The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.
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Peptide dimer structure in an Aβ(1-42) fibril visualized with cryo-EM.SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer´s disease: appealing for ESI-IM-MSIn silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study.Dynamics of heteromolecular filament formation.Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.Monomer-dependent secondary nucleation in amyloid formation.Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoformsPyroglutamate-modified Aβ(3-42) affects aggregation kinetics of Aβ(1-42) by accelerating primary and secondary pathways.Cross-seeding between Aβ40 and Aβ42 in Alzheimer's disease.Comparing the Aggregation Free Energy Landscapes of Amyloid Beta(1-42) and Amyloid Beta(1-40).Effect of metal chelators on the aggregation of beta-amyloid peptides in the presence of copper and iron.Crystallographic insights into the self-assembly of KLVFF amyloid-beta peptides.Imaging Aβ(1-42) fibril elongation reveals strongly polarised growth and growth incompetent states.Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Theory of amyloid fibril nucleation from folded proteins.Stereochemistry and amyloid inhibition: Asymmetric triplex metallohelices enantioselectively bind to Aβ peptide.N-Terminally Truncated Amyloid-β(11-40/42) Cofibrillizes with its Full-Length Counterpart: Implications for Alzheimer's Disease.Depletion of amyloid-β peptides from solution by sequestration within fibril-seeded hydrogels.Amyloid β-peptides 1-40 and 1-42 form oligomers with mixed β-sheets.Structural modelling of the DNAJB6 oligomeric chaperone shows a peptide-binding cleft lined with conserved S/T-residues at the dimer interface.
P2860
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P2860
The Aβ40 and Aβ42 peptides self-assemble into separate homomolecular fibrils in binary mixtures but cross-react during primary nucleation.
description
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name
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@en
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@nl
type
label
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@en
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@nl
prefLabel
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@en
The Aβ40 and Aβ42 peptides sel ...... act during primary nucleation.
@nl
P2093
P2860
P50
P356
P1433
P1476
The Aβ40 and Aβ42 peptides sel ...... eact during primary nucleation
@en
P2093
Birgitta Frohm
Katja Bernfur
Risto Cukalevski
Xiaoting Yang
P2860
P304
P356
10.1039/C4SC02517B
P577
2015-05-08T00:00:00Z