Evidence map›Paper›PMID 30701600›Full record

ArticleRapid communications in mass spectrometry : RCM2019

Comparison of data-acquisition methods for the identification and quantification of histone post-translational modifications on a Q Exactive HF hybrid quadrupole Orbitrap mass spectrometer.

Joby Cole, Eleanor J Hanson, David C James, David H Dockrell, Mark J Dickman

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
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  8. Glycosylation Analysis of Feline Small Intestine FollowingAnimals : an open access journal from MDPI · 2022
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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

5 authors at 2 institutions in 2 countries.

Joby ColeDepartment of Infection, Immunity and Cardiovascular Diseases, University of Sheffield, UK.ORCID https://orcid.org/0000-0002-5258-5835
Eleanor J HansonDepartment of Chemical and Biological Engineering, University of Sheffield, UK.
David C JamesDepartment of Chemical and Biological Engineering, University of Sheffield, UK.
David H DockrellDepartment of Infection, Immunity and Cardiovascular Diseases, University of Sheffield, UK.
Mark J DickmanDepartment of Chemical and Biological Engineering, University of Sheffield, UK.ORCID https://orcid.org/0000-0002-9236-0788
University of Sheffield · GBInstitute of Infection and Immunity · CA

Funding

Biotechnology and Biological Sciences Research Council BB/M012166/1Biotechnology and Biological Sciences Research Council UK BB/J014443/1Biotechnology and Biological Sciences Research Council UK BB/M012166/1Medical Research Council MR/N02995X/1Wellcome Trust 104437/Z/14/Z
6 · The paper itself

Abstract

rationaleHistone post-translational modifications (PTMs) play key roles in regulating eukaryotic gene expression. Mass spectrometry (MS) has emerged as a powerful method to characterize and quantify histone PTMs as it allows unbiased identification and quantification of multiple histone PTMs including combinations of the modifications present.

methodsIn this study we compared a range of data-acquisition methods for the identification and quantification of the histone PTMs using a Q Exactive HF Orbitrap. We compared three different data-dependent analysis (DDA) methods with MS2 resolutions of 120K, 60K, 30K. We also compared a range of data-independent analysis (DIA) methods using MS2 isolation windows of 20 m/z and DIAvw to identify and quantify histone PTMs in Chinese hamster ovary (CHO) cells.

resultsThe increased number of MS2 scans afforded by the lower resolution methods resulted in a higher number of queries, peptide sequence matches (PSMs) and a higher number of peptide proteoforms identified with a Mascot Ion score greater than 46. No difference in the proportion of peptide proteoforms with Delta scores >17 was observed. Lower coefficients of variation (CVs) were obtained in the DIA MS1 60 K MS2 30 K 20 m/z isolation windows compared with the other data-acquisition methods.

conclusionsWe observed that DIA which offers advantages in flexibility and identification of isobaric peptide proteoforms performs as well as DDA in the analysis of histone PTMs. We were able to identify 71 modified histone peptides for histone H3 and H4 and quantified 64 across each of the different acquisition methods.

Indexed as

AnimalsCHO CellsCricetinaeCricetulusHistonesHumansMass SpectrometryMolecular WeightPeptidesProtein Processing, Post-TranslationalHistonesPeptides

Identifiers

PMID30701600
PMCPMC6519233
OpenAlexW2912046117

What OpenQuestion holds

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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.