T
Toyotaka Ishibashi
Researcher at Hong Kong University of Science and Technology
Publications - 67
Citations - 2799
Toyotaka Ishibashi is an academic researcher from Hong Kong University of Science and Technology. The author has contributed to research in topics: Histone & DNA repair. The author has an hindex of 30, co-authored 65 publications receiving 2524 citations. Previous affiliations of Toyotaka Ishibashi include California Institute for Quantitative Biosciences & University of Victoria.
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Journal ArticleDOI
Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes
Yuki Yanagawa,James A. Sullivan,Setsuko Komatsu,Giuliana Gusmaroli,Genki Suzuki,Jianning Yin,Toyotaka Ishibashi,Yusuke Saijo,Vicente Rubio,Seisuke Kimura,Jian Wang,Xing Wang Deng +11 more
TL;DR: The data suggests that COP10, along with COP1 and the CSN, promotes the degradation of positive regulators of photomorphogenesis, such as the transcription factor HY5, via the ubiquitin/26S proteasome system, and the CDD complex may act as a ubiquitylation-promoting factor to regulatePhotomorphogenesis.
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Nucleosomal Elements That Control the Topography of the Barrier to Transcription
Lacramioara Bintu,Toyotaka Ishibashi,Manchuta Dangkulwanich,Yueh-Yi Wu,Lucyna Lubkowska,Mikhail Kashlev,Carlos Bustamante +6 more
TL;DR: Each of these nucleosomal elements controls transcription elongation by affecting distinctly the density and duration of polymerase pauses, thus providing multiple and alternative mechanisms for control of gene expression by chromatin remodeling and transcription factors.
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Complete dissection of transcription elongation reveals slow translocation of RNA polymerase II in a linear ratchet mechanism
Manchuta Dangkulwanich,Toyotaka Ishibashi,Toyotaka Ishibashi,Shixin Liu,Maria L. Kireeva,Lucyna Lubkowska,Mikhail Kashlev,Carlos Bustamante +7 more
TL;DR: Surprisingly, it is found that the forward translocation rate is comparable to the catalysis rate, revealing a linear, non-branched ratchet mechanism for the nucleotide addition cycle in which translocation is one of the rate-limiting steps.
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H2A.Z and H3.3 histone variants affect nucleosome structure: biochemical and biophysical studies.
Amit Thakar,Pooja Gupta,Toyotaka Ishibashi,Ron M. Finn,Begonia Silva-Moreno,Susumu Uchiyama,Kiichi Fukui,Miroslav Tomschik,Juan Ausió,Jordanka Zlatanova +9 more
TL;DR: Comparison of the properties of nucleosomes containing canonical histones and histone variants H2A.Z and H3.3 finds only subtle differences in the compaction and stability of the particles, which could be physiologically significant as nucleosome positions and linker histone binding partly determine factor binding accessibility.
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Acetylation of Vertebrate H2A.Z and Its Effect on the Structure of the Nucleosome
Toyotaka Ishibashi,Deanna Dryhurst,Kristie L. Rose,Jeffrey Shabanowitz,Donald F. Hunt,Juan Ausió +5 more
TL;DR: It is found that the change in NCP conformation induced by global histone acetylation is dependent on H2A/H2A.Z, which suggests that acetylated H 2A variants act synergistically with the acetylate forms of the core histone complement to alter the particle conformation.