M
Masayasu Okochi
Researcher at Osaka University
Publications - 96
Citations - 4648
Masayasu Okochi is an academic researcher from Osaka University. The author has contributed to research in topics: Presenilin & Unfolded protein response. The author has an hindex of 35, co-authored 93 publications receiving 4243 citations. Previous affiliations of Masayasu Okochi include Ludwig Maximilian University of Munich.
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Journal ArticleDOI
Subcellular Localization of Wild-Type and Parkinson's Disease-Associated Mutant α-Synuclein in Human and Transgenic Mouse Brain
Philipp J. Kahle,Manuela Neumann,Laurence Ozmen,Veronika Müller,Helmut Jacobsen,Alice Schindzielorz,Masayasu Okochi,Uwe Leimer,Herman van der Putten,Alphonse Probst,Elisabeth Kremmer,Hans A. Kretzschmar,Christian Haass +12 more
TL;DR: The Parkinson's disease-associated human mutant [A30P]αSYN was found to colocalize with βSYN and synaptophysin in synapses of transgenic mouse brain, however, in addition to their normal presynaptic localization, transgenic wild-type and [A 30P] αSYN abnormally accumulated in neuronal cell bodies and neurites throughout the brain.
Journal ArticleDOI
Constitutive Phosphorylation of the Parkinson's Disease Associated α-Synuclein *
Masayasu Okochi,Jochen Walter,Akihiko Koyama,Shigeo Nakajo,Minami Baba,Takeshi Iwatsubo,Laurent Meijer,Philipp J. Kahle,Christian Haass +8 more
TL;DR: Data demonstrate that α- Synuclein is constitutively phosphorylated within its C terminus and may indicate that the function of α-synuclein are regulated by phosphorylation/dephosphorylation.
Journal Article
Behavioral and psychological symptoms of dementia
Masayasu Okochi,Masatoshi Takeda +1 more
Journal ArticleDOI
Presenilin-dependent intramembrane proteolysis of CD44 leads to the liberation of its intracellular domain and the secretion of an Abeta-like peptide.
Sven Lammich,Masayasu Okochi,Masatoshi Takeda,Christoph Kaether,Anja Capell,Ann-Katrin Zimmer,Dieter Edbauer,Jochen Walter,Harald Steiner,Christian Haass +9 more
TL;DR: In this article, a cell surface adhesion molecule, CD44, undergoes an intramembraneous cleavage to liberate its intracellular domains, which are required for nuclear signaling of Notch and probably ErbB-4, the β-amyloid precursor protein, E-cadherin, and the LDL receptor-related protein as well.
Journal ArticleDOI
Presenilins mediate a dual intramembranous γ‐secretase cleavage of Notch‐1
Masayasu Okochi,Harald Steiner,Akio Fukumori,Hisashi Tanii,Taisuke Tomita,Toshihisa Tanaka,Takeshi Iwatsubo,Takashi Kudo,Masatoshi Takeda,Christian Haass +9 more
TL;DR: It is concluded that Notch‐1 and βAPP are cleaved by a common mechanism utilizing the same protease, i.e. PS/γ‐secretase.