Search Results - "Maruko-Otake, Akiko" :: K.UTB vyhledávací portál | TBU Library Retrieval Portal

Ca2+/calmodulin-dependent protein kinase II promotes neurodegeneration caused by tau phosphorylated at Ser262/356 in a transgenic Drosophila model of tauopathy

Ca2+/calmodulin-dependent protein kinase II promotes neurodegeneration caused by tau phosphorylated at Ser262/356 in a transgenic Drosophila model of tauopathy

by Oka, Mikiko, Fujisaki, Naoki, Maruko-Otake, Akiko, Ohtake, Yosuke, Shimizu, Sawako, Saito, Taro, Hisanaga, Shin-Ichi, Iijima, Koichi M, Ando, Kanae
Published in Journal of biochemistry (Tokyo) (01.11.2017)

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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

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

by Ando, Kanae, Maruko-Otake, Akiko, Ohtake, Yosuke, Hayashishita, Motoki, Sekiya, Michiko, Iijima, Koichi M
Published in PLoS genetics (01.03.2016)

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Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1

Loss of axonal mitochondria promotes tau-mediated neurodegeneration and Alzheimer's disease-related tau phosphorylation via PAR-1

by Iijima-Ando, Kanae, Sekiya, Michiko, Maruko-Otake, Akiko, Ohtake, Yosuke, Suzuki, Emiko, Lu, Bingwei, Iijima, Koichi M
Published in PLoS genetics (01.08.2012)

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EDEM Function in ERAD Protects against Chronic ER Proteinopathy and Age-Related Physiological Decline in Drosophila

EDEM Function in ERAD Protects against Chronic ER Proteinopathy and Age-Related Physiological Decline in Drosophila

by Sekiya, Michiko, Maruko-Otake, Akiko, Hearn, Stephen, Sakakibara, Yasufumi, Fujisaki, Naoki, Suzuki, Emiko, Ando, Kanae, Iijima, Koichi M.
Published in Developmental cell (19.06.2017)

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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 A[beta]42-Induced Tau Toxicity

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and A[beta]42-Induced Tau Toxicity

by Ando, Kanae, Maruko-Otake, Akiko, Ohtake, Yosuke, Hayashishita, Motoki, Sekiya, Michiko, Iijima, Koichi M
Published in PLoS genetics (29.03.2016)

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Epigenetic modifications reveal an effective use of the protein quality control system to suppress accumulation and toxicity of beta-amyloid 42 in the secretory pathway in neurons

Epigenetic modifications reveal an effective use of the protein quality control system to suppress accumulation and toxicity of beta-amyloid 42 in the secretory pathway in neurons

by Iijima, Koichi, Sekiya, Michiko, Maruko-Otake, Akiko, Ando, Kanae
Published in Alzheimer's & dementia (01.07.2013)

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O1–01–02: Epigenetic modifications reveal an effective use of the protein quality control system to suppress accumulation and toxicity of beta‐amyloid 42 in the secretory pathway in neurons

O1–01–02: Epigenetic modifications reveal an effective use of the protein quality control system to suppress accumulation and toxicity of beta‐amyloid 42 in the secretory pathway in neurons

by Iijima, Koichi, Sekiya, Michiko, Maruko‐Otake, Akiko, Ando, Kanae
Published in Alzheimer's & dementia (01.07.2013)

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O3–02–04: A novel mechanism by which beta‐amyloid 42 initiates mitochondrial abnormality in the synapse

O3–02–04: A novel mechanism by which beta‐amyloid 42 initiates mitochondrial abnormality in the synapse

by Sekiya, Michiko, Maruko‐Otake, Akiko, Suzuki, Emiko, Ando, Kanae, Iijima, Koichi
Published in Alzheimer's & dementia (01.07.2013)

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A novel mechanism by which beta-amyloid 42 initiates mitochondrial abnormality in the synapse

A novel mechanism by which beta-amyloid 42 initiates mitochondrial abnormality in the synapse

by Sekiya, Michiko, Maruko-Otake, Akiko, Suzuki, Emiko, Ando, Kanae, Iijima, Koichi
Published in Alzheimer's & dementia (01.07.2013)

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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 A square 42-Induced Tau Toxicity

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and A square 42-Induced Tau Toxicity

by Ando, Kanae, Maruko-Otake, Akiko, Ohtake, Yosuke, Hayashishita, Motoki, Sekiya, Michiko, Iijima, Koichi M
Published in PLoS genetics (01.03.2016)

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