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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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Epigenetics and metabolism.

TL;DR: It is demonstrated that gene regulation underlying phenotypic determinants of adult metabolic health is influenced by maternal and early postnatal diet, and these emerging concepts open new perspectives to combat the rising global epidemic of metabolic disorders.
Journal ArticleDOI

Polyamines and cancer: implications for chemotherapy and chemoprevention

TL;DR: Recent advances made in the polyamine field are described and the roles of polyamines and polyamine metabolism in neoplasia are focused on through a discussion of the current animal models for thepolyamine pathway, chemotherapeutic strategies that target the polyamines pathway, and chemotherAPEutic clinical trials for polyamine pathway-specific drugs and ongoing clinical trials targeting polyamine biosynthesis.
Journal ArticleDOI

The emerging functions of histone demethylases.

TL;DR: The recent identification of proteins with histone demethylase activity has shown that the methylated mark is much more dynamic than previously anticipated, thereby potentially challenging the concept of histone-methylation in stable epigenetic programming.
Journal ArticleDOI

Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis

TL;DR: The regulation of the activity of PADs in vivo remains largely elusive, and it is expected that much will be learned about the role of these enzymes in a normal life cycle and under pathology conditions.
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.
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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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