Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing (Q44120459)

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scientific article published on 16 October 2008

Membrane binding of oligomeric α-synuclein depends on bilayer charge and packing

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English	Membrane binding of oligomeric alpha-synuclein depends on bilayer charge and packing	scientific article published on 16 October 2008	Membrane binding of oligomeric α-synuclein depends on bilayer charge and packing

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scholarly article

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Europe PubMed Central

PubMed publication ID

30 November 2017

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

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Europe PubMed Central

PubMed publication ID

30 November 2017

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based on heuristic

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Bart D van Rooijen

1

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Europe PubMed Central

PubMed publication ID

30 November 2017

Mireille M A E Claessens

2

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Europe PubMed Central

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30 November 2017

Vinod Subramaniam

3

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Europe PubMed Central

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30 November 2017

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publication date

16 October 2008

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Europe PubMed Central

PubMed publication ID

30 November 2017

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Europe PubMed Central

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30 November 2017

582

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Europe PubMed Central

PubMed publication ID

30 November 2017

27

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Europe PubMed Central

PubMed publication ID

30 November 2017

3788-3792

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

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

1 reference

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

21 January 2018

α-Synuclein in Lewy bodies

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

Physiological and pathological properties of alpha-synuclein

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

Neurodegenerative disease: amyloid pores from pathogenic mutations

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

What's so special about cholesterol?

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

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

1 reference

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

21 January 2018

Identifiers

10.1016/J.FEBSLET.2008.10.009

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 November 2017

ResearchGate publication ID

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