Wildtype and A30P mutant alpha-synuclein form different fibril structures.
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Molecular determinants of α-synuclein mutants' oligomerization and membrane interactionsUnexpected 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 mutantsA small-angle X-ray scattering study of alpha-synuclein from human red blood cellsDopaminergic 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 ImagesReview: 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 diseaseAlpha-synuclein oligomers and fibrils originate in two distinct conformer pools: a small angle X-ray scattering and ensemble optimisation modelling study
P2860
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P2860
Wildtype and A30P mutant alpha-synuclein form different fibril structures.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
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
P2093
P2860
P50
P1433
P1476
Wildtype and A30P mutant alpha-synuclein form different fibril structures.
@en
P2093
Anna Sigrid Pii Svane
Francesca Macchi
Gunna Christiansen
Lise Giehm
Niels Christian Nielsen
Samuele Raccosta
Søren Bang Nielsen
P2860
P304
P356
10.1371/JOURNAL.PONE.0067713
P407
P577
2013-07-04T00:00:00Z