Evidence map›Paper›PMID 34709376›Full record

ReviewBiochemical Society transactions2021

Chemical biology approaches to study histone interactors.

Antony J Burton, Ghaith M Hamza, Andrew X Zhang, Tom W Muir

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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

4 authors at 3 institutions in 3 countries.

Antony J BurtonDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, U.S.A.ORCID 0000-0002-2340-3262
Ghaith M HamzaDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, U.S.A.
Andrew X ZhangDiscovery Biology, Discovery Sciences, R&D, AstraZeneca, Boston, MA 02451, U.S.A.
Tom W MuirFrick Chemistry Laboratory, Princeton, NJ 08544, U.S.A.
AstraZeneca (Japan) · JPPrinceton University · USUniversity of New Hampshire · US

Funding

Structure, Function and Applications of InteinsR37GM086868 · NIGMS · PRINCETON UNIVERSITY · PI MUIR, TOM · 2012 to 2021
$5.4M
NIGMS NIH HHS R37 GM086868
6 · The paper itself

Abstract

Protein-protein interactions (PPIs) in the nucleus play key roles in transcriptional regulation and ensure genomic stability. Critical to this are histone-mediated PPI networks, which are further fine-tuned through dynamic post-translational modification. Perturbation to these networks leads to genomic instability and disease, presenting epigenetic proteins as key therapeutic targets. This mini-review will describe progress in mapping the combinatorial histone PTM landscape, and recent chemical biology approaches to map histone interactors. Recent advances in mapping direct interactors of histone PTMs as well as local chromatin interactomes will be highlighted, with a focus on mass-spectrometry based workflows that continue to illuminate histone-mediated PPIs in unprecedented detail.

Indexed as

Crystallography, X-RayHistonesMass SpectrometryProtein BindingProtein Processing, Post-TranslationalHistoneschemical biologychromatinepigeneticsmass spectrometrypost translational modificationprotein–protein interactions

Identifiers

PMID34709376
PMCPMC9785950
OpenAlexW3209453414

What OpenQuestion holds

Textmetadata
LicenceTDM
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.