Evidence map›Paper›PMID 33852996›Full record

ReviewCurrent opinion in chemical biology2021

Improved methods for targeting epigenetic reader domains of acetylated and methylated lysine.

Isabelle A Engelberg, Caroline A Foley, Lindsey I James, Stephen V Frye

Open access · bronzeAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  11. Small-molecule tools for YEATS domain proteins.Current opinion in chemical biology · 2023
    Review
  12. Article
  13. 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

4 authors at 1 institution in 1 country.

Isabelle A EngelbergCenter for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States.
Caroline A FoleyCenter for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States.
Lindsey I JamesCenter for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States.
Stephen V FryeCenter for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, United States. Electronic address: svfrye@email.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

DISCOVERY OF CHEMICAL PROBES FOR METHYL-LYSINE READERSR01GM100919 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FRYE, STEPHEN VERNON · 2012 to 2019
$2.9M
POLYCOMB REPRESSIVE COMLEXE AS KEY REGULATORS OF HIV LATENCY AND TARGETS FOR LATENCY REVERSALR61DA047023 · NIDA · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JAMES, LINDSEY INGERMAN · 2018 to 2020
$2.7M
DISCOVERY OF FIRST-IN-CLASS NSD2 DEGRADERS FOR CANCER THERAPYR01CA242305 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JAMES, LINDSEY INGERMAN · 2019 to 2024
$1.7M
DISCOVERY OF IN VIVO CHEMICAL PROBES FOR POLYCOMB CBX DOMAINSR01CA218392 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI FRYE, STEPHEN VERNON · 2018 to 2020
$1.5M
NCI NIH HHS R01 CA218392NCI NIH HHS R01 CA242305NIDA NIH HHS R61 DA047023NIGMS NIH HHS R01 GM100919
6 · The paper itself

Abstract

Responsible for interpreting histone post-translational modifications, epigenetic reader proteins have emerged as novel therapeutic targets for a wide range of diseases. Chemical probes have been critical in enabling target validation studies and have led to translational advances in cancer and inflammation-related pathologies. Here, we present the most recently reported probes of reader proteins that recognize acylated and methylated lysine. We will discuss challenges associated with achieving potent antagonism of reader domains and review ongoing efforts to overcome these hurdles, focusing on targeting strategies including the use of peptidomimetic ligands, allosteric modulators, and protein degraders.

Indexed as

AcetylationAllosteric RegulationAllosteric SiteEpigenesis, GeneticHistonesHumansLigandsLysineMethylationPeptidomimeticsProtein BindingProtein ConformationProtein Processing, Post-TranslationalStructure-Activity RelationshipHistonesLigandsLysinePeptidomimeticsAcylated and methylated lysineAllosteric modulatorsBromodomainsChemical probesChromatin regulatory factorsEpigenetic reader proteinsHistone post-translational modificationsPeptidomimetic ligandsProtein degradersSmall-molecule antagonists

Identifiers

PMID33852996
PMCPMC8384657
OpenAlexW3153897206

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.