Evidence map›Paper›PMID 23834398›Full record

ReviewAntioxidants & redox signaling2014

S-glutathionylation of ion channels: insights into the regulation of channel functions, thiol modification crosstalk, and mechanosensing.

Yang Yang, Xin Jin, Chun Jiang

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Metabolic Shades of S-D-Lactoylglutathione.Antioxidants (Basel, Switzerland) · 2022
    Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Article
  15. Oxidized glutathione (GSSG) inhibits epithelial sodium channel activity in primary alveolar epithelial cells.American journal of physiology. Lung cellular and molecular physiology · 2015
    Article
  16. Interaction between hydrogen sulfide-induced sulfhydration and tyrosine nitration in the KATP channel complex.American journal of physiology. Gastrointestinal and liver physiology · 2015
    Article
  17. Review
  18. Article
  19. Review
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

3 authors at 1 institution in 2 countries.

Yang Yang1 Department of Neurology, Yale University School of Medicine , New Haven, Connecticut.
Xin Jin
Chun Jiang
Georgia State University · US

Funding

Breathing disorders in a mouse model of Rett syndromeR01NS073875 · NINDS · GEORGIA STATE UNIVERSITY · PI JIANG, CHUN · 2011 to 2015
$1.6M
Vascular KATP Channel Modulation in Hypercapnic AcidosisR01HL067890 · NHLBI · GEORGIA STATE UNIVERSITY · PI JIANG, CHUN · 2003 to 2006
$1.2M
Postnatal CCR disruption in MeCP2-defective miceR21HD060959 · NICHD · GEORGIA STATE UNIVERSITY · PI JIANG, CHUN · 2009 to 2010
$395k
NHLBI NIH HHS R01 HL067890NICHD NIH HHS 1R21HD060959NINDS NIH HHS 1R01NS073875NINDS NIH HHS R01 NS073875
6 · The paper itself

Abstract

significanceIon channels control membrane potential, cellular excitability, and Ca(++) signaling, all of which play essential roles in cellular functions. The regulation of ion channels enables cells to respond to changing environments, and post-translational modification (PTM) is one major regulation mechanism. RECENT ADVANCES: Many PTMs (e.g., S-glutathionylation, S-nitrosylation, S-palmitoylation, S-sulfhydration, etc.) targeting the thiol group of cysteine residues have emerged to be essential for ion channels regulation under physiological and pathological conditions. CRITICAL ISSUES: Under oxidative stress, S-glutathionylation could be a critical PTM that regulates many molecules. In this review, we discuss S-glutathionylation-mediated structural and functional changes of ion channels. Criteria for testing S-glutathionylation, methods and reagents used in ion channel S-glutathionylation studies, and thiol modification crosstalk, are also covered. Mechanotransduction, and S-glutathionylation of the mechanosensitive KATP channel, are discussed. FUTURE DIRECTIONS: Further investigation of the ion channel S-glutathionylation, especially the physiological significance of S-glutathionylation and thiol modification crosstalk, could lead to a better understanding of the thiol modifications in general and the ramifications of such modifications on cellular functions and related diseases.

Indexed as

AnimalsHumansMechanotransduction, CellularReactive Oxygen SpeciesSarcoplasmic ReticulumSignal TransductionSulfhydryl CompoundsReactive Oxygen SpeciesSulfhydryl Compounds

Identifiers

PMID23834398
PMCPMC3924852
OpenAlexW2334579385

What Socratic 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 Socratic graph.