Evidence map›Paper›PMID 29327308›Full record

ReviewNeurochemical research2019

Methionine in Proteins: It's Not Just for Protein Initiation Anymore.

Jung Mi Lim, Geumsoo Kim, Rodney L Levine

Abstract readReview
In one paragraph

Review in Neurochemical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

69 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
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  17. Broadening theChildren (Basel, Switzerland) · 2024
    Article
  18. Article
  19. Review
  20. Fundamentals of redox regulation in biology.Nature reviews. Molecular cell biology · 2024
    Review

9 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.

Jung Mi LimLaboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892-8012, USA.
Geumsoo KimLaboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892-8012, USA.
Rodney L LevineLaboratory of Biochemistry, National Heart, Lung, and Blood Institute, Bethesda, MD, 20892-8012, USA. rlevine@nih.gov.ORCID http://orcid.org/0000-0001-7908-7206
National Heart Lung and Blood Institute · USNational Institutes of Health · US

Funding

Oxidative Modification Of ProteinsZIAHL000225 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEVINE, RODNEY L. · 2009 to 2025
$35.2M
Intramural NIH HHS ZIA HL000225
6 · The paper itself

Abstract

Methionine in proteins is often thought to be a generic hydrophobic residue, functionally replaceable with another hydrophobic residue such as valine or leucine. This is not the case, and the reason is that methionine contains sulfur that confers special properties on methionine. The sulfur can be oxidized, converting methionine to methionine sulfoxide, and ubiquitous methionine sulfoxide reductases can reduce the sulfoxide back to methionine. This redox cycle enables methionine residues to provide a catalytically efficient antioxidant defense by reacting with oxidizing species. The cycle also constitutes a reversible post-translational covalent modification analogous to phosphorylation. As with phosphorylation, enzymatically-mediated oxidation and reduction of specific methionine residues functions as a regulatory process in the cell. Methionine residues also form bonds with aromatic residues that contribute significantly to protein stability. Given these important functions, alteration of the methionine-methionine sulfoxide balance in proteins has been correlated with disease processes, including cardiovascular and neurodegenerative diseases. Methionine isn't just for protein initiation.

Indexed as

AnimalsAntioxidantsCardiovascular DiseasesHumansMethionineNeoplasmsNeurodegenerative DiseasesOxidation-ReductionProtein Processing, Post-TranslationalAntioxidantsMethionineCellular regulationMethionineMethionine sulfoxideMethionine sulfoxide reductaseOxidative defensesProtein structure

Identifiers

PMID29327308
PMCPMC6446232
OpenAlexW2783910833

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.