PTB Domains of IRS-1 and Shc Have Distinct but Overlapping Binding Specificities
Open Access
- 1 November 1995
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 270 (46) , 27407-27410
- https://doi.org/10.1074/jbc.270.46.27407
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Specificity of the PTB Domain of Shc for β Turn-forming Pentapeptide Motifs Amino-terminal to PhosphotyrosinePublished by Elsevier ,1995
- Shc Binding to Nerve Growth Factor Receptor Is Mediated by the Phosphotyrosine Interaction DomainJournal of Biological Chemistry, 1995
- Phosphotyrosine-Dependent Interaction of SHC and Insulin Receptor Substrate 1 with the NPEY Motif of the Insulin Receptor via a Novel Non-SH2 DomainMolecular and Cellular Biology, 1995
- A conserved amino-terminal Shc domain binds to phosphotyrosine motifs in activated receptors and phosphopeptidesCurrent Biology, 1995
- Protein modules and signalling networksNature, 1995
- Modular binding domains in signal transduction proteinsCell, 1995
- An Alternative to SH2 Domains for Binding Tyrosine-Phosphorylated ProteinsScience, 1994
- Pleiotropic insulin signals are engaged by multisite phosphorylation of IRS-1.Molecular and Cellular Biology, 1993
- Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinasesNature, 1992
- Structure of the insulin receptor substrate IRS-1 defines a unique signal transduction proteinNature, 1991