Evidence map›Paper›PMID 28193767›Full record

ReviewCold Spring Harbor perspectives in medicine2017

The Role of Nuclear Receptor-Binding SET Domain Family Histone Lysine Methyltransferases in Cancer.

Richard L Bennett, Alok Swaroop, Catalina Troche, Jonathan D Licht

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in medicine, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 115 papers.

0numbers the graph read from it
0cells of the map it votes in
115citing papers in PubMed
–field-weighted citation impact
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

115 citing papers in PubMed, 215 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Many faces of mammalian NSD methyltransferases.Cellular & molecular biology letters · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains.bioRxiv : the preprint server for biology · 2025
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Sotos Syndrome With NSD1 Mutations in a Chinese Cohort: Identification of Two Novel Mutations and Literature Review.International journal of developmental neuroscience : the official journal of the International Society for Developmental Neuroscience · 2025
    Review

55 more citing papers are in PubMed but not listed here.

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.

Richard L BennettDepartments of Medicine, Biochemistry and Molecular Biology and University of Florida Health Cancer Center, The University of Florida, Gainesville, Florida 32610.
Alok SwaroopDepartments of Medicine, Biochemistry and Molecular Biology and University of Florida Health Cancer Center, The University of Florida, Gainesville, Florida 32610.
Catalina TrocheDepartments of Medicine, Biochemistry and Molecular Biology and University of Florida Health Cancer Center, The University of Florida, Gainesville, Florida 32610.
Jonathan D LichtDepartments of Medicine, Biochemistry and Molecular Biology and University of Florida Health Cancer Center, The University of Florida, Gainesville, Florida 32610.
UF Health Cancer Center

Funding

Trageting the Multiple Myeloma EpigenomeP50CA100707 · NCI · DANA-FARBER CANCER INSTITUTE · PI ANDERSON, KENNETH C. · 2003 to 2023
$45.0M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM008152 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ARDEHALI, HOSSEIN · 1987 to 2021
$24.0M
CARCINOGENESIS TRAINING PROGRAMT32CA009560 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1986 to 2026
$8.4M
The Role of MMSET in the Pathogenesis and Progression of Lymphoid MalignancyR01CA195732 · NCI · UNIVERSITY OF FLORIDA · PI LICHT, JONATHAN D. · 2016 to 2020
$1.8M
Chromatin dysregulation generated by recurrent point mutation in histone methyltransferase, MMSET, drives progression of lymphoid malignanciesF30CA203292 · NCI · UNIVERSITY OF FLORIDA · PI SWAROOP, ALOK · 2016 to 2018
$124k
NCI NIH HHS F30 CA203292NCI NIH HHS P50 CA100707NCI NIH HHS R01 CA195732NCI NIH HHS T32 CA009560NIGMS NIH HHS T32 GM008152
6 · The paper itself

Abstract

The nuclear receptor-binding SET Domain (NSD) family of histone H3 lysine 36 methyltransferases is comprised of NSD1, NSD2 (MMSET/WHSC1), and NSD3 (WHSC1L1). These enzymes recognize and catalyze methylation of histone lysine marks to regulate chromatin integrity and gene expression. The growing number of reports demonstrating that alterations or translocations of these genes fundamentally affect cell growth and differentiation leading to developmental defects illustrates the importance of this family. In addition, overexpression, gain of function somatic mutations, and translocations of NSDs are associated with human cancer and can trigger cellular transformation in model systems. Here we review the functions of NSD family members and the accumulating evidence that these proteins play key roles in tumorigenesis. Because epigenetic therapy is an important emerging anticancer strategy, understanding the function of NSD family members may lead to the development of novel therapies.

Indexed as

AnimalsCell Transformation, NeoplasticGene ExpressionHistone-Lysine N-MethyltransferaseHistonesHumansMiceMutationNeoplasmsProtein Processing, Post-TranslationalPR-SET DomainsReceptors, Cytoplasmic and NuclearRepressor ProteinsHistone-Lysine N-MethyltransferaseHistonesNSD2 protein, humanReceptors, Cytoplasmic and NuclearRepressor Proteins

Identifiers

PMID28193767
PMCPMC5453381
OpenAlexW2587889130

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.