Zobrazeno 1 - 10
of 240
pro vyhledávání: '"Hidetoshi, Kono"'
Autor:
Akiko Fujimura, Hisashi Ishida, Tamiko Nozaki, Shuhei Terada, Yuto Azumaya, Tadashi Ishiguro, Yugo R. Kamimura, Tomoya Kujirai, Hitoshi Kurumizaka, Hidetoshi Kono, Kenzo Yamatsugu, Shigehiro A. Kawashima, Motomu Kanai
Publikováno v:
ACS Central Science, Vol 9, Iss 11, Pp 2115-2128 (2023)
Externí odkaz:
https://doaj.org/article/b35bf482716e4c2ab9429ea65fa36663
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract Intrinsically Disordered Proteins (IDPs) play crucial roles in numerous diseases like Alzheimer's and ALS by forming irreversible amyloid fibrils. The effectiveness of force fields (FFs) developed for globular proteins and their modified ver
Externí odkaz:
https://doaj.org/article/52adee96b2874f82a229a0ea219cad91
Autor:
Junichi Higo, Kota Kasahara, Gert-Jan Bekker, Benson Ma, Shun Sakuraba, Shinji Iida, Narutoshi Kamiya, Ikuo Fukuda, Hidetoshi Kono, Yoshifumi Fukunishi, Haruki Nakamura
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-19 (2022)
Abstract A GA-guided multidimensional virtual-system coupled molecular dynamics (GA-mD-VcMD) simulation was conducted to elucidate binding mechanisms of a middle-sized flexible molecule, bosentan, to a GPCR protein, human endothelin receptor type B (
Externí odkaz:
https://doaj.org/article/07b56a258af1478fb2760e436655ec63
Autor:
Yasuhiro Yunoki, Atsushi Matsumoto, Ken Morishima, Anne Martel, Lionel Porcar, Nobuhiro Sato, Rina Yogo, Taiki Tominaga, Rintaro Inoue, Maho Yagi-Utsumi, Aya Okuda, Masahiro Shimizu, Reiko Urade, Kazuki Terauchi, Hidetoshi Kono, Hirokazu Yagi, Koichi Kato, Masaaki Sugiyama
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-12 (2022)
The revealed full KaiA12B6C6 complex is assembled including the dynamic and asynchronous KaiA N-terminal domains that have been missing in cryo-EM structures.
Externí odkaz:
https://doaj.org/article/190270aaeb514b6fbcb5c9982c22b4e8
Autor:
Ko Sato, Amarjeet Kumar, Keisuke Hamada, Chikako Okada, Asako Oguni, Ayumi Machiyama, Shun Sakuraba, Tomohiro Nishizawa, Osamu Nureki, Hidetoshi Kono, Kazuhiro Ogata, Toru Sengoku
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
An upregulation of NSD2, a histone H3 lysine 36 (H3K36) methyltransferase is linked to multiple myeloma and other types of cancer. Here, the authors provide insights into the regulatory mechanism of NSD2 by determining the 2.8 Å cryo-EM structure of
Externí odkaz:
https://doaj.org/article/a236ab6e4fda4b94ae5feb9f8adae7d1
Publikováno v:
PLoS Computational Biology, Vol 18, Iss 1, p e1009804 (2022)
Nonstructural protein 1 (nsp1) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a 180-residue protein that blocks translation of host mRNAs in SARS-CoV-2-infected cells. Although it is known that SARS-CoV-2's own RNA evades nsp1's h
Externí odkaz:
https://doaj.org/article/722c8425d04442239c1f7f3c8d1318dd
Autor:
Brianna J. Klein, Suk Min Jang, Catherine Lachance, Wenyi Mi, Jie Lyu, Shun Sakuraba, Krzysztof Krajewski, Wesley W. Wang, Simone Sidoli, Jiuyang Liu, Yi Zhang, Xiaolu Wang, Becka M. Warfield, Andrew J. Kueh, Anne K. Voss, Tim Thomas, Benjamin A. Garcia, Wenshe R. Liu, Brian D. Strahl, Hidetoshi Kono, Wei Li, Xiaobing Shi, Jacques Côté, Tatiana G. Kutateladze
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Acetylation of histone H3K23 has emerged as an essential posttranslational modification, yet this epigenetic mark remains poorly understood. Here, the authors identify the native MORF complex as a histone H3K23-specific acetyltransferase and show tha
Externí odkaz:
https://doaj.org/article/78758c527c604e018605e9ed73ff1cd5
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
Eukaryotic genome is packaged in a nucleus in the form of chromatin. The fundamental structural unit of the chromatin is the protein-DNA complex, nucleosome, where DNA of about 150 bp is wrapped around a histone core almost twice. In cellular process
Externí odkaz:
https://doaj.org/article/50efefbd73f94398919097ec764e67de
Publikováno v:
Biophysics and Physicobiology, Vol 16 (2019)
Externí odkaz:
https://doaj.org/article/36209d07683241889989595003fedeb6
Autor:
Jovylyn Gatchalian, Xiaodong Wang, Jinzen Ikebe, Khan L. Cox, Adam H. Tencer, Yi Zhang, Nathaniel L. Burge, Luo Di, Matthew D. Gibson, Catherine A. Musselman, Michael G. Poirier, Hidetoshi Kono, Jeffrey J. Hayes, Tatiana G. Kutateladze
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
The chromatin remodeller CHD4 contains two PHD finger reader domains that have been shown to bivalently recognize H3 histone tails. Here, the authors describe a mechanism by which the PHD fingers bind to the intact nucleosome core particle, revealing
Externí odkaz:
https://doaj.org/article/80503b36d74a4bc3b72aa20bc28f7b84