Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer

Sharad Verma, Steven D. Knight

Research output: Contribution to journalReview article

Abstract

The histone lysine methyltransferase EZH2 is the catalytic component of the multi-protein PRC2 complex and methylates lysine 27 on histone H3. EZH2 overexpression is implicated in tumorigenesis and correlates with poor prognosis in several tumor types. Inhibition of aberrant EZH2 activity might attenuate tumorigenesis resulting from misregulated gene transcription derived from aberrant EZH2 activity. In the last year, the first reports of small molecules demonstrating potent and selective inhibition of EZH2 have been published by multiple groups. Herein, we review recent progress reported in the discovery of small molecule inhibitors of EZH2.

Original languageEnglish (US)
Pages (from-to)1661-1670
Number of pages10
JournalFuture Medicinal Chemistry
Volume5
Issue number14
DOIs
StatePublished - Sep 2013
Externally publishedYes

Fingerprint

Histone-Lysine N-Methyltransferase
Carcinogenesis
Histones
Lysine
Neoplasms
Genes
Proteins

ASJC Scopus subject areas

  • Drug Discovery
  • Pharmacology
  • Molecular Medicine

Cite this

Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer. / Verma, Sharad; Knight, Steven D.

In: Future Medicinal Chemistry, Vol. 5, No. 14, 09.2013, p. 1661-1670.

Research output: Contribution to journalReview article

@article{6832a1653dc84073804cfb023491cb4d,
title = "Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer",
abstract = "The histone lysine methyltransferase EZH2 is the catalytic component of the multi-protein PRC2 complex and methylates lysine 27 on histone H3. EZH2 overexpression is implicated in tumorigenesis and correlates with poor prognosis in several tumor types. Inhibition of aberrant EZH2 activity might attenuate tumorigenesis resulting from misregulated gene transcription derived from aberrant EZH2 activity. In the last year, the first reports of small molecules demonstrating potent and selective inhibition of EZH2 have been published by multiple groups. Herein, we review recent progress reported in the discovery of small molecule inhibitors of EZH2.",
author = "Sharad Verma and Knight, {Steven D.}",
year = "2013",
month = "9",
doi = "10.4155/fmc.13.136",
language = "English (US)",
volume = "5",
pages = "1661--1670",
journal = "Future Medicinal Chemistry",
issn = "1756-8919",
publisher = "Future Science",
number = "14",

}

TY - JOUR

T1 - Recent progress in the discovery of small-molecule inhibitors of the HMT EZH2 for the treatment of cancer

AU - Verma, Sharad

AU - Knight, Steven D.

PY - 2013/9

Y1 - 2013/9

N2 - The histone lysine methyltransferase EZH2 is the catalytic component of the multi-protein PRC2 complex and methylates lysine 27 on histone H3. EZH2 overexpression is implicated in tumorigenesis and correlates with poor prognosis in several tumor types. Inhibition of aberrant EZH2 activity might attenuate tumorigenesis resulting from misregulated gene transcription derived from aberrant EZH2 activity. In the last year, the first reports of small molecules demonstrating potent and selective inhibition of EZH2 have been published by multiple groups. Herein, we review recent progress reported in the discovery of small molecule inhibitors of EZH2.

AB - The histone lysine methyltransferase EZH2 is the catalytic component of the multi-protein PRC2 complex and methylates lysine 27 on histone H3. EZH2 overexpression is implicated in tumorigenesis and correlates with poor prognosis in several tumor types. Inhibition of aberrant EZH2 activity might attenuate tumorigenesis resulting from misregulated gene transcription derived from aberrant EZH2 activity. In the last year, the first reports of small molecules demonstrating potent and selective inhibition of EZH2 have been published by multiple groups. Herein, we review recent progress reported in the discovery of small molecule inhibitors of EZH2.

UR - http://www.scopus.com/inward/record.url?scp=84884567164&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84884567164&partnerID=8YFLogxK

U2 - 10.4155/fmc.13.136

DO - 10.4155/fmc.13.136

M3 - Review article

C2 - 24047271

AN - SCOPUS:84884567164

VL - 5

SP - 1661

EP - 1670

JO - Future Medicinal Chemistry

JF - Future Medicinal Chemistry

SN - 1756-8919

IS - 14

ER -