Evidence map›Paper›PMID 25325711›Full record

ArticleJournal of proteome research2014

High resolution is not a strict requirement for characterization and quantification of histone post-translational modifications.

Kelly R Karch, Barry M Zee, Benjamin A Garcia

Abstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. 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

3 authors.

Kelly R KarchEpigenetics Program, Department of Biochemistry and Biophysics, Smilow Center for Translational Research, Perelman School of Medicine, University of Pennsylvania , 3400 Civic Center Boulevard, Building 421, Philadelphia, Pennsylvania 19104-5157, United States.
Barry M Zee
Benjamin A Garcia

Funding

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
NIGMS NIH HHS R01 GM110174NIGMS NIH HHS R01GM110174NIGMS NIH HHS T32 GM071339NIH HHS DP2 OD007447NIH HHS DP2OD007447
6 · The paper itself

Abstract

Mass spectrometry (MS) is a powerful tool to accurately identify and quantify histone post-translational modifications (PTMs). High-resolution mass analyzers have been regarded as essential for these PTM analyses because the mass accuracy afforded is sufficient to differentiate trimethylation versus acetylation (42.0470 and 42.0106 Da, respectively), whereas lower-resolution mass analyzers cannot. Noting this limitation, we sought to determine whether lower-resolution detectors are nonetheless adequate for histone PTM analysis by comparing the low-resolution LTQ Velos Pro with the high-resolution LTQ-Orbitrap Velos Pro. We first determined that the optimal scan mode on the LTQ Velos Pro is the Enhanced scan mode with respect to apparent resolution, number of MS and MS/MS scans per run, and reproducibility of label-free quantifications. We next compared the performance of the LTQ Velos Pro to the LTQ-Orbitrap Velos Pro using the same criteria for comparison, and we found that the main difference is that the LTQ-Orbitrap Velos Pro is able to resolve the difference between acetylation and trimethylation while the LTQ Velos Pro cannot. However, using heavy isotope labeled synthetic peptide standards and retention time information enables confident assignment of these modifications and comparable quantification between the instruments. Therefore, lower-resolution instruments can confidently be utilized for histone PTM analysis.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceChromatography, LiquidHeLa CellsHistonesHumansLysineMass SpectrometryMethylationPeptidesProteomicsReproducibility of ResultsTandem Mass SpectrometryHistonesLysinePeptideschromatinepigeneticshistonemass spectrometrymodificationproteomicsPTMquantificationstable isotope

Identifiers

PMID25325711
PMCPMC4261946

What OpenQuestion holds

Textmetadata
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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.