Results 11 to 20 of about 399,223 (393)
IRS2 (insulin receptor substrate 2) [PDF]
Insulin receptor substrate 2 (IRS2) belongs to the insulin receptor substrate protein family and was initially discovered as an alternative route for signaling mediated by the insulin receptor. Currently, IRS2 has been well-established to mediate mitogenic and antiapoptotic signaling from several important cellular receptors.
Machado-Neto, Joao Agostinho +2 more
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Insulin Substrate Receptor (IRS) proteins in normal and malignant hematopoiesis
The insulin receptor substrate (IRS) proteins are a family of cytoplasmic proteins that integrate and coordinate the transmission of signals from the extracellular to the intracellular environment via transmembrane receptors, thus regulating cell growth,
João Agostinho Machado-Neto +6 more
doaj +2 more sources
IRS1 (insulin receptor substrate 1) [PDF]
Review on IRS1 (insulin receptor substrate 1), with data on DNA, on the protein encoded, and where the gene is implicated.
Machado-Neto, JA, Traina, F
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Insulin Receptor Substrate 2 Expression and Involvement in Neuronal Insulin Resistance in Diabetic Neuropathy [PDF]
Insulin signaling depends on tyrosine phosphorylation of insulin receptor substrates (IRSs) to mediate downstream effects; however, elevated serine phosphorylation of IRS impairs insulin signaling. Here, we investigated IRS protein expression patterns in
Caleb W. Grote +4 more
openalex +2 more sources
Insulin signaling is critical for neuroplasticity, cerebral metabolism as well as for systemic energy metabolism. In rodent studies, impaired brain insulin signaling with resultant insulin resistance (IR) modulates synaptic plasticity and the ...
C. Nasca +12 more
semanticscholar +1 more source
Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog [PDF]
Stevan R. Hubbard
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Characterization of Drosophila Insulin Receptor Substrate [PDF]
Insulin receptor substrate (IRS) proteins are phosphorylated by multiple tyrosine kinases, including the insulin receptor. Phosphorylated IRS proteins bind to SH2 domain-containing proteins, thereby triggering downstream signaling pathways. The Drosophila insulin receptor (dIR) C-terminal extension contains potential binding sites for signaling ...
R M, Poltilove +4 more
openaire +2 more sources

