A Kinase Divided

Aroon S. Karra; Clinton A. Taylor; Curtis A. Thorne; Melanie H. Cobb

doi:10.1016/j.ccell.2015.07.008

A Kinase Divided

Aroon S. Karra, Clinton A. Taylor, Curtis A. Thorne, Melanie H. Cobb

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

3 Scopus citations

Abstract

In this issue of Cancer Cell, Herrero and colleagues identify an anti-tumorigenic small molecule that blocks ERK dimerization, but neither its catalytic activity nor its phosphorylation by MEK. These findings demonstrate that targeting protein dimerization could be a therapeutic avenue for inhibiting kinase signaling pathways associated with lower drug resistance.

Original language	English (US)
Pages (from-to)	145-147
Number of pages	3
Journal	Cancer Cell
Volume	28
Issue number	2
DOIs	https://doi.org/10.1016/j.ccell.2015.07.008
State	Published - Aug 10 2015

ASJC Scopus subject areas

Oncology
Cell Biology
Cancer Research

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10.1016/j.ccell.2015.07.008

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@article{9da042d3e43b4d80b406893b989655fa,

title = "A Kinase Divided",

abstract = "In this issue of Cancer Cell, Herrero and colleagues identify an anti-tumorigenic small molecule that blocks ERK dimerization, but neither its catalytic activity nor its phosphorylation by MEK. These findings demonstrate that targeting protein dimerization could be a therapeutic avenue for inhibiting kinase signaling pathways associated with lower drug resistance.",

author = "Karra, {Aroon S.} and Taylor, {Clinton A.} and Thorne, {Curtis A.} and Cobb, {Melanie H.}",

note = "Publisher Copyright: {\textcopyright} 2015 Elsevier Inc.",

year = "2015",

month = aug,

day = "10",

doi = "10.1016/j.ccell.2015.07.008",

language = "English (US)",

volume = "28",

pages = "145--147",

journal = "Cancer Cell",

issn = "1535-6108",

publisher = "Cell Press",

number = "2",

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TY - JOUR

T1 - A Kinase Divided

AU - Karra, Aroon S.

AU - Taylor, Clinton A.

AU - Thorne, Curtis A.

AU - Cobb, Melanie H.

PY - 2015/8/10

Y1 - 2015/8/10

N2 - In this issue of Cancer Cell, Herrero and colleagues identify an anti-tumorigenic small molecule that blocks ERK dimerization, but neither its catalytic activity nor its phosphorylation by MEK. These findings demonstrate that targeting protein dimerization could be a therapeutic avenue for inhibiting kinase signaling pathways associated with lower drug resistance.

AB - In this issue of Cancer Cell, Herrero and colleagues identify an anti-tumorigenic small molecule that blocks ERK dimerization, but neither its catalytic activity nor its phosphorylation by MEK. These findings demonstrate that targeting protein dimerization could be a therapeutic avenue for inhibiting kinase signaling pathways associated with lower drug resistance.

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UR - http://www.scopus.com/inward/citedby.url?scp=84939419182&partnerID=8YFLogxK

U2 - 10.1016/j.ccell.2015.07.008

DO - 10.1016/j.ccell.2015.07.008

M3 - Short survey

C2 - 26267529

AN - SCOPUS:84939419182

SN - 1535-6108

VL - 28

SP - 145

EP - 147

JO - Cancer Cell

JF - Cancer Cell

IS - 2

ER -

A Kinase Divided

Abstract

ASJC Scopus subject areas

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