Biochemical and Biophysical Research Communications
Volume 155, Issue 3, 30 September 1988, Pages 1181-1186
Insulin-induced tyrosine-phosphorylation in intact rat adipocytes
References (17)
- et al.
J. Biol. Chem.
(1987) - et al.
J. Biol. Chem.
(1987) J. Biol. Chem.
(1964)- et al.
J. Biol. Chem.
(1982) - et al.
J. Biol. Chem.
(1987) - et al.
J. Biol. Chem.
(1987) - et al.
- et al.
There are more references available in the full text version of this article.
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Imbalanced Insulin Actions in Obesity and Type 2 Diabetes: Key Mouse Models of Insulin Signaling Pathway
2017, Cell MetabolismCitation Excerpt :Different from liver, tyrosine phosphorylation of Irs2 and p85 associated with Irs2 remained unchanged in Irs1-deficient adipocytes. On the other hand, compensatory phosphorylation of Irs3, which is specifically expressed in the adipose tissue, was observed (Momomura et al., 1988). These data suggest that insulin signaling in adipocytes is predominantly transmitted through Irs1 and Irs3.
Chapter 6 Molecular basis of insulin action
1997, Advances in Molecular and Cellular EndocrinologyIdentification of a 190-kDa protein as a novel substrate for the insulin receptor kinase functionally similar to insulin receptor substrate-1
1995, Journal of Biological ChemistryThe stimulation of pp42<sup>mapkinase</sup> by insulin does not correlate with its metabolic actions in cells overexpressing mutant insulin receptors
1993, Biochemical and Biophysical Research CommunicationsIdentification of SHC as a substrate of the insulin receptor kinase distinct from the gap-associated 62 kDa tyrosine phosphoprotein
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