Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
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Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyFormation of soluble amyloid oligomers and amyloid fibrils by the multifunctional protein vitronectinChaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by HipIn vitro perturbation of aggregation processes in beta-amyloid peptides: a spectroscopic studyPre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease modelsStructures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopyNanotechnology, nanotoxicology, and neuroscienceMembrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubesRegulation of protein homeostasis in neurodegenerative diseases: the role of coding and non-coding genesStructural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studiesMembrane Permeabilization by Oligomeric α-Synuclein: In Search of the MechanismStabilization of a -hairpin in monomeric Alzheimer's amyloid- peptide inhibits amyloid formationNMR Structure in a Membrane Environment Reveals Putative Amyloidogenic Regions of the SEVI Precursor Peptide PAP 248−286A Combinatorial NMR and EPR Approach for Evaluating the Structural Ensemble of Partially Folded ProteinsStructural basis for receptor recognition and pore formation of a zebrafish aerolysin-like proteinAnalyzing dendritic spine pathology in Alzheimer's disease: problems and opportunitiesNeurotoxicity of prion peptides mimicking the central domain of the cellular prion proteinAmyloid oligomer neurotoxicity, calcium dysregulation, and lipid raftsEngineered transmembrane pores.Functional truncated membrane pores.Beta-barrel models of soluble amyloid beta oligomers and annular protofibrils.Effect of beta-sheet propensity on peptide aggregation.Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer.Oligomer-targeting with a conformational antibody fragment promotes toxicity in Aβ-expressing flies.Recent progress in understanding Alzheimer's β-amyloid structures.Implications of protein structure instability: from physiological to pathological secondary structure.Polyglutamine toxicity in yeast induces metabolic alterations and mitochondrial defectsSodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.Energy landscapes of the monomer and dimer of the Alzheimer's peptide Abeta(1-28).Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Atomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.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.The clustering and spatial arrangement of beta-sheet sequence, but not order, govern alpha-synuclein fibrillogenesisSimultaneous single-molecule fluorescence and conductivity studies reveal distinct classes of Abeta species on lipid bilayersBeta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrilsInsulin glycation by methylglyoxal results in native-like aggregation and inhibition of fibril formationEqual force recovery in dysferlin-deficient and wild-type muscles following saponin exposure.Mysterious oligomerization of the amyloidogenic proteinsPolymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.
P2860
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P2860
Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@ast
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@en
type
label
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@ast
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@en
prefLabel
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@ast
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@en
P1476
Are amyloid diseases caused by ...... bacterial pore-forming toxins?
@en
P2093
Peter T Lansbury
P304
P356
10.1017/S0033583506004422
P577
2006-05-01T00:00:00Z