Evidence map›Paper›PMID 23157283›Full record

ReviewAntioxidants & redox signaling2013

Specificity in S-nitrosylation: a short-range mechanism for NO signaling?

Antonio Martínez-Ruiz, Inês M Araújo, Alicia Izquierdo-Álvarez, Pablo Hernansanz-Agustín, Santiago Lamas, Juan M Serrador

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
–field-weighted citation impact
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

63 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Soluble guanylyl cyclase, the NO receptor, drives vasorelaxation via endothelial S-nitrosation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Vitamin DExperimental biology and medicine (Maywood, N.J.) · 2025
    Article
  8. Review
  9. Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024
    Review
  10. Mechanisms of Cell Death Induced by Erastin in Human Ovarian Tumor Cells.International journal of molecular sciences · 2024
    Article
  11. Control of astrocytic CaBiological research · 2024
    Article
  12. Science advances · 2024
    Article
  13. A metabolic perspective on nitric oxide function in melanoma.Biochimica et biophysica acta. Reviews on cancer · 2024
    Review
  14. Nitric Oxide: Physiological Functions, Delivery, and Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  15. Regulation of Ras Signaling by S-Nitrosylation.Antioxidants (Basel, Switzerland) · 2023
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

3 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

6 authors.

Antonio Martínez-Ruiz1 Servicio de Inmunología, Hospital Universitario de La Princesa, Instituto de Investigación Sanitaria Princesa (IP) , Madrid, Spain .
Inês M Araújo
Alicia Izquierdo-Álvarez
Pablo Hernansanz-Agustín
Santiago Lamas
Juan M Serrador

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

significanceNitric oxide (NO) classical and less classical signaling mechanisms (through interaction with soluble guanylate cyclase and cytochrome c oxidase, respectively) operate through direct binding of NO to protein metal centers, and rely on diffusibility of the NO molecule. S-Nitrosylation, a covalent post-translational modification of protein cysteines, has emerged as a paradigm of nonclassical NO signaling. RECENT ADVANCES: Several nonenzymatic mechanisms for S-nitrosylation formation and destruction have been described. Enzymatic mechanisms for transnitrosylation and denitrosylation have been also studied as regulators of the modification of specific subsets of proteins. The advancement of modification-specific proteomic methodologies has allowed progress in the study of diverse S-nitrosoproteomes, raising clues and questions about the parameters for determining the protein specificity of the modification. CRITICAL ISSUES: We propose that S-nitrosylation is mainly a short-range mechanism of NO signaling, exerted in a relatively limited range of action around the NO sources, and tightly related to the very controlled regulation of subcellular localization of nitric oxide synthases. We review the nonenzymatic and enzymatic mechanisms that support this concept, as well as physiological examples of mammalian systems that illustrate well the precise compartmentalization of S-nitrosylation. FUTURE DIRECTIONS: Individual and proteomic studies of protein S-nitrosylation-based signaling should take into account the subcellular localization in order to gain further insight into the functional role of this modification in (patho)physiological settings.

Indexed as

AnimalsBrainHumansIntracellular SpaceMyocardiumNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIProtein TransportSignal TransductionS-NitrosothiolsSubstrate SpecificityNitric OxideNitric Oxide SynthaseNitric Oxide Synthase Type IIIS-Nitrosothiols

Identifiers

PMID23157283
PMCPMC3785806

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.