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Narito Morii

Researcher at Kyoto University

Publications -  108
Citations -  6974

Narito Morii is an academic researcher from Kyoto University. The author has contributed to research in topics: Angiotensin II & NPR2. The author has an hindex of 44, co-authored 108 publications receiving 6922 citations. Previous affiliations of Narito Morii include Tokyo Institute of Technology.

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The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase.

TL;DR: It is shown that p160 can associate physically and functionally with Rho both in vitro and in vivo, indicating that the small GTP‐binding protein Rho functions as a molecular switch in the formation of focal adhesions and stress fibers, cytokinesis and transcriptional activation.
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Protein Kinase N (PKN) and PKN-Related Protein Rhophilin as Targets of Small GTPase Rho

TL;DR: This study indicates that a serine-threonine protein kinase is a Rho effector and presents an amino acid sequence motif for binding to GTP-Rho that may be shared by a family of Rho target proteins.
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Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the Rho-binding domain

TL;DR: The N-terminal part of rhotekin, encoded by the initial cDNA and produced in bacteria as a glutathione S-transferase fusion protein, exhibited in vitro binding to 35S-labeled guanosine 5′-3-O-(thio)triphosphate-bound Rho, but not to Rac1 or Cdc42Hs in ligand overlay assays.
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Atrial natriuretic polypeptide: topographical distribution in the rat brain by radioimmunoassay and immunohistochemistry.

TL;DR: An atlas of the distribution of the alpha-atrial natriuretic polypeptide-containing neuronal system in the rat brain is given and the groundwork for studying the influence of this new peptide on various brain functions is provided.
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A rho-like protein is involved in the organisation of the contractile ring in dividing sand dollar eggs.

TL;DR: Results strongly suggest that a rho-like, small GTP-binding protein is selectively involved in the organisation and maintenance of the contractile ring.