Evidence map›Paper›PMID 19406207›Full record

ReviewBiochimica et biophysica acta2009

Functions and evolution of selenoprotein methionine sulfoxide reductases.

Byung Cheon Lee, Alexander Dikiy, Hwa-Young Kim, Vadim N Gladyshev

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

77 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Antioxidants (Basel, Switzerland) · 2026
    Article
  3. Article
  4. Disulfidptosis in tumor progression.Cell death discovery · 2025
    Review
  5. Review
  6. Article
  7. Biological and Catalytic Properties of Selenoproteins.International journal of molecular sciences · 2023
    Review
  8. Article
  9. Article
  10. Stress Response in Bifidobacteria.Microbiology and molecular biology reviews : MMBR · 2022
    Review
  11. Article
  12. Genome-Wide Assessment of Stress-Associated Genes in Bifidobacteria.Applied and environmental microbiology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Sulfur Metabolism Under Stress.Antioxidants & redox signaling · 2020
    Article
  18. Article
  19. Article
  20. [Effects of titanium dioxide nanoparticles on fecal metabolome in rats after oral administration for 90 days].Beijing da xue xue bao. Yi xue ban = Journal of Peking University. Health sciences · 2020
    Article

17 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

4 authors at 3 institutions in 3 countries.

Byung Cheon LeeRedox Biology Center and Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA.
Alexander Dikiy
Hwa-Young Kim
Vadim N Gladyshev
University of Nebraska–Lincoln · USNorwegian University of Science and Technology · NOYeungnam University College

Funding

Methionine sulfoxide reduction, selenium and agingR01AG021518 · NIA · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2003 to 2018
$5.0M
NIA NIH HHS AG021518NIA NIH HHS R01 AG021518
6 · The paper itself

Abstract

Methionine sulfoxide reductases (Msrs) are thiol-dependent enzymes which catalyze conversion of methionine sulfoxide to methionine. Three Msr families, MsrA, MsrB, and fRMsr, are known. MsrA and MsrB are responsible for the reduction of methionine-S-sulfoxide and methionine-R-sulfoxide residues in proteins, respectively, whereas fRMsr reduces free methionine-R-sulfoxide. Besides acting on proteins, MsrA can additionally reduce free methionine-S-sulfoxide. Some MsrAs and MsrBs evolved to utilize catalytic selenocysteine. This includes MsrB1, which is a major MsrB in cytosol and nucleus in mammalian cells. Specialized machinery is used for insertion of selenocysteine into MsrB1 and other selenoproteins at in-frame UGA codons. Selenocysteine offers catalytic advantage to the protein repair function of Msrs, but also makes these proteins dependent on the supply of selenium and requires adjustments in their strategies for regeneration of active enzymes. Msrs have roles in protecting cellular proteins from oxidative stress and through this function they may regulate lifespan in several model organisms.

Indexed as

Evolution, MolecularAgingAnimalsCatalysisHumansMammalsMethionine Sulfoxide ReductasesModels, BiologicalOxidoreductasesSelenoproteinsmethionine sulfoxide reductaseMethionine Sulfoxide ReductasesOxidoreductasesSelenoproteins

Identifiers

PMID19406207
PMCPMC3062201
OpenAlexW2098776116

What OpenQuestion holds

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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.