Y
Yoichi Shinkai
Researcher at Kyoto University
Publications - 151
Citations - 20526
Yoichi Shinkai is an academic researcher from Kyoto University. The author has contributed to research in topics: Histone methyltransferase & Histone H3. The author has an hindex of 57, co-authored 142 publications receiving 18744 citations.
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Journal ArticleDOI
Class Switch Recombination and Hypermutation Require Activation-Induced Cytidine Deaminase (AID), a Potential RNA Editing Enzyme
Masamichi Muramatsu,Kazuo Kinoshita,Sidonia Fagarasan,Shuichi Yamada,Yoichi Shinkai,Tasuku Honjo +5 more
TL;DR: Results suggest that AID may be involved in regulation or catalysis of the DNA modification step of both class switching and somatic hypermutation in CH12F3-2 B lymphoma.
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G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis
Makoto Tachibana,Kenji Sugimoto,Masami Nozaki,Jun Ueda,Tsutomu Ohta,Misao Ohki,Mikiko Fukuda,Naoki Takeda,Hiroyuki Niida,Hiroyuki Kato,Yoichi Shinkai +10 more
TL;DR: The results indicate that euchromatic H3-K9 methylation regulated by G9a is essential for early embryogenesis and is involved in the transcriptional repression of developmental genes.
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Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin
Antoine H.F.M. Peters,Stefan Kubicek,Karl Mechtler,Roderick J. O'Sullivan,Alwin A.H.A. Derijck,Laura Perez-Burgos,Alexander Kohlmaier,Susanne Opravil,Makoto Tachibana,Yoichi Shinkai,Joost H.A. Martens,Thomas Jenuwein +11 more
TL;DR: The data underscore the selective presence of distinct histone lysine methylation states in partitioning chromosomal subdomains but also reveal a surprising plasticity in propagating methylation patterns in eukaryotic chromatin.
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Histone Methyltransferases Direct Different Degrees of Methylation to Define Distinct Chromatin Domains.
Judd C. Rice,Scott D. Briggs,Beatrix Ueberheide,Cynthia M. Barber,Jeffrey Shabanowitz,Donald F. Hunt,Yoichi Shinkai,C. David Allis +7 more
TL;DR: Different methylated states of H3 Lys9 are directed by specific histone methyltransferases to "mark" distinct domains of silent chromatin.
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SET Domain-containing Protein, G9a, Is a Novel Lysine-preferring Mammalian Histone Methyltransferase with Hyperactivity and Specific Selectivity to Lysines 9 and 27 of Histone H3
TL;DR: It is shown that a SET domain-containing protein, G9a, is a novel mammalian lysine-preferring HMTase, like Suv39 h1, but with a 10–20-fold higher activity and may contribute to the organization of the higher order chromatin structure of non-centromeric loci.