神谷成敏

研究者氏名	神谷成敏
	カミヤナルトシ
URL
所属	兵庫県立大学
部署	情報科学研究科
職名	特任教授
科研費研究者番号	80420462
J-Global ID	201801005421048355

研究分野

ライフサイエンス / 生物物理学 /

論文

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Flexibility and Cell Permeability of Cyclic Ras-Inhibitor Peptides Revealed by the Coupled Nosé–Hoover Equation

Kei Moritsugu Koh Takeuchi Narutoshi Kamiya Junichi Higo Isao Yasumatsu Yoshifumi Fukunishi Ikuo Fukuda

Journal of Chemical Information and Modeling 61(4) 1921-1930 2021年4月 [査読有り]

Quantifying the cell permeability of cyclic peptides is crucial for their rational drug design. However, the reasons remain unclear why a minor chemical modification, such as the difference between Ras inhibitors cyclorasin 9A5 and 9A54, can subst...

Difference of binding modes among three ligands to a receptor mSin3B corresponding to their inhibitory activities

Tomonori Hayami Narutoshi Kamiya Kota Kasahara Takeshi Kawabata Jun-ichi Kurita Yoshifumi Fukunishi Yoshifumi Nishimura Haruki Nakamura Junichi Higo

Scientific Reports 11(1) 6178 2021年3月 [査読有り]

<title>Abstract</title>A preceding experiment suggested that a compound, which inhibits binding of the REST/NRSF segment to the cleft of a receptor protein mSin3B, can be a potential drug candidate to ameliorate many neuropathies. We have recently...

Cryptic-site binding mechanism of medium-sized Bcl-xL inhibiting compounds elucidated by McMD-based dynamic docking simulations

Gert-Jan Bekker Ikuo Fukuda Junichi Higo Yoshifumi Fukunishi Narutoshi Kamiya

Scientific Reports 11(1) 5046-5046 2021年3月 [査読有り]

<title>Abstract</title>We have performed multicanonical molecular dynamics (McMD) based dynamic docking simulations to study and compare the binding mechanism between two medium-sized inhibitors (ABT-737 and WEHI-539) that bind to the cryptic site...

Dynamical Methods to Study Interaction in Proteins Facilitating Molecular Understanding of Cancer

Bhaskar Dasgupta Gert-Jan Bekker Narutoshi Kamiya

Handbook of Oxidative Stress in Cancer: Mechanistic Aspects 1-17 2021年 [査読有り]

Structural basis of mutants of PET ‐degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability

Miho Emori Nobutaka Numoto Akane Senga Gert‐Jan Bekker Narutoshi Kamiya Yuma Kobayashi Nobutoshi Ito Fusako Kawai Masayuki Oda

Proteins: Structure, Function, and Bioinformatics 89(5) 502-511 2021年1月 [査読有り]

The cutinase-like enzyme from the thermophile Saccharomonospora viridis AHK190, Cut190, is a good candidate to depolymerize polyethylene terephthalate (PET) efficiently. We previously developed a mutant of Cut190 (S226P/R228S), which we designated...