Evidence map›Paper›PMID 23861393›Full record

ReviewThe Journal of biological chemistry2013

Regulation of protein function and signaling by reversible cysteine S-nitrosylation.

Neal Gould, Paschalis-Thomas Doulias, Margarita Tenopoulou, Karthik Raju, Harry Ischiropoulos

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 1 pooled it
15.3field-weighted citation impact, top 1% 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

126 citing papers in PubMed, 1 synthesis or guideline pooled it, 274 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Trial
  4. Trial
  5. Review
  6. Article
  7. Article
  8. Metabolic modulation of TCA cycle bySynthetic and systems biotechnology · 2026
    Article
  9. Article
  10. Nitrosation of CD36 Regulates Endothelial Function and Serum Lipids.Arteriosclerosis, thrombosis, and vascular biology · 2025
    Article
  11. Article
  12. Article
  13. Review
  14. The chemical biology of dinitrogen trioxide.Redox biochemistry and chemistry · 2024
    Article
  15. Review
  16. Review
  17. Review
  18. On the regulation of human D-aspartate oxidase.Protein science : a publication of the Protein Society · 2023
    Article
  19. Article
  20. Article

66 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Neal GouldFrom the Children's Hospital of Philadelphia Research Institute and Departments of Pediatrics and Pharmacology, Raymond and Ruth Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania 19104.
Paschalis-Thomas Doulias
Margarita Tenopoulou
Karthik Raju
Harry Ischiropoulos
Children's Hospital of Philadelphia · US

Funding

Translational Research Support CoreP30ES013508 · NIEHS · UNIVERSITY OF PENNSYLVANIA · PI Rebecca A Simmons · 2006 to 2026
$35.3M
Training in Alzheimer’s and Age-Related Neurodegenerative DiseasesT32AG000255 · NIA · UNIVERSITY OF PENNSYLVANIA · PI ALICE S CHEN-PLOTKIN, VIRGINIA M LEE · 1997 to 2026
$12.5M
Reactive Species in Vascular Disease: Mechanisms of InjuryR01HL054926 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI ISCHIROPOULOS, HARRY · 1997 to 2023
$7.7M
PEROXYNITRITE IN NEURODEGENERATIVE DISEASES OF AGINGR01AG013966 · NIA · UNIVERSITY OF PENNSYLVANIA · PI ISCHIROPOULOS, HARRY · 1997 to 2014
$4.4M
NHLBI NIH HHS HL054926NHLBI NIH HHS R01 HL054926NIA NIH HHS AG13966NIA NIH HHS R01 AG013966NIA NIH HHS T32 AG000255NIA NIH HHS T32AG000255NIEHS NIH HHS ES013508NIEHS NIH HHS P30 ES013508
6 · The paper itself

Abstract

NO is a versatile free radical that mediates numerous biological functions within every major organ system. A molecular pathway by which NO accomplishes functional diversity is the selective modification of protein cysteine residues to form S-nitrosocysteine. This post-translational modification, S-nitrosylation, impacts protein function, stability, and location. Despite considerable advances with individual proteins, the in vivo biological chemistry, the structural elements that govern the selective S-nitrosylation of cysteine residues, and the potential overlap with other redox modifications are unknown. In this minireview, we explore the functional features of S-nitrosylation at the proteome level and the structural diversity of endogenously modified residues, and we discuss the potential overlap and complementation that may exist with other cysteine modifications.

Indexed as

Gene Expression RegulationAnimalsCysteineHumansMiceMyocardiumNitric OxideNitric Oxide SynthaseNitrogenOxidation-ReductionProtein Processing, Post-TranslationalProteinsProteomicsSignal TransductionS-NitrosothiolsCysteineNitric OxideNitric Oxide SynthaseNitrogenProteinsS-nitrosocysteineS-NitrosothiolsNitric OxideNitric-oxide SynthaseNitrosylationPost-translational ModificationProtein ChemistryProteomicsS-NitrosocysteineS-Nitrosothiols

Identifiers

PMID23861393
PMCPMC3772194
OpenAlexW2000038034

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.