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
Involvement of Histone Demethylase LSD1 in Blimp-1-Mediated Gene Repression during Plasma Cell Differentiation
Shin Tang Su,Hsia-Yuan Ying,Hsia-Yuan Ying,Yi Kai Chiu,Yi Kai Chiu,Fan Ru Lin,Fan Ru Lin,Mei Yu Chen,Kuo-I Lin,Kuo-I Lin +9 more
TL;DR: It is reported that a proline-rich domain in Blimp-1 directly interacts with LSD1, a histone lysine demethylase, and that LSD1 binding correlates with histone modifications of accessible chromatin.
Journal ArticleDOI
The lncRNA GATA6-AS epigenetically regulates endothelial gene expression via interaction with LOXL2
Philipp Neumann,Nicolas Jaé,Andrea Knau,Simone F. Glaser,Youssef Fouani,Oliver Rossbach,Marcus Krüger,David John,Albrecht Bindereif,Phillip Grote,Reinier A. Boon,Stefanie Dimmeler +11 more
TL;DR: It is shown that the long non-coding antisense transcript of GATA6 (GATA6-AS) interacts with the epigenetic regulator LOXL2 to regulate endothelial gene expression via changes in histone methylation, with functional consequences on endothelial-mesenchymal transition and angiogenesis.
Journal ArticleDOI
Epigenetics and its implications for plant biology. 1. The epigenetic network in plants.
TL;DR: How epigenetic systems in plants were elucidated is addressed and there is a discussion on how the different components of the epigenetic system--regulating DNA methylation, histones and their post-translational modification, and pathways recognizing aberrant transcripts--may work together.
Journal ArticleDOI
Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro.
Reinout Raijmakers,Albert J.W. Zendman,Wilma Vree Egberts,Erik R. Vossenaar,Jos M.H. Raats,Claudia Soede-Huijbregts,Floris P. J. T. Rutjes,Peter A. van Veelen,Jan W. Drijfhout,Ger J. M. Pruijn +9 more
TL;DR: Data indicate that it is unlikely that methyl groups at the guanidino position of peptidylarginine can be removed by peptIDylcitrulline deiminases, which has important implications for the recently reported role of these enzymes in gene regulation.
Journal ArticleDOI
Lysine demethylases inhibitors.
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.
Journal ArticleDOI
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).
Journal ArticleDOI
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.