α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers.
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Versatile Structures of α-SynucleinAlpha-synuclein Toxicity in the Early Secretory Pathway: How It Drives Neurodegeneration in Parkinsons DiseaseBiophysical characterization of α-synuclein and its controversial structureNMR Structure of Calmodulin Complexed to an N-Terminally Acetylated α-Synuclein PeptideMembrane remodeling and mechanics: Experiments and simulations of α-SynucleinAlpha-synuclein spreading in Parkinson's diseaseThe Effects of Macromolecular Crowding on Calmodulin Structure and Function.Nonaggregated α-synuclein influences SNARE-dependent vesicle docking via membrane binding.Synucleins regulate the kinetics of synaptic vesicle endocytosis.Alpha-synuclein function and dysfunction on cellular membranes.Purification of α-synuclein from human brain reveals an instability of endogenous multimers as the protein approaches purity.N-alpha-acetylation of α-synuclein increases its helical folding propensity, GM1 binding specificity and resistance to aggregation.α-Synuclein Reduces Tension and Increases Undulations in Simulations of Small Unilamellar Vesicles.β-Amyloid and α-synuclein cooperate to block SNARE-dependent vesicle fusionBiophysics of α-synuclein induced membrane remodellingAggregated Alpha-Synuclein Transfer Efficiently between Cultured Human Neuron-Like Cells and Localize to Lysosomesα-Synuclein oligomers with broken helical conformation form lipoprotein nanoparticles.Membrane remodeling by α-synuclein and effects on amyloid formation.The function of α-synuclein.Studies of protein folding and dynamics using single molecule fluorescence spectroscopy.Impaired intracellular trafficking defines early Parkinson's diseaseSynaptic failure and α-synuclein.Calcium: Alpha-Synuclein Interactions in Alpha-Synucleinopathies.The Multifaceted Role of SNARE Proteins in Membrane Fusion.Synaptic Vesicle-Recycling Machinery Components as Potential Therapeutic Targets.α-Synuclein promotes dilation of the exocytotic fusion pore.The Neuroprotective Role of Protein Quality Control in Halting the Development of Alpha-Synuclein Pathology.Membrane bound α-synuclein is fully embedded in the lipid bilayer while segments with higher flexibility remain.Distinct α-Synuclein strains and implications for heterogeneity among α-Synucleinopathies.Stimulation of synaptoneurosome glutamate release by monomeric and fibrillated α-synuclein.Rationally Designed Variants of α-Synuclein Illuminate Its Structural Properties in Health and Disease
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P2860
α-Synuclein can inhibit SNARE-mediated vesicle fusion through direct interactions with lipid bilayers.
description
2013 nî lūn-bûn
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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
2013年论文
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2013年论文
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name
α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
@en
type
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α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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prefLabel
α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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P2860
P356
P1433
P1476
α-Synuclein can inhibit SNARE- ...... eractions with lipid bilayers.
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P2093
David C DeWitt
Elizabeth Rhoades
P2860
P304
P356
10.1021/BI4002369
P407
P577
2013-03-27T00:00:00Z