Evidence map›Paper›PMID 23811297›Full record

ReviewMethods (San Diego, Calif.)2013

S-sulfhydration/desulfhydration and S-nitrosylation/denitrosylation: a common paradigm for gasotransmitter signaling by H2S and NO.

Changyuan Lu, Adam Kavalier, Eugene Lukyanov, Steven S Gross

Open access · hybridAbstract readReview
In one paragraph

Review in Methods (San Diego, Calif.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

32 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Impact of Reactive Sulfur Species onAntioxidants (Basel, Switzerland) · 2024
    Article
  6. Transcriptomic analysis reveals the functions of HFrontiers in plant science · 2023
    Article
  7. HPlant cell reports · 2022
    Article
  8. Hydrogen Sulfide Actions in the Vasculature.Comprehensive Physiology · 2021
    Article
  9. Review
  10. The role of mitochondrial reactive oxygen species, NO and HJournal of cellular and molecular medicine · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

4 authors at 1 institution in 1 country.

Changyuan LuDepartment of Pharmacology, Weill Cornell College of Medicine, 1300 York Avenue, New York, NY, USA.
Adam Kavalier
Eugene Lukyanov
Steven S Gross
Cornell University · US

Funding

Risk Genes and Environment Interactions in NTDsP01HD067244 · NICHD · WEILL MEDICAL COLL OF CORNELL UNIV · PI ROSS, MARGARET ELIZABETH · 2011 to 2020
$12.6M
CANCER PHARMACOLOGYT32CA062948 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI LORRAINE J GUDAS · 1994 to 2026
$12.1M
Diabetic Vasculopathy and Mitochondrial eNOSR37HL087062 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI GROSS, STEVEN S · 2007 to 2016
$4.2M
Pulmonary Genetic Medicine Training ProgramT32HL094284 · NHLBI · WEILL MEDICAL COLL OF CORNELL UNIV · PI CRYSTAL, RONALD G · 2009 to 2019
$3.0M
NCI NIH HHS T32 CA 062948NCI NIH HHS T32 CA062948NHLBI NIH HHS R37 HL087062NHLBI NIH HHS R37 HL87062NHLBI NIH HHS T32 HL 094284NHLBI NIH HHS T32 HL094284NICHD NIH HHS P01 HD067244NICHD NIH HHS P01 HD 67244
6 · The paper itself

Abstract

Sulfhydryl groups on protein Cys residues undergo an array of oxidative reactions and modifications, giving rise to a virtual redox zip code with physiological and pathophysiological relevance for modulation of protein structure and functions. While over two decades of studies have established NO-dependent S-nitrosylation as ubiquitous and fundamental for the regulation of diverse protein activities, proteomic methods for studying H2S-dependent S-sulfhydration have only recently been described and now suggest that this is also an abundant modification with potential for global physiological importance. Notably, protein S-sulfhydration and S-nitrosylation bear striking similarities in terms of their chemical and biological determinants, as well as reversal of these modifications via group-transfer to glutathione, followed by the removal from glutathione by enzymes that have apparently evolved to selectively catalyze denitrosylation and desulfhydration. Here we review determinants of protein and low-molecular-weight thiol S-sulfhydration/desulfhydration, similarities with S-nitrosylation/denitrosylation, and methods that are being employed to investigate and quantify these gasotransmitter-mediated cell signaling systems.

Indexed as

Signal TransductionAnimalsChromatography, AffinityCysteineGasotransmittersGlutathione DisulfideHumansHydrogen SulfideNitric OxideProtein Processing, Post-TranslationalProteomeReference StandardsS-NitrosothiolsStaining and LabelingTandem Mass SpectrometryCysteineGasotransmittersGlutathione DisulfideHydrogen SulfideNitric OxideProteomeS-Nitrosothiols2-(4-carboxyphenyl)-4,5-dihydro-4,4,5,5-tetramethyl-1H-imidazolyl-1-oxy-3-oxideBiotin-HPDPBiotin Switchcarboxy-PTIOCBSCSEcystathionine β-synthasecystathionine γ-lyaseCysteineETHE1Glutathioneglutathione persulfideGSNOGSSHHydrogen sulfidemercaptopyruvate sulfurtransferasemethyl methane thiosulfonateMMTSMS/MSMST(N-[(6-biotinamido) hexyl]-3′-(2′-pyridyldithio) propionamide)Nitric oxidePersulfidepersulfide dioxygenaseSHS-nitrosoglutathioneSNOSIDSQRSRBsulfate reducing bacteriaSulfhydrationSulfhydrylsulfide quinone reductasetandem mass spectrometrythiolthiosulfate sulfur transferase (a.k.a. rhodanese)TST

Identifiers

PMID23811297
PMCPMC3923419
OpenAlexW2079099306

What OpenQuestion holds

Textmetadata
LicenceTDM
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.