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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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JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer

TL;DR: JARID1B is identified as a demethylase capable of removing three methyl groups from histone H3 lysine 4 and up-regulated in prostate cancer and associates with androgen receptor and regulates its transcriptional activity.
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Functions of lncRNA HOTAIR in lung cancer

TL;DR: The molecular mechanisms underlying HotaIR-mediated aggressive phenotypes of lung cancer are reviewed and HOTAIR’s potential in diagnosis and treatment of lung cancers is discussed, as well as the challenges of exploiting HOTA IR for intervention of Lung cancer.
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MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties.

TL;DR: Ch Chromatin immunoprecipitation experiments revealed that PRMT5 and MBD2 are recruited to CpG islands in a methylation-dependent manner in vivo and that H4R3, a substrate of PRMT, is methylated at these loci.
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Chromatin modifier enzymes, the histone code and cancer

TL;DR: Several families of transcription activators and repressors that catalyse histone post-translational modifications (acetylation, methylation, phosphorylation, ubiquitination and SUMOylation) are focused on; and how these enzymatic activities might alter the correct cell proliferation program, leading to cancer.
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Structural and Sequence Motifs of Protein (Histone) Methylation Enzymes

TL;DR: This review describes structural aspects of methylation of histone lysine residues by two enzyme families with entirely different structural scaffolding (the SET proteins and Dot1p) andmethylation of protein arginine residue by PRMTs.
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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