Evidence map›Paper›PMID 29329550›Full record

ArticleEpigenetics & chromatin2018

Systematic quantitative analysis of H2A and H2B variants by targeted proteomics.

Sara El Kennani, Annie Adrait, Olga Permiakova, Anne-Marie Hesse, Côme Ialy-Radio, Myriam Ferro, Virginie Brun, Julie Cocquet, Jérôme Govin, Delphine Pflieger

Abstract read
In one paragraph

Article in Epigenetics & chromatin, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–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

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  12. Proteomics for cancer drug design.Expert review of proteomics · 2019
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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

10 authors.

Sara El KennaniINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Annie AdraitINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Olga PermiakovaINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Anne-Marie HesseINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Côme Ialy-RadioINSERM U1016, Institut Cochin, CNRS UMR8104, Université Paris Descartes, Sorbonne Paris Cité, Paris, France.
Myriam FerroINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Virginie BrunINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France.
Julie CocquetINSERM U1016, Institut Cochin, CNRS UMR8104, Université Paris Descartes, Sorbonne Paris Cité, Paris, France.
Jérôme GovinINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France. Jerome.Govin@inserm.fr.
Delphine PfliegerINSERM U1038, CEA, BIG-BGE, Univ. Grenoble Alpes, Grenoble, France. Delphine.Pflieger@cea.fr.

Funding

Agence Nationale de la Recherche ANR-10-LABX-49-01Agence Nationale de la Recherche ANR-11-PDOC-0011Agence Nationale de la Recherche ANR-12-JSV2-0005-01Agence Nationale de la Recherche (FR) ANR-10-INBS-08Agence Nationale de la Recherche (FR) ANR-14-CE19-0014-01European Union FP7 Marie Curie Action 304003
6 · The paper itself

Abstract

backgroundHistones organize DNA into chromatin through a variety of processes. Among them, a vast diversity of histone variants can be incorporated into chromatin and finely modulate its organization and functionality. Classically, the study of histone variants has largely relied on antibody-based assays. However, antibodies have a limited efficiency to discriminate between highly similar histone variants.

resultsIn this study, we established a mass spectrometry-based analysis to address this challenge. We developed a targeted proteomics method, using selected reaction monitoring or parallel reaction monitoring, to quantify a maximum number of histone variants in a single multiplexed assay, even when histones are present in a crude extract. This strategy was developed on H2A and H2B variants, using 55 peptides corresponding to 25 different histone sequences, among which a few differ by a single amino acid. The methodology was then applied to mouse testis extracts in which almost all histone variants are expressed. It confirmed the abundance profiles of several testis-specific histones during successive stages of spermatogenesis and the existence of predicted H2A.L.1 isoforms. This methodology was also used to explore the over-expression pattern of H2A.L.1 isoforms in a mouse model of male infertility.

conclusionsOur results demonstrate that targeted proteomics is a powerful method to quantify highly similar histone variants and isoforms. The developed method can be easily transposed to the study of human histone variants, whose abundance can be deregulated in various diseases.

Indexed as

Amino Acid SequenceAnimalsEpigenesis, GeneticHistonesHumansMaleMass SpectrometryMiceOrgan SpecificityPeptidesProteomicsSpermatogenesisTestisHistonesPeptidesChromatinHistone variantsPRMProteomicsSpermatogenesisSRMTargeted proteomics

Identifiers

PMID29329550
PMCPMC5767011

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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.