Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

about

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

Item

http://www.wikidata.org/entity/Q52325908

description

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

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@en

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@nl

type

Item

label

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@en

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@nl

prefLabel

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@en

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@nl

P1476

Dimerization of the cellular prion protein inhibits propagation of scrapie prions.

@en

P2093

Anika Gonsberg

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

Anna D Engelke

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

Martin Engelhard

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

Michael Baier

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

Ralf P Seidel

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

Sarah Ulbrich

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

Simrika Thapa

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

P2860

Prion Protein Biology

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

Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease

Prion diseases of humans and animals: their causes and molecular basis

Mice devoid of PrP are resistant to scrapie

Anchorless prion protein results in infectious amyloid disease without clinical scrapie

Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein

Prion protein attenuates excitotoxicity by inhibiting NMDA receptors

GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.

The N-terminus of the prion protein is a toxic effector regulated by the C-terminus.

P304

8020-8031

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

P31

scholarly article

P356

10.1074/JBC.RA117.000990

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

P407

English

P433

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

P478

293

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

P50

Konstanze F Winklhofer

P577

2018-04-10T00:00:00Z

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

P698

29636413

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

P921

Prion protein family

P932

5971439

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