Different species of alpha-synuclein oligomers induce calcium influx and seeding. (Q52581429)

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title

Different species of alpha-synuclein oligomers induce calcium influx and seeding (English)

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Simon Moussaud

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Karin M Danzer

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author name string

Dorothea Haasen

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Anne R Karow

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Matthias Habeck

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Hans Kretzschmar

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Bastian Hengerer

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Marcus Kostka

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language of work or name

English

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publication date

1 August 2007

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published in

Journal of Neuroscience

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volume

27

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issue

34

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page(s)

9220-9232

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alpha-synuclein fibrillogenesis is nucleation-dependent. Implications for the pathogenesis of Parkinson's disease

3 January 2020

cites work

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Fluorescence-intensity distribution analysis and its application in biomolecular detection technology

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Structure of alpha-latrotoxin oligomers reveals that divalent cation-dependent tetramers form membrane pores

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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

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E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy

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Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders

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Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments

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Alzheimer's beta-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line

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

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

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

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Alpha-synuclein and neurodegenerative diseases

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Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure

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

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Dysregulation of cellular calcium homeostasis in Alzheimer's disease: bad genes and bad habits

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Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease

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

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Neurodegenerative disease: amyloid pores from pathogenic mutations

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Dependence of alpha-synuclein aggregate morphology on solution conditions

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

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

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Staging of brain pathology related to sporadic Parkinson's disease

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Beta-synuclein inhibits formation of alpha-synuclein protofibrils: a possible therapeutic strategy against Parkinson's disease

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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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Parkinson's disease: mechanisms and models

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alpha-Synuclein locus triplication causes Parkinson's disease

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

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Architecture of the Alzheimer's A beta P ion channel pore

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

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Prefibrillar amyloid protein aggregates share common features of cytotoxicity.

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

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Endothelin receptor in virus-like particles: ligand binding observed by fluorescence fluctuation spectroscopy.

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Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.

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

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Alpha-synuclein locus duplication as a cause of familial Parkinson's disease

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Annular alpha-synuclein oligomers are potentially toxic agents in alpha-synucleinopathy. Hypothesis

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

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Single particle analysis of manganese-induced prion protein aggregates

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Intravesicular localization and exocytosis of alpha-synuclein and its aggregates.

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In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein.

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

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Comparison of G-protein coupled receptor desensitization-related beta-arrestin redistribution using confocal and non-confocal imaging

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12 December 2020

Detection of oligomeric forms of alpha-synuclein protein in human plasma as a potential biomarker for Parkinson's disease

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12 December 2020

Amino acid sequence motifs and mechanistic features of the membrane translocation of alpha-synuclein

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12 December 2020

Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases

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12 December 2020

Plasma membrane ion permeability induced by mutant alpha-synuclein contributes to the degeneration of neural cells

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12 December 2020

Automated high content screening for phosphoinositide 3 kinase inhibition using an AKT 1 redistribution assay.

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12 December 2020

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

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12 December 2020

Conformation-dependent anti-amyloid oligomer antibodies

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12 December 2020

Alpha-synuclein potentiates Ca2 influx through voltage-dependent Ca2 channels

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12 December 2020

Dynamics of alpha-synuclein aggregation and inhibition of pore-like oligomer development by beta-synuclein

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12 December 2020

beta-Amyloid peptide decreases membrane fluidity.

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Molecular membrane interactions of a phospholipid metabolite. Implications for Alzheimer's disease pathophysiology.

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

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Lipid Binding to Amyloid β‐Peptide Aggregates: Preferential Binding of Cholesterol as Compared with Phosphatidylcholine and Fatty Acids

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Staphylococcal α-Toxin: Formation of the Heptameric Pore Is Partially Cooperative and Proceeds through Multiple Intermediate Stages

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

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10.1523/JNEUROSCI.2617-07.2007

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17715357 AND SRC:MED&resulttype=core&format=json

3 January 2020

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3 January 2020

PubMed publication ID

17715357

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