Evidence map›Paper›PMID 32604817›Full record

ReviewBiology2020

Mass Spectrometry to Study Chromatin Compaction.

Stephanie Stransky, Jennifer Aguilan, Jake Lachowicz, Carlos Madrid-Aliste, Edward Nieves, Simone Sidoli

Open access · goldAbstract readReview
In one paragraph

Review in Biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
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

6 authors at 1 institution in 1 country.

Stephanie StranskyDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Jennifer AguilanDepartment of Pathology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Jake LachowiczDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Carlos Madrid-AlisteDepartment of System & Computational Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Edward NievesDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Simone SidoliDepartment of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Albert Einstein College of Medicine · US

Funding

Japan Agency for Medical Research and Development Interstellar InitiativeNew York Academy of Sciences Interstellar Initiative
6 · The paper itself

Abstract

Chromatin accessibility is a major regulator of gene expression. Histone writers/erasers have a critical role in chromatin compaction, as they "flag" chromatin regions by catalyzing/removing covalent post-translational modifications on histone proteins. Anomalous chromatin decondensation is a common phenomenon in cells experiencing aging and viral infection. Moreover, about 50% of cancers have mutations in enzymes regulating chromatin state. Numerous genomics methods have evolved to characterize chromatin state, but the analysis of (in)accessible chromatin from the protein perspective is not yet in the spotlight. We present an overview of the most used approaches to generate data on chromatin accessibility and then focus on emerging methods that utilize mass spectrometry to quantify the accessibility of histones and the rest of the chromatin bound proteome. Mass spectrometry is currently the method of choice to quantify entire proteomes in an unbiased large-scale manner; accessibility on chromatin of proteins and protein modifications adds an extra quantitative layer to proteomics dataset that assist more informed data-driven hypotheses in chromatin biology. We speculate that this emerging new set of methods will enhance predictive strength on which proteins and histone modifications are critical in gene regulation, and which proteins occupy different chromatin states in health and disease.

Indexed as

chromatinDNA methylationhistonemass spectrometrypost-translational modificationproteome

Identifiers

PMID32604817
PMCPMC7345930
OpenAlexW3037308627

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.