4.6 Review

Redox regulation of protein-tyro sine phosphatases

期刊

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 434, 期 1, 页码 11-15

出版社

ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2004.05.024

关键词

protein-tyrosine phosphatase; regulation; oxidation; redox; conformational change; dimerization

向作者/读者索取更多资源

The protein-tyrosine phosphatases (PTPs) form a large family of signaling proteins with essential functions in embryonic development and adult physiology. The PTPs are characterized by an absolutely conserved catalytic site cysteine with a low pK(a) due to its microenvironment, making it vulnerable to oxidation. PTPs are differentially oxidized and inactivated in vitro and in living cells. Many cellular stimuli induce a shift in the cellular redox state towards oxidation and evidence is accumulating that at least part of the cellular responses to these stimuli are due to specific, transient inactivation of PTPs, indicating that PTPs are important sensors of the cellular redox state. (C) 2004 Elsevier Inc. All rights reserved.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据