(Q38041484)

27 August 2017

title

α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions (English)

1 reference

27 August 2017

1 reference

Martin T Stöckl

1

1 reference

27 August 2017

Niels Zijlstra

series ordinal

2

1 reference

27 August 2017

Vinod Subramaniam

series ordinal

3

1 reference

27 August 2017

publication date

6 September 2012

1 reference

27 August 2017

published in

Molecular Neurobiology

1 reference

27 August 2017

volume

47

1 reference

27 August 2017

issue

2

1 reference

27 August 2017

page(s)

613-621

1 reference

Protein misfolding, functional amyloid, and human disease

27 August 2017

cites work

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Mysterious oligomerization of the amyloidogenic proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

What drives amyloid molecules to assemble into oligomers and fibrils?

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

3D structure of Alzheimer's amyloid-beta(1-42) fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

The aggregation and fibrillation of alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Morphology and toxicity of Abeta-(1-42) dimer derived from neuritic and vascular amyloid deposits of Alzheimer's disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Different species of alpha-synuclein oligomers induce calcium influx and seeding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Neurodegenerative disease: amyloid pores from pathogenic mutations

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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/10.1007%2FS12035-012-8331-4

Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

In vivo demonstration that alpha-synuclein oligomers are toxic

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Imaging nanometer-sized α-synuclein aggregates by superresolution fluorescence localization microscopy.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

The structure of dopamine induced alpha-synuclein oligomers.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

The lipid peroxidation products 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote the formation of α-synuclein oligomers with distinct biochemical, morphological, and functional properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Characterization of oligomeric intermediates in alpha-synuclein fibrillation: FRET studies of Y125W/Y133F/Y136F alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Structural characteristics of alpha-synuclein oligomers stabilized by the flavonoid baicalein

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Rapid self-assembly of alpha-synuclein observed by in situ atomic force microscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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/10.1007%2FS12035-012-8331-4

Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Calcium(II) selectively induces alpha-synuclein annular oligomers via interaction with the C-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Lipid bilayer disruption by oligomeric alpha-synuclein depends on bilayer charge and accessibility of the hydrophobic core.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Tryptophan fluorescence reveals structural features of alpha-synuclein oligomers

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Characterization of oligomers during alpha-synuclein aggregation using intrinsic tryptophan fluorescence

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Spontaneous curvature of phosphatidic acid and lysophosphatidic acid.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Examining the contributions of lipid shape and headgroup charge on bilayer behavior

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Locally resolved membrane binding affinity of the N-terminus of α-synuclein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

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/10.1007%2FS12035-012-8331-4

Soluble amyloid oligomers increase bilayer conductance by altering dielectric structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Structural properties of pore-forming oligomers of alpha-synuclein

21 January 2018

1 reference

https://api.crossref.org/works/10.1007%2FS12035-012-8331-4

Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease?

21 January 2018

1 reference

12 December 2020

alpha-Synuclein membrane interactions and lipid specificity

1 reference

12 December 2020

Polymorphic phase behavior of cardiolipin derivatives studied by 31P NMR and X-ray diffraction

1 reference

12 December 2020

Molecular composition of sub-stoichiometrically labeled α-synuclein oligomers determined by single-molecule photobleaching

1 reference

12 December 2020

Kinetic measurements give new insights into lipid membrane permeabilization by α-synuclein oligomers

1 reference

12 December 2020

Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway

1 reference

12 December 2020

Secondary structure of alpha-synuclein oligomers: characterization by raman and atomic force microscopy

1 reference

12 December 2020

Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?

1 reference

12 December 2020

10.1007/S12035-012-8331-4

Identifiers

DOI

1 reference

Dimensions Publication ID

27 August 2017

1000101004

0 references

1 reference