Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes.
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The synaptic pathology of alpha-synuclein aggregation in dementia with Lewy bodies, Parkinson's disease and Parkinson's disease dementiaDefinition of a molecular pathway mediating α-synuclein neurotoxicityElectrochemistry of nonconjugated proteins and glycoproteins. Toward sensors for biomedicine and glycomicsMisfolding and amyloid aggregation of apomyoglobinExploring the accessible conformations of N-terminal acetylated α-synucleinRepA-WH1, the agent of an amyloid proteinopathy in bacteria, builds oligomeric pores through lipid vesicles.Dopamine and paraquat enhance α-synuclein-induced alterations in membrane conductanceFormation of toxic oligomeric alpha-synuclein species in living cellsAnnular protofibrils are a structurally and functionally distinct type of amyloid oligomer.The glaucoma-associated olfactomedin domain of myocilin forms polymorphic fibrils that are constrained by partial unfolding and peptide sequenceComparisons with amyloid-β reveal an aspartate residue that stabilizes fibrils of the aortic amyloid peptide medin.Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFMAt low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillationTyrosine Hydroxylase Binding to Phospholipid Membranes Prompts Its Amyloid Aggregation and Compromises Bilayer Integrity.Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicityInsights into the effects of alpha-synuclein expression and proteasome inhibition on glutathione metabolism through a dynamic in silico model of Parkinson's disease: validation by cell culture data.Mechanisms of hybrid oligomer formation in the pathogenesis of combined Alzheimer's and Parkinson's diseases.Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC regionDetecting morphologically distinct oligomeric forms of alpha-synuclein.Unfoldomics of human diseases: linking protein intrinsic disorder with diseasesRole of small oligomers on the amyloidogenic aggregation free-energy landscapeDifferential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopyBinding of alpha-synuclein with Fe(III) and with Fe(II) and biological implications of the resultant complexes.Structure-function relationships of pre-fibrillar protein assemblies in Alzheimer's disease and related disordersMechanisms of Parkinson's disease-related proteins in mediating secondary brain damage after cerebral ischemia.Tryptophan probes at the alpha-synuclein and membrane interface.Amyloid ion channels: a common structural link for protein-misfolding diseaseIn-cell aggregation of a polyglutamine-containing chimera is a multistep process initiated by the flanking sequence.Orthogonal cross-seeding: an approach to explore protein aggregates in living cells.Mysterious oligomerization of the amyloidogenic proteinsEffects of Various Flavonoids on the α-Synuclein Fibrillation Process.Direct observation of the interconversion of normal and toxic forms of α-synucleinDistinct annular oligomers captured along the assembly and disassembly pathways of transthyretin amyloid protofibrilsIdentification of ciliary neurotrophic factor receptor alpha as a mediator of neurotoxicity induced by alpha-synucleinLewy bodies.The formation of tau pore-like structures is prevalent and cell specific: possible implications for the disease phenotypes.Effects of curvature and composition on α-synuclein binding to lipid vesiclesHuman α4β2 nicotinic acetylcholine receptor as a novel target of oligomeric α-synuclein.Side-chain interactions determine amyloid formation by model polyglutamine peptides in molecular dynamics simulations.Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.
P2860
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P2860
Annular alpha-synuclein protofibrils are produced when spherical protofibrils are incubated in solution or bound to brain-derived membranes.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@en
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@nl
type
label
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@en
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@nl
prefLabel
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@en
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@nl
P2093
P356
P1433
P1476
Annular alpha-synuclein protof ...... nd to brain-derived membranes.
@en
P2093
Jean-Christophe Rochet
Peter T Lansbury
Tomas T Ding
P304
10209-10217
P356
10.1021/BI020139H
P407
P577
2002-08-01T00:00:00Z