A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.
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Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicityGaucher disease glucocerebrosidase and α-synuclein form a bidirectional pathogenic loop in synucleinopathiesChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hipp25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathiesIdentification of an amyloid fibril forming peptide comprising residues 46-59 of apolipoprotein A-IMisfolded proteinase K-resistant hyperphosphorylated alpha-synuclein in aged transgenic mice with locomotor deterioration and in human alpha-synucleinopathiesIntrabody and Parkinson's diseasePrediction of "hot spots" of aggregation in disease-linked polypeptidesSystematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activitiesDynamic structural flexibility of α-synucleinTargeting heat shock proteins to modulate α-synuclein toxicityGenetics of Parkinson's diseaseIntrabodies as neuroprotective therapeuticsM1 and M2 immune activation in Parkinson's Disease: Foe and ally?Propagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Sequestration of a β-hairpin for control of α-synuclein aggregationAlpha-Synuclein in Parkinson's Disease: From Pathogenetic Dysfunction to Potential Clinical ApplicationThe phosphorylation of α-synuclein: development and implication for the mechanism and therapy of the Parkinson's diseaseDistinct α-synuclein strains differentially promote tau inclusions in neuronsThe fluorescent Congo red derivative, (trans, trans)-1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene (BSB), labels diverse beta-pleated sheet structures in postmortem human neurodegenerative disease brainsSite-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46KInvestigation of intramolecular dynamics and conformations of α-, β- and γ-synucleinAntibodies against alpha-synuclein reduce oligomerization in living cellsInteractions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assemblyAggregation properties of a short peptide that mediates amyloid fibril formation in model proteins unrelated to disease.Clustering of alpha-synuclein on supported lipid bilayers: role of anionic lipid, protein, and divalent ion concentrationHuman and Tree Shrew Alpha-synuclein: Comparative cDNA Sequence and Protein Structure Analysis.Biophysics of α-synuclein membrane interactions.Many overlapping peptides for protein hydrogen exchange experiments by the fragment separation-mass spectrometry method.Bacterial in-cell NMR of human α-synuclein: a disordered monomer by nature?Alpha-synuclein-induced aggregation of cytoplasmic vesicles in Saccharomyces cerevisiaeA β-synuclein mutation linked to dementia produces neurodegeneration when expressed in mouse brainIntramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice.Biochemical characterization of the core structure of alpha-synuclein filaments.alpha-Synuclein affects the MAPK pathway and accelerates cell death.AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides.Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicityAn scFv intrabody against the nonamyloid component of alpha-synuclein reduces intracellular aggregation and toxicityProducts of Cu(II)-catalyzed oxidation of alpha-synuclein fragments containing M1-D2 and H50 residues in the presence of hydrogen peroxide.Protein aggregation and protein instability govern familial amyotrophic lateral sclerosis patient survival.
P2860
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P2860
A hydrophobic stretch of 12 amino acid residues in the middle of alpha-synuclein is essential for filament assembly.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh-hant
name
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@en
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@nl
type
label
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@en
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@nl
prefLabel
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@en
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@nl
P2093
P356
P1476
A hydrophobic stretch of 12 am ...... sential for filament assembly.
@en
P2093
Giasson BI
Trojanowski JQ
P304
P356
10.1074/JBC.M008919200
P407
P577
2000-11-01T00:00:00Z