PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8024589-0 1994 Dithiothreitol stimulates insulin receptor autophosphorylation at the juxtamembrane domain. Dithiothreitol 0-14 insulin receptor Homo sapiens 26-42 2552266-3 1989 Affinity cross-linking study revealed that molecular weight of the insulin receptor was 210 kDa and that it could not be dissociated to alpha- and beta-subunit with dithiothreitol treatment. Dithiothreitol 165-179 insulin receptor Homo sapiens 67-83 8389126-6 1993 These results contrast with those obtained with dithiothreitol which appears to activate phosphorylation in association with reduction of the extracellular insulin-receptor disulphides, but is without effect on the EGF receptor or the IRK protein. Dithiothreitol 48-62 insulin receptor Homo sapiens 156-172 2039503-1 1991 The disulfide structure of the insulin receptor was probed using dithiothreitol and [3H]-N-ethylmaleimide to reduce purified human placental receptor and label the cysteine residues. Dithiothreitol 65-79 insulin receptor Homo sapiens 31-47 3597378-2 1987 Treatment of the soluble insulin receptor from human placenta with 1.25 mM dithiothreitol and 75 mM Tris at pH 8.5 results in complete reduction of interhalf disulfide bonds (class 1 disulfides) and dissociation of the tetrameric receptor into the dimeric alpha beta form. Dithiothreitol 75-89 insulin receptor Homo sapiens 25-41 3316225-1 1987 The dissociation of the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex into an alpha beta heterodimeric state was found to occur in a pH- and dithiothreitol (DTT)-dependent manner. Dithiothreitol 177-191 insulin receptor Homo sapiens 81-97 3316225-1 1987 The dissociation of the purified human placental alpha 2 beta 2 heterotetrameric insulin receptor complex into an alpha beta heterodimeric state was found to occur in a pH- and dithiothreitol (DTT)-dependent manner. Dithiothreitol 193-196 insulin receptor Homo sapiens 81-97 2669959-10 1989 Mild reduction of the insulin receptor preparation with dithiothreitol (DTT) activated the total kinase activity by 3.5-fold. Dithiothreitol 56-70 insulin receptor Homo sapiens 22-38 2669959-10 1989 Mild reduction of the insulin receptor preparation with dithiothreitol (DTT) activated the total kinase activity by 3.5-fold. Dithiothreitol 72-75 insulin receptor Homo sapiens 22-38 3026445-0 1986 Dithiothreitol activation of the insulin receptor/kinase does not involve subunit dissociation of the native alpha 2 beta 2 insulin receptor subunit complex. Dithiothreitol 0-14 insulin receptor Homo sapiens 33-49 3026445-1 1986 The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions. Dithiothreitol 31-45 insulin receptor Homo sapiens 63-79 3026445-1 1986 The subunit composition of the dithiothreitol- (DTT) activated insulin receptor/kinase was examined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis and gel filtration chromatography under denaturing (0.1% SDS) or nondenaturing (0.1% Triton X-100) conditions. Dithiothreitol 48-51 insulin receptor Homo sapiens 63-79 3026445-2 1986 Pretreatment of 32P-labeled insulin receptors with 50 mM DTT followed by gel filtration chromatography in 0.1% SDS demonstrated the dissociation of the alpha 2 beta 2 insulin receptor complex (Mr 400,000) into the monomeric 95,000 beta subunit. Dithiothreitol 57-60 insulin receptor Homo sapiens 28-44 3026445-5 1986 This suggests that the insulin receptor can reoxidize into the Mr 400,000 complex after the removal of DTT by gel filtration chromatography. Dithiothreitol 103-106 insulin receptor Homo sapiens 23-39 4084284-0 1985 Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor. Dithiothreitol 22-36 insulin receptor Homo sapiens 75-91 3019388-0 1986 Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor. Dithiothreitol 82-96 insulin receptor Homo sapiens 43-59 3019388-0 1986 Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor. Dithiothreitol 131-145 insulin receptor Homo sapiens 43-59 3019388-1 1986 Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin. Dithiothreitol 0-14 insulin receptor Homo sapiens 131-147 3019388-1 1986 Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin. Dithiothreitol 16-19 insulin receptor Homo sapiens 131-147 3019388-3 1986 The activation of the insulin receptor/kinase by both DTT and thioredoxin was found to be additive with that of insulin. Dithiothreitol 54-57 insulin receptor Homo sapiens 22-38 3019388-6 1986 In the presence of relatively low concentrations of DTT, insulin was found to potentiate the apparent insulin receptor subunit reduction of the native alpha 2 beta 2 heterotetrameric complex into alpha beta heterodimers, when observed by silver staining of sodium dodecyl sulfate-polyacrylamide gels. Dithiothreitol 52-55 insulin receptor Homo sapiens 102-118 3007126-9 1986 These characteristics of the phosphatidylinositol kinase activity of the purified insulin receptor and its metal ion preference paralleled those of the receptor tyrosine kinase activity and differed from bulk phosphatidylinositol kinase activity in cell extracts, which was not significantly inhibited by (Glu80Tyr20)n, stimulated by dithiothreitol or depleted by immunoprecipitation with anti-(insulin receptor) antibody. Dithiothreitol 334-348 insulin receptor Homo sapiens 82-98 4084284-0 1985 Urea treatment allows dithiothreitol to release the binding subunit of the insulin receptor from the cell membrane: implications for the structural organization of the insulin receptor. Dithiothreitol 22-36 insulin receptor Homo sapiens 168-184 2412229-1 1985 The relationship between the structure of the insulin receptor and its kinase activity was studied on the purified receptor treated with different concentrations of dithiothreitol. Dithiothreitol 165-179 insulin receptor Homo sapiens 46-62 6693383-3 1984 From two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of dithiothreitol, the purified insulin receptor was shown to be composed of heterogeneous disulfide-linked complexes of (alpha 2, 2 beta), (alpha 2, beta, beta 1), (alpha 2, 2 beta 1), (alpha 2), (alpha beta), and (alpha beta 1). Dithiothreitol 110-124 insulin receptor Homo sapiens 139-155 7045094-6 1982 In the present studies, dithiothreitol added directly to intact rat fat cells or to membranes prepared from rat fat cell, rat liver, or human placenta, reduced the class I disulfides, but not the class II disulfides, of the insulin receptor. Dithiothreitol 24-38 insulin receptor Homo sapiens 224-240