Evidence map›Paper›PMID 27324931›Full record

ReviewAntioxidants & redox signaling2017

Tyrosine-Nitrated Proteins: Proteomic and Bioanalytical Aspects.

Carlos Batthyány, Silvina Bartesaghi, Mauricio Mastrogiovanni, Analía Lima, Verónica Demicheli, Rafael Radi

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
7.7field-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

36 citing papers in PubMed, 81 citations in OpenAlex.

  1. Nitration in cancer signaling.Redox biology · 2026
    Review
  2. Review
  3. Article
  4. Review
  5. Small molecule probes for peroxynitrite detection.Redox biochemistry and chemistry · 2024
    Article
  6. Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Role of papillary thyroid carcinoma patients with Hashimoto thyroiditis: evaluation of oxidative stress and inflammatory markers.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. The mitochondrial thioredoxin reductase system (TrxR2) in vascular endothelium controls peroxynitrite levels and tissue integrity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. The Hypoxia Tolerance of the Goldfish (Antioxidants (Basel, Switzerland) · 2020
    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

6 authors at 2 institutions in 1 country.

Carlos Batthyány1 Unidad de Bioquímica y Proteómica Analíticas, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Silvina Bartesaghi3 Facultad de Medicina, Center for Free Radical and Biomedical Research , Universidad de la República, Montevideo, Uruguay .
Mauricio Mastrogiovanni2 Departamento de Bioquímica, Facultad de Medicina, Universidad de la República , Montevideo, Uruguay .
Analía Lima1 Unidad de Bioquímica y Proteómica Analíticas, Institut Pasteur de Montevideo , Montevideo, Uruguay .
Verónica Demicheli2 Departamento de Bioquímica, Facultad de Medicina, Universidad de la República , Montevideo, Uruguay .
Rafael Radi2 Departamento de Bioquímica, Facultad de Medicina, Universidad de la República , Montevideo, Uruguay .
Universidad de la República · UYInstitut Pasteur de Montevideo · UY

Funding

Trypanosoma cruzi Antioxidant Systems, Virulence and Parasite Persistence in ChagR01AI095173 · NIAID · FACULTAD DE MEDICINA · PI RADI, RAFAEL · 2011 to 2014
$412k
NIAID NIH HHS R01 AI095173
6 · The paper itself

Abstract

significance"Nitroproteomic" is under active development, as 3-nitrotyrosine in proteins constitutes a footprint left by the reactions of nitric oxide-derived oxidants that are usually associated to oxidative stress conditions. Moreover, protein tyrosine nitration can cause structural and functional changes, which may be of pathophysiological relevance for human disease conditions. Biological protein tyrosine nitration is a free radical process involving the intermediacy of tyrosyl radicals; in spite of being a nonenzymatic process, nitration is selectively directed toward a limited subset of tyrosine residues. Precise identification and quantitation of 3-nitrotyrosine in proteins has represented a "tour de force" for researchers. Recent Advances: A small number of proteins are preferential targets of nitration (usually less than 100 proteins per proteome), contrasting with the large number of proteins modified by other post-translational modifications such as phosphorylation, acetylation, and, notably, S-nitrosation. Proteomic approaches have revealed key features of tyrosine nitration both in vivo and in vitro, including selectivity, site specificity, and effects in protein structure and function. CRITICAL ISSUES: Identification of 3-nitrotyrosine-containing proteins and mapping nitrated residues is challenging, due to low abundance of this oxidative modification in biological samples and its unfriendly behavior in mass spectrometry (MS)-based technologies, that is, MALDI, electrospray ionization, and collision-induced dissociation. FUTURE DIRECTIONS: The use of (i) classical two-dimensional electrophoresis with immunochemical detection of nitrated proteins followed by protein ID by regular MS/MS in combination with (ii) immuno-enrichment of tyrosine-nitrated peptides and (iii) identification of nitrated peptides by a MIDAS™ experiment is arising as a potent methodology to unambiguously map and quantitate tyrosine-nitrated proteins in vivo. Antioxid. Redox Signal. 26, 313-328.

Indexed as

Protein Processing, Post-TranslationalAnimalsHumansMass SpectrometryNitratesNitrosationProteinsProteomeProteomicsSensitivity and SpecificityTyrosine3-nitrotyrosineNitratesProteinsProteomeTyrosinefree radicalsnitrationperoxynitriteprotein oxidationproteomics

Identifiers

PMID27324931
PMCPMC5326983
OpenAlexW2500532125

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.