Evidence map›Paper›PMID 37832177›Full record

ReviewCurrent opinion in structural biology2023

Recent developments in catalysis and inhibition of the Jumonji histone demethylases.

Letitia Sarah, Danica Galonić Fujimori

Open access · hybridAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-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

10 citing papers in PubMed, 7 citations in OpenAlex.

  1. Iron dysregulation in the central nervous system: implications for autism spectrum disorder.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
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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

2 authors at 2 institutions in 1 country.

Letitia SarahChemistry and Chemical Biology Graduate Program, University of California San Francisco; San Francisco, CA 94158, USA; Department of Cellular and Molecular Pharmacology, University of California San Francisco; San Francisco, CA 94158, USA.
Danica Galonić FujimoriDepartment of Cellular and Molecular Pharmacology, University of California San Francisco; San Francisco, CA 94158, USA; Department of Pharmaceutical Chemistry, University of California San Francisco; San Francisco, CA 94158, USA; Quantitative Biosciences Institute (QBI), University of California San Francisco; San Francisco, CA 94158, USA. Electronic address: danica.fujimori@ucsf.edu.
QB3 · USUniversity of California, San Francisco · US

Funding

Research Training in Chemistry and Chemical BiologyT32GM145460 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jason E Gestwicki · 2022 to 2026
$3.1M
Discovery of Small Molecule Ligands for PHD1 Reader Domain of Histone Demethylase KDM5AR01CA250459 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ARKIN, MICHELLE, FUJIMORI, DANICA GALONIC · 2020 to 2023
$2.3M
NCI NIH HHS R01 CA250459NIGMS NIH HHS T32 GM145460
6 · The paper itself

Abstract

Histone methylation, one of the most common histone modifications, has fundamental roles in regulating chromatin-based processes. Jumonji histone lysine demethylases (JMJC KDMs) influence regulation of gene transcription through both their demethylation and chromatin scaffolding functions. It has recently been demonstrated that dysregulation of JMJC KDMs contributes to pathogenesis and progression of several diseases, including cancer. These observations have led to an increased interest in modulation of enzymes that regulate lysine methylation. Here, we highlight recent progress in understanding catalysis of JMJC KDMs. Specifically, we focus on recent research advances on elucidation of JMJC KDM substrate recognition and interactomes. We also highlight recently reported JMJC KDM inhibitors and describe their therapeutic potentials and challenges. Finally, we discuss alternative strategies to target these enzymes, which rely on targeting JMJC KDMs accessory domains as well as utilization of the targeted protein degradation strategy.

Indexed as

Histone DemethylasesHistonesCatalysisChromatinJumonji Domain-Containing Histone DemethylasesChromatinHistone DemethylasesHistonesJumonji Domain-Containing Histone DemethylasesAllosteric inhibitorsCatalysisDomain crosstalkJumonji histone demethylasesLysine demethylationOrthosteric inhibitorsPost-translational modifications

Identifiers

PMID37832177
PMCPMC10769511
OpenAlexW4387552205

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.