Výsledky vyhledávání - "Ryong-Woon Shin"

Reduction of β-Amyloid Accumulation by Reticulon 3 in Transgenic Mice

Autor: Masayuki Itoh, Akiko Oda, Shigeki Yuasa, Yoshihiro Konishi, Akira Tamaoka, Kotaro Hattori, Wataru Araki, Koichi Ogino, Kazumi Motoki, Ryong-Woon Shin

Publikováno v: Current Alzheimer Research. 10:135-142

Inhibition of the β-secretase, BACE1, which cleaves amyloid precursor protein (APP) to produce β-amyloid protein (Aβ), is thought to be a feasible therapeutic strategy for Alzheimer's disease. Reticulon (RTN) proteins such as RTN3 have been identi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f2c94faf657fd3248ecf4b589c6fac1
https://doi.org/10.2174/1567205011310020003

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Age-dependent increase in lysosome-associated membrane protein 1 and early-onset behavioral deficits in APPSL transgenic mouse model of Alzheimer's disease

Autor: Tetsuya Hashimoto, Ryong Woon Shin, Noriaki Shimizu, Tetsuro Kikuchi, Tetsuyuki Kitamoto, Koichi Ogino

Publikováno v: Neuroscience Letters. 469:273-277

Amyloid precursor protein (APP) is strongly related to the onset of Alzheimer's disease. It possesses cleavage sites for beta- and gamma-secretases, and the resulting cleaved products (amyloid-beta peptides) are capable of causing neurotoxicity. Such

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e64afbeb324bbfc1e7fd6ef95aa1d9b2
https://doi.org/10.1016/j.neulet.2009.12.015

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A Novel Role for hGas7b in Microtubular Maintenance

Autor: Hiroyuki Arai, Aina Gotoh, Chiyoko Uchida, Ryong Woon Shin, Takafumi Uchida, Akira Sawa, Akihiro Harada, Tomoe Koga, Hirotada Akiyama, Tsubasa Ohashi, Wataru Sakamoto

Publikováno v: Journal of Biological Chemistry. 284:32695-32699

Here, we report a novel role for hGas7b (human growth arrest specific protein 7b) in the regulation of microtubules. Using a bioinformatic approach, we studied the actin-binding protein hGas7b with a structural similarity to the WW domain of a peptid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c637d75afb360400a2419adf35aa989c
https://doi.org/10.1074/jbc.m109.035998

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Amyloid precursor protein cytoplasmic domain with phospho-Thr668 accumulates in Alzheimer’s disease and its transgenic models: a role to mediate interaction of Aβ and tau

Autor: Ryong Woon Shin, Alfredo Shimabuku, Tetsuyuki Kitamoto, Hanae Nakashima, Koichi Ogino, Takeshi Ishihara, Takao Taki

Publikováno v: Acta Neuropathologica. 113:627-636

Abnormal accumulation of Abeta and tau in senile plaques (SP) and neurofibrillary tangles (NFTs) is a key event in Alzheimer's disease (AD). Here, we show that T668-phosphorylated cytoplasmic domain of APP (pT668-ACD) accumulates Abeta and tau in AD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ecf4e571b0a0f6d379c19d537de8fa6
https://doi.org/10.1007/s00401-007-0211-z

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[Untitled]

Autor: Ryong-Woon SHIN, Hirotada AKIYAMA, Takafumi UCHIDA

Publikováno v: Kagaku To Seibutsu. 44:447-452

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f3e1f1780446d93fdbf67f3a4f5ab506
https://doi.org/10.1271/kagakutoseibutsu1962.44.447

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Pin1 promotes production of Alzheimer’s amyloid β from β-cleaved amyloid precursor protein

Autor: Takafumi Uchida, Chiyoko Uchida, Tetsuyuki Kitamoto, Ryong Woon Shin, Hirotada Akiyama

Publikováno v: Biochemical and Biophysical Research Communications. 336:521-529

Here we show that prolyl isomerase Pin1 is involved in the Abeta production central to the pathogenesis of Alzheimer's disease. Enzyme immunoassay of brains of the Pin1-deficient mice revealed that production of Abeta40 and Abeta42 was lower than tha

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4da26cceefcd108230466e7e6acd0f68
https://doi.org/10.1016/j.bbrc.2005.08.130

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Iron (III) induces aggregation of hyperphosphorylated τ and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease

Autor: Fumio Yoshimasu, Hironobu Naiki, Akira Yamamoto, Tetsuyuki Kitamoto, Ryong-Woon Shin, Hiroyuki Sato, Kazuhiro Hasegawa

Publikováno v: Journal of Neurochemistry. 82:1137-1147

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1d121cba4918acaa3856ed4926419f63
https://doi.org/10.1046/j.1471-4159.2002.t01-1-01061.x

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NEDD8 protein is involved in ubiquitinated inclusion bodies

Autor: Ryong-Woon Shin, Afroz Dil Kuazi, Norifumi Ueda, Tetsu Kamitani, Yasuhito Abe, Katsumi Kito

Publikováno v: The Journal of Pathology. 199:259-266

Proteolysis by the ubiquitin-proteasome system is considered to play a pathological role in several degenerative diseases that involve ubiquitinated inclusion bodies. In recent years, several ubiquitin-like proteins have been isolated, but it is unce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a908ea2b084d3028485d90f1847b1c2
https://doi.org/10.1002/path.1283

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