Chemical probes for histone-modifying enzymes

Philip A. Cole

Research output: Contribution to journalArticle

Abstract

The histone-modifying enzymes that catalyze reversible lysine acetylation and methylation are central to the epigenetic regulation of chromatin remodeling. From the early discovery of histone deacetylase inhibitors to the more recent identification of histone demethylase blockers, chemical approaches offer increasingly sophisticated tools for the investigation of the structure and function of these lysine-modifying enzymes. This review summarizes progress to date on compounds identified from screens or by design that can modulate the activity of classical histone deacetylases, sirtuins, histone acetyltransferases, histone methyltransferases and histone demethylases. We highlight applications of compounds to mechanistic and functional studies involving these enzymes and discuss future challenges regarding target specificity and general utility.

Original languageEnglish (US)
Pages (from-to)590-597
Number of pages8
JournalNature Chemical Biology
Volume4
Issue number10
DOIs
StatePublished - Oct 2008

Fingerprint

Histone Demethylases
Histones
Lysine
Enzymes
Sirtuins
Histone Acetyltransferases
Histone Deacetylase Inhibitors
Histone Deacetylases
Chromatin Assembly and Disassembly
Acetylation
Epigenomics
Methylation

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Chemical probes for histone-modifying enzymes. / Cole, Philip A.

In: Nature Chemical Biology, Vol. 4, No. 10, 10.2008, p. 590-597.

Research output: Contribution to journalArticle

Cole, Philip A. / Chemical probes for histone-modifying enzymes. In: Nature Chemical Biology. 2008 ; Vol. 4, No. 10. pp. 590-597.
@article{c30e8b803b584c14aaf0b5224359dac4,
title = "Chemical probes for histone-modifying enzymes",
abstract = "The histone-modifying enzymes that catalyze reversible lysine acetylation and methylation are central to the epigenetic regulation of chromatin remodeling. From the early discovery of histone deacetylase inhibitors to the more recent identification of histone demethylase blockers, chemical approaches offer increasingly sophisticated tools for the investigation of the structure and function of these lysine-modifying enzymes. This review summarizes progress to date on compounds identified from screens or by design that can modulate the activity of classical histone deacetylases, sirtuins, histone acetyltransferases, histone methyltransferases and histone demethylases. We highlight applications of compounds to mechanistic and functional studies involving these enzymes and discuss future challenges regarding target specificity and general utility.",
author = "Cole, {Philip A.}",
year = "2008",
month = "10",
doi = "10.1038/nchembio.111",
language = "English (US)",
volume = "4",
pages = "590--597",
journal = "Nature Chemical Biology",
issn = "1552-4450",
publisher = "Nature Publishing Group",
number = "10",

}

TY - JOUR

T1 - Chemical probes for histone-modifying enzymes

AU - Cole, Philip A.

PY - 2008/10

Y1 - 2008/10

N2 - The histone-modifying enzymes that catalyze reversible lysine acetylation and methylation are central to the epigenetic regulation of chromatin remodeling. From the early discovery of histone deacetylase inhibitors to the more recent identification of histone demethylase blockers, chemical approaches offer increasingly sophisticated tools for the investigation of the structure and function of these lysine-modifying enzymes. This review summarizes progress to date on compounds identified from screens or by design that can modulate the activity of classical histone deacetylases, sirtuins, histone acetyltransferases, histone methyltransferases and histone demethylases. We highlight applications of compounds to mechanistic and functional studies involving these enzymes and discuss future challenges regarding target specificity and general utility.

AB - The histone-modifying enzymes that catalyze reversible lysine acetylation and methylation are central to the epigenetic regulation of chromatin remodeling. From the early discovery of histone deacetylase inhibitors to the more recent identification of histone demethylase blockers, chemical approaches offer increasingly sophisticated tools for the investigation of the structure and function of these lysine-modifying enzymes. This review summarizes progress to date on compounds identified from screens or by design that can modulate the activity of classical histone deacetylases, sirtuins, histone acetyltransferases, histone methyltransferases and histone demethylases. We highlight applications of compounds to mechanistic and functional studies involving these enzymes and discuss future challenges regarding target specificity and general utility.

UR - http://www.scopus.com/inward/record.url?scp=51949111451&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=51949111451&partnerID=8YFLogxK

U2 - 10.1038/nchembio.111

DO - 10.1038/nchembio.111

M3 - Article

C2 - 18800048

AN - SCOPUS:51949111451

VL - 4

SP - 590

EP - 597

JO - Nature Chemical Biology

JF - Nature Chemical Biology

SN - 1552-4450

IS - 10

ER -