Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates

about

Ultrasensitive Measurement of Ca2+ Influx into Lipid Vesicles Induced by Protein Aggregates

Item

http://www.wikidata.org/entity/Q57401266

description

im Mai 2017 veröffentlichter wissenschaftlicher Artikel

@de

wetenschappelijk artikel

@nl

наукова стаття, опублікована в травні 2017

@uk

name

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@en

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@nl

type

Item

label

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@en

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@nl

prefLabel

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@en

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@nl

P1476

Ultrasensitive Measurement of ...... Induced by Protein Aggregates

@en

P2093

Cécile Vincke

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

David C. Wirthensohn

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

Sonia Gandhi

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

Steven F. Lee

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

Suman De

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

Tuomas P. J. Knowles

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

P2860

The extracellular chaperone clusterin influences amyloid formation and toxicity by interacting with prefibrillar structures

Individual aggregates of amyloid beta induce temporary calcium influx through the cell membrane of neuronal cells.

Protein misfolding, functional amyloid, and human disease

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide

Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones

Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein

The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide

Aβ42 assembles into specific β-barrel pore-forming oligomers in membrane-mimicking environments.

Cerebrospinal fluid-induced retardation of amyloid β aggregation correlates with Alzheimer's disease and the APOE ε4 allele.

Encapsulation efficiency measured on single small unilamellar vesicles.

P304

7858-7862

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

P31

scholarly article

P356

10.1002/ANGE.201700966

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

P433

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

P478

129

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

P50

P577

2017-05-05T00:00:00Z

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