Evidence map›Paper›PMID 27151432›Full record

ReviewCurrent opinion in genetics & development2016

Histone demethylases in physiology and cancer: a tale of two enzymes, JMJD3 and UTX.

Kelly Marie Arcipowski, Carlos Alberto Martinez, Panagiotis Ntziachristos

Abstract readReview
In one paragraph

Review in Current opinion in genetics & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 94 citations in OpenAlex.

  1. Review
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  17. H3K27me3 Demethylase UTX Restrains Plasma Cell Formation.Journal of immunology (Baltimore, Md. : 1950) · 2022
    Article
  18. Review
  19. 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

3 authors at 1 institution in 1 country.

Kelly Marie ArcipowskiDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, 320 E. Superior Street, Chicago, IL 60611, USA.
Carlos Alberto MartinezDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, 320 E. Superior Street, Chicago, IL 60611, USA.
Panagiotis NtziachristosDepartment of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, 320 E. Superior Street, Chicago, IL 60611, USA; Robert H. Lurie Comprehensive Cancer Center, Northwestern University Feinberg School of Medicine, 320 E. Superior Street, Chicago, IL 60611, USA. Electronic address: panos.ntz@northwestern.edu.
Northwestern University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Daniela E Matei · 1993 to 2026
$153.9M
TRAINING PROGRAM IN ONCOGENESIS &DEVELOPMENT BIOLOGYT32CA080621 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI EKLUND, ELIZABETH ANN · 2001 to 2018
$4.1M
Exploring a new therapeutic approach through targeting epigenetic enzymes in ALLR00CA188293 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI NTZIACHRISTOS, PANAGIOTIS · 2015 to 2017
$747k
NCI NIH HHS P30 CA060553NCI NIH HHS R00 CA188293NCI NIH HHS T32 CA080621
6 · The paper itself

Abstract

Gene regulation is fine-tuned by a dynamic balance between transcriptionally activating and repressive modifications of histone tails. It has been well-established that lysine and arginine methylation can be reversed by two groups of evolutionarily conserved enzymes known as histone demethylases, which have been shown to play critical roles in development, differentiation and diseases like cancer. Recent work has demonstrated demethylase-independent functions of these proteins, highlighting the complex mechanisms by which these proteins exert their effects on gene expression. Here, we discuss the roles of lysine 27 demethylases, JMJD3 and UTX, in cancer and potential therapeutic avenues targeting these enzymes. Despite a high degree of sequence similarity in the catalytic domain between JMJD3 and UTX, numerous studies revealed surprisingly contrasting roles in cellular reprogramming and cancer, particularly leukemia. Understanding the demethylase-dependent and demethylase-independent functions of the enzymes affecting histone methylation, their post-translational modifications and participation in different complexes, as well as in vivo modeling of the mutations affecting those enzymes in cancer, can shed light on their unique physiological roles. This information cumulated in the future will aid in the development of improved inhibitors to treat cancers affected by demethylase mutations and aberrant gene activation.

Indexed as

Cell DifferentiationCellular ReprogrammingGene Expression Regulation, NeoplasticHistone DemethylasesHistonesHumansJumonji Domain-Containing Histone DemethylasesMolecular Targeted TherapyNeoplasmsNuclear ProteinsHistone DemethylasesHistonesJumonji Domain-Containing Histone DemethylasesKDM6A protein, humanKDM6B protein, humanNuclear Proteins

Identifiers

PMID27151432
PMCPMC4880520
OpenAlexW2346893706

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.