Evidence map›Paper›PMID 11179387›Full record

ReviewThe Journal of physiology2001

Regulation of cell function by methionine oxidation and reduction.

T Hoshi, S Heinemann

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
6.5field-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

137 citing papers in PubMed, 386 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Principles ofbioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  18. Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024
    Review
  19. Review
  20. Article

77 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

2 authors at 2 institutions in 2 countries.

T HoshiDepartment of Physiology and Biophysics, The University of Iowa, BSB 5-660, Iowa City, IA 52242, USA.
S Heinemann
Friedrich Schiller University Jena · DEUniversity of Iowa · US

Funding

VASOPRESSIN IN CARDIOVASCULAR REGULATIONP01HL014388 · NHLBI · UNIVERSITY OF IOWA · PI ABBOUD, FRANCOIS M · 1985 to 2018
$40.3M
REGULATION OF ION CHANNELS BY METHIONINE OXIDATIONR01GM057654 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOSHI, TOSHINORI, OLCESE, RICCARDO · 1998 to 2014
$5.0M
NHLBI NIH HHS HL 14388NHLBI NIH HHS HL 64645NHLBI NIH HHS P01 HL014388NIGMS NIH HHS GM 57654NIGMS NIH HHS R01 GM057654
6 · The paper itself

Abstract

Reactive oxygen species (ROS) are generated during normal cellular activity and may exist in excess in some pathophysiological conditions, such as inflammation or reperfusion injury. These molecules oxidize a variety of cellular constituents, but sulfur-containing amino acid residues are especially susceptible. While reversible cysteine oxidation and reduction is part of well-established signalling systems, the oxidation and the enzymatically catalysed reduction of methionine is just emerging as a novel molecular mechanism for cellular regulation. Here we discuss how the oxidation of methionine to methionine sulfoxide in signalling proteins such as ion channels affects the function of these target proteins. Methionine sulfoxide reductase, which reduces methionine sulfoxide to methionine in a thioredoxin-dependent manner, is therefore not only an enzyme important for the repair of age- or degenerative disease-related protein modifications. It is also a potential missing link in the post-translational modification cycle involved in the specific oxidation and reduction of methionine residues in cellular signalling proteins, which may give rise to activity-dependent plastic changes in cellular excitability.

Indexed as

Cell Physiological PhenomenaAnimalsHumansMethionineOxidation-ReductionReactive Oxygen SpeciesMethionineReactive Oxygen Species

Identifiers

PMID11179387
PMCPMC2278441
OpenAlexW2135110724

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.