Evidence map›Paper›PMID 20972425›Full record

ArticleNature cell biology2010

GAPDH mediates nitrosylation of nuclear proteins.

Michael D Kornberg, Nilkantha Sen, Makoto R Hara, Krishna R Juluri, Judy Van K Nguyen, Adele M Snowman, Lindsey Law, Lynda D Hester, Solomon H Snyder

Open access · greenAbstract read
In one paragraph

Article in Nature cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed, 1 pooled it
15.4field-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

225 citing papers in PubMed, 1 synthesis or guideline pooled it, 388 citations in OpenAlex.

  1. Interplay Between Glucose Metabolism and Chromatin Modifications in Cancer.Frontiers in cell and developmental biology · 2021
    Pooled it
  2. Review
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  6. The moonlighting functions of glycolytic enzymes in tumorigenesis.Cellular oncology (Dordrecht, Netherlands) · 2026
    Review
  7. Cysteine-S-nitrosylation inhibits Rop5-mediated immune evasion inbioRxiv : the preprint server for biology · 2025
    Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Aspirin-Mediated Acetylation of SIRT1 Maintains Intestinal Immune Homeostasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Michael D KornbergDepartment of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Nilkantha Sen
Makoto R Hara
Krishna R Juluri
Judy Van K Nguyen
Adele M Snowman
Lindsey Law
Lynda D Hester
Solomon H Snyder
Johns Hopkins Medicine · USJohns Hopkins University · USDuke University · US

Funding

UNDERSTANDING NO SIGNALING RESULTING IN NEUROPROTECTION.P50DA000266 · NIDA · JOHNS HOPKINS UNIVERSITY · PI WORLEY, PAUL F · 1985 to 2017
$45.2M
NEUROTRANSMITTER RECEPTORSK05DA000074 · NIDA · JOHNS HOPKINS UNIVERSITY · PI SNYDER, SOLOMON H. · 1985 to 2009
$1.3M
NIDA NIH HHS DA-000266NIDA NIH HHS DA-00074NIDA NIH HHS K05 DA000074NIDA NIH HHS P50 DA000266
6 · The paper itself

Abstract

S-nitrosylation of proteins by nitric oxide is a major mode of signalling in cells. S-nitrosylation can mediate the regulation of a range of proteins, including prominent nuclear proteins, such as HDAC2 (ref. 2) and PARP1 (ref. 3). The high reactivity of the nitric oxide group with protein thiols, but the selective nature of nitrosylation within the cell, implies the existence of targeting mechanisms. Specificity of nitric oxide signalling is often achieved by the binding of nitric oxide synthase (NOS) to target proteins, either directly or through scaffolding proteins such as PSD-95 (ref. 5) and CAPON. As the three principal isoforms of NOS--neuronal NOS (nNOS), endothelial NOS (eNOS) and inducible NOS (iNOS)--are primarily non-nuclear, the mechanisms by which nuclear proteins are selectively nitrosylated have been elusive. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is physiologically nitrosylated at its Cys 150 residue. Nitrosylated GAPDH (SNO-GAPDH) binds to Siah1, which possesses a nuclear localization signal, and is transported to the nucleus. Here, we show that SNO-GAPDH physiologically transnitrosylates nuclear proteins, including the deacetylating enzyme sirtuin-1 (SIRT1), histone deacetylase-2 (HDAC2) and DNA-activated protein kinase (DNA-PK). Our findings reveal a novel mechanism for targeted nitrosylation of nuclear proteins and suggest that protein-protein transfer of nitric oxide groups may be a general mechanism in cellular signal transduction.

Indexed as

Cells, CulturedDNA-Activated Protein KinaseGlyceraldehyde-3-Phosphate DehydrogenasesHistone Deacetylase 2HumansNitric OxideNitric Oxide DonorsNuclear ProteinsSignal TransductionSirtuin 1DNA-Activated Protein KinaseGlyceraldehyde-3-Phosphate DehydrogenasesHDAC2 protein, humanHistone Deacetylase 2Nitric OxideNitric Oxide DonorsNuclear ProteinsPRKDC protein, humanSIRT1 protein, humanSirtuin 1

Identifiers

PMID20972425
PMCPMC2972384
OpenAlexW1977535645

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.