Evidence map›Paper›PMID 28096900›Full record

ArticleEpigenetics & chromatin2017

MS_HistoneDB, a manually curated resource for proteomic analysis of human and mouse histones.

Sara El Kennani, Annie Adrait, Alexey K Shaytan, Saadi Khochbin, Christophe Bruley, Anna R Panchenko, David Landsman, Delphine Pflieger, Jérôme Govin

Open access · goldAbstract read
In one paragraph

Article in Epigenetics & chromatin, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 52 citations in OpenAlex.

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  18. The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 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

9 authors at 6 institutions in 2 countries.

Sara El KennaniINSERM, U1038, CEA, BIG FR CNRS 3425-BGE, Université Grenoble Alpes, Grenoble, France.
Annie AdraitINSERM, U1038, CEA, BIG FR CNRS 3425-BGE, Université Grenoble Alpes, Grenoble, France.
Alexey K ShaytanNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894 USA.
Saadi KhochbinCNRS UMR 5309 INSERM U1209, Institute of Advanced Biosciences, Université Grenoble Alpes, Grenoble, France.
Christophe BruleyINSERM, U1038, CEA, BIG FR CNRS 3425-BGE, Université Grenoble Alpes, Grenoble, France.
Anna R PanchenkoNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894 USA.
David LandsmanNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894 USA.
Delphine PfliegerINSERM, U1038, CEA, BIG FR CNRS 3425-BGE, Université Grenoble Alpes, Grenoble, France.
Jérôme GovinINSERM, U1038, CEA, BIG FR CNRS 3425-BGE, Université Grenoble Alpes, Grenoble, France.
CEA Grenoble · FRNational Center for Biotechnology Information · USUniversité Grenoble Alpes · FRCentre National de la Recherche Scientifique · FRCommissariat à l'Énergie Atomique et aux Énergies Alternatives · FRNational Institutes of Health · US

Funding

Protein-protein binding: regulation and effect of disease mutationsZIALM090313 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PANCHENKO, ANNA · 2013 to 2018
$5.2M
Structural And Functional Analysis Of Protein Sequence FamiliesZIALM000071 · NLM · NATIONAL LIBRARY OF MEDICINE · PI LANDSMAN, DAVID · 2009 to 2025
$3.7M
6 · The paper itself

Abstract

backgroundHistones and histone variants are essential components of the nuclear chromatin. While mass spectrometry has opened a large window to their characterization and functional studies, their identification from proteomic data remains challenging. Indeed, the current interpretation of mass spectrometry data relies on public databases which are either not exhaustive (Swiss-Prot) or contain many redundant entries (UniProtKB or NCBI). Currently, no protein database is ideally suited for the analysis of histones and the complex array of mammalian histone variants.

resultsWe propose two proteomics-oriented manually curated databases for mouse and human histone variants. We manually curated >1700 gene, transcript and protein entries to produce a non-redundant list of 83 mouse and 85 human histones. These entries were annotated in accordance with the current nomenclature and unified with the "HistoneDB2.0 with Variants" database. This resource is provided in a format that can be directly read by programs used for mass spectrometry data interpretation. In addition, it was used to interpret mass spectrometry data acquired on histones extracted from mouse testis. Several histone variants, which had so far only been inferred by homology or detected at the RNA level, were detected by mass spectrometry, confirming the existence of their protein form.

conclusionsMouse and human histone entries were collected from different databases and subsequently curated to produce a non-redundant protein-centric resource, MS_HistoneDB. It is dedicated to the proteomic study of histones in mouse and human and will hopefully facilitate the identification and functional study of histone variants.

Indexed as

Databases, ProteinAnimalsHistonesHumansMass SpectrometryMicePhylogenyProtein IsoformsProteomicsRNAHistonesProtein IsoformsRNAChromatinHistoneHistone variantsMass spectrometryProteomics

Identifiers

PMID28096900
PMCPMC5223428
OpenAlexW2569242246

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.