Oligomeric, neurotoxic amyloid protein assemblies are thought to be causative agents in
Alzheimer's and other neurodegenerative diseases. Development of oligomer-specific …

Amyloid cascades that lead to peptide β-sheet fibrils and plaques are central to many
important diseases. Recently, intermediate assemblies of these cascades were identified as …

The self-assembly of abnormally folded proteins into amyloid fibrils is a hallmark of many
debilitating diseases, from Alzheimer's and Parkinson diseases to prion-related disorders …

Amyloidogenic diseases are characterised by the formation of amyloid aggregates inside or
outside the cell. Amyloid-associated human diseases include Alzheimer's disease …

Several human degenerative diseases involve amyloidogenic peptides/proteins with high
conformational plasticity and propensity to self-aggregate into polymeric fibrillar assemblies …

Amyloids result from the aggregation of a set of diverse proteins, due to either specific
mutations or promoting intra-or extra-cellular conditions. Structurally, they are rich in …

Amyloid fibrils are a pathologically and functionally relevant state of protein folding, which is
generally accessible to polypeptide chains and differs fundamentally from the globular state …

Background: A wide class of human diseases and neurodegenerative disorders, such as
Alzheimer's disease, is due to the failure of a specific peptide or protein to keep its native …

There is an increasing amount of evidence that biomolecular condensates are linked to
neurodegenerative diseases associated with protein aggregation, such as Alzheimer's …

By using an amyloid sequence pattern, here we have identified putative six-residue
amyloidogenic stretches in several relevant amyloid proteins. Hexapeptides synthesized on …