LSD1 and the chemistry of histone demethylation

Jeffrey C. Culhane; Philip A. Cole

doi:10.1016/j.cbpa.2007.07.014

LSD1 and the chemistry of histone demethylation

Jeffrey C. Culhane, Philip A. Cole

School of Medicine

Research output: Contribution to journal › Review article

Abstract

The recent discovery that histone demethylation can be catalyzed by the flavin-dependent amine oxidase LSD1 has ushered in a new chapter in the chromatin-remodeling community. Herein, we discuss the rapid progress of the histone demethylase field including the recent identification of the non-heme iron-dependent histone demethylases (JmjC family), the basis for LSD1 substrate site specificity and the newly emerging potential for inhibition of these enzymes in structural and functional analysis.

Original language	English (US)
Pages (from-to)	561-568
Number of pages	8
Journal	Current Opinion in Chemical Biology
Volume	11
Issue number	5
DOIs	https://doi.org/10.1016/j.cbpa.2007.07.014
State	Published - Oct 2007

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry

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Culhane, J. C., & Cole, P. A. (2007). LSD1 and the chemistry of histone demethylation. Current Opinion in Chemical Biology, 11(5), 561-568. https://doi.org/10.1016/j.cbpa.2007.07.014

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