Minako Hoshi

Summary

Affiliation: Mitsubishi Kagaku Institute of Life Sciences
Country: Japan

Publications

  1. pmc Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    Minako Hoshi
    Mitsubishi Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194 8511, Japan
    Proc Natl Acad Sci U S A 100:6370-5. 2003
  2. ncbi [Amylospheroid and the 'morphometabolism' disease (conformational disease)]
    Minako Hoshi
    Tanpakushitsu Kakusan Koso 49:1098-100. 2004
  3. ncbi [Morphology and neurotoxicity of newly identified spherical beta-amyloid aggregates, 'amylospheroid', aiming at elucidation of the neurodegenerative cascades in Alzheimer's disease]
    Minako Hoshi
    Unit of Neurodegenerative Disease, Mitsubishi Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194 8511, Japan
    Seikagaku 76:631-9. 2004
  4. pmc Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains
    Akihiko Noguchi
    Mitsubishi Kagaku Institute of Life Sciences, Tokyo 194 8511, Japan
    J Biol Chem 284:32895-905. 2009
  5. pmc Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses
    Satoko Matsumura
    Mitsubishi Kagaku Institute of Life Sciences, Tokyo, Japan
    J Biol Chem 286:11555-62. 2011

Collaborators

  • Shin Ichi Muramatsu
  • Hitoshi Takahashi
  • Kazutomo Imahori
  • Yo ichi Nabeshima
  • Satoko Matsumura
  • Akane Ito
  • Manami Akioka
  • Michio Sato
  • David B Teplow
  • Akihiko Noguchi
  • Masataka Kinjo
  • Kiyokazu Nemoto
  • Satoshi Yokojima
  • Yoshihiro Nakamura
  • Kazuya Kikuchi
  • Yutaka Hasegawa
  • Shinsuke Takagi
  • Keiko Shinoda
  • Masafumi Inoue
  • Haruo Inoue
  • Dai Masui
  • Shinichiro Nakamura
  • Hisayoshi Takamoto
  • Takayuki Ohnishi
  • Tetsuya Shimada
  • Shigeki Hashimoto
  • Mayumi Yamada
  • Kazuki Sato
  • Masako Yanazawa
  • Yutaka Itokazu
  • Satoru Kikuchi
  • Akiyoshi Kakita
  • Mari Dezawa
  • Mari Tada
  • Munehiro Noda
  • Atsushi Fukunari
  • Shouji Ideno

Detail Information

Publications5

  1. pmc Spherical aggregates of beta-amyloid (amylospheroid) show high neurotoxicity and activate tau protein kinase I/glycogen synthase kinase-3beta
    Minako Hoshi
    Mitsubishi Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194 8511, Japan
    Proc Natl Acad Sci U S A 100:6370-5. 2003
    ..Here we describe the identification and characterization of ASPD and discuss its possible role in the neurodegeneration in Alzheimer's disease...
  2. ncbi [Amylospheroid and the 'morphometabolism' disease (conformational disease)]
    Minako Hoshi
    Tanpakushitsu Kakusan Koso 49:1098-100. 2004
  3. ncbi [Morphology and neurotoxicity of newly identified spherical beta-amyloid aggregates, 'amylospheroid', aiming at elucidation of the neurodegenerative cascades in Alzheimer's disease]
    Minako Hoshi
    Unit of Neurodegenerative Disease, Mitsubishi Kagaku Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194 8511, Japan
    Seikagaku 76:631-9. 2004
  4. pmc Isolation and characterization of patient-derived, toxic, high mass amyloid beta-protein (Abeta) assembly from Alzheimer disease brains
    Akihiko Noguchi
    Mitsubishi Kagaku Institute of Life Sciences, Tokyo 194 8511, Japan
    J Biol Chem 284:32895-905. 2009
    ..Thus, our findings indicate that native ASPDs with a distinct toxic surface induce neuronal loss through a different mechanism from other Abeta assemblies...
  5. pmc Two distinct amyloid beta-protein (Abeta) assembly pathways leading to oligomers and fibrils identified by combined fluorescence correlation spectroscopy, morphology, and toxicity analyses
    Satoko Matsumura
    Mitsubishi Kagaku Institute of Life Sciences, Tokyo, Japan
    J Biol Chem 286:11555-62. 2011
    ..These differences in the assembly pathways clearly indicated that ASPDs are not fibril precursors. The method we have developed should facilitate identifying Aβ assembly steps at which inhibition may be beneficial...