Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.

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Structural and mechanistic aspects influencing the ADAM10-mediated shedding of the prion protein.Cellular Receptors of Amyloid β Oligomers (AβOs) in Alzheimer's Disease Prions activate a p38 MAPK synaptotoxic signaling pathway

P2860

Q52602016-A81454BA-8BC1-4C7C-BE42-0E56BDFEB2E5 Q57779647-0D1F0CA7-FA36-4305-9234-42D670419269 Q58712857-41D65107-456E-40E6-816C-0A6A0DD8DAE6

P2860

Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.

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http://www.wikidata.org/entity/Q46316131

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

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name

Cellular prion protein targets ...... domain to prevent elongation.

@en

Cellular prion protein targets ...... domain to prevent elongation.

@nl

type

Item

label

Cellular prion protein targets ...... domain to prevent elongation.

@en

Cellular prion protein targets ...... domain to prevent elongation.

@nl

prefLabel

Cellular prion protein targets ...... domain to prevent elongation.

@en

Cellular prion protein targets ...... domain to prevent elongation.

@nl

P1476

Cellular prion protein targets ...... domain to prevent elongation.

@en

P2093

Erin Bove-Fenderson

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

John E Straub

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

P2860

A Oligomer-Induced Aberrations in Synapse Composition, Shape, and Density Provide a Molecular Basis for Loss of Connectivity in Alzheimer's Disease

Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers

Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein

Synthetic amyloid-beta oligomers impair long-term memory independently of cellular prion protein

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Out-of-register -sheets suggest a pathway to toxic amyloid aggregates

Protein production by auto-induction in high density shaking cultures

Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation

Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons.

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

P304

16858-16871

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scholarly article

P356

10.1074/JBC.M117.789990

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

P407

English

P433

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

P478

292

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

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David A Harris

Ryo Urano

P577

2017-08-23T00:00:00Z

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

P698

28842494

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

P921

Prion protein family

P932

5641888

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

Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.

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P2860

P2860

Cellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P921

P932