Pin-Pointing a New DAP Kinase Function: The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation

Shani Bialik; Adi Kimchi

doi:10.1016/j.molcel.2011.04.002

Pin-Pointing a New DAP Kinase Function: The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation

Shani Bialik, Adi Kimchi^*

^*Corresponding author for this work

Department of Molecular Genetics

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

7 Citations (Scopus)

Abstract

In this issue of Molecular Cell, Lee et al. (2011) identify the peptidyl-prolyl isomerase Pin1 as a substrate of DAP kinase, simultaneously providing a critical regulatory mechanism for Pin1 inhibition and a potential mechanism that accounts for DAPK's tumor-suppressive activities.

Original language	English
Pages (from-to)	139-141
Number of pages	3
Journal	Molecular Cell
Volume	42
Issue number	2
DOIs	https://doi.org/10.1016/j.molcel.2011.04.002
Publication status	Published - 22 Apr 2011

All Science Journal Classification (ASJC) codes

Molecular Biology
Cell Biology

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10.1016/j.molcel.2011.04.002

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@article{f116d9be3f2e415eaa67426f74d318ed,

title = "Pin-Pointing a New DAP Kinase Function: The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation",

abstract = "In this issue of Molecular Cell, Lee et al. (2011) identify the peptidyl-prolyl isomerase Pin1 as a substrate of DAP kinase, simultaneously providing a critical regulatory mechanism for Pin1 inhibition and a potential mechanism that accounts for DAPK's tumor-suppressive activities.",

author = "Shani Bialik and Adi Kimchi",

year = "2011",

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doi = "10.1016/j.molcel.2011.04.002",

language = "English",

volume = "42",

pages = "139--141",

journal = "Molecular Cell",

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number = "2",

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T1 - Pin-Pointing a New DAP Kinase Function

T2 - The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation

AU - Bialik, Shani

AU - Kimchi, Adi

PY - 2011/4/22

Y1 - 2011/4/22

N2 - In this issue of Molecular Cell, Lee et al. (2011) identify the peptidyl-prolyl isomerase Pin1 as a substrate of DAP kinase, simultaneously providing a critical regulatory mechanism for Pin1 inhibition and a potential mechanism that accounts for DAPK's tumor-suppressive activities.

AB - In this issue of Molecular Cell, Lee et al. (2011) identify the peptidyl-prolyl isomerase Pin1 as a substrate of DAP kinase, simultaneously providing a critical regulatory mechanism for Pin1 inhibition and a potential mechanism that accounts for DAPK's tumor-suppressive activities.

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U2 - 10.1016/j.molcel.2011.04.002

DO - 10.1016/j.molcel.2011.04.002

M3 - Short survey

SN - 1097-2765

VL - 42

SP - 139

EP - 141

JO - Molecular Cell

JF - Molecular Cell

IS - 2

ER -

Pin-Pointing a New DAP Kinase Function: The Peptidyl-Proly Isomerase Pin1 Is Negatively Regulated by DAP Kinase-Mediated Phosphorylation

Abstract

All Science Journal Classification (ASJC) codes

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