Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes (Q34374310)

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10 February 2020

title

Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes (English)

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10 February 2020

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1 reference

2

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10 February 2020

Armin Giese

5

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10 February 2020

author name string

Felix Schmidt

1

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10 February 2020

Frits Kamp

3

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10 February 2020

Hans Kretzschmar

4

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10 February 2020

Kai Bötzel

6

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10 February 2020

language of work or name

English

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publication date

3 August 2012

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10 February 2020

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10 February 2020

volume

7

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10 February 2020

issue

8

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10 February 2020

page(s)

e42545

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Creative Commons Attribution 4.0 International

10 February 2020

copyright license

start time

3 August 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

Two different binding modes of α-synuclein to lipid vesicles depending on its aggregation state

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

6 July 2018

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Inhibition of mitochondrial fusion by α-synuclein is rescued by PINK1, Parkin and DJ-1.

6 July 2018

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Converse modulation of toxic alpha-synuclein oligomers in living cells by N'-benzylidene-benzohydrazide derivates and ferric iron

6 July 2018

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6 July 2018

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Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System

6 July 2018

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

6 July 2018

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6 July 2018

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Function and modulation of bacterial porins: insights from electrophysiology

6 July 2018

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Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore

6 July 2018

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Ion selectivity of gram-negative bacterial porins

6 July 2018

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Pore formation by the Escherichia coli hemolysin: evidence for an association-dissociation equilibrium of the pore-forming aggregates

6 July 2018

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Characterisation of channels induced in planar bilayer membranes by detergent solubilised Escherichia coli porins.

6 July 2018

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Generation of ferric iron links oxidative stress to α-synuclein oligomer formation

6 July 2018

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Mechanism of membrane interaction and disruption by α-synuclein.

27 October 2018

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AMPA-receptor-mediated excitatory synaptic transmission is enhanced by iron-induced α-synuclein oligomers

27 October 2018

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Single particle characterization of iron-induced pore-forming alpha-synuclein oligomers

27 October 2018

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The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils

27 October 2018

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Alpha-synuclein has a high affinity for packing defects in a bilayer membrane: a thermodynamics study

27 October 2018

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Golgi fragmentation occurs in the cells with prefibrillar alpha-synuclein aggregates and precedes the formation of fibrillar inclusion

27 October 2018

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Asymmetry of orientation and voltage gating of the Acidovorax delafieldii porin Omp34 in lipid bilayers

27 October 2018

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Polyphenolic compounds are novel protective agents against lipid membrane damage by α-synuclein aggregates in vitro

27 October 2018

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PubMed

https://pubmed.ncbi.nlm.nih.gov/22880029

12 December 2020

inferred from PubMed ID database lookup

Increased iron (III) and total iron content in post mortem substantia nigra of parkinsonian brain

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22880029

12 December 2020

inferred from PubMed ID database lookup

The structure of Staphylococcus aureus alpha-toxin-induced ionic channel

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/22880029

12 December 2020

inferred from PubMed ID database lookup

Identifiers

DOI

10.1371/JOURNAL.PONE.0042545

1 reference

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10 February 2020

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Fatcat

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24 November 2022

mapped directly with Wikidata item

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10 February 2020

PubMed publication ID

22880029

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