Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

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Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

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2018 nî lūn-bûn

@nan

2018年の論文

@ja

2018年学术文章

@wuu

2018年学术文章

@zh

2018年学术文章

@zh-cn

2018年学术文章

@zh-hans

2018年学术文章

@zh-my

2018年学术文章

@zh-sg

2018年學術文章

@yue

2018年學術文章

@zh-hant

name

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@en

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@nl

type

Item

label

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@en

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@nl

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Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@en

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@nl

P1476

Nature of Tau-Associated Neurodegeneration and the Molecular Mechanisms.

@en

P2093

Jian-Zhi Wang

http://www.w3.org/2001/XMLSchema#string

Ying Yang

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P275

Creative Commons Attribution-NonCommercial 4.0 License

P2860

Hyperphosphorylation induces self-assembly of tau into tangles of paired helical filaments/straight filaments

Human wild-type full-length tau accumulation disrupts mitochondrial dynamics and the functions via increasing mitofusins.

Opposite monosynaptic scaling of BLP-vCA1 inputs governs hopefulness- and helplessness-modulated spatial learning and memory

Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase

Magnesium protects cognitive functions and synaptic plasticity in streptozotocin-induced sporadic Alzheimer's model

Protein phosphatase 2A facilitates axonogenesis by dephosphorylating CRMP2

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

Paternal spatial training enhances offspring's cognitive performance and synaptic plasticity in wild-type but not improve memory deficit in Alzheimer's mice.

Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer's disease.

Silencing PP2A inhibitor by lenti-shRNA interference ameliorates neuropathologies and memory deficits in tg2576 mice.

P304

1305-1317

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P31

scholarly article

review article

P356

10.3233/JAD-170788

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2018-01-01T00:00:00Z

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P698

29562535

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P921

nerve degeneration

cytoskeletal proteins

nerve tissue proteins

P932

5870018

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