Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Mika Nobuhara"'
Autor:
Taro Saito, Saori Abe, Mika Nobuhara, Akiko Asada, Toshiya Oba, Tomoki Chiku, Satoko Wada-Kakuda, Akihiko Takashima, Mikiko Oka, Kanae Ando, Tomohiro Miyasaka, Kanako Shinno, Akio Sumioka
Publikováno v:
Human Molecular Genetics
Accumulation of microtubule-associated tau protein is thought to cause neuron loss in a group of neurodegenerative diseases called tauopathies. In diseased brains, tau molecules adopt pathological structures that propagate into insoluble forms with d
Autor:
Satoko Wada-Kakuda, Tomohiro Miyasaka, Mika Nobuhara, Hitomi Fujiwara, Minori Iwata, Shoji Watanabe, Shouyou Ueda, Hiroaki Misonou
Publikováno v:
Biochemical and Biophysical Research Communications. 521:779-785
Neurofibrillary tangles, a pathological hallmark of Alzheimer’s disease (AD), are somatodendritic filamentous inclusions composed of hyperphosphorylated tau. Microtubule loss is also a common feature of affected neurons in AD. However, whether and
Publikováno v:
Biochemical and biophysical research communications. 560
Microtubules form a major cytoskeleton and exhibit dynamic instability through the repetitive polymerization/depolymerization of tubulin dimers. Although microtubule stability should be precisely controlled to maintain various cellular functions, it
Publikováno v:
Biochemical and Biophysical Research Communications. 502:98-103
γ-Secretase complex, the assembly of nicastrin (NCT), Presenilin (PS), Presenilin Enhancer-2 (PEN-2) and Anterior pharynx defective 1 (Aph-1), catalyzes the cleavage of amyloid precursor protein to generate amyloid-β protein (Aβ), the main culprit
Publikováno v:
Journal of Neurochemistry. 140:955-962
The amyloid β (Aβ) protein is a major component of senile plaques, one of the neuropathological hallmarks of Alzheimer's disease. Amyloidogenic processing of amyloid precursor protein (APP) by β- and γ-secretases leads to production of Aβ. APP c
Autor:
Mika Nobuhara, Satoru Funamoto, Satoko Osawa, Sosuke Yagishita, Yasuo Ihara, Masafumi Shimojo, Satoko Wada-Kakuda
Publikováno v:
Journal of Biological Chemistry. 283:19283-19292
gamma-Secretase is an aspartic protease that hydrolyzes type I membrane proteins within the hydrophobic environment of the lipid bilayer. Using the CHAPSO-solubilized gamma-secretase assay system, we previously found that gamma-secretase activity was
Autor:
Minori Iwata, Mika Nobuhara, Hitomi Fujiwara, Satoru Funamoto, Asuka Kokawa, Seiko Ishihara, Yasuo Ihara
Publikováno v:
Acta Neuropathologica Communications
Introduction The A673T mutation in the amyloid precursor protein (APP) protects against Alzheimer’s disease by reducing β-amyloid protein (Aβ) production. This mutation reduced the release of the soluble APP fragment (sAPPβ), which is processed
Autor:
Seiko Ishihara, Mika Nobuhara, Toru Sasaki, Nobuto Kakuda, Kiyotaka Nishikawa, Takaomi C. Saido, Takashi Saito, Miho Watanabe-Takahashi, Satoru Funamoto, Yasuo Ihara, Tomohiro Miyasaka, Masaki Nakano
Publikováno v:
Nature Communications
Understanding the substrate recognition mechanism of γ-secretase is a key step for establishing substrate-specific inhibition of amyloid β-protein (Aβ) production. However, it is widely believed that γ-secretase is a promiscuous protease and that
Publikováno v:
Alzheimer's & Dementia. 6
Publikováno v:
Acta Neuropathologica Communications; 11/4/2015, Vol. 3 Issue 1, p1-12, 12p