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Akihiko Takashima
Researcher at Gakushuin University
Publications - 165
Citations - 12595
Akihiko Takashima is an academic researcher from Gakushuin University. The author has contributed to research in topics: Tau protein & Tauopathy. The author has an hindex of 57, co-authored 162 publications receiving 11404 citations. Previous affiliations of Akihiko Takashima include Doshisha University & Tokyo Institute of Technology.
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Journal ArticleDOI
Imaging of Tau Pathology in a Tauopathy Mouse Model and in Alzheimer Patients Compared to Normal Controls
Masahiro Maruyama,Hitoshi Shimada,Tetsuya Suhara,Hitoshi Shinotoh,Bin Ji,Jun Maeda,Ming-Rong Zhang,John Q. Trojanowski,Virginia M.-Y. Lee,Maiko Ono,Kazuto Masamoto,Harumasa Takano,Naruhiko Sahara,Naruhiko Sahara,Nobuhisa Iwata,Nobuyuki Okamura,Shozo Furumoto,Yukitsuka Kudo,Qing Chang,Takaomi C. Saido,Akihiko Takashima,Jada Lewis,Ming Kuei Jang,Ichio Aoki,Hiroshi Ito,Makoto Higuchi +25 more
TL;DR: A class of tau ligands, phenyl/pyridinyl-butadienyl-benzothiazoles/benZothiazoliums (PBBs), for visualizing diverse tau inclusions in brains of living patients with AD or non-AD tauopathies and animal models of these disorders are developed.
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Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease
Kenjiro Ono,Yuji Yoshiike,Akihiko Takashima,Kazuhiro Hasegawa,Hironobu Naiki,Masahito Yamada +5 more
TL;DR: Although the mechanisms by which these polyphenols inhibit fAβ formation from Aβ, and destabilize pre‐formed fA βin vitro are still unclear, polyphenol could be a key molecule for the development of preventives and therapeutics for AD.
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Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
Taiichi Katayama,Kazunori Imaizumi,Naoya Sato,Ko Miyoshi,Takashi Kudo,Junichi Hitomi,Takashi Morihara,Takunari Yoneda,Fumi Gomi,Yasutake Mori,Yuka Nakano,Junji Takeda,T. Tsuda,Yasuto Itoyama,Ohoshi Murayama,Akihiko Takashima,Peter St George-Hyslop,Masatoshi Takeda,Masaya Tohyama +18 more
TL;DR: It is reported that mutations in PS1 affect the unfolded-protein response (UPR), which responds to the increased amount of unfolded proteins that accumulate in the endoplasmic reticulum (ER) under conditions that cause ER stress.
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Chaperones increase association of tau protein with microtubules
Fei Dou,William J. Netzer,Kentaro Tanemura,Feng Li,F. Ulrich Hartl,Akihiko Takashima,Gunnar K. Gouras,Paul Greengard,Huaxi Xu +8 more
TL;DR: The results suggest that up-regulation of molecular chaperones may suppress formation of neurofibrillary tangles by partitioning tau into a productive folding pathway and thereby preventing tau aggregation.
Journal ArticleDOI
Presenilin 1 associates with glycogen synthase kinase-3β and its substrate tau
Akihiko Takashima,Miyuki Murayama,Ohoshi Murayama,Toshiyuki Kohno,Toshiyuki Honda,Kaori Yasutake,Naomi Nihonmatsu,Marc Mercken,Haruyasu Yamaguchi,Shiro Sugihara,Benjamin Wolozin +10 more
TL;DR: Mutations in PS1 that cause Alzheimer's disease increase the ability of PS1 to bind GSK-3beta and, correspondingly, increase its tau-directed kinase activity, and it is proposed that the increased association of GSK3beta with mutant PS1 leads to increased phosphorylation of tau.