Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
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The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicitySystematic mutagenesis of α-synuclein reveals distinct sequence requirements for physiological and pathological activitiesPropagation of alpha-synuclein pathology: hypotheses, discoveries, and yet unresolved questions from experimental and human brain studies.Implications of protein structure instability: from physiological to pathological secondary structure.Intramuscular injection of α-synuclein induces CNS α-synuclein pathology and a rapid-onset motor phenotype in transgenic mice.Residue Glu83 plays a major role in negatively regulating alpha-synuclein amyloid formationThe clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesisA novel, high-efficiency cellular model of fibrillar alpha-synuclein inclusions and the examination of mutations that inhibit amyloid formationBent out of shape: α-Synuclein misfolding and the convergence of pathogenic pathways in Parkinson's disease.α-Synuclein-induced lysosomal dysfunction occurs through disruptions in protein trafficking in human midbrain synucleinopathy models.Amyloidogenic α-synuclein seeds do not invariably induce rapid, widespread pathology in mice.The C-terminal α-helices of mammalian Hsc70 play a critical role in the stabilization of α-synuclein binding and inhibition of aggregation.Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synucleinRobust Central Nervous System Pathology in Transgenic Mice following Peripheral Injection of α-Synuclein Fibrils.Alpha-synuclein: relating metals to structure, function and inhibition.Amyloids of alpha-synuclein affect the structure and dynamics of supported lipid bilayers.Contribution of Alanine-76 and Serine Phosphorylation in α-Synuclein Membrane Association and Aggregation in Yeasts.C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets.Creation of aggregation-defective α-synuclein variants by engineering the sequence connecting β-strand-forming domains.Taking a Bite Out of Amyloid: Mechanistic Insights into α-Synuclein Degradation by Cathepsin L.Contact between the β1 and β2 Segments of α-Synuclein that Inhibits Amyloid Formation.
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P2860
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on October 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@en
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@nl
type
label
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@en
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@nl
prefLabel
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@en
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@nl
P2093
P2860
P921
P356
P1433
P1476
Characterization of hydrophobic residue requirements for alpha-synuclein fibrillization.
@en
P2093
Benoit I Giasson
Elisa A Waxman
Joseph R Mazzulli
P2860
P304
P356
10.1021/BI900539P
P407
P577
2009-10-01T00:00:00Z