Evidence map›Paper›PMID 25641854›Full record

ArticleProteomics2015

Drawbacks in the use of unconventional hydrophobic anhydrides for histone derivatization in bottom-up proteomics PTM analysis.

Simone Sidoli, Zuo-Fei Yuan, Shu Lin, Kelly Karch, Xiaoshi Wang, Natarajan Bhanu, Anna M Arnaudo, Laura-Mae Britton, Xing-Jun Cao, Michelle Gonzales-Cope and 6 more

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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Enhanced plant bottom-up histone proteomics.Journal of experimental botany · 2026
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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

16 authors at 1 institution in 1 country.

Simone SidoliDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, USA.
Zuo-Fei Yuan
Shu Lin
Kelly Karch
Xiaoshi Wang
Natarajan Bhanu
Anna M Arnaudo
Laura-Mae Britton
Xing-Jun Cao
Michelle Gonzales-Cope
Yumiao Han
Shichong Liu
Rosalynn C Molden
Samuel Wein
Leila Afjehi-Sadat
Benjamin A Garcia
University of Pennsylvania · US

Funding

Viral modulation of epitranscriptomic mechanismsR01AI118891 · NIAID · WASHINGTON UNIVERSITY · PI GARCIA, BENJAMIN A, WEITZMAN, MATTHEW D. · 2015 to 2025
$5.4M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM071339 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN, SPEICHER, DAVID W. · 2005 to 2019
$3.2M
Novel Methodology for Quantitative High-throughput Cancer EpigeneticsDP2OD007447 · OD · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2010 to 2010
$2.4M
Understanding the Role of Combinatorial Histone PTM PatternsR01GM110174 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GARCIA, BENJAMIN A · 2014 to 2017
$1.3M
NIAID NIH HHS R01 AI118891NIGMS NIH HHS R01GM11017NIGMS NIH HHS R01 GM110174NIGMS NIH HHS T32 GM071339NIH HHS DP2 OD007447NIH HHS DP2OD007447
6 · The paper itself

Abstract

MS-based proteomics has become the most utilized tool to characterize histone PTMs. Since histones are highly enriched in lysine and arginine residues, lysine derivatization has been developed to prevent the generation of short peptides (<6 residues) during trypsin digestion. One of the most adopted protocols applies propionic anhydride for derivatization. However, the propionyl group is not sufficiently hydrophobic to fully retain the shortest histone peptides in RP LC, and such procedure also hampers the discovery of natural propionylation events. In this work we tested 12 commercially available anhydrides, selected based on their safety and hydrophobicity. Performance was evaluated in terms of yield of the reaction, MS/MS fragmentation efficiency, and drift in retention time using the following samples: (i) a synthetic unmodified histone H3 tail, (ii) synthetic modified histone peptides, and (iii) a histone extract from cell lysate. Results highlighted that seven of the selected anhydrides increased peptide retention time as compared to propionic, and several anhydrides such as benzoic and valeric led to high MS/MS spectra quality. However, propionic anhydride derivatization still resulted, in our opinion, as the best protocol to achieve high MS sensitivity and even ionization efficiency among the analyzed peptides.

Indexed as

Amino Acid SequenceAnhydridesChromatography, High Pressure LiquidHeLa CellsHistonesHumansHydrophobic and Hydrophilic InteractionsMolecular Sequence DataPeptidesProteomicsTandem Mass SpectrometryAnhydridesHistonesPeptidesAnhydrideBottom-up proteomicsHistonesMass spectrometryProtein derivatizationTechnology

Identifiers

PMID25641854
PMCPMC4441824
OpenAlexW2090924257

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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.