Evidence map›Paper›PMID 26726824›Full record

ArticleACS chemical biology2016

Regulation of Methyllysine Readers through Phosphorylation.

Forest H Andrews, Jovylyn Gatchalian, Krzysztof Krajewski, Brian D Strahl, Tatiana G Kutateladze

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

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  12. Epigenetic mechanisms and implications in tendon inflammation (Review).International journal of molecular medicine · 2019
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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

5 authors at 2 institutions in 1 country.

Forest H AndrewsDepartment of Pharmacology, University of Colorado School of Medicine , Aurora, Colorado 80045, United States.
Jovylyn GatchalianDepartment of Pharmacology, University of Colorado School of Medicine , Aurora, Colorado 80045, United States.
Krzysztof KrajewskiDepartment of Biochemistry & Biophysics, The University of North Carolina School of Medicine , Chapel Hill, North Carolina 27599, United States.
Brian D StrahlDepartment of Biochemistry & Biophysics, The University of North Carolina School of Medicine , Chapel Hill, North Carolina 27599, United States.
Tatiana G KutateladzeDepartment of Pharmacology, University of Colorado School of Medicine , Aurora, Colorado 80045, United States.
University of Colorado Denver · USUniversity of North Carolina at Chapel Hill · US

Funding

BEHAVIORAL PHARMACOGENETICS OF DRUG AND ALCOHOL ABUSET32AA007464 · NIAAA · UNIVERSITY OF COLORADO DENVER · PI HOFFMAN, PAULA · 1987 to 2017
$4.8M
Epigenetic regulation by PHF1R01GM106416 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2015 to 2018
$1.5M
Molecular mechanism of chromatin targeting by BRPF1R01GM100907 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI KUTATELADZE, TATIANA G · 2015 to 2018
$1.4M
Factors that regulate chromatin organization and gene transcriptionR01GM110058 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI STRAHL, BRIAN D · 2014 to 2017
$1.2M
Role of Polycomblike1-histone interaction in PRC2 activitiesF31CA189487 · NCI · UNIVERSITY OF COLORADO DENVER · PI GATCHALIAN, JOVYLYN · 2014 to 2016
$70k
NCI NIH HHS F31 CA189487NIAAA NIH HHS T32 AA007464NIAAA NIH HHS T32AA007464NIGMS NIH HHS GM100907NIGMS NIH HHS R01 GM100907NIGMS NIH HHS R01 GM106416NIGMS NIH HHS R01 GM110058
6 · The paper itself

Abstract

Methyllysine post-translational modifications (PTMs) of histones create binding sites for evolutionarily conserved reader domains that link nuclear host proteins and chromatin-modifying complexes to specific genomic regions. In the context of these events, adjacent histone PTMs are capable of altering the binding activity of readers toward their target marks. This provides a mechanism of "combinatorial readout" of PTMs that can enhance, decrease, or eliminate the association of readers with chromatin. In this Perspective, we focus on recent studies describing the impact of dynamic phospho-serine/threonine/tyrosine marks on the interaction of methyllysine readers with histones, summarize mechanistic aspects of the phospho/methyl readout, and highlight the significance of crosstalk between these PTMs. We also demonstrate that in addition to inhibiting binding and serving as a true switch, promoting dissociation of the methyllysine readers from chromatin, the phospho/methyl combination can act together in a cooperative manner--thus adding a new layer of regulatory information that can be encoded in these dual histone PTMs.

Indexed as

Epigenesis, GeneticBinding SitesChromatinHistonesHumansLysineMethylationModels, MolecularNuclear ProteinsPhosphorylationProtein BindingProtein ConformationProtein Processing, Post-TranslationalChromatinHistonesLysineNuclear Proteins

Identifiers

PMID26726824
PMCPMC4861070
OpenAlexW2225265012

What OpenQuestion holds

Textmetadata
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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.