PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9890907-0	1999	The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin).	Glutathione	31-42	glutaredoxin-1	Sus scrofa	92-108
9890907-0	1999	The catalytic mechanism of the glutathione-dependent dehydroascorbate reductase activity of thioltransferase (glutaredoxin).	Glutathione	31-42	glutaredoxin-1	Sus scrofa	110-122
9890907-1	1999	The catalytic mechanism of the glutathione (GSH)-dependent dehydroascorbic acid (DHA) reductase activity of recombinant pig liver thioltransferase (RPLTT) was investigated.	Glutathione	31-42	glutaredoxin-1	Sus scrofa	130-146
9890907-1	1999	The catalytic mechanism of the glutathione (GSH)-dependent dehydroascorbic acid (DHA) reductase activity of recombinant pig liver thioltransferase (RPLTT) was investigated.	Glutathione	44-47	glutaredoxin-1	Sus scrofa	130-146
9245898-0	1997	Relationship of protein-glutathione mixed disulfide and thioltransferase in H2O2-induced cataract in cultured pig lens.	Hydrogen Peroxide	76-80	glutaredoxin-1	Sus scrofa	56-72
9245898-18	1997	TTase lost 50% activity in these lenses during 24-hr H2O3 exposure but regained most of it under recovery.	h2o3	53-57	glutaredoxin-1	Sus scrofa	0-5
9245898-20	1997	It was found that in the H2O2 (0.5 mM)-exposed rat lenses, the TTase activity was depleted but PSSG accumulation was accelerated within 8 hr.	Hydrogen Peroxide	25-29	glutaredoxin-1	Sus scrofa	63-68
1953747-3	1991	When thioltransferase was not reduced, inhibition by preincubation with the platinum complexes required molar excesses of 1,300 and 675 to one for cis-platin and trans-platin, respectively or 400-500 microM for 50% inhibition.	Platinum	76-84	glutaredoxin-1	Sus scrofa	5-21
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Glutathione	0-11	glutaredoxin-1	Sus scrofa	73-89
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Glutathione	0-11	glutaredoxin-1	Sus scrofa	91-103
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Glutathione	0-11	glutaredoxin-1	Sus scrofa	126-142
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Alloxan	35-42	glutaredoxin-1	Sus scrofa	73-89
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Alloxan	35-42	glutaredoxin-1	Sus scrofa	91-103
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	Alloxan	35-42	glutaredoxin-1	Sus scrofa	126-142
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	dialuric acid	46-59	glutaredoxin-1	Sus scrofa	73-89
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	dialuric acid	46-59	glutaredoxin-1	Sus scrofa	91-103
9215802-0	1997	Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.	dialuric acid	46-59	glutaredoxin-1	Sus scrofa	126-142
9215802-1	1997	Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH).	Alloxan	74-81	glutaredoxin-1	Sus scrofa	22-38
9215802-1	1997	Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH).	dialuric acid	85-98	glutaredoxin-1	Sus scrofa	22-38
9215802-1	1997	Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH).	Glutathione	102-113	glutaredoxin-1	Sus scrofa	22-38
9215802-1	1997	Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH).	Glutathione	115-118	glutaredoxin-1	Sus scrofa	22-38
9215802-2	1997	This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase.	Disulfides	23-32	glutaredoxin-1	Sus scrofa	86-102
9215802-2	1997	This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase.	Dehydroascorbic Acid	50-70	glutaredoxin-1	Sus scrofa	86-102
9215802-6	1997	This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues.	Alloxan	105-112	glutaredoxin-1	Sus scrofa	25-41
9215802-6	1997	This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues.	Alloxan	105-112	glutaredoxin-1	Sus scrofa	43-55
8914835-0	1996	S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase, and glutathione.	Disulfides	49-59	glutaredoxin-1	Sus scrofa	91-103
8914835-1	1996	The disulfide-reducing activities of glutaredoxin, thioredoxin, protein disulfide isomerase, glutathione, and cysteine were directly compared with a mixture of hepatocyte 35S-glutathiolated proteins as the substrate.	Disulfides	4-13	glutaredoxin-1	Sus scrofa	37-49
8914835-3	1996	All of the 35S-labeled protein bands could be completely dethiolated by glutaredoxin, thioredoxin, protein disulfide isomerase, glutathione, or cysteine.	Sulfur-35	11-14	glutaredoxin-1	Sus scrofa	72-84
8914835-8	1996	The rate of dethiolation by glutathione alone was low compared to the glutaredoxin-catalyzed process, but all 35S-labeled protein bands could be reduced by glutathione, cysteine, or dithiothreitol.	Sulfur-35	110-113	glutaredoxin-1	Sus scrofa	70-82
8914835-8	1996	The rate of dethiolation by glutathione alone was low compared to the glutaredoxin-catalyzed process, but all 35S-labeled protein bands could be reduced by glutathione, cysteine, or dithiothreitol.	Glutathione	156-167	glutaredoxin-1	Sus scrofa	70-82
8914835-8	1996	The rate of dethiolation by glutathione alone was low compared to the glutaredoxin-catalyzed process, but all 35S-labeled protein bands could be reduced by glutathione, cysteine, or dithiothreitol.	Cysteine	169-177	glutaredoxin-1	Sus scrofa	70-82
8914835-8	1996	The rate of dethiolation by glutathione alone was low compared to the glutaredoxin-catalyzed process, but all 35S-labeled protein bands could be reduced by glutathione, cysteine, or dithiothreitol.	Dithiothreitol	182-196	glutaredoxin-1	Sus scrofa	70-82
8914835-19	1996	Thus, protein disulfide isomerase and thioredoxin are more effective than glutaredoxin as reductants of insulin protein disulfides.	Disulfides	120-130	glutaredoxin-1	Sus scrofa	74-86
8914835-20	1996	The apparent reduction potential of pig liver glutaredoxin (-0.159 +/- 0.004 V) was determined by measuring the amount of reduced glutaredoxin in equilibrium with mixtures of glutathione and glutathione disulfide.	Glutathione	175-186	glutaredoxin-1	Sus scrofa	46-58
8914835-20	1996	The apparent reduction potential of pig liver glutaredoxin (-0.159 +/- 0.004 V) was determined by measuring the amount of reduced glutaredoxin in equilibrium with mixtures of glutathione and glutathione disulfide.	Glutathione Disulfide	191-212	glutaredoxin-1	Sus scrofa	46-58
8914835-23	1996	A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures.	Glutathione	2-13	glutaredoxin-1	Sus scrofa	52-64
8914835-23	1996	A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures.	dithiol	34-41	glutaredoxin-1	Sus scrofa	52-64
8914835-23	1996	A glutathione binding site at the dithiol region of glutaredoxin may be of primary importance for its function in protein dethiolation, while a different specific peptide binding site in thioredoxin may be more suited to certain protein disulfide structures.	Disulfides	237-246	glutaredoxin-1	Sus scrofa	52-64
1953747-0	1991	Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.	Platinum	16-24	glutaredoxin-1	Sus scrofa	40-56
1953747-0	1991	Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.	Platinum	16-24	glutaredoxin-1	Sus scrofa	57-69
1953747-1	1991	Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro.	Carboplatin	138-150	glutaredoxin-1	Sus scrofa	50-66
1953747-1	1991	Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro.	Carboplatin	138-150	glutaredoxin-1	Sus scrofa	68-80
1953747-1	1991	Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro.	transplatin	182-194	glutaredoxin-1	Sus scrofa	50-66
1953747-1	1991	Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro.	transplatin	182-194	glutaredoxin-1	Sus scrofa	68-80
1953747-2	1991	By extrapolation to total inhibition, the ratio of platinum drug/thioltransferase was approximately 1.0 for cis and carbo-platin, but greater than 1.0 for trans-platin.	Carboplatin	116-128	glutaredoxin-1	Sus scrofa	65-81
1953747-2	1991	By extrapolation to total inhibition, the ratio of platinum drug/thioltransferase was approximately 1.0 for cis and carbo-platin, but greater than 1.0 for trans-platin.	transplatin	155-167	glutaredoxin-1	Sus scrofa	65-81
8944550-9	1996	The presence of TTase in the lens was confirmed further with the slot blot analysis where it demonstrated a 32P-labeled cDNA from pig liver TTase hybridizing with the RNA in the pig lens or rabbit lens epithelium cells.	Phosphorus-32	108-111	glutaredoxin-1	Sus scrofa	16-21
8944550-9	1996	The presence of TTase in the lens was confirmed further with the slot blot analysis where it demonstrated a 32P-labeled cDNA from pig liver TTase hybridizing with the RNA in the pig lens or rabbit lens epithelium cells.	Phosphorus-32	108-111	glutaredoxin-1	Sus scrofa	140-145
8944550-12	1996	It is speculated that, lens TTase may be primary antioxidant in the lens along with GSH and GR by protecting the vulnerable lens proteins against oxidative damage.	Glutathione	84-87	glutaredoxin-1	Sus scrofa	28-33
7766681-0	1995	Nuclear magnetic resonance study of the thioltransferase-catalyzed glutathione/glutathione disulfide interchange reaction.	Glutathione	67-78	glutaredoxin-1	Sus scrofa	40-56
7766681-0	1995	Nuclear magnetic resonance study of the thioltransferase-catalyzed glutathione/glutathione disulfide interchange reaction.	Glutathione Disulfide	79-100	glutaredoxin-1	Sus scrofa	40-56
7766681-1	1995	The kinetics of the thioltransferase-catalyzed symmetrical glutathione/glutathione disulfide (GSH/GSSG) interchange reaction have been studied by 1H-nuclear magnetic resonance spectroscopy.	Glutathione	59-70	glutaredoxin-1	Sus scrofa	20-36
7766681-1	1995	The kinetics of the thioltransferase-catalyzed symmetrical glutathione/glutathione disulfide (GSH/GSSG) interchange reaction have been studied by 1H-nuclear magnetic resonance spectroscopy.	Glutathione Disulfide	71-92	glutaredoxin-1	Sus scrofa	20-36
7766681-1	1995	The kinetics of the thioltransferase-catalyzed symmetrical glutathione/glutathione disulfide (GSH/GSSG) interchange reaction have been studied by 1H-nuclear magnetic resonance spectroscopy.	Glutathione	94-97	glutaredoxin-1	Sus scrofa	20-36
7766681-1	1995	The kinetics of the thioltransferase-catalyzed symmetrical glutathione/glutathione disulfide (GSH/GSSG) interchange reaction have been studied by 1H-nuclear magnetic resonance spectroscopy.	Glutathione Disulfide	98-102	glutaredoxin-1	Sus scrofa	20-36
7766681-1	1995	The kinetics of the thioltransferase-catalyzed symmetrical glutathione/glutathione disulfide (GSH/GSSG) interchange reaction have been studied by 1H-nuclear magnetic resonance spectroscopy.	Hydrogen	146-148	glutaredoxin-1	Sus scrofa	20-36
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione Disulfide	38-42	glutaredoxin-1	Sus scrofa	48-64
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione Disulfide	38-42	glutaredoxin-1	Sus scrofa	75-91
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione	92-103	glutaredoxin-1	Sus scrofa	48-64
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione	92-103	glutaredoxin-1	Sus scrofa	75-91
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Disulfides	110-119	glutaredoxin-1	Sus scrofa	48-64
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Disulfides	110-119	glutaredoxin-1	Sus scrofa	75-91
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione	124-127	glutaredoxin-1	Sus scrofa	48-64
7766681-3	1995	The rate constant for the reaction of GSSG with thioltransferase to form a thioltransferase-glutathione mixed disulfide and GSH was estimated to be > or = 7.1(+/- 0.4).10(5) M-1 s-1.	Glutathione	124-127	glutaredoxin-1	Sus scrofa	75-91
7766681-4	1995	This reaction is proposed to be the first step in the mechanism by which the activity of some proteins is modulated by the thioltransferase-catalyzed formation of protein-glutathione mixed disulfides.	Glutathione	171-182	glutaredoxin-1	Sus scrofa	123-139
7766681-4	1995	This reaction is proposed to be the first step in the mechanism by which the activity of some proteins is modulated by the thioltransferase-catalyzed formation of protein-glutathione mixed disulfides.	Disulfides	189-199	glutaredoxin-1	Sus scrofa	123-139
7766681-5	1995	The rate constant for the reaction of GSSG with thioltransferase is 4-5 orders of magnitude larger than rate constants for the analogous reaction of the thiolate groups of a variety of small molecules with GSSG.	Glutathione Disulfide	38-42	glutaredoxin-1	Sus scrofa	48-64
7766681-5	1995	The rate constant for the reaction of GSSG with thioltransferase is 4-5 orders of magnitude larger than rate constants for the analogous reaction of the thiolate groups of a variety of small molecules with GSSG.	thiolate	153-161	glutaredoxin-1	Sus scrofa	48-64
7766681-5	1995	The rate constant for the reaction of GSSG with thioltransferase is 4-5 orders of magnitude larger than rate constants for the analogous reaction of the thiolate groups of a variety of small molecules with GSSG.	Glutathione Disulfide	206-210	glutaredoxin-1	Sus scrofa	48-64
7766681-7	1995	The GCSH/GCSSCG interchange reaction was found to be catalyzed by thioltransferase, and the rate constant for the reaction of GCSSCG with thioltransferase was estimated to be > or = 5.7(+/- 1.7).10(4) M-1 s-1.	gcsscg	9-15	glutaredoxin-1	Sus scrofa	66-82
7766681-7	1995	The GCSH/GCSSCG interchange reaction was found to be catalyzed by thioltransferase, and the rate constant for the reaction of GCSSCG with thioltransferase was estimated to be > or = 5.7(+/- 1.7).10(4) M-1 s-1.	gcsscg	9-15	glutaredoxin-1	Sus scrofa	138-154
7766681-9	1995	The results suggest that the gamma-L-glutamyl-L-cysteinyl moiety of GSSG and of GSH-containing mixed disulfides is essential for their recognition by thioltransferase.	gamma-l-glutamyl-l-cysteinyl	29-57	glutaredoxin-1	Sus scrofa	150-166
7766681-9	1995	The results suggest that the gamma-L-glutamyl-L-cysteinyl moiety of GSSG and of GSH-containing mixed disulfides is essential for their recognition by thioltransferase.	Glutathione Disulfide	68-72	glutaredoxin-1	Sus scrofa	150-166
7766681-9	1995	The results suggest that the gamma-L-glutamyl-L-cysteinyl moiety of GSSG and of GSH-containing mixed disulfides is essential for their recognition by thioltransferase.	Glutathione	80-83	glutaredoxin-1	Sus scrofa	150-166
7766681-9	1995	The results suggest that the gamma-L-glutamyl-L-cysteinyl moiety of GSSG and of GSH-containing mixed disulfides is essential for their recognition by thioltransferase.	Disulfides	101-111	glutaredoxin-1	Sus scrofa	150-166
1953747-4	1991	The inhibition of thioltransferase at high drug concentrations in the presence of oxygen was associated with cross-linking of monomers into dimers within 5 min and, in the case of cis-platin treatment, to trimers in 20 min incubation.	Oxygen	82-88	glutaredoxin-1	Sus scrofa	18-34
1953747-4	1991	The inhibition of thioltransferase at high drug concentrations in the presence of oxygen was associated with cross-linking of monomers into dimers within 5 min and, in the case of cis-platin treatment, to trimers in 20 min incubation.	Cisplatin	180-190	glutaredoxin-1	Sus scrofa	18-34
3571278-5	1987	Pig liver thioltransferase is a single polypeptide with 105 amino acid residues and an acetylated glutamine N terminus.	Glutamine	98-107	glutaredoxin-1	Sus scrofa	10-26
2061338-1	1991	By using site-directed mutagenesis techniques, the essential amino acids at the catalytic center of porcine thioltransferase (glutaredoxin) were determined.	Amino Acids, Essential	51-72	glutaredoxin-1	Sus scrofa	108-124
2061338-1	1991	By using site-directed mutagenesis techniques, the essential amino acids at the catalytic center of porcine thioltransferase (glutaredoxin) were determined.	Amino Acids, Essential	51-72	glutaredoxin-1	Sus scrofa	126-138
2061338-2	1991	Seven oligonucleotides were designed, synthesized, and used to construct mutants, ETT-C22S, ETT-C25S, ETT-C25A, ETT-R26V, ETT-K27Q, ETT-R26V: K27Q, and ETT-C78S:C82S, by altering their codons in pig liver thioltransferase cDNA/M13mp18 clones.	Oligonucleotides	6-22	glutaredoxin-1	Sus scrofa	205-221
2061339-1	1991	To evaluate potential catalytic mechanism for thioltransferase thiol-disulfide exchange reactions, seven pig liver mutants were constructed by site-directed mutagenesis.	Disulfides	69-78	glutaredoxin-1	Sus scrofa	46-62
2061339-7	1991	These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH.	Disulfides	68-77	glutaredoxin-1	Sus scrofa	33-49
2061339-7	1991	These data indicate that reduced thioltransferase reacts first with disulfide substrates, then with a thiol substrate, e.g. GSH.	Glutathione	124-127	glutaredoxin-1	Sus scrofa	33-49
2583530-4	1989	For verification, we successfully hybridized three oligodeoxyribonucleotide nucleotide probes, synthesized according to three different regions of the pig liver TT amino acid (aa) sequence, to both of the positive clones.	oligodeoxyribonucleotide nucleotide	51-86	glutaredoxin-1	Sus scrofa	161-163
2583530-6	1989	The TT cDNA was subcloned into the EcoRI site of M13mp18 replicative form and sequenced by the dideoxy chain-termination method using 35S-labeled nucleotides.	Sulfur-35	134-137	glutaredoxin-1	Sus scrofa	4-6
2454232-8	1988	Pig liver thioltransferase was cleaved by trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and cyanogen bromide.	Cyanogen Bromide	104-120	glutaredoxin-1	Sus scrofa	10-26
3571279-1	1987	The active site cysteine of pig liver thioltransferase was identified as Cys22.	Cysteine	16-24	glutaredoxin-1	Sus scrofa	38-54
19223666-0	2009	Role of glutaredoxin-mediated protein S-glutathionylation in cellular nitroglycerin tolerance.	Nitroglycerin	70-83	glutaredoxin-1	Sus scrofa	8-20
3605592-0	1987	Preparation of homogeneous pig liver thioltransferase by a thiol:disulfide mediated pI shift.	Disulfides	65-74	glutaredoxin-1	Sus scrofa	37-53
3605592-1	1987	An enzyme catalyzing thiol-disulfide exchange, thioltransferase, was purified to homogeneity from pig liver.	Sulfhydryl Compounds	21-26	glutaredoxin-1	Sus scrofa	47-63
3605592-1	1987	An enzyme catalyzing thiol-disulfide exchange, thioltransferase, was purified to homogeneity from pig liver.	Disulfides	27-36	glutaredoxin-1	Sus scrofa	47-63
3605592-7	1987	The plots of thioltransferase activity as a function of S-sulfocysteine, 2-hydroxyethyl disulfide, and reduced glutathione concentrations did not display Michaelis-Menten kinetics.	S-sulphocysteine	56-71	glutaredoxin-1	Sus scrofa	13-29
3605592-7	1987	The plots of thioltransferase activity as a function of S-sulfocysteine, 2-hydroxyethyl disulfide, and reduced glutathione concentrations did not display Michaelis-Menten kinetics.	2-hydroxyethyl disulfide	73-97	glutaredoxin-1	Sus scrofa	13-29
3605592-7	1987	The plots of thioltransferase activity as a function of S-sulfocysteine, 2-hydroxyethyl disulfide, and reduced glutathione concentrations did not display Michaelis-Menten kinetics.	Glutathione	111-122	glutaredoxin-1	Sus scrofa	13-29
3605592-10	1987	The results suggest that the active center of thioltransferase is cysteine dependent.	Cysteine	66-74	glutaredoxin-1	Sus scrofa	46-62
19223666-3	2009	Cells overexpressing GRX exhibited reduced cellular protein S-glutathionylation (PSSG) and absence of NTG tolerance, whereas those with silenced GRX showed increased extent of NTG-induced tolerance.	Nitroglycerin	102-105	glutaredoxin-1	Sus scrofa	21-24
19223666-3	2009	Cells overexpressing GRX exhibited reduced cellular protein S-glutathionylation (PSSG) and absence of NTG tolerance, whereas those with silenced GRX showed increased extent of NTG-induced tolerance.	Nitroglycerin	176-179	glutaredoxin-1	Sus scrofa	145-148
19223666-7	2009	These results indicate that the hallmark events of NTG tolerance, such as reduced bioactivation and redox signaling, are associated with GRX-dependent protein deglutathionylation.	Nitroglycerin	51-54	glutaredoxin-1	Sus scrofa	137-140
19223666-2	2009	In LLC-PK1 cells, we found that nitrate tolerance, as indicated by cGMP accumulation toward NTG, was accompanied by increased protein [(35)S]cysteine incorporation, significant S-glutathionylation of multiple proteins, and decreased metabolic activity of several SH-sensitive enzymes, including creatine kinase, xanthine oxidoreductase, and glutaredoxin (GRX).	Nitrates	32-39	glutaredoxin-1	Sus scrofa	341-353
19223666-2	2009	In LLC-PK1 cells, we found that nitrate tolerance, as indicated by cGMP accumulation toward NTG, was accompanied by increased protein [(35)S]cysteine incorporation, significant S-glutathionylation of multiple proteins, and decreased metabolic activity of several SH-sensitive enzymes, including creatine kinase, xanthine oxidoreductase, and glutaredoxin (GRX).	Nitrates	32-39	glutaredoxin-1	Sus scrofa	355-358
17681533-0	2007	Stabilization of the catalytic thiolate in a mammalian glutaredoxin: structure, dynamics and electrostatics of reduced pig glutaredoxin and its mutants.	thiolate	31-39	glutaredoxin-1	Sus scrofa	123-135
17681533-12	2007	The edge of the aromatic ring of Phe24 is polar enough to contribute to stabilize the thiolate, consistent with the conserved aromatic side-chain at this position in the glutaredoxin motif.	thiolate	86-94	glutaredoxin-1	Sus scrofa	170-182