K
Kouki Nishikawa
Researcher at Nagoya University
Publications - 21
Citations - 2127
Kouki Nishikawa is an academic researcher from Nagoya University. The author has contributed to research in topics: Biology & Aquaporin. The author has an hindex of 14, co-authored 19 publications receiving 1849 citations. Previous affiliations of Kouki Nishikawa include Kyoto University.
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Journal ArticleDOI
Unique multipotent cells in adult human mesenchymal cell populations
Yasumasa Kuroda,Masaaki Kitada,Shohei Wakao,Kouki Nishikawa,Yukihiro Tanimura,Hideki Makinoshima,Makoto Goda,Hideo Akashi,Ayumu Inutsuka,Akira Niwa,Taeko Shigemoto,Yoko Nabeshima,Tatsutoshi Nakahata,Yo-ichi Nabeshima,Yoshinori Fujiyoshi,Mari Dezawa +15 more
TL;DR: Adult human stem cells that can generate, from a single cell, cells with the characteristics of the three germ layers can be obtained through easily accessible adult human mesenchymal cells without introducing exogenous genes.
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Recent introduction of a chytrid fungus endangers Western Palearctic salamanders
An Martel,Mark Blooi,Connie Adriaensen,P. Van Rooij,Wouter Beukema,Matthew C. Fisher,Rhys A. Farrer,Benedikt R. Schmidt,Ursina Tobler,Koichi Goka,Karen R. Lips,Carly R. Muletz,Kelly R. Zamudio,Jaime Bosch,Stefan Lötters,Emma Wombwell,Emma Wombwell,Trenton W. J. Garner,Andrew A. Cunningham,A. Spitzen-van der Sluijs,Sebastiano Salvidio,R. Ducatelle,Kouki Nishikawa,Tao Thien Nguyen,Jonathan E. Kolby,I. Van Bocxlaer,Franky Bossuyt,Frank Pasmans +27 more
TL;DR: Results show that B. salamandrivorans is restricted to, but highly pathogenic for, salamanders and newts (Urodela), and likely originated and remained in coexistence with a clade of salamander hosts for millions of years in Asia.
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Implications of the aquaporin-4 structure on array formation and cell adhesion.
Yoko Hiroaki,Kazutoshi Tani,Akiko Kamegawa,Nobuhiko Gyobu,Kouki Nishikawa,Hiroshi Suzuki,Thomas Walz,Sei Sasaki,Kaoru Mitsuoka,Kazushi Kimura,Akira Mizoguchi,Yoshinori Fujiyoshi,Yoshinori Fujiyoshi +12 more
TL;DR: Aquaporin-4 contains a short 3(10) helix in an extracellular loop, which mediates weak but specific interactions between AQP4 molecules in adjoining membranes, which suggests a previously unexpected role for AQP 4 in cell adhesion.
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Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin
Yasunori Saitoh,Hiroshi Suzuki,Kazutoshi Tani,Kouki Nishikawa,Katsumasa Irie,Yuki Ogura,Atsushi Tamura,Sachiko Tsukita,Yoshinori Fujiyoshi +8 more
TL;DR: The structure of mammalian claudin-19 in complex with C-CPE at 3.7 Å resolution shows that C- CPE forms extensive hydrophobic and hydrophilic interactions with the two extracellular segments of claud in-19, and shows that helix displacement may underlie C-CCPE–mediated disassembly of TJs.
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Mechanism of aquaporin-4's fast and highly selective water conduction and proton exclusion
Kazutoshi Tani,Tadanori Mitsuma,Yoko Hiroaki,Akiko Kamegawa,Kouki Nishikawa,Yukihiro Tanimura,Yoshinori Fujiyoshi,Yoshinori Fujiyoshi +7 more
TL;DR: The structure of AQP4, the predominant water channel in the brain, reveals eight water molecules in the channel and visualizes five lipids, showing that direct interactions of the extracellular surface of AQp4 with three lipids in the adjoining membrane help stabilize the membrane junction.