How Single Site Mutations Can Help Understanding Structure Formation of Amyloid β1−40
Amyloid fibrils represent the structural endpoint on the energetic (mis) folding landscape of
very many proteins. Physiologically, amyloid fibrils are observed as a characteristic hallmark …
very many proteins. Physiologically, amyloid fibrils are observed as a characteristic hallmark …
Multi-target-directed triazole derivatives as promising agents for the treatment of Alzheimer's disease
A novel series of triazole-based compounds have been designed, synthesised and
evaluated as multi-target-directed ligands (MTDLs) against Alzheimer disease (AD). The …
evaluated as multi-target-directed ligands (MTDLs) against Alzheimer disease (AD). The …
Major reaction coordinates linking transient amyloid-β oligomers to fibrils measured at atomic level
The structural underpinnings for the higher toxicity of the oligomeric intermediates of
amyloidogenic peptides, compared to the mature fibrils, remain unknown at present. The …
amyloidogenic peptides, compared to the mature fibrils, remain unknown at present. The …
Multifunctional Mono-Triazole Derivatives Inhibit Aβ42 Aggregation and Cu2+-Mediated Aβ42 Aggregation and Protect Against Aβ42-Induced Cytotoxicity
Amyloid beta (Aβ) peptide aggregation is considered as one of the key hallmarks of
Alzheimer's disease (AD). Moreover, Aβ peptide aggregation increases considerably in the …
Alzheimer's disease (AD). Moreover, Aβ peptide aggregation increases considerably in the …
Inhibition of Alzheimer's amyloid-β42 peptide aggregation by a bi-functional bis-tryptoline triazole: key insights from molecular dynamics simulations
Alzheimer's disease (AD) is a neurodegenerative disease mainly caused by amyloid-β 42
(Aβ 42) peptide self-assembly in the brain. During last years, numerous multifunctional small …
(Aβ 42) peptide self-assembly in the brain. During last years, numerous multifunctional small …
A Toxicogenic Interaction between Intracellular Amyloid-β and Apolipoprotein-E
Alzheimer's disease (AD) is associated with the aggregation of amyloid β (Aβ) and tau
proteins. Why ApoE variants are significant genetic risk factors remains a major unsolved …
proteins. Why ApoE variants are significant genetic risk factors remains a major unsolved …
β-Amyloid peptide interactions with biomimetic membranes: A multiparametric characterization
Alzheimer's disease is the most common form of senile dementia in the world, and amyloid β
peptide1-42 (Aβ 1-42) is one of its two principal biological hallmarks. While interactome …
peptide1-42 (Aβ 1-42) is one of its two principal biological hallmarks. While interactome …
Impact of K16A and K28A mutation on the structure and dynamics of amyloid-β42 peptide in Alzheimer's disease: key insights from molecular dynamics simulations
The aggregation of amyloid-β 42 (Aβ 42) peptide into toxic oligomers and fibrils is a key step
in the Alzheimer disease pathogenesis. The recent studies highlighted that lysine residues …
in the Alzheimer disease pathogenesis. The recent studies highlighted that lysine residues …
Application of the double-mutant cycle strategy to protein aggregation reveals transient interactions in amyloid-β Oligomers
Transient oligomeric intermediates in the peptide or protein aggregation pathway are
suspected to be the key toxic species in many amyloid diseases, but deciphering their …
suspected to be the key toxic species in many amyloid diseases, but deciphering their …
Probing the influence of single-site mutations in the central cross-β region of amyloid β (1–40) peptides
Amyloid β (Aβ) is a peptide known to form amyloid fibrils in the brain of patients suffering
from Alzheimer's disease. A complete mechanistic understanding how Aβ peptides form …
from Alzheimer's disease. A complete mechanistic understanding how Aβ peptides form …