Evidence map›Paper›PMID 35877897›Full record

ArticleMembranes2022

Mechanism Study of Proteins under Membrane Environment.

Yue Zhang, Xiaohong Zhu, Honghui Zhang, Junfang Yan, Peiyi Xu, Peng Wu, Song Wu, Chen Bai

Abstract read
In one paragraph

Article in Membranes, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

8 authors.

Yue ZhangSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.
Xiaohong ZhuSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.ORCID 0000-0003-3364-258X
Honghui ZhangSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.ORCID 0000-0003-2173-4540
Junfang YanSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.ORCID 0000-0001-6236-9848
Peiyi XuSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.
Peng WuSchool of Biomedical Engineering, Health Science Center, Shenzhen University, Shenzhen 518055, China.
Song WuSouth China Hospital, Health Science Center, Shenzhen University, Shenzhen 518116, China.
Chen BaiSchool of Life and Health Sciences, School of Medicine, The Chinese University of Hong Kong, Shenzhen 518172, China.

Funding

the 2021 Basic Research General Project of Shenzhen, China 20210316202830001the National Natural Science Foundation of Youth Fund Project 22103066
6 · The paper itself

Abstract

Membrane proteins play crucial roles in various physiological processes, including molecule transport across membranes, cell communication, and signal transduction. Approximately 60% of known drug targets are membrane proteins. There is a significant need to deeply understand the working mechanism of membrane proteins in detail, which is a challenging work due to the lack of available membrane structures and their large spatial scale. Membrane proteins carry out vital physiological functions through conformational changes. In the current study, we utilized a coarse-grained (CG) model to investigate three representative membrane protein systems: the TMEM16A channel, the family C GPCRs mGlu2 receptor, and the P4-ATPase phospholipid transporter. We constructed the reaction pathway of conformational changes between the two-end structures. Energy profiles and energy barriers were calculated. These data could provide reasonable explanations for TMEM16A activation, the mGlu2 receptor activation process, and P4-ATPase phospholipid transport. Although they all belong to the members of membrane proteins, they behave differently in terms of energy. Our work investigated the working mechanism of membrane proteins and could give novel insights into other membrane protein systems of interest.

Indexed as

coarse-grained modelconformational changesmembrane protein

Identifiers

PMID35877897
PMCPMC9322369

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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.