Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

about

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

Item

http://www.wikidata.org/entity/Q58795353

description

im August 2018 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published on 08 August 2018

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2018

@uk

name

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@en

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@nl

type

Item

label

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@en

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@nl

prefLabel

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@en

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@nl

P1476

Prion acute synaptotoxicity is largely driven by protease-resistant PrPSc species

@en

P2093

Feng Chen

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

Harold Arthur Coleman

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

Matteo Senesi

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

Paul Anthony Adlard

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

Shannon Sarros

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

Victoria Lewis

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

P2860

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

Synaptophysin, a major synaptic vesicle protein, is not essential for neurotransmitter release

Hijacking PrP(c)-dependent signal transduction: when prions impair Aβ clearance

PK-sensitive PrP is infectious and shares basic structural features with PK-resistant PrP

Essential roles in synaptic plasticity for synaptogyrin I and synaptophysin I

Evidence of presynaptic location and function of the prion protein

Mice devoid of prion protein have cognitive deficits that are rescued by reconstitution of PrP in neurons

Mice devoid of PrP are resistant to scrapie

Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway

Dendritic spine changes associated with hippocampal long-term synaptic plasticity

P304

e1007214

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

P31

scholarly article

P356

10.1371/JOURNAL.PPAT.1007214

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

P407

English

P433

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

P478

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

P50

Simote Totauhelotu Foliaki

Abu Mohammed Taufiqual Islam

P577

2018-08-08T00:00:00Z

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

P698

30089152

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

P921

P932

6101418

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