Fake Inhibitors: AMPK Activation Trumps Inhibition

Christopher G. Langendorf; John W. Scott; Bruce E. Kemp

doi:10.1016/j.chembiol.2017.07.005

Fake Inhibitors: AMPK Activation Trumps Inhibition

Christopher G. Langendorf, John W. Scott, Bruce E. Kemp

Research output: Contribution to journal › Editorial › Other › peer-review

3 Citations (Scopus)

Abstract

Protein kinase inhibitors have become increasingly important therapeutic drugs for the treatment of human diseases; however, resistance and off-target effects can limit their use. In this issue of Cell Chemical Biology, Ross et al. (2017) reveal a novel off-target mechanism where the Src kinase inhibitor SU6656 paradoxically primes AMPK for phosphorylation and activation by the upstream kinase LKB1.

Original language	English
Pages (from-to)	775-777
Number of pages	3
Journal	Cell Chemical Biology
Volume	24
Issue number	7
DOIs	https://doi.org/10.1016/j.chembiol.2017.07.005
Publication status	Published - 20 Jul 2017
Externally published	Yes

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10.1016/j.chembiol.2017.07.005Licence: CC BY

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title = "Fake Inhibitors: AMPK Activation Trumps Inhibition",

abstract = "Protein kinase inhibitors have become increasingly important therapeutic drugs for the treatment of human diseases; however, resistance and off-target effects can limit their use. In this issue of Cell Chemical Biology, Ross et al. (2017) reveal a novel off-target mechanism where the Src kinase inhibitor SU6656 paradoxically primes AMPK for phosphorylation and activation by the upstream kinase LKB1.",

author = "Langendorf, {Christopher G.} and Scott, {John W.} and Kemp, {Bruce E.}",

note = "Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",

year = "2017",

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doi = "10.1016/j.chembiol.2017.07.005",

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journal = "Cell Chemical Biology",

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T1 - Fake Inhibitors

T2 - AMPK Activation Trumps Inhibition

AU - Langendorf, Christopher G.

AU - Scott, John W.

AU - Kemp, Bruce E.

PY - 2017/7/20

Y1 - 2017/7/20

N2 - Protein kinase inhibitors have become increasingly important therapeutic drugs for the treatment of human diseases; however, resistance and off-target effects can limit their use. In this issue of Cell Chemical Biology, Ross et al. (2017) reveal a novel off-target mechanism where the Src kinase inhibitor SU6656 paradoxically primes AMPK for phosphorylation and activation by the upstream kinase LKB1.

AB - Protein kinase inhibitors have become increasingly important therapeutic drugs for the treatment of human diseases; however, resistance and off-target effects can limit their use. In this issue of Cell Chemical Biology, Ross et al. (2017) reveal a novel off-target mechanism where the Src kinase inhibitor SU6656 paradoxically primes AMPK for phosphorylation and activation by the upstream kinase LKB1.

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U2 - 10.1016/j.chembiol.2017.07.005

DO - 10.1016/j.chembiol.2017.07.005

M3 - Editorial

AN - SCOPUS:85024884849

SN - 2451-9456

VL - 24

SP - 775

EP - 777

JO - Cell Chemical Biology

JF - Cell Chemical Biology

IS - 7

ER -

Fake Inhibitors: AMPK Activation Trumps Inhibition

Abstract

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