Evidence map›Paper›PMID 9275229›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Modulation of potassium channel function by methionine oxidation and reduction.

M A Ciorba, S H Heinemann, H Weissbach, N Brot, T Hoshi

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

83 citing papers in PubMed, 225 citations in OpenAlex.

  1. Article
  2. Article
  3. Role of mitochondrial reactive oxygen species in homeostasis regulation.Redox report : communications in free radical research · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Oxidation of methionine residues activates the high-threshold heat-sensitive ion channel TRPV2.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. The Effects of 4-Hydroxybenzoic Acid Identified from Bamboo (The Malaysian journal of medical sciences : MJMS · 2018
    Article
  16. Article
  17. Article
  18. Role of N-terminal methionine residues in the redox activity of copper bound to alpha-synuclein.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016
    Article
  19. Article
  20. Article

23 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

5 authors at 3 institutions in 1 country.

M A CiorbaDepartment of Physiology and Biophysics, Bowen 5660, The University of Iowa, Iowa City, IA 52242, USA.
S H Heinemann
H Weissbach
N Brot
T Hoshi
Cornell University · USFlorida Atlantic University · USUniversity of Iowa · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oxidation of amino acid residues in proteins can be caused by a variety of oxidizing agents normally produced by cells. The oxidation of methionine in proteins to methionine sulfoxide is implicated in aging as well as in pathological conditions, and it is a reversible reaction mediated by a ubiquitous enzyme, peptide methionine sulfoxide reductase. The reversibility of methionine oxidation suggests that it could act as a cellular regulatory mechanism although no such in vivo activity has been demonstrated. We show here that oxidation of a methionine residue in a voltage-dependent potassium channel modulates its inactivation. When this methionine residue is oxidized to methionine sulfoxide, the inactivation is disrupted, and it is reversed by coexpression with peptide methionine sulfoxide reductase. The results suggest that oxidation and reduction of methionine could play a dynamic role in the cellular signal transduction process in a variety of systems.

Indexed as

Ion Channel GatingAmino Acid SequenceAnimalsMethionineMolecular Sequence DataOocytesOxidation-ReductionPatch-Clamp TechniquesPotassium ChannelsXenopusMethioninePotassium Channels

Identifiers

PMID9275229
PMCPMC23300
OpenAlexW2091291195

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.