Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.
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Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disordersAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsInteractions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assemblyDopamine-induced α-synuclein oligomers show self- and cross-propagation properties.Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.From model system to clinical medicine: pathophysiologic links of common proteinopathies.Temperature-dependent structural changes of Parkinson's alpha-synuclein reveal the role of pre-existing oligomers in alpha-synuclein fibrillizationResidue-specific fluorescent probes of α-synuclein: detection of early events at the N- and C-termini during fibril assemblySelf-propagative replication of Aβ oligomers suggests potential transmissibility in Alzheimer disease.Dynamical Behavior of Human α-Synuclein Studied by Quasielastic Neutron Scattering.Common structural features of toxic intermediates from α-synuclein and GroES fibrillogenesis detected using cryogenic coherent X-ray diffraction imaging.Oligomerization and Membrane-binding Properties of Covalent Adducts Formed by the Interaction of α-Synuclein with the Toxic Dopamine Metabolite 3,4-Dihydroxyphenylacetaldehyde (DOPAL).Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients.2D gel blood serum biomarkers reveal differential clinical proteomics of the neurodegenerative diseases.Bacterial curli protein promotes the conversion of PAP248-286 into the amyloid SEVI: cross-seeding of dissimilar amyloid sequencesA small-angle X-ray scattering study of alpha-synuclein from human red blood cellsApplication and use of differential scanning calorimetry in studies of thermal fluctuation associated with amyloid fibril formation.Functionally different α-synuclein inclusions yield insight into Parkinson's disease pathology.Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions.Role of C-terminal negative charges and tyrosine residues in fibril formation of α-synuclein.SERF protein is a direct modifier of amyloid fiber assembly.Suppression of amyloid fibrils using the GroEL apical domain.Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrilsDeamidation of alpha-synuclein.Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: insight into intrinsically disordered proteins.C-Terminal Truncated α-Synuclein Fibrils Contain Strongly Twisted β-Sheets.Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture.
P2860
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P2860
Amyloid fibril formation of alpha-synuclein is accelerated by preformed amyloid seeds of other proteins: implications for the mechanism of transmissible conformational diseases.
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-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
2005年學術文章
@zh-hant
name
Amyloid fibril formation of al ...... sible conformational diseases.
@en
Amyloid fibril formation of al ...... sible conformational diseases.
@nl
type
label
Amyloid fibril formation of al ...... sible conformational diseases.
@en
Amyloid fibril formation of al ...... sible conformational diseases.
@nl
prefLabel
Amyloid fibril formation of al ...... sible conformational diseases.
@en
Amyloid fibril formation of al ...... sible conformational diseases.
@nl
P2093
P2860
P356
P1476
Amyloid fibril formation of al ...... sible conformational diseases.
@en
P2093
Eiko Kusaka
Hisashi Yagi
Kunihiro Hongo
Tomohiro Mizobata
Yasushi Kawata
P2860
P304
38609-38616
P356
10.1074/JBC.M508623200
P407
P577
2005-09-14T00:00:00Z