Evidence map›Paper›PMID 21440604›Full record

ReviewBiochimica et biophysica acta2012

Methodologies for the characterization, identification and quantification of S-nitrosylated proteins.

Matthew W Foster

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  3. Review
  4. Review
  5. Detection of ProteinBio-protocol · 2017
    Article
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  8. Review
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  12. Review
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  19. S-nitrosylation: a radical way to protect the heart.Journal of molecular and cellular cardiology · 2012
    Review
  20. Article
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

1 author at 1 institution in 1 country.

Matthew W FosterDivision of Pulmonary, Allergy and Critical Care Medicine, Duke University Medical Center, Durham, NC 27710, USA. mwfoster@duke.edu
Duke University Hospital · US

Funding

S-nitrosothiol-regulated pathways in acute lung injuryR21HL106121 · NHLBI · DUKE UNIVERSITY · PI FOSTER, MATTHEW WOLF, MARSHALL, HARVEY E · 2011 to 2012
$391k
NHLBI NIH HHS HL106121NHLBI NIH HHS R21 HL106121
6 · The paper itself

Abstract

backgroundProtein S-nitrosylation plays a central role in signal transduction by nitric oxide (NO), and aberrant S-nitrosylation of specific proteins is increasingly implicated in disease. SCOPE OF REVIEW: Here, methodologies for the characterization, identification and quantification of SNO-proteins are reviewed, focusing on techniques suitable for the structural characterization and absolute quantification of isolated SNO-proteins, the identification and relative quantification of SNO-proteins from complex mixtures as well as the mass spectrometry-based identification and relative quantification of sites of S-nitrosylation (SNO-sites) in proteins. MAJOR

conclusionsStructural characterization of SNO-proteins by X-ray crystallography is increasingly being utilized to understand both the relationships between protein structure and Cys thiol reactivity as well as the consequences of S-nitrosylation on protein structure and function. New methods for the proteomic identification and quantification of SNO-proteins and SNO-sites have greatly impacted the ability to study protein S-nitrosylation in complex biological systems. GENERAL SIGNIFICANCE: The ability to identify and quantify SNO-proteins has long been rate-determining for scientific advances in the field of protein S-nitrosylation. Therefore, it is critical that investigators in the field have a good understand the utility and limitations of modern analytical techniques for SNO-protein analysis. This article is part of a Special Issue entitled: Regulation of cellular processes by S-nitrosylation.

Indexed as

Crystallography, X-RayIntracellular Signaling Peptides and ProteinsMass SpectrometryNitric OxideNitrosationProteinsProtein Structure, SecondaryProteomicsSignal TransductionS-NitrosothiolsIntracellular Signaling Peptides and ProteinsNitric OxideProteinsS-Nitrosothiols

Identifiers

PMID21440604
PMCPMC3151544
OpenAlexW2093162508

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.