Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein.
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Structures of the E46K mutant-type α-synuclein protein and impact of E46K mutation on the structures of the wild-type α-synuclein proteinAlpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recyclingFK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53Tc-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's diseaseResidual structure, backbone dynamics, and interactions within the synuclein familyPrediction of "hot spots" of aggregation in disease-linked polypeptidesGenetically engineered mouse models of Parkinson's diseasePropagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46KClustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentrationBiophysics of α-synuclein membrane interactions.α-Synuclein-induced tubule formation in lipid bilayersGlial A30P alpha-synuclein pathology segregates neurogenesis from anxiety-related behavior in conditional transgenic mice.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein.Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formationDifferential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopyPost translational changes to α-synuclein control iron and dopamine trafficking; a concept for neuron vulnerability in Parkinson's disease.Baicalein reduces E46K alpha-synuclein aggregation in vitro and protects cells against E46K alpha-synuclein toxicity in cell models of familiar Parkinsonism.Residue histidine 50 plays a key role in protecting α-synuclein from aggregation at physiological pH.Pathological alpha-synuclein propagates through neural networksPotentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins.Monomeric synucleins generate membrane curvature.Effects of curvature and composition on α-synuclein binding to lipid vesiclesAlpha-synuclein function and dysfunction on cellular membranes.Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.E46K human alpha-synuclein transgenic mice develop Lewy-like and tau pathology associated with age-dependent, detrimental motor impairmentParkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivoAccelerated formation of alpha-synuclein oligomers by concerted action of the 20S proteasome and familial Parkinson mutations.Mutant protein A30P α-synuclein adopts wild-type fibril structure, despite slower fibrillation kineticsDistinct clinical and neuropathological features of G51D SNCA mutation cases compared with SNCA duplication and H50Q mutationCharacterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein.Evolution of neurodegeneration.Parkinson's disease: the genetics of a heterogeneous disorder.Expression of human E46K-mutated α-synuclein in BAC-transgenic rats replicates early-stage Parkinson's disease features and enhances vulnerability to mitochondrial impairment.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson diseaseAutosomal dominant Parkinson's disease and the route to new therapies.α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson's disease and multiple system atrophy?Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly
P2860
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P2860
Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Mutation E46K increases phosph ...... ents of human alpha-synuclein.
@en
type
label
Mutation E46K increases phosph ...... ents of human alpha-synuclein.
@en
prefLabel
Mutation E46K increases phosph ...... ents of human alpha-synuclein.
@en
P2093
P2860
P1433
P1476
Mutation E46K increases phosph ...... ents of human alpha-synuclein.
@en
P2093
Bazbek Davletov
Michel Goedert
R Anthony Crowther
Ross Jakes
Shahin Zibaee
Woong Choi
P2860
P304
P356
10.1016/J.FEBSLET.2004.09.038
P407
P577
2004-10-01T00:00:00Z