Breakthroughs in molecular medicine have positioned the amyloid-β (Aβ) pathway at the
center of Alzheimer's disease (AD) pathophysiology. While the detailed molecular …

The ability to relate bulk experimental measurements of amyloid formation to the
microscopic assembly processes that underlie protein aggregation is critical in order to …

Parkinson's disease is a progressive neuropathological disorder that belongs to the class of
synucleinopathies, in which the protein alpha-synuclein is found at abnormally high …

Amyloid-β (Aβ) is present in humans as a 39-to 42-amino acid residue metabolic product of
the amyloid precursor protein. Although the two predominant forms, Aβ (1–40) and Aβ (1 …

Expression of many disease-related aggregation-prone proteins results in cytotoxicity and
the formation of large intracellular inclusion bodies. To gain insight into the role of inclusions …

We present an analytical treatment of a set of coupled kinetic equations that governs the self-
assembly of filamentous molecular structures. Application to the case of protein aggregation …

Parkinson's disease belongs to a group of currently incurable neurodegenerative disorders
characterized by the misfolding and accumulation of alpha‐synuclein aggregates that are …

Amyloids, fibrillar assembly of (poly) peptide chains, are associated with neurodegenerative
illnesses such as Alzheimer's and Parkinson's diseases, for which there are no cures. The …

Protein misfolding and/or aggregation has been implicated as the cause of several human
diseases, such as Alzheimer's and Parkinson's diseases and familial amyloid …

An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils
reveals that this structural form is likely to be the most stable one that protein molecules can …