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PatentDOI

Histone demethylation mediated by the nuclear amine oxidase homolog lsd1

Yang Shi, +1 more
- 16 Dec 2005 - 
- Vol. 119, Iss: 7, pp 941-953
TLDR
In this paper, the authors identify a histone demethylase conserved from S. pombe to human and reveal dynamic regulation of histone methylation by both histonemethylases and demethylases.
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This article is published in Cell.The article was published on 2005-12-16. It has received 3281 citations till now. The article focuses on the topics: Histone lysine demethylation & Histone demethylation.

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Citations
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A Role for H3K4 Monomethylation in Gene Repression and Partitioning of Chromatin Readers

TL;DR: It is found that MLL3/4 provokes monomethylation of promoter regions and the conditional repression of muscle and inflammatory response genes in myoblasts and this point to a unique role for H3K4 monometHylation in establishing boundaries that restrict the recruitment of chromatin-modifying enzymes to defined regions within promoters.
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Identification of cell-active lysine specific demethylase 1-selective inhibitors.

TL;DR: The first small-molecule LSD1-selective inhibitors are identified and show in vivo H3K4-methylating activity and antiproliferative activity and should be useful as lead structures for anticancer drugs and as tools for studying the biological roles of LSD1.
Journal ArticleDOI

The histone trimethyllysine demethylase JMJD2A promotes cardiac hypertrophy in response to hypertrophic stimuli in mice

TL;DR: The studies reveal that JMJD2A promotes cardiac hypertrophy under pathological conditions and suggest what the authors believe to be a novel mechanism for JM JD2A in reprogramming of gene expression involved in cardiachypertrophy.
Journal ArticleDOI

Methylation: lost in hydroxylation?

TL;DR: It is proposed that the fission yeast protein Epe1 is a putative histone demethylase that could act by oxidative demethylation, and certain other chromatin‐associated JmjC‐domain proteins may be protein hydroxylases that catalyse a novel histone modification.
Journal ArticleDOI

Dynamic protein methylation in chromatin biology

TL;DR: This work examines how dynamic histone methylation contributes to normal cellular function in mammals and focuses on the recent advances in the understanding of the hist one methylation system.
References
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Journal ArticleDOI

Translating the Histone Code

TL;DR: It is proposed that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.
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Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing

TL;DR: The purification and characterization of an EED-EZH2 complex, the human counterpart of the Drosophila ESC-E(Z) complex, is reported, and it is demonstrated that the complex specifically methylates nucleosomal histone H3 at lysine 27 (H3-K27).
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Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins.

TL;DR: It is shown that mammalian methyltransferases that selectively methylate histone H3 on lysine 9 (Suv39h HMTases) generate a binding site for HP1 proteins—a family of heterochromatic adaptor molecules implicated in both gene silencing and supra-nucleosomal chromatin structure.
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Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.

TL;DR: A stepwise model for the formation of a transcriptionally silent heterochromatin is provided: SUV39H1 places a ‘methyl marker’ on histone H3, which is then recognized by HP1 through its chromo domain, which may also explain the stable inheritance of theheterochromatic state.
Journal ArticleDOI

Regulation of chromatin structure by site-specific histone H3 methyltransferases

TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
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