Evidence map›Paper›PMID 31087289›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2019

High-Resolution Mass Spectrometry to Identify and Quantify Acetylation Protein Targets.

Birgit Schilling, Jesse G Meyer, Lei Wei, Melanie Ott, Eric Verdin

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
  2. Article
  3. Resveratrol attenuates the CoClBMC neurology · 2025
    Article
  4. YkuR functions as a protein deacetylase inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Insights into the Lysine Acetylome of the HaloarchaeonAntioxidants (Basel, Switzerland) · 2023
    Article
  14. Review
  15. Article
  16. Review
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.

Birgit SchillingBuck Institute for Research on Aging, Novato, CA, USA. bschilling@buckinstitute.org.
Jesse G MeyerBuck Institute for Research on Aging, Novato, CA, USA.
Lei WeiBuck Institute for Research on Aging, Novato, CA, USA.
Melanie OttGladstone Institutes, University of California, San Francisco, San Francisco, CA, USA.
Eric VerdinBuck Institute for Research on Aging, Novato, CA, USA.

Funding

REVERSIBLE MITOCHONDRIAL PROTEIN ACETYLATION AND METABOLIC REGULATIONR24DK085610 · NIDDK · J. DAVID GLADSTONE INSTITUTES · PI VERDIN, ERIC M. · 2010 to 2019
$16.0M
Training in Basic Research on Aging and Age-Related DiseaseT32AG000266 · NIA · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI Lisa M Ellerby · 1998 to 2026
$13.8M
Regulation of Peroxisomal Metabolism by Lysine AcylationR01DK090242 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GOETZMAN, ERIC S · 2011 to 2024
$5.4M
TripleTOF 5600 High Resolution Mass SpectrometerS10OD016281 · OD · BUCK INSTITUTE FOR RESEARCH ON AGING · PI GIBSON, BRADFORD WAYNE · 2013 to 2013
$597k
NIA NIH HHS T32 AG000266NIDDK NIH HHS R01 DK090242NIDDK NIH HHS R24 DK085610NIH HHS S10 OD016281
6 · The paper itself

Abstract

The dynamic nature of protein posttranslational modification (PTM) allows cells to rapidly respond to changes in their environment, such as nutrition, stress, or signaling. Lysine residues are targets for several types of modifications, including methylation, ubiquitination, and various acylation groups, especially acetylation. Currently, one of the best methods for identification and quantification of protein acetylation is immunoaffinity enrichment in combination with high-resolution mass spectrometry. As we are using a relatively novel and comprehensive mass spectrometric approach, data-independent acquisition (DIA), this protocol provides high-throughput, accurate, and reproducible label-free PTM quantification. Here we describe detailed protocols to process relatively small amounts of mouse liver tissue that integrate isolation of proteins, proteolytic digestion into peptides, immunoaffinity enrichment of acetylated peptides, identification of acetylation sites, and comprehensive quantification of relative abundance changes for thousands of identified lysine acetylation sites.

Indexed as

Chromatography, LiquidProtein Processing, Post-TranslationalTandem Mass SpectrometryAcetylationAnimalsLiverMicePeptidesProteolysisProteomeProteomicsWorkflowPeptidesProteomeAcetylationData-independent acquisitionMass spectrometryPosttranslational modificationsQuantification

Identifiers

PMID31087289
PMCPMC6825508

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.