Progress in the Structural Studies and Inhibitor Development of Protein Disulfide Isomerase

被引：0

作者：

Liang Cheng-Hui ^{[1
]}

Chen Dan ^{[2
]}

Liao Xin-Yuan ^{[2
]}

Jiang Long-Guang ^{[2
]}

Yuan Cai ^{[1
]}

Huang Ming-Dong ^{[2
]}

机构：

[1] Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou 350108, Peoples R China

[2] Fuzhou Univ, Coll Chem, Fuzhou 350108, Peoples R China

来源：

PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS | 2020年 / 47卷 / 07期

关键词：

protein disulfide isomerase; structure; function; inhibitor; SUBSTRATE-BINDING; THIOL ISOMERASES; DISCOVERY; BACITRACIN; CONFORMATIONS; CHAPERONE; SEQUENCE; VARIANTS; DISEASE; REGION;

D O I：

10.16476/j.pibb.2020.0065

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：

Protein disulfide isomerase (PDI) can catalyze the formation, breakage and rearrangement of disulfide bonds, and promote protein folding, which is essential to stabilize the three-dimensional structure of proteins. The dysregulation of PDI expression or enzyme activity is closely related to a series of diseases, such as cancer, neurodegenerative diseases, and thrombosis. In this review, we summarized the structure of PDI, its relationship with diseases and the research progress of its inhibitors. We also pointed out the current problems and the development direction of PDI inhibitors, which will provide references for its further research.

引用

页码：595 / 606

页数：12

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