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Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells.

Data up to Jan 2025

Published1993
Citations207
References41

Total Citations Per Year

Abstract

References (41)

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1992 • 471 citations

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1993 • 221 citations

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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

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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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Nck associates with the SH2 domain-docking protein IRS-1 in insulin-stimulated cells. (1993) – Proceedings of the National Academy of Sciences | Metascience Observatory Explorer