Evidence map›Paper›PMID 23592332›Full record

ArticleMolecular & cellular proteomics : MCP2013

Discovery of histone modification crosstalk networks by stable isotope labeling of amino acids in cell culture mass spectrometry (SILAC MS).

Xiaoyan Guan, Neha Rastogi, Mark R Parthun, Michael A Freitas

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

13 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Is There a Histone Code for Cellular Quiescence?Frontiers in cell and developmental biology · 2021
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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.

Xiaoyan GuanDepartment of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Neha Rastogi
Mark R Parthun
Michael A Freitas
The Ohio State University · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
Type B Histone Acetyltransferases and the Assembly of Chromatin StructureR01GM062970 · NIGMS · OHIO STATE UNIVERSITY · PI PARTHUN, MARK R · 2001 to 2018
$5.1M
Assays for Screening Histone Modifications in CancerR01CA107106 · NCI · OHIO STATE UNIVERSITY · PI FREITAS, MICHAEL A. · 2004 to 2013
$1.8M
Identification of Histone Modification Interaction NetworksR21DK082634 · NIDDK · OHIO STATE UNIVERSITY · PI FREITAS, MICHAEL A., PARTHUN, MARK R · 2009 to 2010
$525k
NCI NIH HHS P30 CA016058NCI NIH HHS R01 CA107106NIDDK NIH HHS R21 DK082634NIGMS NIH HHS R01 GM062970NIGMS NIH HHS R01 GM62970
6 · The paper itself

Abstract

In this paper we describe an approach that combines stable isotope labeling of amino acids in cells culture, high mass accuracy liquid chromatography tandem mass spectrometry and a novel data analysis approach to accurately determine relative peptide post-translational modification levels. This paper describes the application of this approach to the discovery of novel histone modification crosstalk networks in Saccharomyces cerevisiae. Yeast histone mutants were generated to mimic the presence/absence of 44 well-known modifications on core histones H2A, H2B, H3, and H4. In each mutant strain the relative change in H3 K79 methylation and H3 K56 acetylation were determined using stable isotope labeling of amino acids in cells culture. This approach showed relative changes in H3 K79 methylation and H3 K56 acetylation that are consistent with known histone crosstalk networks. More importantly, this study revealed additional histone modification sites that affect H3 K79 methylation and H3 K56 acetylation.

Indexed as

AcetylationAmino AcidsChromatography, LiquidHistonesIsotope LabelingMethylationMutagenesis, Site-DirectedPeptidesProtein Processing, Post-TranslationalSaccharomyces cerevisiae ProteinsTandem Mass SpectrometryAmino AcidsHistonesPeptidesSaccharomyces cerevisiae Proteins

Identifiers

PMID23592332
PMCPMC3734568
OpenAlexW2008351296

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.