K
Kozo Kaibuchi
Researcher at Nagoya University
Publications - 508
Citations - 63012
Kozo Kaibuchi is an academic researcher from Nagoya University. The author has contributed to research in topics: Rho-associated protein kinase & Phosphorylation. The author has an hindex of 129, co-authored 493 publications receiving 60461 citations. Previous affiliations of Kozo Kaibuchi include Nara Institute of Science and Technology & Indiana University – Purdue University Indianapolis.
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Journal ArticleDOI
Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
TL;DR: Kinetic analysis indicates that TPA can substitute for diacylglycerol and greatly increases the affinity of the enzyme for Ca2+ as well as for phospholipid, and various phorbol derivatives which have been shown to be active in tumor promotion are also capable of activating this protein kinase in in vitro systems.
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Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
Kazushi Kimura,Masaaki Ito,Mutsuki Amano,Kazuyasu Chihara,Yuko Fukata,Masato Nakafuku,Bunpei Yamamori,Jianhua Feng,Takeshi Nakano,Katsuya Okawa,Akihiro Iwamatsu,Kozo Kaibuchi +11 more
TL;DR: Rho appears to inhibit myosin phosphatase through the action of Rho-kinase, which is activated by GTP·RhoA, phosphorylation of MBS and MLC in NIH 3T3 cells.
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Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase).
Mutsuki Amano,Masaaki Ito,Kazushi Kimura,Yuko Fukata,Kazuyasu Chihara,Takeshi Nakano,Yoshiharu Matsuura,Kozo Kaibuchi +7 more
TL;DR: The phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase, which may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction.
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Formation of Actin Stress Fibers and Focal Adhesions Enhanced by Rho-Kinase
Mutsuki Amano,Kazuyasu Chihara,Kazushi Kimura,Yuko Fukata,Nao Nakamura,Yoshiharu Matsuura,Kozo Kaibuchi +6 more
TL;DR: Rho-kinase appears to mediate signals from Rho and to induce the formation of stress fibers and focal adhesions.
Journal ArticleDOI
Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho
Takeshi Matsui,Mutsuki Amano,Takaharu Yamamoto,Kazuyasu Chihara,Masato Nakafuku,Mikako Ito,Takeshi Nakano,K. Okawa,A. Iwamatsu,Kozo Kaibuchi +9 more
TL;DR: P purified a Rho‐interacting protein with a molecular mass of approximately 164 kDa (p164) from bovine brain that bound to GTPgammaS (a non‐hydrolyzable GTP analog) and is likely to be a putative target serine/threonine kinase for Rho and serves as a mediator of the RHo‐dependent signaling pathway.