Structure, Function, and Mechanism of Thioredoxin Proteins

被引：319

作者：

Collet, Jean-Francois ^{[2
,3
]}

Messens, Joris ^{[1
,3
]}

机构：

[1] Vrije Univ Brussel, VIB, Dept Mol & Cellular Interact, B-1050 Brussels, Belgium

[2] Catholic Univ Louvain, Duve Inst, B-1200 Brussels, Belgium

[3] Brussels Ctr Redox Biol, Brussels, Belgium

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2010年 / 13卷 / 08期

关键词：

ESCHERICHIA-COLI THIOREDOXIN; DISULFIDE BOND FORMATION; ACTIVE-SITE RESIDUES; T7; DNA-POLYMERASE; CRYSTAL-STRUCTURE; OXIDATIVE STRESS; S-NITROSATION; IN-VIVO; CHLAMYDOMONAS-REINHARDTII; SACCHAROMYCES-CEREVISIAE;

D O I：

10.1089/ars.2010.3114

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：

Thioredoxins are ubiquitous antioxidant enzymes that play important roles in many health-related cellular processes. As such, the fundamental knowledge of how these enzymes work is of prime importance for understanding cellular redox mechanisms and for laying the ground for the development of future therapeutic approaches. Over the past 40 years, a really impressive amount of data has been published on thioredoxins. Here, we review the most significant results that have contributed to our knowledge regarding the structure, the function, and the mechanism of these crucial enzymes. Antioxid. Redox Signal. 13, 1205-1216.

引用

页码：1205 / 1216

页数：12

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