Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Kyoko Hiragami-Hamada"'
Autor:
Kyoko Hiragami-Hamada, Szabolcs Soeroes, Miroslav Nikolov, Bryan Wilkins, Sarah Kreuz, Carol Chen, Inti A. De La Rosa-Velázquez, Hans Michael Zenn, Nils Kost, Wiebke Pohl, Aleksandar Chernev, Dirk Schwarzer, Thomas Jenuwein, Matthew Lorincz, Bastian Zimmermann, Peter Jomo Walla, Heinz Neumann, Tuncay Baubec, Henning Urlaub, Wolfgang Fischle
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Heterochromatin protein 1 (HP1), including HP1 α, β and γ, is a family of non-histone chromatin factors thought to be involved in chromatin organization. Here, the authors show that dimeric HP1β interacts dynamically with H3K9me3, a hallmark of h
Externí odkaz:
https://doaj.org/article/daad9f601a9746829955629c5cc1bf39
Autor:
Benoit Guillemette, Paul Drogaris, Hsiu-Hsu Sophia Lin, Harry Armstrong, Kyoko Hiragami-Hamada, Axel Imhof, Eric Bonneil, Pierre Thibault, Alain Verreault, Richard J Festenstein
Publikováno v:
PLoS Genetics, Vol 7, Iss 3, p e1001354 (2011)
Methylation of histone H3 lysine 4 (H3K4me) is an evolutionarily conserved modification whose role in the regulation of gene expression has been extensively studied. In contrast, the function of H3K4 acetylation (H3K4ac) has received little attention
Externí odkaz:
https://doaj.org/article/b429b746debb42b39155c8db3261d43c
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2161
Chromatin serves as a platform for a multitude of biological processes, including transcription and co-transcriptional RNA processing. Consequently, chromatin is likely to be covered with many RNA molecules.Here we describe a simple, reliable, and cr
Publikováno v:
Methods in Molecular Biology ISBN: 9781071606797
Chromatin serves as a platform for a multitude of biological processes, including transcription and co-transcriptional RNA processing. Consequently, chromatin is likely to be covered with many RNA molecules.Here we describe a simple, reliable, and cr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d9e19d1284a6040b640960cabdd4f6b
https://doi.org/10.1007/978-1-0716-0680-3_8
https://doi.org/10.1007/978-1-0716-0680-3_8
Publikováno v:
Journal of Biochemistry
The chromodomain (CD) is a member of the Royal family of conserved chromatin-binding motifs with methylated substrate binding ability, and is often found in ‘readers’ or ‘writers’ of repressive histone marks. The regions upstream or downstrea
Autor:
Yuriko Yoshimura, Gohei Nishibuchi, Kyoko Hiragami-Hamada, Hideaki Tagami, Shinichi Machida, Hitoshi Kurumizaka, Reiko Nakagawa, Jun-ichi Nakayama, Yusuke Abe
Publikováno v:
Journal of biochemistry. 165(5)
Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that plays a crucial role in heterochromatin-mediated gene silencing. We previously showed that mammalian HP1α is constitutively phosphorylated at its N-terminal seri
Various coding and non-coding transcripts are known to associate with chromatin and now there is accumulating evidence that interaction between RNA-binding proteins (RBPs) and RNA molecules regulate not only co-transcriptional mRNA processing, but al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::780a027fdaf51b080ee200a04bf17537
Autor:
Yoshifumi Nishimura, Hideaki Tagami, Hitoshi Kurumizaka, Jun-ichi Nakayama, Gohei Nishibuchi, Shinichi Machida, Wolfgang Fischle, Hiromu Murakoshi, Akihisa Osakabe, Reiko Nakagawa, Kyoko Hiragami-Hamada
Publikováno v:
Nucleic Acids Research
Heterochromatin protein 1 (HP1) is an evolutionarily conserved chromosomal protein that binds to lysine 9-methylated histone H3 (H3K9me), a hallmark of heterochromatin. Although HP1 phosphorylation has been described in several organisms, the biologi
Autor:
Stefan Winter, Kathy Ann Gelato, Alexander Lemak, Yvette Bultsma, Wolfgang Fischle, Maria Tauber, Julia Sindlinger, Cheryl H. Arrowsmith, Nullin Divecha, Scott Houliston, Dirk Schwarzer, Michelle S. Ong, Kyoko Hiragami-Hamada
Publikováno v:
Molecular Cell
UHRF1 is a multidomain protein crucially linking histone H3 modification states and DNA methylation. While the interaction properties of its specific domains are well characterized, little is known about the regulation of these functionalities. We sh
Autor:
Tuncay Baubec, Sarah Kreuz, Henning Urlaub, Carol Chen, Matthew C. Lorincz, Dirk Schwarzer, Wiebke H. Pohl, Szabolcs Soeroes, Bastian Zimmermann, Thomas Jenuwein, Miroslav Nikolov, Inti A. De La Rosa-Velázquez, Wolfgang Fischle, Aleksandar Chernev, Peter Walla, Bryan J. Wilkins, Heinz Neumann, Nils Kost, Hans Michael Zenn, Kyoko Hiragami-Hamada
Publikováno v:
Europe PubMed Central
Nature communications
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Nature communications
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanis