Evidence map›Paper›PMID 23049513›Full record

ArticleFrontiers in physiology2012

Oxidative modification of proteins: an emerging mechanism of cell signaling.

Stephanie B Wall, Joo-Yeun Oh, Anne R Diers, Aimee Landar

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Redox regulation of memory formation by Rrp1 inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Article
  15. A new fibrillization mechanism of β-lactoglobulin in glycine solutions.International journal of biological macromolecules · 2022
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  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

4 authors at 2 institutions in 1 country.

Stephanie B WallDepartments of Pathology, University of Alabama at Birmingham Birmingham, AL, USA ; Center for Free Radical Biology, University of Alabama at Birmingham Birmingham, AL, USA.
Joo-Yeun Oh
Anne R Diers
Aimee Landar
University of Alabama at Birmingham · USMedical College of Wisconsin · US

Funding

Training Program in Cardiovascular PathophysiologyT32HL007918 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BALLINGER, SCOTT W. · 1999 to 2018
$3.6M
The role of the mitochondrial protein thiol modification in endothelial dysfunctiR01HL096638 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI LANDAR, AIMEE LEIGH · 2010 to 2014
$1.8M
NHLBI NIH HHS R01 HL096638NHLBI NIH HHS T32 HL007918
6 · The paper itself

Abstract

There are a wide variety of reactive species which can affect cell function, including reactive oxygen, nitrogen, and lipid species. Some are formed endogenously through enzymatic or non-enzymatic pathways, and others are introduced through diet or environmental exposure. Many of these reactive species can interact with biomolecules and can result in oxidative post-translational modification of proteins. It is well documented that some oxidative modifications cause macromolecular damage and cell death. However, a growing body of evidence suggests that certain classes of reactive species initiate cell signaling by reacting with specific side chains of peptide residues without causing cell death. This process is generally termed "redox signaling," and its role in physiological and pathological processes is a subject of active investigation. This review will give an overview of oxidative protein modification as a mechanism of redox signaling, including types of reactive species and how they modify proteins, examples of modified proteins, and a discussion about the current concepts in this area.

Indexed as

15-deoxy-prostaglandin J2 (15d-PGJ2)electrophilereactive speciesredox signalingthiol

Identifiers

PMID23049513
PMCPMC3442266
OpenAlexW2171303848

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.