Evidence map›Paper›PMID 23281369›Full record

ArticleScience signaling2013

Nitric oxide regulates mitochondrial fatty acid metabolism through reversible protein S-nitrosylation.

Paschalis-Thomas Doulias, Margarita Tenopoulou, Jennifer L Greene, Karthik Raju, Harry Ischiropoulos

Abstract read
In one paragraph

Article in Science signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
152citing papers in PubMed, 1 pooled it
12.6field-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

152 citing papers in PubMed, 1 synthesis or guideline pooled it, 245 citations in OpenAlex.

  1. Pooled it
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  17. Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024
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92 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.

Paschalis-Thomas DouliasChildren'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, PA 19104, USA.
Margarita Tenopoulou
Jennifer L Greene
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

Cysteine S-nitrosylation is a posttranslational modification by which nitric oxide regulates protein function and signaling. Studies of individual proteins have elucidated specific functional roles for S-nitrosylation, but knowledge of the extent of endogenous S-nitrosylation, the sites that are nitrosylated, and the regulatory consequences of S-nitrosylation remains limited. We used mass spectrometry-based methodologies to identify 1011 S-nitrosocysteine residues in 647 proteins in various mouse tissues. We uncovered selective S-nitrosylation of enzymes participating in glycolysis, gluconeogenesis, tricarboxylic acid cycle, and oxidative phosphorylation, indicating that this posttranslational modification may regulate metabolism and mitochondrial bioenergetics. S-nitrosylation of the liver enzyme VLCAD [very long chain acyl-coenzyme A (CoA) dehydrogenase] at Cys(238), which was absent in mice lacking endothelial nitric oxide synthase, improved its catalytic efficiency. These data implicate protein S-nitrosylation in the regulation of β-oxidation of fatty acids in mitochondria.

Indexed as

Acyl-CoA Dehydrogenase, Long-ChainAnalysis of VarianceAnimalsCysteineDNA PrimersEnergy MetabolismFatty AcidsLiverMass SpectrometryMiceMitochondriaMutagenesis, Site-DirectedNitric OxideOxidation-ReductionProtein Processing, Post-TranslationalProteomicsAcyl-CoA Dehydrogenase, Long-ChainCysteineDNA PrimersFatty AcidsNitric OxideS-nitrosocysteineS-Nitrosothiols

Identifiers

PMID23281369
PMCPMC4010156
OpenAlexW2160610690

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.