The Redox Proteome

被引：189

作者：

Go, Young-Mi ^{[1
]}

Jones, Dean P. ^{[1
]}

机构：

[1] Emory Univ, Dept Med, Div Pulm Allergy & Crit Care Med, Atlanta, GA 30322 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2013年 / 288卷 / 37期

基金：

美国国家卫生研究院;

关键词：

CYSTEINE-SULFINIC ACID; NITRIC-OXIDE SYNTHASE; S-NITROSYLATION; OXIDATIVE STRESS; POSTTRANSLATIONAL MODIFICATION; GLUTATHIONYLATED PROTEINS; THIOREDOXIN REDUCTASE; HYDROGEN-SULFIDE; ACTIVE-SITE; AMINO-ACIDS;

D O I：

10.1074/jbc.R113.464131

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The redox proteome consists of reversible and irreversible covalent modifications that link redox metabolism to biologic structure and function. These modifications, especially of Cys, function at the molecular level in protein folding and maturation, catalytic activity, signaling, and macromolecular interactions and at the macroscopic level in control of secretion and cell shape. Interaction of the redox proteome with redox-active chemicals is central to macromolecular structure, regulation, and signaling during the life cycle and has a central role in the tolerance and adaptability to diet and environmental challenges.

引用

页码：26512 / 26520

页数：9

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