PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15950210-6 2005 The results indicate that, in the presence of the reducing agent DTT, GAPDH inhibition by 9,10-PQ under aerobic conditions was mostly indirect and comparable to the direct actions of exogenously-added H2O2 on this enzyme. Dithiothreitol 65-68 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 70-75 24064205-3 2013 In assays containing dithiothreitol (DTT) and NAD(+), the GTN reductase activity of purified GAPDH produces nitrite and 1,2-GDN as the major products. Dithiothreitol 21-35 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-98 24064205-3 2013 In assays containing dithiothreitol (DTT) and NAD(+), the GTN reductase activity of purified GAPDH produces nitrite and 1,2-GDN as the major products. Dithiothreitol 37-40 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 93-98 24064205-5 2013 Reductive denitration of GTN in the absence of DTT results in dose- and time-dependent inhibition of GAPDH dehydrogenase activity. Dithiothreitol 47-50 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 101-106 11878824-15 2002 The inactivated cellular G-3PD in the cell extract could be partially reactivated by DTT (6m M) or by recombinant human lens thioltransferase (RHLT) but not by GSH (1m M), GR or GST. Dithiothreitol 85-88 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 25-30 10391884-1 1999 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is covalently modified by NAD in the presence of nitric oxide (NO) and dithiothreitol. Dithiothreitol 120-134 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-40 10516189-6 1999 GAPDH activity could be regenerated on reincubation of cells in Hanks" balanced salt solution or reduction with dithiothreitol. Dithiothreitol 112-126 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 0-5 11245448-9 2001 The extent of reversible oxidation-dependent inactivation of GAPDH in situ was determined by comparing the enzyme activity before and after reduction of cell extracts with DTT. Dithiothreitol 172-175 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 61-66 10391884-1 1999 Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is covalently modified by NAD in the presence of nitric oxide (NO) and dithiothreitol. Dithiothreitol 120-134 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 42-47 9706739-6 1998 Dithiothreitol (DTT), which at concentrations of less than 1 mM catalyzed the S-nitrosylation of GAPDH and the consequent modification of the binding properties described above, the concentrations higher than 5 mM restored both the enzyme activity and the binding properties. Dithiothreitol 16-19 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 97-102 10092623-5 1999 The GSH-mixed protein disulfide formed led to a permanent enzyme inhibition, but upon dithiothreitol addition a functional active GAPDH was recovered. Dithiothreitol 86-100 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 130-135 9706739-6 1998 Dithiothreitol (DTT), which at concentrations of less than 1 mM catalyzed the S-nitrosylation of GAPDH and the consequent modification of the binding properties described above, the concentrations higher than 5 mM restored both the enzyme activity and the binding properties. Dithiothreitol 0-14 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 97-102 10403526-7 1999 On the other hand, DTT posttreatment after the treatment of GAPDH with SNP, SNAP, or H2O2 did not completely restore the modified thiols and the inhibited enzyme activity. Dithiothreitol 19-22 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 60-65 8504856-5 1993 Ka for GA3P was at least 50-fold lower and maximal activation was somewhat higher than these values for other aldehydes that were also able to enhance GAPDH ADP-ribosylation in the presence of DTT. Dithiothreitol 193-196 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 151-156 9354374-7 1997 In addition, we found that basal and glyceraldehyde-3-phosphate-induced modifications of GAPDH, both of which have also been explained as ADP-ribosylation, were not ADP-ribosylation, and that the modification of GAPDH in the absence and presence of NO or GA3P was distinct in the dithiothreitol effect or resistance to HgCl2. Dithiothreitol 280-294 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 89-94 7673130-6 1995 The similarity of the inactivation with SNAP and reactivation with dithiothreitol of GPx to that of glyceraldehyde-3-phosphate dehydrogenase, suggested that NO released from SNAP modified a cysteine-like essential residue on GPx. Dithiothreitol 67-81 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 100-140 8262231-1 1993 The rate of hydrolysis of 3-phosphoglyceroyl-holoenzyme, a covalent intermediate of glyceraldehyde-3-phosphate dehydrogenase catalyzed reaction, is considerably decreased in the presence of micromolar concentrations of reduced glutathione, cysteine or dithiothreitol with Ki values of 0.78 microM, 0.6 microM and 10 microM, respectively. Dithiothreitol 252-266 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 84-124 2297224-4 1990 Incubation of the cells, following oxidative treatment, in saline for 30 min or with 20 mM dithiothreitol (DTT) partially reversed both changes in GPD. Dithiothreitol 91-105 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 147-150 2297224-4 1990 Incubation of the cells, following oxidative treatment, in saline for 30 min or with 20 mM dithiothreitol (DTT) partially reversed both changes in GPD. Dithiothreitol 107-110 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 147-150 2936349-5 1986 Pre-incubation of ivalin with dithiothreitol decreased its inhibiting effect on phosphofructokinase, hexokinase and glyceraldehyde-3-phosphate dehydrogenase activities. Dithiothreitol 30-44 glyceraldehyde-3-phosphate dehydrogenase Homo sapiens 116-156