The ins and outs of EGFR asymmetry

Daniel J. Leahy

doi:10.1016/j.cell.2010.08.003

The ins and outs of EGFR asymmetry

Daniel J. Leahy

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

8 Scopus citations

Abstract

The epidermal growth factor receptor (EGFR) regulates cell proliferation in many tissues. A new structure of the Drosophila EGFR presented by Alvarado et al. (2010) reveals an asymmetric dimer with the ligand bound to only one subunit. The structure provides a rationale for the receptor's negative cooperativity and necessitates a reconsideration of models for activation of human EGFR.

Original language	English (US)
Pages (from-to)	513-515
Number of pages	3
Journal	Cell
Volume	142
Issue number	4
DOIs	https://doi.org/10.1016/j.cell.2010.08.003
State	Published - Aug 2010
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/j.cell.2010.08.003

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title = "The ins and outs of EGFR asymmetry",

abstract = "The epidermal growth factor receptor (EGFR) regulates cell proliferation in many tissues. A new structure of the Drosophila EGFR presented by Alvarado et al. (2010) reveals an asymmetric dimer with the ligand bound to only one subunit. The structure provides a rationale for the receptor's negative cooperativity and necessitates a reconsideration of models for activation of human EGFR.",

author = "Leahy, {Daniel J.}",

year = "2010",

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doi = "10.1016/j.cell.2010.08.003",

language = "English (US)",

volume = "142",

pages = "513--515",

journal = "Cell",

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T1 - The ins and outs of EGFR asymmetry

AU - Leahy, Daniel J.

PY - 2010/8

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N2 - The epidermal growth factor receptor (EGFR) regulates cell proliferation in many tissues. A new structure of the Drosophila EGFR presented by Alvarado et al. (2010) reveals an asymmetric dimer with the ligand bound to only one subunit. The structure provides a rationale for the receptor's negative cooperativity and necessitates a reconsideration of models for activation of human EGFR.

AB - The epidermal growth factor receptor (EGFR) regulates cell proliferation in many tissues. A new structure of the Drosophila EGFR presented by Alvarado et al. (2010) reveals an asymmetric dimer with the ligand bound to only one subunit. The structure provides a rationale for the receptor's negative cooperativity and necessitates a reconsideration of models for activation of human EGFR.

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U2 - 10.1016/j.cell.2010.08.003

DO - 10.1016/j.cell.2010.08.003

M3 - Short survey

C2 - 20723751

AN - SCOPUS:77955595923

SN - 0092-8674

VL - 142

SP - 513

EP - 515

JO - Cell

JF - Cell

IS - 4

ER -

The ins and outs of EGFR asymmetry

Abstract

ASJC Scopus subject areas

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