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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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CRISPR-suppressor scanning reveals a nonenzymatic role of LSD1 in AML.

TL;DR: A CRISPR–Cas9 screening-based structure–activity relationship profiling method reveals that LSD1 inhibitors suppress acute myeloid leukemia by disruption of the interaction between LSD1 and GFI1B instead of the enzyme activity of LSD1.
Journal ArticleDOI

Overexpression of a histone H3K4 demethylase, JMJ15, accelerates flowering time in Arabidopsis.

TL;DR: Overexpression of a histone H3K4 demethylase, JMJ15, represses FLC expression by decreasing its chromatin H3k4me3 level, thereby controlling flowering time in Arabidopsis.
Journal ArticleDOI

The role of the histone demethylase KDM4A in cancer

TL;DR: The role of K DM4A in cancer development and the importance of KDM4A as a potential therapeutic target are discussed.
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Splicing- and demethylase-independent functions of LSD1 in zebrafish primitive hematopoiesis.

TL;DR: Interestingly, LSD1+8al/LSD1+2al8al, which corresponded to mammalian neuron-specific variants, expressed ubiquitously in zebrafish, suggesting that the LSD1 functions inZebrafish primitive hematopoiesis are free from any splicing-dependent regulation or demethylation reaction.
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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