PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10805962-3 2000 NO generated from S-nitroso-N-acetyl penicillamine (SNAP) or sodium nitroprusside (SNP) inhibited glucose uptake (by 50% after 1 h of incubation) and lactate production by 16% (SNAP) and 8.5% (SNP) after 3 h. Both NO donors also reduced production of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), an enzyme of the glycolytic pathway. Nitroprusside 61-81 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 251-291 10805962-3 2000 NO generated from S-nitroso-N-acetyl penicillamine (SNAP) or sodium nitroprusside (SNP) inhibited glucose uptake (by 50% after 1 h of incubation) and lactate production by 16% (SNAP) and 8.5% (SNP) after 3 h. Both NO donors also reduced production of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), an enzyme of the glycolytic pathway. Nitroprusside 61-81 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 293-298 10037463-10 1999 Sodium nitroprusside-induced NAD labeling of nuclear GAPDH showed a 60% loss of GAPDH labeling after AraC treatment, suggesting that the active site of GAPDH may be covalently modified, denatured, or improperly folded. Nitroprusside 0-20 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 53-58 10403526-3 1999 NO donors, sodium nitroprusside (SNP), and S-nitroso-N-acetyl-DL-penicillamine (SNAP) decreased the number of free thiols with a concomitant inhibition of GAPDH activity in a concentration- and time-dependent manner. Nitroprusside 11-31 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 155-160 10037463-10 1999 Sodium nitroprusside-induced NAD labeling of nuclear GAPDH showed a 60% loss of GAPDH labeling after AraC treatment, suggesting that the active site of GAPDH may be covalently modified, denatured, or improperly folded. Nitroprusside 0-20 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 80-85 10037463-10 1999 Sodium nitroprusside-induced NAD labeling of nuclear GAPDH showed a 60% loss of GAPDH labeling after AraC treatment, suggesting that the active site of GAPDH may be covalently modified, denatured, or improperly folded. Nitroprusside 0-20 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 80-85 9486123-6 1998 GAPDH induction by hypoxia or transitional metals was partially blocked by sodium nitroprusside but was not altered by the inhibitor of nitric oxide synthase N omega-nitro-L-arginine. Nitroprusside 75-95 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 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. Nitroprusside 70-90 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. Nitroprusside 70-90 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 216-221 7573405-5 1995 Although under certain conditions both GSNO and the NO donor, sodium nitroprusside (SNP), led to the covalent NAD(+)-dependent modification of GAPDH, this putative ADP ribosylation was unlikely to be the primary mechanism for inhibition, since the stoichiometry was extremely low, and, in the case of GSNO, inhibition was completely reversed by thiol reagents. Nitroprusside 62-82 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 143-148 7902582-1 1993 Nitric oxide (NO) or NO-generating compounds like sodium nitroprusside (SNP) increase cellular levels of cGMP and produce S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase [GAPDH; D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12]. Nitroprusside 50-70 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 141-181 7902582-1 1993 Nitric oxide (NO) or NO-generating compounds like sodium nitroprusside (SNP) increase cellular levels of cGMP and produce S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase [GAPDH; D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12]. Nitroprusside 50-70 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 183-188 8327504-2 1993 Incubations of GAPDH with the NO-releasing agent sodium nitroprusside (SNP) and NAD resulted, however, in essentially equal incorporation of radiolabel from the adenine, phosphate, and nicotinamide moieties to the extent of approximately 0.02 mol of NAD.mol of GAPDH-1. Nitroprusside 49-69 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 15-20 8327504-2 1993 Incubations of GAPDH with the NO-releasing agent sodium nitroprusside (SNP) and NAD resulted, however, in essentially equal incorporation of radiolabel from the adenine, phosphate, and nicotinamide moieties to the extent of approximately 0.02 mol of NAD.mol of GAPDH-1. Nitroprusside 49-69 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 261-266 1547895-0 1992 Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. Nitroprusside 0-13 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 73-113 7639707-3 1995 In the present study, we show that 3-morpholino-sydnonimine (SIN-1) is much more efficient than sodium nitroprusside (SNP) in stimulating the covalent labelling of GAPDH from cultured striatal neurones in the presence of [adenylate-32P]NAD+ (877 +/- 110 and 266 +/- 33% increase in NAD(+)-labelling induced by maximally effective concentrations of SIN-1 and SNP respectively). Nitroprusside 96-116 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 164-169