N-glycosylation processing and glycoprotein folding -: Lessons from the tyrosinase-related proteins

被引：36
|
作者：
Branza-Nichita, N
Petrescu, AJ
Negroiu, G
Dwek, RA
Petrescu, SM
机构：
[1] Romanian Acad, Inst Biochem, Bucharest 77700 17, Romania
[2] Univ Oxford, Dept Biochem, Oxford Glycobiol Inst, Oxford OX1 3QU, England
来源：
CHEMICAL REVIEWS | 2000年 / 100卷 / 12期
关键词：
D O I：
10.1021/cr990291y
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Tyrosinase is an attractive model because of its long in vivo processing time in the endoplastic reticulum (ER). Tyrosinase-derived antigenic peptides are a model system to study human leukocyte antigen (HLA) loading and presentation mechanisms which take place in the ER. This review outlines the results that have been obtained from tyrosinase and some tyrosinase-related proteins which provide insight into the role of ER chaperones in processes related to glycoprotein folding and degradation in vivo.
引用
收藏
页码：4697 / +
页数：16
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