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Journal of Zhejiang University SCIENCE B 2024 Vol.25 No.3 P.212-232


Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells

Author(s):  Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU

Affiliation(s):  Department of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China; more

Corresponding email(s):   junzou@sus.edu.cn, linan@immunol.org

Key Words:  Endoplasmic reticulum-associated degradation (ERAD), Protein folding, Ubiquitination, Retrotranslocation

Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU. Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells[J]. Journal of Zhejiang University Science B, 2024, 25(3): 212-232.

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journal="Journal of Zhejiang University Science B",
publisher="Zhejiang University Press & Springer",

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A1 - Xuchang ZHOU
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A1 - Nan LI
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DOI - 10.1631/jzus.B2300403

The endoplasmic reticulum is a key site for protein production and quality control. More than one-third of proteins are synthesized and folded into the correct three-dimensional conformation in the endoplasmic reticulum. However, during protein folding, unfolded and/or misfolded proteins are prone to occur, which may lead to endoplasmic reticulum stress. Organisms can monitor the quality of the proteins produced by endoplasmic reticulum quality control (ERQC) and endoplasmic reticulum-associated degradation (ERAD), which maintain endoplasmic reticulum protein homeostasis by degrading abnormally folded proteins. The underlying mechanisms of protein folding and ERAD in mammals have not yet been fully explored. Therefore, this paper reviews the process and function of protein folding and ERAD in mammalian cells, in order to help clinicians better understand the mechanism of ERAD and to provide a scientific reference for the treatment of diseases caused by abnormal ERAD.


曹红1, 2,周绪昌1,徐博文2,胡涵2,郭健民1,马誉玮1,王淼1,李楠2,邹军1


Darkslateblue:Affiliate; Royal Blue:Author; Turquoise:Article


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