Evidence map›Paper›PMID 23157221›Full record

ReviewAntioxidants & redox signaling2013

Proteomic approaches to analyze protein tyrosine nitration.

Maria B Feeney, Christian Schöneich

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 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Myeloid-derived suppressor cells inhibit T cell activation through nitrating LCK in mouse cancers.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Synthetic approaches to protein phosphorylation.Current opinion in chemical biology · 2015
    Review
  11. Review
  12. Review
  13. Article
  14. Review
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.

Maria B FeeneyDepartment of Pharmaceutical Chemistry, The University of Kansas , Lawrence, Kansas.
Christian Schöneich

Funding

SARCOPENIA AND APOPTOSIS: ROLE OF SERCA AND BCL-2P01AG012993 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI MICHAELIS, ELIAS K · 1995 to 2012
$14.0M
Proteomic characterization of aging cerebellumR01AG025350 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI SCHONEICH, CHRISTIAN · 2004 to 2008
$1.4M
Multifunctional reagents for proteomic analysisR01AG023551 · NIA · UNIVERSITY OF KANSAS LAWRENCE · PI SCHONEICH, CHRISTIAN · 2004 to 2008
$1.1M
NIA NIH HHS AG12993NIA NIH HHS AG23551NIA NIH HHS AG25350NIA NIH HHS P01 AG012993NIA NIH HHS R01 AG023551NIA NIH HHS R01 AG025350
6 · The paper itself

Abstract

significanceThe conversion of protein-bound Tyr residues to 3-nitrotyrosine (3NY) can occur during nitrative stress and has been correlated to aging and many disease states. Proteomic analysis of this post-translational modification, using mass spectrometry-based techniques, is crucial for understanding its potential role in pathological and physiological processes. RECENT ADVANCES: To overcome some of the disadvantages inherent to well-established nitroproteomic methods using anti-3NY antibodies and gel-based separations, methods involving multidimensional chromatography, precursor ion scanning, and/or chemical derivatization have emerged for both identification and quantitation of protein nitration sites. A few of these methods have successfully detected endogenous 3NY modifications from biological samples. CRITICAL ISSUES: While model systems often show promising results, identification of endogenous 3NY modifications remains largely elusive. The frequently low abundance of nitrated proteins in vivo, even under inflammatory conditions, is especially challenging, and sample loss due to derivatization and cleaning may become significant. FUTURE DIRECTIONS: Continued efforts to avoid interference from non-nitrated peptides without sacrificing recovery of nitrated peptides are needed. Quantitative methods are emerging and are crucial for identifying endogenous modifications that may have significant biological impacts.

Indexed as

ProteomicsAnimalsChromatographyHumansOxidation-ReductionProteinsTyrosine3-nitrotyrosineProteinsTyrosine

Identifiers

PMID23157221
PMCPMC3785798

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.