Add to ORKGAffiliations EcofectInternational audienceDespite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints
Small oligomers of the amyloid β (Aβ) peptide, rather than the monomers or the fibrils, are suspecte...
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-residue hu...
Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein ...
Affiliations EcofectInternational audienceDespite its central importance for understanding the molec...
Alzheimer’s disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a pepti...
Alzheimer's disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a pepti...
International audienceAmyloid-β (Aβ) is present in humans as a 39- to 42-amino acid residue metaboli...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
SummaryIn vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that de...
We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue β-...
We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue β-...
AbstractWe report constraints on the supramolecular structure of amyloid fibrils formed by the 40-re...
The amyloid-β (Aβ) peptide of Alzheimer’s disease (AD) forms polymorphic fibrils on the micrometer a...
Small oligomers of the amyloid β (Aβ) peptide, rather than the monomers or the fibrils, are suspecte...
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-residue hu...
Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein ...
Affiliations EcofectInternational audienceDespite its central importance for understanding the molec...
Alzheimer’s disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a pepti...
Alzheimer's disease (AD) is the most common form of dementia. Aggregation of amyloid β (Aβ), a pepti...
International audienceAmyloid-β (Aβ) is present in humans as a 39- to 42-amino acid residue metaboli...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
The amyloid-β (Aβ) peptide of Alzheimer's disease (AD) forms polymorphic fibrils on the micrometer a...
SummaryIn vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that de...
We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue β-...
We report constraints on the supramolecular structure of amyloid fibrils formed by the 40-residue β-...
AbstractWe report constraints on the supramolecular structure of amyloid fibrils formed by the 40-re...
The amyloid-β (Aβ) peptide of Alzheimer’s disease (AD) forms polymorphic fibrils on the micrometer a...
Small oligomers of the amyloid β (Aβ) peptide, rather than the monomers or the fibrils, are suspecte...
Increasing evidence suggests that formation and propagation of misfolded aggregates of 42-residue hu...
Amyloid-β (Aβ) is a 39-42 residue protein produced by the cleavage of the amyloid precursor protein ...