Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.
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Conformational equilibria in monomeric alpha-synuclein at the single-molecule levelDefinition of a molecular pathway mediating α-synuclein neurotoxicityα-Synuclein assembles into higher-order multimers upon membrane binding to promote SNARE complex formationSystematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activitiesDynamic -Helix Structure of Micelle-bound Human AmylinThree-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR SpectroscopyA Combinatorial NMR and EPR Approach for Evaluating the Structural Ensemble of Partially Folded ProteinsA CC-SAM, for coiled coil-sterile α motif, domain targets the scaffold KSR-1 to specific sites in the plasma membraneBiophysics of α-synuclein membrane interactions.Dynamic transport and localization of alpha-synuclein in primary hippocampal neurons.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactionsAssessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy.Membrane-Induced Folding of the Plant Stress Dehydrin Lti30.NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC regionDifferential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopyThe lipid-binding domain of wild type and mutant alpha-synuclein: compactness and interconversion between the broken and extended helix forms.Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregationMonomeric synucleins generate membrane curvature.Probing the micelle-bound aggregation-prone state of α-synuclein with (19)F NMR spectroscopyAcute increase of α-synuclein inhibits synaptic vesicle recycling evoked during intense stimulation.The N-terminus of the intrinsically disordered protein α-synuclein triggers membrane binding and helix folding.Alpha-synuclein function and dysfunction on cellular membranes.Alpha-synuclein populates both elongated and broken helix states on small unilamellar vesicles.Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour.Parkinson's Protein α-Synuclein Binds Efficiently and with a Novel Conformation to Two Natural Membrane MimicsCysteine cathepsins are essential in lysosomal degradation of α-synuclein.α-synuclein-lanthanide metal ions interaction: binding sites, conformation and fibrillationNMR study of the tetrameric KcsA potassium channel in detergent micelles.Mitochondrial import and accumulation of alpha-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain.Modulating the Amyloidogenesis of α-SynucleinCurvature dynamics of alpha-synuclein familial Parkinson disease mutants: molecular simulations of the micelle- and bilayer-bound forms.The interplay between lipids and dopamine on α-synuclein oligomerization and membrane binding.Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopyStructural basis of synaptic vesicle assembly promoted by α-synuclein.Effect of pseudorepeat rearrangement on alpha-synuclein misfolding, vesicle binding, and micelle bindingα-Synuclein posttranslational modification and alternative splicing as a trigger for neurodegeneration.An extracellular mechanism that can explain the neurotoxic effects of α-synuclein aggregates in the brainDT-diaphorase Protects Against Autophagy Induced by Aminochrome-Dependent Alpha-Synuclein Oligomers.Alpha-synuclein: relating metals to structure, function and inhibition.
P2860
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P2860
Comparison of structure and dynamics of micelle-bound human alpha-synuclein and Parkinson disease variants.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
Comparison of structure and dy ...... nd Parkinson disease variants.
@en
Comparison of structure and dy ...... nd Parkinson disease variants.
@nl
type
label
Comparison of structure and dy ...... nd Parkinson disease variants.
@en
Comparison of structure and dy ...... nd Parkinson disease variants.
@nl
prefLabel
Comparison of structure and dy ...... nd Parkinson disease variants.
@en
Comparison of structure and dy ...... nd Parkinson disease variants.
@nl
P2860
P921
P356
P1476
Comparison of structure and dy ...... nd Parkinson disease variants.
@en
P2093
Tobias S Ulmer
P2860
P304
43179-43187
P356
10.1074/JBC.M507624200
P407
P577
2005-09-15T00:00:00Z