CALNEXIN - A MEMBRANE-BOUND CHAPERONE OF THE ENDOPLASMIC-RETICULUM

被引：475

作者：

BERGERON, JJM

BRENNER, MB

THOMAS, DY

WILLIAMS, DB

机构：

[1] HARVARD UNIV,BRIGHAM & WOMENS HOSP,SCH MED,DEPT RHEUMATOL & IMMUNOL,BOSTON,MA 02115

[2] NATL RES COUNCIL CANADA,BIOTECHNOL RES INST,GENET GRP,MONTREAL H4P 2R2,PQ,CANADA

[3] UNIV TORONTO,DEPT BIOCHEM,TORONTO M5S 1A8,ON,CANADA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 1994年 / 19卷 / 03期

关键词：

D O I：

10.1016/0968-0004(94)90205-4

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：

Calnexin is a new type of molecular chaperone that interacts with many nascent membrane and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular chaperones of the Hsp60, Hsp70 and Hsp90 families, and is further distinguished from them in that it is an integral membrane protein. One of its demonstrated functions is the retention of incorrectly or incompletely folded proteins, suggesting that calnexin is a component of the quality control system of the endoplasmic reticulum.

引用

页码：124 / 128

页数：5

共 27 条

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