Evidence map›Paper›PMID 24836640›Full record

ArticleJournal of the American Chemical Society2014

Chemoproteomic profiling of lysine acetyltransferases highlights an expanded landscape of catalytic acetylation.

David C Montgomery, Alexander W Sorum, Jordan L Meier

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Hierarchical small molecule inhibition of MYST acetyltransferases.bioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Article
  8. Article
  9. Cytidine Acetylation Across the Tree of Life.Accounts of chemical research · 2024
    Article
  10. Review
  11. Article
  12. Functionalised Cofactor Mimics for Interactome Discovery and Beyond.Angewandte Chemie (International ed. in English) · 2022
    Review
  13. Activity-based profiling in RNA.Nature chemical biology · 2021
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 2 institutions in 1 country.

David C MontgomeryChemical Biology Laboratory, National Cancer Institute , Frederick, Maryland 21702, United States.
Alexander W Sorum
Jordan L Meier
Frederick National Laboratory for Cancer Research · USNational Cancer Institute · US

Funding

Targeting Cancer Through Modifications and MetabolismZIABC011488 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MEIER, JORDAN L · 2013 to 2025
$21.3M
Intramural NIH HHS ZIA BC011488NCI NIH HHS ZIA BC011488-01
6 · The paper itself

Abstract

Lysine acetyltransferases (KATs) play a critical role in the regulation of gene expression, metabolism, and other key cellular functions. One shortcoming of traditional KAT assays is their inability to study KAT activity in complex settings, a limitation that hinders efforts at KAT discovery, characterization, and inhibitor development. To address this challenge, here we describe a suite of cofactor-based affinity probes capable of profiling KAT activity in biological contexts. Conversion of KAT bisubstrate inhibitors to clickable photoaffinity probes enables the selective covalent labeling of three phylogenetically distinct families of KAT enzymes. Cofactor-based affinity probes report on KAT activity in cell lysates, where KATs exist as multiprotein complexes. Chemical affinity purification and unbiased LC-MS/MS profiling highlights an expanded landscape of orphan lysine acetyltransferases present in the human genome and provides insight into the global selectivity and sensitivity of CoA-based proteomic probes that will guide future applications. Chemoproteomic profiling provides a powerful method to study the molecular interactions of KATs in native contexts and will aid investigations into the role of KATs in cell state and disease.

Indexed as

ProteomicsAcetylationAcetyltransferasesBiocatalysisChromatography, LiquidHeLa CellsHumansLysineMolecular StructureTandem Mass SpectrometryTumor Cells, CulturedAcetyltransferasesLysine

Identifiers

PMID24836640
PMCPMC4227742
OpenAlexW1992318497

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.