Evidence map›Paper›PMID 27431976›Full record

ArticleJournal of proteome research2016

Label-Free Relative Quantitation of Isobaric and Isomeric Human Histone H2A and H2B Variants by Fourier Transform Ion Cyclotron Resonance Top-Down MS/MS.

Xibei Dang, Amar Singh, Brian D Spetman, Krystal D Nolan, Jennifer S Isaacs, Jonathan H Dennis, Stephen Dalton, Alan G Marshall, Nicolas L Young

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 39 citations in OpenAlex.

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  14. Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023
    Review
  15. An Improved Top-Down Mass Spectrometry Characterization ofJournal of the American Society for Mass Spectrometry · 2021
    Article
  16. Article
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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 4 institutions in 1 country.

Xibei DangDepartment of Chemistry and Biochemistry, Florida State University , 95 Chieftain Way, Tallahassee, Florida 32306-4390, United States.
Amar SinghDepartment of Biochemistry and Molecular Biology, University of Georgia , 724 Biological Sciences Building, Athens, Georgia 30602-2607, United States.
Brian D SpetmanDepartment of Biological Science, Florida State University , 319 Stadium Drive, Tallahassee, Florida 32306-4295, United States.
Krystal D NolanCell and Molecular Pharmacology & Experimental Therapeutics, Medical University of South Carolina , 173 Ashley Avenue, Charleston, South Carolina 29425, United States.
Jennifer S IsaacsCell and Molecular Pharmacology & Experimental Therapeutics, Medical University of South Carolina , 173 Ashley Avenue, Charleston, South Carolina 29425, United States.
Jonathan H DennisDepartment of Biological Science, Florida State University , 319 Stadium Drive, Tallahassee, Florida 32306-4295, United States.
Stephen DaltonDepartment of Biochemistry and Molecular Biology, University of Georgia , 724 Biological Sciences Building, Athens, Georgia 30602-2607, United States.
Alan G MarshallDepartment of Chemistry and Biochemistry, Florida State University , 95 Chieftain Way, Tallahassee, Florida 32306-4390, United States.
Nicolas L YoungIon Cyclotron Resonance Program, National High Magnetic Field Laboratory , 1800 East Paul Dirac Drive, Tallahassee, Florida 32310-4005, United States.
Florida State University · USMedical University of South Carolina · USUniversity of Georgia · USBaylor College of Medicine · US

Funding

UNDERSTANDING MECHANISMS OF hESC SELF-RENEWAL AND CELL FATE COMMITMENTP01GM085354 · NIGMS · UNIVERSITY OF GEORGIA · PI DALTON, STEPHEN · 2008 to 2018
$18.3M
NIGMS NIH HHS P01 GM085354
6 · The paper itself

Abstract

Histone variants are known to play a central role in genome regulation and maintenance. However, many variants are inaccessible by antibody-based methods or bottom-up tandem mass spectrometry due to their highly similar sequences. For many, the only tractable approach is with intact protein top-down tandem mass spectrometry. Here, ultra-high-resolution FT-ICR MS and MS/MS yield quantitative relative abundances of all detected HeLa H2A and H2B isobaric and isomeric variants with a label-free approach. We extend the analysis to identify and relatively quantitate 16 proteoforms from 12 sequence variants of histone H2A and 10 proteoforms of histone H2B from three other cell lines: human embryonic stem cells (WA09), U937, and a prostate cancer cell line LaZ. The top-down MS/MS approach provides a path forward for more extensive elucidation of the biological role of many previously unstudied histone variants and post-translational modifications.

Indexed as

Cell LineCyclotronsGenetic VariationGenomic Structural VariationHistonesHumansProtein Processing, Post-TranslationalProteomicsTandem Mass SpectrometryHistonesFT-ICRFTMShistonepost-translational modificationproteoformsequence variants

Identifiers

PMID27431976
PMCPMC6261780
OpenAlexW2497408826

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.