Evidence map›Paper›PMID 26010583›Full record

ArticleProteomics2015

Pitfalls in histone propionylation during bottom-up mass spectrometry analysis.

Paulien Meert, Elisabeth Govaert, Ellen Scheerlinck, Maarten Dhaenens, Dieter Deforce

Abstract read
In one paragraph

Article in Proteomics, 2015. 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
–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

23 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Paulien MeertLaboratory of Pharmaceutical Biotechnology, Ghent University, Belgium.
Elisabeth GovaertLaboratory of Pharmaceutical Biotechnology, Ghent University, Belgium.
Ellen ScheerlinckLaboratory of Pharmaceutical Biotechnology, Ghent University, Belgium.
Maarten DhaenensLaboratory of Pharmaceutical Biotechnology, Ghent University, Belgium.
Dieter DeforceLaboratory of Pharmaceutical Biotechnology, Ghent University, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite their important role in regulating gene expression, posttranslational histone modifications remain technically challenging to analyze. For identification by bottom-up MS, propionylation is required prior to and following trypsin digestion. Hereby, more hydrophobic peptides are generated enabling RP HPLC separation. When histone dynamics are studied in a quantitative manner, specificity, and efficiency of this chemical derivatization are crucial. Therefore we examined eight different protocols, including two different propionylation reagents. This revealed amidation (up to 70%) and methylation (up to 9%) of carboxyl groups as a side reaction. Moreover, incomplete (up to 85%) as well as a specific propionylation (up to 63%) can occur, depending on the protocol. These results highlight the possible pitfalls and implications for data analysis when doing bottom-up MS on histones.

Indexed as

Amino Acid SequenceAnimalsCattleHistonesHydrophobic and Hydrophilic InteractionsMass SpectrometryMethylationMolecular Sequence DataPropionatesProteomicsTandem Mass SpectrometryHistonesPropionatesCell biologyHistoneMethod optimizationMS-LC-MSPropionylation

Identifiers

PMID26010583
PMCPMC5032999

What OpenQuestion holds

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Registered trials

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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.