Title : Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor.

Pub. Date : 1986 Jul 29

PMID : 3019388






6 Functional Relationships(s)
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1 Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor. Dithiothreitol insulin receptor Homo sapiens
2 Alteration of intramolecular disulfides in insulin receptor/kinase by insulin and dithiothreitol: insulin potentiates the apparent dithiothreitol-dependent subunit reduction of insulin receptor. Dithiothreitol insulin receptor Homo sapiens
3 Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin. Dithiothreitol insulin receptor Homo sapiens
4 Dithiothreitol (DTT) was observed to increase both beta-subunit autophosphorylation and exogenous substrate phosphorylation of the insulin receptor in the absence of insulin. Dithiothreitol insulin receptor Homo sapiens
5 The activation of the insulin receptor/kinase by both DTT and thioredoxin was found to be additive with that of insulin. Dithiothreitol insulin receptor Homo sapiens
6 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 insulin receptor Homo sapiens