Výsledky vyhledávání - "Motoki Hayashishita"

Akademický článek

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity.

Autor: Kanae Ando, Akiko Maruko-Otake, Yosuke Ohtake, Motoki Hayashishita, Michiko Sekiya, Koichi M Iijima

Publikováno v: PLoS Genetics, Vol 12, Iss 3, p e1005917 (2016)

Abnormal accumulation of the microtubule-interacting protein tau is associated with neurodegenerative diseases including Alzheimer's disease (AD). β-amyloid (Aβ) lies upstream of abnormal tau behavior, including detachment from microtubules, phosph

Externí odkaz: https://doaj.org/article/18e3fc9c09d0432693cd26eb85b17eaa

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S6K/p70S6K1 protects against tau-mediated neurodegeneration by decreasing the level of tau phosphorylated at Ser262 in a Drosophila model of tauopathy

Autor: Taro Saito, Motoki Hayashishita, Sawako Shimizu, Tomoki Chiku, Yosuke Ohtake, Akiko Asada, Kanae Ando, Koichi M. Iijima, Kanako Shinno, Mikiko Oka, Shin-ichi Hisanaga

Publikováno v: Neurobiology of aging. 71

Abnormal accumulation of the microtubule-associated protein tau is thought to cause neuronal cell death in a group of age-associated neurodegenerative disorders. Tau is phosphorylated at multiple sites in diseased brains, and phosphorylation of tau a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af5217430ccef560e2e98822a0e2b86f
https://pubmed.ncbi.nlm.nih.gov/30172839

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Tau phosphorylation at Alzheimer's disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated

Autor: Koichi M. Iijima, Sawako Shimizu, Mikiko Oka, Kanae Ando, Yosuke Ohtake, Shin-ichi Hisanaga, Motoki Hayashishita

Publikováno v: Biochemical and biophysical research communications. 478(2)

Abnormal phosphorylation of the microtubule-associated protein tau is observed in many neurodegenerative diseases, including Alzheimer's disease (AD). AD-related phosphorylation of two tau residues, Ser262 and Ser356, by PAR-1/MARK stabilizes tau in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60a2d17e8f0c4f34848f394fb3670424
https://pubmed.ncbi.nlm.nih.gov/27520376

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Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity

Autor: Kanae Ando, Yosuke Ohtake, Motoki Hayashishita, Akiko Maruko-Otake, Michiko Sekiya, Koichi M. Iijima

Publikováno v: PLoS Genetics
PLoS Genetics, Vol 12, Iss 3, p e1005917 (2016)

Abnormal accumulation of the microtubule-interacting protein tau is associated with neurodegenerative diseases including Alzheimer’s disease (AD). β-amyloid (Aβ) lies upstream of abnormal tau behavior, including detachment from microtubules, phos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2290e46f1aa152c7540cb6c97702560a
https://pubmed.ncbi.nlm.nih.gov/27023670

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Akademický článek

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of ADRelated Phosphorylation and Aβ42-Induced Tau Toxicity.

Autor: Kanae Ando, Akiko Maruko-Otake, Yosuke Ohtake, Motoki Hayashishita, Michiko Sekiya, Iijima, Koichi M.

Publikováno v: PLoS Genetics; 3/29/2016, Vol. 12 Issue 3, p1-28, 28p

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