Wildtype and A30P mutant alpha-synuclein form different fibril structures. - Wikidata - wikimedia - TriplyDB

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

http://www.wikidata.org/entity/Q34825913

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Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions Unexpected improvements of spatial learning and memory abilities in chronic rotenone intoxicated mice.Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson's disease genetically related mutants A small-angle X-ray scattering study of alpha-synuclein from human red blood cells Dopaminergic Receptors on CD4+ T Naive and Memory Lymphocytes Correlate with Motor Impairment in Patients with Parkinson's Disease.Emerging applications of small angle solution scattering in structural biology.MpUL-multi: Software for Calculation of Amyloid Fibril Mass per Unit Length from TB-TEM Images Review: Spreading the word: precise animal models and validated methods are vital when evaluating prion-like behaviour of alpha-synuclein.Exercise and Nutritional Benefits in PD: Rodent Models and Clinical Settings.ɑ-Synuclein strains and the variable pathologies of synucleinopathies.α-Synuclein vaccination modulates regulatory T cell activation and microglia in the absence of brain pathology.Coupling of the non-amyloid-component (NAC) domain and the KTK(E/Q)GV repeats stabilize the α-synuclein fibrils.Cross-seeding of prions by aggregated α-synuclein leads to transmissible spongiform encephalopathy.Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth.C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets.SAS-Based Studies of Protein Fibrillation.Fluorescence spectroscopy reveals N-terminal order in fibrillar forms of α-synuclein.CD4 T cells react to local increase of α-synuclein in a pathology-associated variant-dependent manner and modify brain microglia in absence of brain pathology.Alpha-synuclein overexpression in the olfactory bulb initiates prodromal symptoms and pathology of Parkinson's disease Alpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study

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P2860

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

http://www.wikidata.org/entity/Q34825913

description

2013 nî lūn-bûn

@nan

2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@ast

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@en

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@nl

type

label

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@ast

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@en

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@nl

prefLabel

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@ast

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@en

Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@nl

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JOURNAL.PONE.0067713

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Wildtype and A30P mutant alpha-synuclein form different fibril structures.

@en

P2093

Anna Sigrid Pii Svane

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Francesca Macchi

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Gunna Christiansen

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

Lise Giehm

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

Niels Christian Nielsen

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

Samuele Raccosta

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

Søren Bang Nielsen

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P2860

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

Alpha-synuclein in Lewy bodies

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

Protein fiber linear dichroism for structure determination and kinetics in a low-volume, low-wavelength couette flow cell

The inhomogeneous structure of water at ambient conditions

Small-angle scattering and the structure of ambient liquid water.

Distinct hydration properties of wild-type and familial point mutant A53T of α-synuclein associated with Parkinson's disease.

Accelerated oligomerization by Parkinson's disease linked alpha-synuclein mutants.

Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein.

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e67713

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scholarly article

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10.1371/JOURNAL.PONE.0067713

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Bente Vestergaard

Annette Eva Langkilde

Lene B Oddershede

Anders Kyrsting

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2013-07-04T00:00:00Z

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