Single particle characterization of iron-induced pore-forming alpha-synuclein oligomers. - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q46765690

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Alzheimer's disease as homeostatic responses to age-related myelin breakdown Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds Confocal Spectroscopy to Study Dimerization, Oligomerization and Aggregation of Proteins: A Practical Guide Dynamic structural flexibility of α-synuclein Function and dysfunction of α-synuclein: probing conformational changes and aggregation by single molecule fluorescence Membrane Permeabilization by Oligomeric α-Synuclein: In Search of the Mechanism Seeking a mechanism for the toxicity of oligomeric α-synuclein Dopamine and paraquat enhance α-synuclein-induced alterations in membrane conductance Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease.Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers Early aggregation steps in alpha-synuclein as measured by FCS and FRET: evidence for a contagious conformational change.Seeding and transgenic overexpression of alpha-synuclein triggers dendritic spine pathology in the neocortex Binding of alpha-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes.Detection of rotavirus in clinical specimens using an immunosensor prototype based on the photon burst counting technique.Baicalein reduces E46K alpha-synuclein aggregation in vitro and protects cells against E46K alpha-synuclein toxicity in cell models of familiar Parkinsonism.Unravelling the role of defective genes.Direct observation of the interconversion of normal and toxic forms of α-synuclein Structures formed by a cell membrane-associated arabinogalactan-protein on graphite or mica alone and with Yariv phenylglycosides.Single-channel electrophysiology reveals a distinct and uniform pore complex formed by α-synuclein oligomers in lipid membranes Abnormal mitochondrial dynamics, mitochondrial loss and mutant huntingtin oligomers in Huntington's disease: implications for selective neuronal damage.Prevalent iron metabolism gene variants associated with increased brain ferritin iron in healthy older men.Probing fibril dissolution of the repeat domain of a functional amyloid, Pmel17, on the microscopic and residue level Accelerated formation of alpha-synuclein oligomers by concerted action of the 20S proteasome and familial Parkinson mutations.Effect of EGCG on Fe(III)-induced conformational transition of silk fibroin, a model of protein related to neurodegenerative diseases.Heme Stabilization of α-Synuclein Oligomers during Amyloid Fibril Formation.Patterns of Brain Iron Accumulation in Vascular Dementia and Alzheimer's Dementia Using Quantitative Susceptibility Mapping Imaging.Phosphorylation of α-Synuclein at Y125 and S129 alters its metal binding properties: implications for understanding the role of α-Synuclein in the pathogenesis of Parkinson's Disease and related disorders X-ray fluorescence analysis of iron and manganese distribution in primary dopaminergic neurons A delicate balance: Iron metabolism and diseases of the brain.Molecular mechanisms of alpha-synuclein neurodegeneration.In vitro phosphorylation does not influence the aggregation kinetics of WT α-synuclein in contrast to its phosphorylation mutants.Metal Dyshomeostasis and Their Pathological Role in Prion and Prion-Like Diseases: The Basis for a Nutritional Approach.New Insights into the Crosstalk between NMDARs and Iron: Implications for Understanding Pathology of Neurological Diseases.Drug targets from genetics: α-synuclein.Role of metal ions in aggregation of intrinsically disordered proteins in neurodegenerative diseases.Interaction between pathogenic proteins in neurodegenerative disorders.α-Synuclein in Parkinson's disease.α-Synuclein and neuronal cell death.α-Synuclein oligomers: an amyloid pore? Insights into mechanisms of α-synuclein oligomer-lipid interactions.

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P2860

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

http://www.wikidata.org/entity/Q46765690

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

@yue

2008年學術文章

@zh-hant

name

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

@en

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

@nl

type

label

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

@en

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

@nl

prefLabel

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

@en

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

@nl

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P1433

Journal of Biological Chemistry

P1476

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

@en

P2093

Andreas Wirth

http://www.w3.org/2001/XMLSchema#string

Armin Giese

http://www.w3.org/2001/XMLSchema#string

Charles G Glabe

http://www.w3.org/2001/XMLSchema#string

Hans Kretzschmar

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Karin M Danzer

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Marcus Kostka

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Matthias Habeck

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Patrick Garidel

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Richard Wagner

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Sabine Finger

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P2860

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

alpha-Synuclein locus triplication causes Parkinson's disease

Alpha-synuclein in Lewy bodies

Alpha-synuclein and neurodegenerative diseases

Soluble Abeta oligomers ultrastructurally localize to cell processes and might be related to synaptic dysfunction in Alzheimer's disease brain

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

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

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

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

Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 --> Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice.

P304

10992-11003

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scholarly article

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10.1074/JBC.M709634200

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P433

16

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P478

283

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Christopher A Ross

P577

2008-02-07T00:00:00Z

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18258594

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