Evidence map›Paper›PMID 22657837›Full record

ReviewAntioxidants & redox signaling2013

Emerging role of protein-protein transnitrosylation in cell signaling pathways.

Tomohiro Nakamura, Stuart A Lipton

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 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

84 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
  2. Article
  3. Intracellular Crosstalk of the Gasotransmitter Trio (NO, CO, HInternational journal of molecular sciences · 2026
    Review
  4. Review
  5. Cysteine-S-nitrosylation inhibits Rop5-mediated immune evasion inbioRxiv : the preprint server for biology · 2025
    Article
  6. Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  7. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
  8. Article
  9. Identification of Protein Targets ofACS chemical biology · 2024
    Article
  10. Review
  11. Article
  12. Nitric Oxide: Physiological Functions, Delivery, and Biomedical Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Review
  20. Review

24 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.

Tomohiro NakamuraDel E. Webb Center for Neuroscience, Aging, and Stem Cell Research, Sanford-Burnham Medical Research Institute, La Jolla, California 92037, USA. tnakamura@sanfordburnham.org
Stuart A Lipton
University of California, San Diego · US

Funding

PROJECT III - GENETIC APPROACH TO EXCITATORY TRANSMISSIONP01HD029587 · NICHD · SCINTILLON INSTITUTE FOR PHOTOBIOLOGY · PI LIPTON, STUART A · 1992 to 2016
$21.9M
La Jolla Interdisciplinary Neuroscience Center Cores - Vital VP30NS057096 · NINDS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LIPTON, STUART A · 2006 to 2010
$12.7M
Project 4: A Developmental Perspective to Nitrosative/Oxidative SusceptibilityP01ES016738 · NIEHS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI RIEDL, STEFAN J · 2008 to 2012
$8.5M
RETINAL GANGLION CELLS: ION CHANNEL &TRANSMITTERSR01EY005477 · NEI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LIPTON, STUART A · 1985 to 2010
$5.0M
CA++ CHANNEL ANTAGONISTS AND AIDS-RELATED NEUROTOXICITYR01EY009024 · NEI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI LIPTON, STUART A · 1991 to 2009
$3.9M
NEI NIH HHS R01 EY05477NEI NIH HHS R01 EY09024NICHD NIH HHS P01 HD29587NIEHS NIH HHS P01 ES016738NINDS NIH HHS P30 NS057096
6 · The paper itself

Abstract

significanceProtein S-nitrosylation, a covalent reaction of a nitric oxide (NO) group with a critical protein thiol (or more properly thiolate anion), mediates an important form of redox-related signaling as well as aberrant signaling in disease states. RECENT ADVANCES: A growing literature suggests that over 3000 proteins are S-nitrosylated in cell systems. Our laboratory and several others have demonstrated that protein S-nitrosylation can regulate protein function by directly inhibiting catalytically active cysteines, by reacting with allosteric sites, or via influencing protein-protein interaction. For example, S-nitrosylation of critical cysteine thiols in protein-disulfide isomerase and in parkin alters their activity, thus contributing to protein misfolding in Parkinson's disease. CRITICAL ISSUES: However, the mechanism by which specific protein S-nitrosylation occurs in cell signaling pathways is less well investigated. Interestingly, the recent discovery of protein-protein transnitrosylation reactions (transfer of an NO group from one protein to another) has revealed a unique mechanism whereby NO can S-nitrosylate a particular set of protein thiols, and represents a major class of nitrosylating/denitrosylating enzymes in mammalian systems. In this review, we will discuss recent evidence for transnitrosylation reactions between (i) hemoglobin/anion exchanger 1, (ii) thioredoxin/caspase-3, (iii) X-linked inhibitor of apoptosis/caspase-3, (iv) GAPDH-HDAC2/SIRT1/DNA-PK, and (v) Cdk5/dynamin related protein 1 (Drp1). This review also discusses experimental techniques useful in characterizing protein-protein transnitrosylations. FUTURE DIRECTIONS: Elucidation of additional transnitrosylation cascades will further our understanding of the enzymes that catalyze nitrosation, thereby contributing to NO-mediated signaling pathways.

Indexed as

Protein Processing, Post-TranslationalSignal TransductionAlzheimer DiseaseAnimalsCell DeathCysteineErythrocytesHumansNitric OxideNitrosationOxidation-ReductionProteinsS-NitrosothiolsCysteineNitric OxideProteinsS-nitrosocysteineS-Nitrosothiols

Identifiers

PMID22657837
PMCPMC3518546
OpenAlexW2017054448

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.