Evidence map›Paper›PMID 22361849›Full record

ReviewJournal of molecular medicine (Berlin, Germany)2012

Enzymatic mechanisms regulating protein S-nitrosylation: implications in health and disease.

Puneet Anand, Jonathan S Stamler

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular medicine (Berlin, Germany), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
11.8field-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

123 citing papers in PubMed, 269 citations in OpenAlex.

  1. Review
  2. Dysregulated ProteinCirculation research · 2025
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. A metabolic perspective on nitric oxide function in melanoma.Biochimica et biophysica acta. Reviews on cancer · 2024
    Review
  14. Review
  15. Review
  16. Article
  17. Unraveling the Molecular Mechanism ofInorganic chemistry · 2023
    Article
  18. Inhaled Nitric Oxide Promotes Angiogenesis in the Rodent Developing Brain.International journal of molecular sciences · 2023
    Article
  19. Review
  20. Review

63 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

2 authors at 1 institution in 1 country.

Puneet AnandInstitute for Transformative Molecular Medicine and Department of Medicine, Case Western Reserve University and University Hospitals Case Medical Center, Cleveland, OH 44106, USA.
Jonathan S Stamler
University Hospitals Case Medical Center · US

Funding

Regulation of Beta-Adrenergic Receptor Signaling by S-NitrosylationP01HL075443 · NHLBI · DUKE UNIVERSITY · PI STAMLER, JONATHAN S. · 2004 to 2019
$26.1M
Redox Signalling by Nitric Oxide in Skeletal MuscleR01HL059130 · NHLBI · DUKE UNIVERSITY · PI STAMLER, JONATHAN S. · 1997 to 2011
$3.1M
Red Blood Cell S-nitrosothiols and OxygenationR01HL091876 · NHLBI · DUKE UNIVERSITY · PI STAMLER, JONATHAN S. · 2009 to 2012
$1.6M
Restoration and Function of S-nitrosothiol in Stored BloodR01HL095463 · NHLBI · CASE WESTERN RESERVE UNIVERSITY · PI STAMLER, JONATHAN S. · 2009 to 2012
$1.5M
NHLBI NIH HHS P01 HL075443NHLBI NIH HHS P01HL75443NHLBI NIH HHS R01 HL059130NHLBI NIH HHS R01HL059130NHLBI NIH HHS R01 HL091876NHLBI NIH HHS R01HL091876NHLBI NIH HHS R01 HL095463NHLBI NIH HHS R01HL095463
6 · The paper itself

Abstract

Nitric oxide participates in cellular signal transduction largely through S-nitrosylation of allosteric and active-site cysteine thiols within proteins, forming S-nitroso-proteins (SNO-proteins). S-nitrosylation of proteins has been demonstrated to affect a broad range of functional parameters including enzymatic activity, subcellular localization, protein-protein interactions, and protein stability. Analogous to other ubiquitous posttranslational modifications that are regulated enzymatically, including phosphorylation and ubiquitinylation, accumulating evidence suggests the existence of enzymatic mechanisms for regulating protein S-nitrosylation. In particular, studies have led to the identification of multiple enzymes (nitrosylases and denitrosylases) that participate in targeted S-nitrosylation or denitrosylation of proteins in physiological settings. Nitrosylases are best characterized in the context of transnitrosylation in which a SNO-protein transfers an NO group to an acceptor protein (Cys-to-Cys transfer), but examples of transnitrosylation catalyzed by metalloproteins (Metal-to-Cys transfer) also exist. By contrast, denitrosylases remove the NO group from SNO-proteins, ultimately using reducing equivalents derived from NADH or NADPH. Here, we focus on the recent discoveries of nitrosylases and denitrosylases and the notion that their aberrant activities may play roles in health and disease.

Indexed as

Signal TransductionAnimalsDiseaseHumansNitric OxideProtein Processing, Post-TranslationalProteinsS-NitrosothiolsNitric OxideProteinsS-Nitrosothiols

Identifiers

PMID22361849
PMCPMC3379879
OpenAlexW1997692317

What OpenQuestion holds

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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.