K
Kunihiro Kitamura
Researcher at Taisho Pharmaceutical Co.
Publications - 82
Citations - 2263
Kunihiro Kitamura is an academic researcher from Taisho Pharmaceutical Co.. The author has contributed to research in topics: Hydrogen bond & Crystal structure. The author has an hindex of 24, co-authored 82 publications receiving 2155 citations. Previous affiliations of Kunihiro Kitamura include Honda & Osaka University of Pharmaceutical Sciences.
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Journal ArticleDOI
Hydrogen Bonding of Water to Phosphatidylcholine in the Membrane As Studied by a Molecular Dynamics Simulation: Location, Geometry, and Lipid-Lipid Bridging via Hydrogen-Bonded Water
TL;DR: In this paper, a molecular dynamics simulation of a hydrated phosphatidylcholine bilayer membrane in the liquid crystalline phase was studied using H-bonding between water and DMPC molecules, and it was shown that water bridges are involved in reducing head group mobility and in stabilizing the membrane structure.
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Charge pairing of headgroups in phosphatidylcholine membranes : a molecular dynamics simulation study
TL;DR: It is shown that relatively stable charge associations (charge pairs) are formed between the positively and negatively charged groups of two DMPC molecules.
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Crystal structures of 7-methylguanosine 5'-triphosphate (m(7)GTP)- and P(1)-7-methylguanosine-P(3)-adenosine-5',5'-triphosphate (m(7)GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region
Koji Tomoo,Xu Shen,Koumei Okabe,Yoshiaki Nozoe,Shoichi Fukuhara,Shigenobu Morino,Toshimasa Ishida,Taizo Taniguchi,Hiroshi Hasegawa,Akira Terashima,Masahiro Sasaki,Yoshio Katsuya,Kunihiro Kitamura,Hiroshi Miyoshi,Masahide Ishikawa,Kin-ichiro Miura +15 more
TL;DR: The present results provide the structural basis for the biological function of both N- and C-terminal mobile regions of eIF4E in translation initiation, especially the regulatory function through the switch-on/off of eif4E-binding protein-eIF 4E phosphorylation.
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Structural basis of inhibition of cysteine proteases by E-64 and its derivatives.
Keita Matsumoto,Kazutoshi Mizoue,Kunihiro Kitamura,Wai-Ching Tse,Carol P. Huber,Toshimasa Ishida +5 more
TL;DR: This paper focuses on the inhibitory mechanism of E-64 and its derivatives (epoxysuccinyl-based inhibitors) with some cysteine proteases, based on the binding modes observed in the x-ray crystal structures of their enzyme-inhibitor complexes.
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Molecular characterization of mammalian dicarbonyl/L-xylulose reductase and its localization in kidney.
Junichi Nakagawa,Syuhei Ishikura,Jun Asami,Tomoya Isaji,Noriyuki Usami,Akira Hara,Takanobu Sakurai,Katsuki Tsuritani,Koji Oda,Masayoshi Takahashi,Makoto Yoshimoto,Noboru Otsuka,Kunihiro Kitamura +12 more
TL;DR: The results imply that P34H and diacetyl reductase are identical tol-xylulose reduct enzyme, which is involved in the uronate cycle of glucose metabolism, and the unique localization of the enzyme in kidney suggests that it has a role other than in general carbohydrate metabolism.