Evidence map›Paper›PMID 27139031›Full record

ArticleProteomics2016

Tackling aspecific side reactions during histone propionylation: The promise of reversing overpropionylation.

Paulien Meert, Sebastiaan Dierickx, Elisabeth Govaert, Laura De Clerck, Sander Willems, Maarten Dhaenens, Dieter Deforce

Open access · hybridAbstract read
In one paragraph

Article in Proteomics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  17. Conserved Residues LysFrontiers in molecular biosciences · 2018
    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

7 authors at 1 institution in 1 country.

Paulien MeertLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Sebastiaan DierickxLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Elisabeth GovaertLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Laura De ClerckLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Sander WillemsLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Maarten DhaenensLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Dieter DeforceLaboratory of Pharmaceutical Biotechnology, Ghent University, Ghent, Belgium.
Ghent University · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone proteins are essential elements for DNA packaging. Moreover, the PTMs that are extremely abundant on these proteins, contribute in modeling chromatin structure and recruiting enzymes involved in gene regulation, DNA repair and chromosome condensation. This fundamental aspect, together with the epigenetic inheritance of histone PTMs, underlines the importance of having biochemical techniques for their characterization. Over the past two decades, significant improvements in mass accuracy and resolution of mass spectrometers have made LC-coupled MS the strategy of choice for accurate identification and quantification of protein PTMs. Nevertheless, in previous work we disclosed the limitations and biases of the most widely adopted sample preparation protocols for histone propionylation, required prior to bottom-up MS analysis. In this work, however, we put forward a new specific and efficient propionylation strategy by means of propionic anhydride. In this method, aspecific overpropionylation at serine (S), threonine (T) and tyrosine (Y) is reversed by adding hydroxylamine (HA). We recommend using this method for future analysis of histones through bottom-up MS.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAmmonium HydroxideAnhydridesArginineArtifactsHistone CodeHistonesHumansHydrogen-Ion ConcentrationHydroxylamineLysineMass SpectrometryPeptide FragmentsPeptide MappingPropionatesAmmonium HydroxideAnhydridesArginineHistonesHydroxylamineLysinePeptide FragmentsPropionatespropionic anhydrideSolventsTrypsinHistoneMass spectrometryMethod optimizationPropionylationTechnology

Identifiers

PMID27139031
PMCPMC5096241
OpenAlexW2346528954

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.