Insider Influence on ErbB Activity

Ben Zion Shilo

doi:10.1016/j.cell.2010.09.042

Insider Influence on ErbB Activity

Ben Zion Shilo^*

^*Corresponding author for this work

Department of Molecular Genetics

Research output: Contribution to journal › Short survey › peer-review

1 Citation (Scopus)

Abstract

The receptor tyrosine kinase ErbB is activated by ligand-induced dimerization, leading to transphosphorylation of the cytoplasmic kinase domains. Bill et al. (2010) now demonstrate that transphosphorylation can be modulated from within the cell by the cytoplasmic protein cytohesin, providing new insights into ErbB-dependent processes during normal development and cancer.

Original language	English
Pages (from-to)	181-182
Number of pages	2
Journal	Cell
Volume	143
Issue number	2
DOIs	https://doi.org/10.1016/j.cell.2010.09.042
Publication status	Published - 15 Oct 2010

All Science Journal Classification (ASJC) codes

General Biochemistry,Genetics and Molecular Biology

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10.1016/j.cell.2010.09.042

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title = "Insider Influence on ErbB Activity",

abstract = "The receptor tyrosine kinase ErbB is activated by ligand-induced dimerization, leading to transphosphorylation of the cytoplasmic kinase domains. Bill et al. (2010) now demonstrate that transphosphorylation can be modulated from within the cell by the cytoplasmic protein cytohesin, providing new insights into ErbB-dependent processes during normal development and cancer.",

author = "Shilo, {Ben Zion}",

year = "2010",

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day = "15",

doi = "10.1016/j.cell.2010.09.042",

language = "English",

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journal = "Cell",

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T1 - Insider Influence on ErbB Activity

AU - Shilo, Ben Zion

PY - 2010/10/15

Y1 - 2010/10/15

N2 - The receptor tyrosine kinase ErbB is activated by ligand-induced dimerization, leading to transphosphorylation of the cytoplasmic kinase domains. Bill et al. (2010) now demonstrate that transphosphorylation can be modulated from within the cell by the cytoplasmic protein cytohesin, providing new insights into ErbB-dependent processes during normal development and cancer.

AB - The receptor tyrosine kinase ErbB is activated by ligand-induced dimerization, leading to transphosphorylation of the cytoplasmic kinase domains. Bill et al. (2010) now demonstrate that transphosphorylation can be modulated from within the cell by the cytoplasmic protein cytohesin, providing new insights into ErbB-dependent processes during normal development and cancer.

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U2 - 10.1016/j.cell.2010.09.042

DO - 10.1016/j.cell.2010.09.042

M3 - Short survey

SN - 0092-8674

VL - 143

SP - 181

EP - 182

JO - Cell

JF - Cell

IS - 2

ER -

Insider Influence on ErbB Activity

Abstract

All Science Journal Classification (ASJC) codes

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