Evidence map›Paper›PMID 27983699›Full record

ReviewMolecules (Basel, Switzerland)2016

Redox Signaling Regulated by Cysteine Persulfide and Protein Polysulfidation.

Shingo Kasamatsu, Akira Nishimura, Masanobu Morita, Tetsuro Matsunaga, Hisyam Abdul Hamid, Takaaki Akaike

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 4% 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

54 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 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 1 institution in 1 country.

Shingo KasamatsuDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. shingok@med.tohoku.ac.jp.
Akira NishimuraDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. Akira.Nishimura@med.tohoku.ac.jp.
Masanobu MoritaDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. morita@med.tohoku.ac.jp.
Tetsuro MatsunagaDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. matsunag@med.tohoku.ac.jp.
Hisyam Abdul HamidDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. hisyamabdulhamid@gmail.com.
Takaaki AkaikeDepartment of Environmental Health Science and Molecular Toxicology, Tohoku University Graduate School of Medicine, Sendai 980-8575, Japan. takaike@tohoku.med.ac.jp.
Tohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For decades, reactive persulfide species including cysteine persulfide (CysSSH) have been known to exist endogenously in organisms. However, the physiological significance of endogenous persulfides remains poorly understood. That cystathionine β-synthase and cystathionine γ-lyase produced CysSSH from cystine was recently demonstrated. An endogenous sulfur transfer system involving CysSSH evidently generates glutathione persulfide (GSSH) that exists at concentrations greater than 100 μM in vivo. Because reactive persulfide species such as CysSSH and GSSH have higher nucleophilicity than parental cysteine (Cys) and glutathione do, these reactive species exhibit strong scavenging activities against oxidants, e.g., hydrogen peroxide, and electrophiles, which contributes to redox signaling regulation. Also, several papers indicated that various proteins and enzymes have Cys polysulfides including CysSSH at their specific Cys residues, which is called protein polysulfidation. Apart from the redox signaling regulatory mechanism, another plausible function of protein polysulfidation is providing protection for protein thiol residues against irreversible chemical modification caused by oxidants and electrophiles. Elucidation of the redox signaling regulatory mechanism of reactive persulfide species including small thiol molecules and thiol-containing proteins should lead to the development of new therapeutic strategies and drug discoveries for oxidative and electrophilic stress-related diseases.

Indexed as

Cystathionine beta-SynthaseCystathionine gamma-LyaseCysteineDisulfidesGlutathioneHumansHydrogen PeroxideOxidation-ReductionSignal TransductionSuperoxidesCystathionine beta-SynthaseCystathionine gamma-LyaseCysteinecysteine persulfideDisulfidesGlutathioneglutathione persulfideHydrogen PeroxideSuperoxidesprotein polysulfidationreactive persulfide speciesredox signalingthiol modification

Identifiers

PMID27983699
PMCPMC6273478
OpenAlexW2567174755

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.