Intravenously Injected Amyloid-β Peptide With Isomerized Asp7 and Phosphorylated Ser8 Residues Inhibits Cerebral β-Amyloidosis in AβPP/PS1 Transgenic Mice Model of Alzheimer's Disease

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Intravenously Injected Amyloid-β Peptide With Isomerized Asp7 and Phosphorylated Ser8 Residues Inhibits Cerebral β-Amyloidosis in AβPP/PS1 Transgenic Mice Model of Alzheimer's Disease

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http://www.wikidata.org/entity/Q57721642

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im Januar 2018 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована у 2018

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ശാസ്ത്രപ്രബന്ധം

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name

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

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Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

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Item

label

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

@en

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

@nl

prefLabel

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

@en

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

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P1476

Intravenously Injected Amyloid ...... e Model of Alzheimer's Disease

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P2093

Alexander A Makarov

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Alexander S Chernov

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Alexei A Adzhubei

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Evgeny P Barykin

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Georgy B Telegin

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Sergey P Radko

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Vladimir A Mitkevich

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P2860

Extracellular phosphorylation of the amyloid β-peptide promotes formation of toxic aggregates during the pathogenesis of Alzheimer's disease.

beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease

NMR solution structure of rat aβ(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

Three dimensions of the amyloid hypothesis: time, space and 'wingmen'

Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

Synthesis, aggregation, and neurotoxicity of the Alzheimer's Abeta1-42 amyloid peptide and its isoaspartyl isomers.

Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging.

Zinc ions promote Alzheimer Abeta aggregation via population shift of polymorphic states.

Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.

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518

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scholarly article

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10.3389/FNINS.2018.00518

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English

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Sergey Kozin

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2018-01-01T00:00:00Z

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P698

30210271

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P921

phosphorylation

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6119768

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