Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:25 |
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| Enthalten in: |
Journal of Zhejiang University. Science. B - 25(2024), 3 vom: 15. März, Seite 212-232 |
| Sprache: |
Englisch |
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| Weiterer Titel: |
哺乳动物细胞蛋白质折叠和内质网相关降解的研究进展 |
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| Beteiligte Personen: |
Cao, Hong [VerfasserIn] |
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| Links: |
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| Themen: |
Endoplasmic reticulum-associated degradation (ERAD) |
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| Anmerkungen: |
Date Completed 11.03.2024 Date Revised 11.03.2024 published: Print Citation Status MEDLINE |
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| doi: |
10.1631/jzus.B2300403 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 245 | 1 | 0 | |a Advances in the study of protein folding and endoplasmic reticulum-associated degradation in mammal cells |
| 246 | 3 | 3 | |a 哺乳动物细胞蛋白质折叠和内质网相关降解的研究进展 |
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| 520 | |a 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 | ||
| 650 | 4 | |a Review | |
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Endoplasmic reticulum-associated degradation (ERAD) | |
| 650 | 4 | |a Protein folding | |
| 650 | 4 | |a Retrotranslocation | |
| 650 | 4 | |a Ubiquitination | |
| 650 | 7 | |a Proteins |2 NLM | |
| 700 | 1 | |a Zhou, Xuchang |e verfasserin |4 aut | |
| 700 | 1 | |a Xu, Bowen |e verfasserin |4 aut | |
| 700 | 1 | |a Hu, Han |e verfasserin |4 aut | |
| 700 | 1 | |a Guo, Jianming |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Yuwei |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Miao |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Nan |e verfasserin |4 aut | |
| 700 | 1 | |a Jun, Zou |e verfasserin |4 aut | |
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