Evidence map›Paper›PMID 21999833›Full record

ReviewExpert review of proteomics2011

Breaking the histone code with quantitative mass spectrometry.

Laura-Mae P Britton, Michelle Gonzales-Cope, Barry M Zee, Benjamin A Garcia

Abstract readReview
In one paragraph

Review in Expert review of proteomics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Review
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  17. Review
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2 more citing papers are in PubMed but not listed here.

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.

Laura-Mae P BrittonDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
Michelle Gonzales-Cope
Barry M Zee
Benjamin A Garcia

Funding

Novel Methodology for Quantitative High-throughput Cancer EpigeneticsDP2OD007447 · OD · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2010 to 2010
$2.4M
NIH HHS DP2 OD007447NIH HHS DP2OD007447
6 · The paper itself

Abstract

Histone post-translational modifications (PTMs) comprise one of the most intricate nuclear signaling networks that govern gene expression in a long-term and dynamic fashion. These PTMs are considered to be 'epigenetic' or heritable from one cell generation to the next and help establish genomic expression patterns. While much of the analyses of histones have historically been performed using site-specific antibodies, these methods are replete with technical obstacles (i.e., cross-reactivity and epitope occlusion). Mass spectrometry-based proteomics has begun to play a significant role in the interrogation of histone PTMs, revealing many new aspects of these modifications that cannot be easily determined with standard biological approaches. Here, we review the accomplishments of mass spectrometry in the histone field, and outline the future roadblocks that must be overcome for mass spectrometry-based proteomics to become the method of choice for chromatin biologists.

Indexed as

ChromatinEpigenesis, GeneticGenetic CodeHistonesHumansIsotope LabelingMass SpectrometryMethylationProtein Processing, Post-TranslationalProteomeChromatinHistonesProteome

Identifiers

PMID21999833
PMCPMC3249422

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.