Evidence map›Paper›PMID 34953141›Full record

ArticleCellular and molecular life sciences : CMLS2021

The gut metabolite, trimethylamine N-oxide inhibits protein folding by affecting cis-trans isomerization and induces cell cycle arrest.

Kritika Kumari, Marina Warepam, Aniket Kumar Bansal, Tanveer Ali Dar, Vladimir N Uversky, Laishram Rajendrakumar Singh

Open access · greenAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

4 citing papers in PubMed, 14 citations in OpenAlex.

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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

6 authors at 4 institutions in 3 countries.

Kritika KumariDr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi, 110007, India.
Marina WarepamDepartment of Biotechnology, Manipur University, Manipur, 795003, India.
Aniket Kumar BansalDr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi, 110007, India.
Tanveer Ali DarDepartment of Clinical Biochemistry, University of Kashmir, Srinagar, 190006, Jammu and Kashmir, India.
Vladimir N UverskyDepartment of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, 33620, USA.
Laishram Rajendrakumar SinghDr. B. R. Ambedkar Center for Biomedical Research, University of Delhi, Delhi, 110007, India. lairksingh@gmail.com.ORCID http://orcid.org/0000-0002-5062-0596
University of Delhi · INManipur University · INUniversity of Kashmir · INUniversity of South Florida · US

Funding

Council of Scientific and Industrial Research, India 09/045(1619)/2019-EMR-I
6 · The paper itself

Abstract

Trimethylamine N-Oxide (TMAO) is an important metabolite, which is derived from choline, betaine, and carnitine in various organisms. In humans, it is synthesized through gut microbiota and is abundantly found in serum and cerebrospinal fluid (CSF). Although TMAO is a stress protectant especially in urea-rich organisms, it is an atherogenic agent in humans and is associated with various diseases. Studies have also unveiled its exceptional role in protein folding and restoration of mutant protein functions. However, most of these data were obtained from studies carried on fast-folding proteins. In the present study, we have investigated the effect of TMAO on the folding behavior of a well-characterized protein with slow folding kinetics, carbonic anhydrase (CA). We discovered that TMAO inhibits the folding of this protein via its effect on proline cis-trans isomerization. Furthermore, TMAO is capable of inducing cell cycle arrest. This study highlights the potential role of TMAO in developing proteopathies and associated diseases.

Indexed as

Cell Cycle CheckpointsProtein FoldingCalorimetryCarbonic AnhydrasesCell SurvivalChymotrypsinGastrointestinal TractHeLa CellsHorseradish PeroxidaseHumansIsomerismKineticsMethylaminesProtein AggregatesProtein ConformationProtein RefoldingCarbonic AnhydrasesChymotrypsinHorseradish PeroxidaseMethylaminesProtein AggregatestrimethyloxamineCis–trans isomerizationProlineProtein misfoldingTMAO

Identifiers

PMID34953141
PMCPMC11072907
OpenAlexW4200378650

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.