(Q44120459)

30 November 2017

Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing (English)

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30 November 2017

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Bart D van Rooijen

1

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30 November 2017

Mireille M A E Claessens

series ordinal

2

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30 November 2017

Vinod Subramaniam

series ordinal

3

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30 November 2017

language of work or name

English

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publication date

16 October 2008

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30 November 2017

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30 November 2017

582

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30 November 2017

27

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30 November 2017

3788-3792

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The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease.

30 November 2017

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Alpha-synuclein in Lewy bodies

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Physiological and pathological properties of alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Quantification of alpha-synuclein binding to lipid vesicles using fluorescence correlation spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Conformational properties of alpha-synuclein in its free and lipid-associated states

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Neurodegenerative disease: amyloid pores from pathogenic mutations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Amyloid ion channels: a common structural link for protein-misfolding disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Vesicle permeabilization by protofibrillar alpha-synuclein is sensitive to Parkinson's disease-linked mutations and occurs by a pore-like mechanism.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Quantitative morphological analysis reveals ultrastructural diversity of amyloid fibrils from alpha-synuclein mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

What's so special about cholesterol?

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

Formation of a High Affinity Lipid-Binding Intermediate during the Early Aggregation Phase of α-Synuclein†

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2008.10.009

10.1016/J.FEBSLET.2008.10.009

21 January 2018

Identifiers

DOI

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30 November 2017

1 reference