Evidence map›Paper›PMID 26120868›Full record

ArticleJournal of proteome research2015

Quantification of SAHA-Dependent Changes in Histone Modifications Using Data-Independent Acquisition Mass Spectrometry.

Kimberly A Krautkramer, Lukas Reiter, John M Denu, James A Dowell

Abstract read
In one paragraph

Article in Journal of proteome research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed, 70 citations in OpenAlex.

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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.

Kimberly A Krautkramer
Lukas Reiter§BiognoSYS AG, Wagistrasse 25, CH-8952 Schlieren, Switzerland.
John M Denu
James A Dowell
Biognosys (Switzerland) · CH

Funding

INTEGRATED TRAINING FOR PHYSICIAN-SCIENTISTST32GM008692 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI BURKARD, MARK E · 1998 to 2020
$10.3M
TRAINING IN NUTRITIONT32DK007665 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI GUY E GROBLEWSKI, Chi- Liang Eric Yen · 1993 to 2026
$9.2M
Molecular mechanisms of histone modification - Alzheimer’s supplement NOT-AG-18-008R37GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2013 to 2022
$3.7M
Molecular Mechanisms of Histone AcetyltransferasesR01GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 1999 to 2012
$2.9M
NIDDK NIH HHS T32 DK007665NIGMS NIH HHS GM059785-15/P250VANIGMS NIH HHS R01 GM059785NIGMS NIH HHS R37 GM059785NIGMS NIH HHS T32 GM008692
6 · The paper itself

Abstract

Histone post-translational modifications (PTMs) are important regulators of chromatin structure and gene expression. Quantitative analysis of histone PTMs by mass spectrometry remains extremely challenging due to the complex and combinatorial nature of histone PTMs. The most commonly used mass spectrometry-based method for high-throughput histone PTM analysis is data-dependent acquisition (DDA). However, stochastic precursor selection and dependence on MS1 ions for quantification impede comprehensive interrogation of histone PTM states using DDA methods. To overcome these limitations, we utilized a data-independent acquisition (DIA) workflow that provides superior run-to-run consistency and postacquisition flexibility in comparison to DDA methods. In addition, we developed a novel DIA-based methodology to quantify isobaric, co-eluting histone peptides that lack unique MS2 transitions. Our method enabled deconvolution and quantification of histone PTMs that are otherwise refractory to quantitation, including the heavily acetylated tail of histone H4. Using this workflow, we investigated the effects of the histone deacetylase inhibitor SAHA (suberoylanilide hydroxamic acid) on the global histone PTM state of human breast cancer MCF7 cells. A total of 62 unique histone PTMs were quantified, revealing novel SAHA-induced changes in acetylation and methylation of histones H3 and H4.

Indexed as

AcetylationAmino Acid SequenceBlotting, WesternChromatography, LiquidHistone CodeHistone Deacetylase InhibitorsHistonesHumansHydroxamic AcidsMass SpectrometryMCF-7 CellsMethylationMolecular Sequence DataPeptidesProtein Processing, Post-TranslationalProteomicsHistone Deacetylase InhibitorsHistonesHydroxamic AcidsPeptidesVorinostatacetylationdata-independent acquisitionDIAepigeneticsHistone PTMmass spectrometrymethylationproteomicsSAHA

Identifiers

PMID26120868
PMCPMC4564294
OpenAlexW2405172807

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.