Evidence map›Paper›PMID 42030158›Full record

ArticleCell reports2026

Comprehensive mass spectrometry screening-derived atlas of HDAC inhibitors reveals histone-specific acetylation changes.

Rashmi Karki, Francisca N De Luna Vitorino, Richard M Searfoss, Joanna K Lempiäinen, Cheryl H Arrowsmith, Benjamin A Garcia

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

6 authors.

Rashmi KarkiDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.
Francisca N De Luna VitorinoDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.
Richard M SearfossDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.
Joanna K LempiäinenDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA.
Cheryl H ArrowsmithStructural Genomics Consortium, University of Toronto, Toronto, ON, Canada; Princess Margaret Center, Toronto, ON, Canada.
Benjamin A GarciaDepartment of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO, USA. Electronic address: bagarcia@wustl.edu.

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI TIMOTHY J. EBERLEIN · 2001 to 2026
$128.0M
Shared Resources Core 2: Quantitative Proteomics CoreP01CA196539 · NCI · ROCKEFELLER UNIVERSITY · PI MUIR, TOM · 2015 to 2024
$17.6M
Viral modulation of epitranscriptomic mechanismsR01AI118891 · NIAID · WASHINGTON UNIVERSITY · PI GARCIA, BENJAMIN A, WEITZMAN, MATTHEW D. · 2015 to 2025
$5.4M
Quantitative mass spectrometry for comprehending epigenetic mechanisms in a new underlying neurological developmental disorderR01HD106051 · NICHD · WASHINGTON UNIVERSITY · PI Benjamin A Garcia · 2022 to 2026
$2.6M
Development and Application of Chemical Biology Approaches for Understanding Protein ArginylationR01HL177113 · NHLBI · WASHINGTON UNIVERSITY · PI Benjamin A Garcia, Zongtao Lin · 2025 to 2026
$1.2M
NCI NIH HHS P01 CA196539NCI NIH HHS P30 CA091842NHLBI NIH HHS R01 HL177113NIAID NIH HHS R01 AI118891NICHD NIH HHS R01 HD106051
6 · The paper itself

Abstract

Histone deacetylase inhibitors (HDACis) have emerged as valuable therapeutics for cancer and other diseases; however, their effects on histone post-translational modification remain poorly characterized. Here, we applied quantitative mass spectrometry and high-throughput sequencing to systematically profile site-specific changes in histone modifications in response to a panel of HDACis. This platform enabled mapping of histone modification changes across hundreds of sites, including low-abundance histone marks. Furthermore, an integrative analysis of chromatin immunoprecipitation followed by sequencing (ChIP-seq) and RNA-sequencing (RNA-seq) data identified genome-wide binding sites for the low-abundance histone modification of H2A.Z acetylation in HeLa and MDA-MB-231 breast cancer cells, highlighting the role of H2A.Z acetylation in regulating gene expression across diverse biological pathways, including specific genes involved in tumor suppressor pathways. Our findings provide a functional resource for identifying and quantifying histone modification changes and transcriptional regulation of histone H2A.Z acetylation following pharmacological perturbation.

Indexed as

Histone Deacetylase InhibitorsHistonesMass SpectrometryAcetylationCell Line, TumorHeLa CellsHumansProtein Processing, Post-TranslationalHistone Deacetylase InhibitorsHistonesbreast cancerChIP-seqCP: genomicsEntinostathistone deacetylase inhibitorshistone H2A.Z acetylationmass spectrometrypost-translational modificationRNA-seq

Identifiers

PMID42030158
PMCPMC13560840

What OpenQuestion holds

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Registered trials

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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.