Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells.
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References (41)
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Nck, a melanoma cDNA encoding a cytoplasmic protein consisting of the src homology units SH2 and SH3
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SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange.
1993 • 177 citations
The SH2 and SH3 domain-containing Nck protein is oncogenic and a common target for phosphorylation by different surface receptors.
1992 • 174 citations
Phosphorylation of Nek in Response to a Variety of Receptors, Phorbol Myristate Acetate, and Cyclic AMP
1992 • 94 citations
The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment.
1992 • 88 citations
The SH2- and SH3-containing Nck protein transforms mammalian fibroblasts in the absence of elevated phosphotyrosine levels.
1992 • 85 citations
Cytoplasmic juxtamembrane region of the insulin receptor: a critical role in ATP binding, endogenous substrate phosphorylation, and insulin-stimulated bioeffects in CHO cells
1991 • 39 citations
SH2 Domains Exhibit High-Affinity Binding to Tyrosine-Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange
1993 • 30 citations
The SH2 and SH3 Domain-Containing Nek Protein Is Oncogenic and a Common Target for Phosphorylation by Different Surface Receptors
1992 • 29 citations
The SH2- and SH3-Containing Nck Protein Transforms Mammalian Fibroblasts in the Absence of Elevated Phosphotyrosine Levels
1992 • 16 citations
The SH2/SH3 Domain-Containing Protein Nck Is Recognized by Certain Anti-Phospholipase C-γl Monoclonal Antibodies, And Its Phosphorylation on Tyrosine Is Stimulated by Platelet-Derived Growth Factor and Epidermal Growth Factor Treatment
1992 • 16 citations
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