Evidence map›Paper›PMID 35235327›Full record

ArticleJournal of proteome research2022

FAIMS Enhances the Detection of PTM Crosstalk Sites.

Kish R Adoni, Debbie L Cunningham, John K Heath, Aneika C Leney

Abstract read
In one paragraph

Article in Journal of proteome research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Review
  2. Review
  3. 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
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Posttranslational Modifications ofPharmacological reviews · 2024
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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.

Kish R AdoniSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.ORCID 0000-0001-7390-501X
Debbie L CunninghamSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
John K HeathSchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.
Aneika C LeneySchool of Biosciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, U.K.ORCID 0000-0002-2066-4950

Funding

Biotechnology and Biological Sciences Research Council BB/M01116X/1Biotechnology and Biological Sciences Research Council BB/S019456/1Wellcome Trust
6 · The paper itself

Abstract

Protein post-translational modifications (PTMs) enable cells to rapidly change in response to biological stimuli. With hundreds of different PTMs, understanding these control mechanisms is complex. To date, efforts have focused on investigating the effect of a single PTM on protein function. Yet, many proteins contain multiple PTMs. Moreover, one PTM can alter the prevalence of another, a phenomenon termed PTM crosstalk. Understanding PTM crosstalk is critical; however, its detection is challenging since PTMs occur substoichiometrically. Here, we develop an enrichment-free, label-free proteomics method that utilizes high-field asymmetric ion mobility spectrometry (FAIMS) to enhance the detection of PTM crosstalk. We show that by searching for multiple combinations of dynamic PTMs on peptide sequences, a 6-fold increase in candidate PTM crosstalk sites is identified compared with that of standard liquid chromatography-tandem mass spectrometry (LC-MS/MS) workflows. Additionally, by cycling through FAIMS compensation voltages within a single LC-FAIMS-MS/MS run, we show that our LC-FAIMS-MS/MS workflow can increase multi-PTM-containing peptide identifications without additional increases in run times. With 159 novel candidate crosstalk sites identified, we envisage LC-FAIMS-MS/MS to play an important role in expanding the repertoire of multi-PTM identifications. Moreover, it is only by detecting PTM crosstalk that we can "see" the full picture of how proteins are regulated.

Indexed as

Ion Mobility SpectrometryTandem Mass SpectrometryChromatography, LiquidProtein Processing, Post-TranslationalProteomicscrosstalkFAIMSmass spectrometrypost-translational modificationsproteomics

Identifiers

PMID35235327
PMCPMC8981314

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.