Evidence map›Paper›PMID 27371874›Full record

ReviewCurrent opinion in chemical biology2016

Epiproteomics: quantitative analysis of histone marks and codes by mass spectrometry.

Yupeng Zheng, Xiaoxiao Huang, Neil L Kelleher

Abstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

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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.

Yupeng ZhengDepartment of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, United States; Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, United States. Electronic address: ypzheng@gmail.com.
Xiaoxiao HuangDepartment of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, United States; Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, United States.
Neil L KelleherDepartment of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, IL 60208, United States; Department of Molecular Biosciences, Northwestern University, 2205 Tech Drive, Evanston, IL 60208, United States. Electronic address: n-kelleher@northwestern.edu.

Funding

TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
NIGMS NIH HHS P41 GM108569
6 · The paper itself

Abstract

Histones are a group of proteins with a high number of post-translational modifications, including methylation, acetylation, phosphorylation, and monoubiquitination, which play critical roles in every chromatin-templated activity. The quantitative analysis of these modifications using mass spectrometry (MS) has seen significant improvements over the last decade. It is now possible to perform large-scale surveys of dozens of histone marks and hundreds of their combinations on global chromatin. Here, we review the development of three MS strategies for analyzing histone modifications that have come to be known as Bottom Up, Middle Down, and Top Down. We also discuss challenges and innovative solutions for characterizing and quantifying complicated isobaric species arising from multiple modifications on the same histone molecule.

Indexed as

ProteomicsAmino Acid SequenceChromatography, LiquidHistonesMass SpectrometryHistones

Identifiers

PMID27371874
PMCPMC5129744

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.