Evidence map›Paper›PMID 23648414›Full record

ReviewBiochimica et biophysica acta2014

Methionine oxidation and reduction in proteins.

Geumsoo Kim, Stephen J Weiss, Rodney L Levine

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

139 citing papers in PubMed, 302 citations in OpenAlex.

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  11. [COResearch square · 2026
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  13. Review
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  17. A roadmap to chemically reactive species: how diverse oxidants affectMicrobiology and molecular biology reviews : MMBR · 2025
    Review
  18. Article
  19. Article
  20. Article

79 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

3 authors at 2 institutions in 1 country.

Geumsoo KimLaboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD 20892, USA.
Stephen J Weiss
Rodney L Levine
National Heart Lung and Blood Institute · USUniversity of Michigan–Ann Arbor · US

Funding

Oxidative Modification Of ProteinsZIAHL000225 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEVINE, RODNEY L. · 2009 to 2025
$35.2M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
Intramural NIH HHS ZIA HL000225NIDDK NIH HHS P30 DK020572
6 · The paper itself

Abstract

backgroundCysteine and methionine are the two sulfur containing amino acids in proteins. While the roles of protein-bound cysteinyl residues as endogenous antioxidants are well appreciated, those of methionine remain largely unexplored. SCOPE: We summarize the key roles of methionine residues in proteins. MAJOR

conclusionRecent studies establish that cysteine and methionine have remarkably similar functions. GENERAL SIGNIFICANCE: Both cysteine and methionine serve as important cellular antioxidants, stabilize the structure of proteins, and can act as regulatory switches through reversible oxidation and reduction. This article is part of a Special Issue entitled Current methods to study reactive oxygen species - pros and cons and biophysics of membrane proteins. Guest Editor: Christine Winterbourn.

Indexed as

AnimalsHumansMethionineOxidation-ReductionProteinsMethionineProteinsA(2)MMethioninemethionine sulfoxideMethionine sulfoxidemethionine sulfoxide reductaseMethionine sulfoxide reductaseMetOMsrOxidant defenseα(2)macroglobulin

Identifiers

PMID23648414
PMCPMC3766491
OpenAlexW2044036144

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.