S
Sadao Shiosaka
Researcher at Nara Institute of Science and Technology
Publications - 138
Citations - 5773
Sadao Shiosaka is an academic researcher from Nara Institute of Science and Technology. The author has contributed to research in topics: Long-term potentiation & Image sensor. The author has an hindex of 37, co-authored 138 publications receiving 5480 citations. Previous affiliations of Sadao Shiosaka include Osaka University & Kindai University.
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Journal ArticleDOI
Autophagy Is Activated for Cell Survival after Endoplasmic Reticulum Stress
Maiko Ogata,Shin-ichiro Hino,Atsushi Saito,Keisuke Morikawa,Shinichi Kondo,Soshi Kanemoto,Tomohiko Murakami,Manabu Taniguchi,Ichiro Tanii,Kazuya Yoshinaga,Sadao Shiosaka,James A. Hammarback,Fumihiko Urano,Kazunori Imaizumi +13 more
TL;DR: It is found that the autophagy system is activated as a novel signaling pathway in response to ER stress and played important roles in cell survival after ER stress.
Journal ArticleDOI
Neuropsin cleaves EphB2 in the amygdala to control anxiety
Benjamin K. Attwood,Julie-Myrtille Bourgognon,Satyam Patel,Mariusz Mucha,Emanuele Schiavon,Anna E. Skrzypiec,Kenneth W. Young,Sadao Shiosaka,Michal Korostynski,Marcin Piechota,Ryszard Przewlocki,Robert Pawlak +11 more
TL;DR: It is shown in mice that the serine protease neuropsin is critical for stress-related plasticity in the amygdala by regulating the dynamics of the EphB2–NMDA-receptor interaction, the expression of Fkbp5 and anxiety-like behaviour.
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New Nomenclature for the Human Tissue Kallikrein Gene Family
Eleftherios P. Diamandis,Eleftherios P. Diamandis,George M. Yousef,George M. Yousef,Judith A. Clements,Linda K. Ashworth,Shigetaka Yoshida,Torbjörn Egelrud,Peter S. Nelson,Sadao Shiosaka,Sheila P. Little,Hans Lilja,Ulf-Håkan Stenman,Harry G. Rittenhouse,H Wain +14 more
TL;DR: The human kallikrein gene family is important to the discipline of clinical chemistry because it contains genes that encode for valuable cancer biomarkers, including the best tumor marker available today, prostate-specific antigen (PSA).
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NMDA-Dependent Proteolysis of Presynaptic Adhesion Molecule L1 in the Hippocampus by Neuropsin
Kazumasa Matsumoto-Miyai,Ayako Ninomiya,Hironobu Yamasaki,Hideki Tamura,Yukiko Nakamura,Sadao Shiosaka +5 more
TL;DR: It is shown that a serine protease, neuropsin, directly and specifically modifies the synaptic adhesion molecule L1, which was localized to the presynaptic site of the asymmetric synapse in the mouse hippocampus, which is involved in NMDA receptor-dependent synaptic plasticity.
Journal ArticleDOI
Characterization of Recombinant and Brain Neuropsin, a Plasticity-related Serine Protease
Chigusa Shimizu,Shigetaka Yoshida,Masao Shibata,Keiko Kato,Yoshiharu Momota,Kazumasa Matsumoto,Takahiko Shiosaka,Ryosuke Midorikawa,Tomohiro Kamachi,Akiko Kawabe,Sadao Shiosaka +10 more
TL;DR: Results indicate that this protease, which is enzymatically novel, has significant limbic effects by changing the extracellular matrix environment by cleaving Arg-X and Lys-X bonds in the synthetic chromogenic substrates.