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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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Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36

TL;DR: It is shown thatSplicing can also contribute to histone modification, which implies bidirectional communication between epigenetic mechanisms and RNA processing, and is proposed that splicing is mechanistically coupled to recruitment of HYPB/Setd2 to elongating RNA polymerase II.
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Mitochondria and Epigenetics - Crosstalk in Homeostasis and Stress.

TL;DR: The function of mitochondria in the regulation of epigenetic mechanisms as a new aspect of mitonuclear communication is summarized and the essential role of some histone modifications in regulating the mitochondrial unfolded protein response (UPRmt) and the mitochondrial stress-dependent lifespan extension is described.
Journal ArticleDOI

Oestrogen-receptor-mediated transcription and the influence of co-factors and chromatin state.

TL;DR: Improved understanding of the nature of these interactions with ER means that scientists are better placed to relate these with ER activity and potentially with the activity of breast cancer drugs, including tamoxifen.
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Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?

TL;DR: The discovery of protein regulation via hydroxylation raises the possibility that other Fe(II)- and 2-oxoglutarate-dependent dioxygenases might also serve in a similar capacity.
Journal ArticleDOI

Histone Lysine Demethylases and Their Impact on Epigenetics

TL;DR: Methylation marks on the lysine residues of histone proteins are thought to contribute to epigenetic phenomena in part because of their apparent irreversibility, but will this view change with the recent discovery of Histone lysines demethylases that reversibly remove methyl marks?
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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