100-102 18423212-4 2008 Disulfides in microtubule proteins are substrates for both the thioredoxin reductase system and the glutaredoxin/glutathione reductase system. Disulfides 0-10 glutathione-disulfide reductase Homo sapiens 113-134 14713336-1 2004 Most cells contain high levels of glutathione and multiple glutaredoxins, which utilize the reducing power of glutathione to catalyze disulfide reductions in the presence of NADPH and glutathione reductase (the glutaredoxin system). Disulfides 134-143 glutathione-disulfide reductase Homo sapiens 184-205 14733943-2 2004 We report that peroxynitrite-induced disulfides in porcine brain tubulin are repaired by the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Disulfides 37-47 glutathione-disulfide reductase Homo sapiens 135-156 14733943-3 2004 Reduction of disulfide bonds between the alpha- and beta-tubulin subunits by the glutathione reductase system was assessed by Western blot. Disulfides 13-22 glutathione-disulfide reductase Homo sapiens 81-102 15351709-2 2004 We report that peroxynitrite and H2O2-induced disulfides in the porcine brain microtubule-associated proteins tau and microtubule-associated protein-2 are substrates for the glutaredoxin reductase system composed of glutathione reductase, human or Escherichia coli glutaredoxin, reduced glutathione, and NADPH. Disulfides 46-56 glutathione-disulfide reductase Homo sapiens 216-237 12747729-7 2003 Further, upon disulfide formation, dixanthogens are reduced by glutathione reductase to a redox active xanthate. Disulfides 14-23 glutathione-disulfide reductase Homo sapiens 63-84 11481439-8 2001 The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide. Disulfides 134-143 glutathione-disulfide reductase Homo sapiens 245-247 11705998-2 2002 The crystal structure of modified human GR at 1.9-A resolution provides the first picture of protein inactivation by peroxynitrite and reveals that this is due to the exclusive nitration of 2 Tyr residues (residues 106 and 114) at the glutathione disulfide-binding site. Disulfides 247-256 glutathione-disulfide reductase Homo sapiens 40-42 11705998-4 2002 By oxidizing the catalytic dithiol to a disulfide, peroxynitrite itself can act as a substrate of unmodified and bisnitrated P. falciparum glutathione reductase. Disulfides 40-49 glutathione-disulfide reductase Homo sapiens 139-160 11481439-8 2001 The C-terminal extension typical of mammalian TrxRs has two functions: (i) it extends the electron transport chain from the catalytic disulfide to the enzyme surface, where it can react with Trx, and (ii) it prevents the enzyme from acting as a GR by blocking the redox-active disulfide. Disulfides 277-286 glutathione-disulfide reductase Homo sapiens 245-247 8838810-1 1996 Glutaredoxin is a small protein (12 kDa) catalyzing glutathione-dependent disulfide oxidoreduction reactions in a coupled system with NADPH, GSH, and glutathione reductase. Disulfides 74-83 glutathione-disulfide reductase Homo sapiens 150-171 11399772-8 2001 Specificity for the amidated disulfide cofactor partly can be explained by the substitution of Arg-37, shown by x-ray crystallographic data of the human glutathione reductase to hydrogen-bond one of the glutathione glycyl carboxylates, by the negatively charged Glu-21. Disulfides 29-38 glutathione-disulfide reductase Homo sapiens 153-174 10801974-2 2000 In the oxidized enzyme, we demonstrated two nonflavin redox centers by chemical modification and peptide sequencing: one was a disulfide within the sequence -Cys(59)-Val-Asn-Val-Gly-Cys(64), identical to the active site of GR; the other was a selenenylsulfide formed from Cys(497)-SeCys(498) and confirmed by mass spectrometry. Disulfides 127-136 glutathione-disulfide reductase Homo sapiens 223-225 9986706-2 1999 The 2.1-A resolution crystal structure of GR inhibited by (E)-ajoene revealed a mixed disulfide between the active site Cys58 and the CH2=CH-CH2-SO-CH2-CH=CH-S moiety of ajoene. Disulfides 86-95 glutathione-disulfide reductase Homo sapiens 42-44 11012661-3 2000 Glutaredoxins catalyze glutathione-disulfide oxidoreductions overlapping the functions of thioredoxins and using electrons from NADPH via glutathione reductase. Disulfides 35-44 glutathione-disulfide reductase Homo sapiens 138-159 24178881-0 1995 Synthesis of symmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 1. Disulfides 23-33 glutathione-disulfide reductase Homo sapiens 102-123 8628734-3 1996 Of particular importance for inhibitor binding are four amino acid residues in the disulfide substrate-binding site of TR that are not conserved in human GR, namely, Glu-18 (Ala-34 in GR), Trp-21 (Arg-37), Ser-109 (Ile-113), and Met-113 (Asn-117). Disulfides 83-92 glutathione-disulfide reductase Homo sapiens 184-186 24178881-1 1995 The synthesis of a series of symmetrical disulfides as potential substrates of trypanothione reductase and glutathione reductase was described. Disulfides 41-51 glutathione-disulfide reductase Homo sapiens 107-128 24178882-0 1995 Synthesis of asymmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 2. Disulfides 24-34 glutathione-disulfide reductase Homo sapiens 103-124 7711038-1 1995 Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase. Disulfides 177-187 glutathione-disulfide reductase Homo sapiens 197-218 7711038-1 1995 Multiple sequence alignments including the enterococcal NADH peroxidase and NADH oxidase indicate that residues Ser38 and Cys42 align with the two cysteines of the redox-active disulfides found in glutathione reductase (GR), lipoamide dehydrogenase, mercuric reductase, and trypanothione reductase. Disulfides 177-187 glutathione-disulfide reductase Homo sapiens 220-222 2171674-7 1990 The results of additional experiments using erythrocyte lysate and of kinetic experiments on solutions containing PSSG and/or GSH, NADPH and glutathione reductase suggest that the predominant mechanism for reduction of PSSG is by a thiol-disulfide exchange reaction with GSH to form PSH and GSSG, which in turn undergoes enzyme-catalyzed reduction by NADPH. Disulfides 238-247 glutathione-disulfide reductase Homo sapiens 141-162 2007114-4 1991 To assess the basis of host vs parasite enzyme recognition for their disulfide substrates, the interaction of bound glutathione with active-site residues in human red cell glutathione reductase as defined by prior X-ray analysis was used as the starting point for mutagenesis of three residues in trypanothione reductase from Trypanosoma congolense, a cattle parasite. Disulfides 69-78 glutathione-disulfide reductase Homo sapiens 172-193