Evidence map›Paper›PMID 38453636›Full record

ReviewJournal of Zhejiang University. Science. B2024

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

Hong Cao, Xuchang Zhou, Bowen Xu, Han Hu, Jianming Guo, Yuwei Ma, Miao Wang, Nan Li, Zou Jun

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of Zhejiang University. Science. B, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
2.3field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
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  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Hong CaoDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China.
Xuchang ZhouDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China.
Bowen XuNational Key Laboratory of Immunity and Inflammation, Naval Medical University, Shanghai 200433, China.
Han HuNational Key Laboratory of Immunity and Inflammation, Naval Medical University, Shanghai 200433, China.
Jianming GuoDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China.
Yuwei MaDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China.
Miao WangDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China.
Nan LiNational Key Laboratory of Immunity and Inflammation, Naval Medical University, Shanghai 200433, China. linan@immunol.org.
Zou JunDepartment of Sport Rehabilitation, Shanghai University of Sport, Shanghai 200438, China. junzou@sus.edu.cn.
Shanghai University of Sport · CNNaval University of Engineering · CNInstitute of Infection and Immunity · CA

Funding

the 2021 Capacity Building of Shanghai Universities 21010503600the National Natural Science Foundation of China 82071762the Shanghai Key Lab of Human Performance (Shanghai University of Sport) 11DZ2261100
6 · The paper itself

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.

Indexed as

Endoplasmic Reticulum-Associated DegradationProtein FoldingAnimalsEndoplasmic Reticulum StressMammalsProteinsProteinsEndoplasmic reticulum-associated degradation (ERAD)Protein foldingRetrotranslocationUbiquitination

Identifiers

PMID38453636
PMCPMC10918413
OpenAlexW4392866738

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.