PatentDOI
Histone demethylation mediated by the nuclear amine oxidase homolog lsd1
Yang Shi,Yujiang Shi +1 more
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.About:
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.read more
Citations
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Journal ArticleDOI
Comparative analysis of small molecules and histone substrate analogues as LSD1 lysine demethylase inhibitors.
TL;DR: This work re-explored MAO antidepressant agent phenelzine (phenethylhydrazine), previously reported to be a weak LSD1 inhibitor, and found that it is far more potent than previously appreciated, validating it as a pharmacologic tool and potential lead structure for anticancer therapy.
Journal ArticleDOI
Targeting histone lysine demethylases — Progress, challenges, and the future
Cyrille C. Thinnes,Katherine S. England,Akane Kawamura,Rasheduzzaman Chowdhury,Christopher J. Schofield,Richard J. Hopkinson +5 more
TL;DR: An introduction to the enzymology of the KDMs and the therapeutic possibilities and challenges associated with targeting them are provided, followed by a review of reported KDM inhibitors and their mechanisms of action from kinetic and structural perspectives.
Journal ArticleDOI
Aire employs a histone-binding module to mediate immunological tolerance, linking chromatin regulation with organ-specific autoimmunity.
Andrew S. Koh,Alex J. Kuo,Sang Youn Park,Peggie Cheung,Jakub Abramson,Dennis J. Bua,Dylan Carney,Steven E. Shoelson,Or Gozani,Robert E. Kingston,Christophe Benoist,Diane Mathis +11 more
TL;DR: Aire's activity as a histone-binding module mediates the thymic display of PTAs that promotes self-tolerance and prevents organ-specific autoimmunity.
Journal ArticleDOI
MicroRNA targets in immune genes and the Dicer/Argonaute and ARE machinery components.
Ananthi J. Asirvatham,Christopher J. Gregorie,Zihua Hu,William J. Magner,Thomas B. Tomasi,Thomas B. Tomasi +5 more
TL;DR: Factors involved in regulating message stability via AU-rich elements (ARE) were heavily targeted suggesting that a subset of miRNAs may indirectly control their own production as well as other miRNAAs.
Journal ArticleDOI
KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation
Datsun A. Hsia,Clifford G. Tepper,Mamata R. Pochampalli,Elaine Y.C. Hsia,Chie Izumiya,Steve B. Huerta,Michael E. Wright,Hongwu Chen,Hsing Jien Kung,Yoshihiro Izumiya +9 more
TL;DR: It is shown that JMJD5 (now renamed KDM8), a JmjC family member, demethylates H3K36me2 and is required for cell cycle progression and is identified as an important cell cycle regulator.
References
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Journal ArticleDOI
Translating the Histone Code
Thomas Jenuwein,C. David Allis +1 more
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
Ru Cao,Liangjun Wang,Hengbin Wang,Li Xia,Hediye Erdjument-Bromage,Paul Tempst,Richard S. Jones,Yi Zhang +7 more
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.
Journal ArticleDOI
Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain.
Andrew J. Bannister,Philip Zegerman,Janet F. Partridge,Eric A. Miska,Jean O. Thomas,Robin C. Allshire,Tony Kouzarides +6 more
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
Stephen Rea,Frank Eisenhaber,Dónal O'Carroll,Brian D. Strahl,Zu-Wen Sun,Manfred Schmid,Susanne Opravil,Karl Mechtler,Chris P. Ponting,C D Allis,Thomas Jenuwein +10 more
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.