ASSOCIATION OF FOLDING INTERMEDIATES OF GLYCOPROTEINS WITH CALNEXIN DURING PROTEIN MATURATION

被引：519

作者：

OU, WJ

CAMERON, PH

THOMAS, DY

BERGERON, JJM

机构：

[1] MCGILL UNIV,DEPT BIOL,MONTREAL H3A 2B2,QUEBEC,CANADA

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

来源：

NATURE | 1993年 / 364卷 / 6440期

关键词：

D O I：

10.1038/364771a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Calnexin, an endoplasmic reticulum transmembrane protein, represents a new type of molecular chaperone that selectively associates in a transient fashion with newly synthesized monomeric glycoproteins in HepG2 cells. Calnexin only recognizes glycoproteins when they are incompletely folded. Dissociation of glycoproteins from calnexin occurs at different rates and is related to the time taken for their folding, which may then initiate their differential transport rates from the endoplasmic reticulum.

引用

页码：771 / 776

页数：6

共 35 条

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