Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability.

about

Toxic HypF-N Oligomers Selectively Bind the Plasma Membrane to Impair Cell Adhesion Capability.

Item

http://www.wikidata.org/entity/Q51730305

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

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@en

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@nl

type

Item

label

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@en

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@nl

prefLabel

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@en

Toxic HypF-N Oligomers Selecti ...... pair Cell Adhesion Capability.

@nl

P1476

Toxic HypF-N Oligomers Selecti ...... mpair Cell Adhesion Capability

@en

P2093

Alberto Diaspro

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

Claudia Capitini

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

Fabrizio Chiti

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

Massimo Stefani

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

Reinier Oropesa-Nuñez

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

Sandeep Keshavan

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

Silvia Dante

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

P2860

Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice

Amyloid-β Receptors: The Good, the Bad, and the Prion Protein

Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism

A specific amyloid-beta protein assembly in the brain impairs memory

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.

Revealing early steps of alpha2beta1 integrin-mediated adhesion to collagen type I by using single-cell force spectroscopy.

Oligomeric amyloid beta associates with postsynaptic densities and correlates with excitatory synapse loss near senile plaques

Toxic fibrillar oligomers of amyloid-β have cross-β structure.

Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: an atomic force microscopy study.

P304

1357-1367

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

P31

scholarly article

P356

10.1016/J.BPJ.2018.02.003

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

P407

English

P433

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

P478

114

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

P50

Claudio Canale

Cristina Cecchi

Benedetta Mannini

P577

2018-03-01T00:00:00Z

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

P698

29590593

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

P932

5883620

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