CLC number:
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
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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.
@article{title="Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells",
author="Hong CAO, Xuchang ZHOU, Bowen XU, Han HU, Jianming GUO, Yuwei MA, Miao WANG, Nan LI, Jun ZOU",
journal="Journal of Zhejiang University Science B",
volume="25",
number="3",
pages="212-232",
year="2024",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B2300403"
}
%0 Journal Article
%T Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells
%A Hong CAO
%A Xuchang ZHOU
%A Bowen XU
%A Han HU
%A Jianming GUO
%A Yuwei MA
%A Miao WANG
%A Nan LI
%A Jun ZOU
%J Journal of Zhejiang University SCIENCE B
%V 25
%N 3
%P 212-232
%@ 1673-1581
%D 2024
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B2300403
TY - JOUR
T1 - Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells
A1 - Hong CAO
A1 - Xuchang ZHOU
A1 - Bowen XU
A1 - Han HU
A1 - Jianming GUO
A1 - Yuwei MA
A1 - Miao WANG
A1 - Nan LI
A1 - Jun ZOU
J0 - Journal of Zhejiang University Science B
VL - 25
IS - 3
SP - 212
EP - 232
%@ 1673-1581
Y1 - 2024
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B2300403
Abstract: 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.
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