Evidence map›Paper›PMID 21278135›Full record

ArticleAmerican journal of physiology. Heart and circulatory physiology2011

Characterization of potential S-nitrosylation sites in the myocardium.

Mark J Kohr, Angel M Aponte, Junhui Sun, Guanghui Wang, Elizabeth Murphy, Marjan Gucek, Charles Steenbergen

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Heart and circulatory physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed, 1 pooled it
8.7field-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

81 citing papers in PubMed, 1 synthesis or guideline pooled it, 133 citations in OpenAlex.

  1. Pooled it
  2. GSNOR deletion differentially alters age-related cardiac function in a sex-dependent manner.American journal of physiology. Heart and circulatory physiology · 2026
    Article
  3. Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.Journal of cardiovascular development and disease · 2026
    Review
  4. Review
  5. Review
  6. Proteomics of the heart.Physiological reviews · 2024
    Review
  7. Mitochondrial permeability transition pore-dependent necrosis.Journal of molecular and cellular cardiology · 2023
    Review
  8. Review
  9. Review
  10. Article
  11. Mitochondrial redox regulation and myocardial ischemia-reperfusion injury.American journal of physiology. Cell physiology · 2022
    Review
  12. Article
  13. Ribosomal Protein S6: A Potential Therapeutic Target against Cancer?International journal of molecular sciences · 2021
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

21 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

7 authors at 4 institutions in 1 country.

Mark J KohrDepartment of Pathology, Johns Hopkins Medical Institutions, Baltimore, MD 21257, USA.
Angel M Aponte
Junhui Sun
Guanghui Wang
Elizabeth Murphy
Marjan Gucek
Charles Steenbergen
Center for Systems Biology · USJohns Hopkins University · USNational Institutes of Health · USNational Heart Lung and Blood Institute · US

Funding

Proteomics CoreZICHL005903 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI GUCEK, MARJAN · 2009 to 2022
$23.3M
Role of S-nitrosylation in regulating cardiac function and diseaseZIAHL006059 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI MURPHY, ELIZABETH · 2010 to 2025
$7.2M
ELEVATED CALCIUM AND MYOCARDIAL ISCHEMIC INJURYR01HL039752 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI STEENBERGEN, CHARLES · 1993 to 2019
$6.6M
Role of protein S-nitrosation in cardioprotectionF32HL096142 · NHLBI · JOHNS HOPKINS UNIVERSITY · PI KOHR, MARK JEFFREY · 2009 to 2011
$144k
Intramural NIH HHSNHLBI NIH HHS 1F32HL096142NHLBI NIH HHS 5R01HL039752NHLBI NIH HHS F32 HL096142NHLBI NIH HHS R01 HL039752
6 · The paper itself

Abstract

S-nitrosylation (SNO) is a reversible protein modification that has the ability to alter the activity of target proteins. However, only a small number of SNO proteins have been found in the myocardium, and even fewer specific sites of SNO have been identified. Therefore, this study aims to characterize potential SNO sites in the myocardium. We utilized a modified version of the SNO-resin-assisted capture technique in tandem with mass spectrometry. In brief, a modified biotin switch was performed using perfused mouse heart homogenates incubated with or without the S-nitrosylating agent S-nitrosoglutathione. Our modified SNO-resin-assisted capture protocol identified 116 unique SNO-modified proteins under basal conditions, and these represent the constitutive SNO proteome. These constitutive SNO proteins are likely to be physiologically relevant targets, since nitric oxide has been shown to play an important role in the regulation of normal cardiovascular physiology. Following S-nitrosoglutathione treatment, we identified 951 unique SNO proteins, many of which contained multiple SNO sites. These proteins show the potential for SNO. This study provides novel information regarding the constitutive SNO proteome of the myocardium, as well as potential myocardial SNO sites, and yields additional information on the SNO sites for many key proteins involved in myocardial contraction, metabolism, and cellular signaling.

Indexed as

AnimalsMaleMiceMice, Inbred C57BLMyocardiumProteinsProteomicsS-NitrosoglutathioneS-NitrosothiolsProteinsS-NitrosoglutathioneS-Nitrosothiols

Identifiers

PMID21278135
PMCPMC3075037
OpenAlexW2006044521

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.