Evidence map›Paper›PMID 31801345›Full record

ArticleJournal of proteome research2020

Quantitative Analysis of in Vivo Methionine Oxidation of the Human Proteome.

John Q Bettinger, Kevin A Welle, Jennifer R Hryhorenko, Sina Ghaemmaghami

Abstract read
In one paragraph

Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Enrichment-free deep proteomics enables proteome-scale analysis of methionine oxidation.DNA research : an international journal for rapid publication of reports on genes and genomes · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. The emergence and loss of cyclic peptides inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Formylation facilitates the reduction of oxidized initiator methionines.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Folding stabilities of ribosome-bound nascent polypeptides probed by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Uncovering Protein Networks in Cardiovascular Proteomics.Molecular & cellular proteomics : MCP · 2023
    Review
  18. High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023
    Article
  19. Article
  20. Article
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 1 institution in 1 country.

John Q BettingerDepartment of Biology , University of Rochester , Rochester , New York 14627 , United States.
Kevin A WelleUniversity of Rochester Mass Spectrometry Resource Laboratory , Rochester , New York 14627 , United States.
Jennifer R HryhorenkoUniversity of Rochester Mass Spectrometry Resource Laboratory , Rochester , New York 14627 , United States.
Sina GhaemmaghamiDepartment of Biology , University of Rochester , Rochester , New York 14627 , United States.ORCID 0000-0002-8696-2950
University of Rochester · US

Funding

The prevalence and mechanism of selectivity in basal autophagyR35GM119502 · NIGMS · UNIVERSITY OF ROCHESTER · PI SINA GHAEMMAGHAMI · 2016 to 2026
$5.9M
Orbitrap Fusion Lumos Mass Spectrometer for UR Proteomics ResearchS10OD025242 · OD · UNIVERSITY OF ROCHESTER · PI GHAEMMAGHAMI, SINA · 2018 to 2018
$1.1M
QExactive for UR Proteomics ResearchS10OD021486 · OD · UNIVERSITY OF ROCHESTER · PI GHAEMMAGHAMI, SINA · 2016 to 2016
$309k
NIGMS NIH HHS R35 GM119502NIH HHS S10 OD021486NIH HHS S10 OD025242
6 · The paper itself

Abstract

The oxidation of methionine is an important post-translational modification of proteins with numerous roles in physiology and pathology. However, the quantitative analysis of methionine oxidation on a proteome-wide scale has been hampered by technical limitations. Methionine is readily oxidized in vitro during sample preparation and analysis. In addition, there is a lack of enrichment protocols for peptides that contain an oxidized methionine residue, making the accurate quantification of methionine oxidation difficult to achieve on a global scale. Herein, we report a methodology to circumvent these issues by isotopically labeling unoxidized methionines with

Indexed as

MethionineProteomeHumansOxidation-ReductionPeptidesProtein Processing, Post-TranslationalMethioninePeptidesProteomehydrogen peroxidemethionine oxidationoxidative protein damagequantitative proteomicsredox chemistry

Identifiers

PMID31801345
PMCPMC7077757
OpenAlexW2993143608

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.