Liquid and Hydrogel Phases of PrP Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers

about

Liquid and Hydrogel Phases of PrP Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers

Item

http://www.wikidata.org/entity/Q58568468

description

im November 2018 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована в листопаді 2018

@uk

name

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@en

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@nl

type

Item

label

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@en

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@nl

prefLabel

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@en

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@nl

P1476

Liquid and Hydrogel Phases of ...... lzheimer's Amyloid-β Oligomers

@en

P2093

Erik C Gunther

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

Hideyuki Takahashi

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

Kurt W Zilm

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

Lauren E Klein

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

Marcus D Tuttle

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

Mikhail A Kostylev

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

Suho Lee

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

Timothy O Cox

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

P2860

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

A smoothed backbone-dependent rotamer library for proteins derived from adaptive kernel density estimates and regressions

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

The amyloid hypothesis of Alzheimer's disease at 25 years

NMR solution structure of the human prion protein

Influence of pH on NMR structure and stability of the human prion protein globular domain

The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site

Structural rearrangements at physiological pH: nuclear magnetic resonance insights from the V210I human prion protein mutant

Probing the N-terminal β-sheet conversion in the crystal structure of the human prion protein bound to a nanobody

P304

426-443.e12

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

P31

scholarly article

P356

10.1016/J.MOLCEL.2018.10.009

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

Stephen M. Strittmatter

P577

2018-11-01T00:00:00Z

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

P698

30401430

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

P921

molecular biology

hydrogel

P932

6226277

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