Recent experimental evidence points to intermediates populated during the process of
amyloid fibril formation as the toxic moieties primarily responsible for the development of …

Light chain, or AL, amyloidosis is a pathological condition arising from systemic extracellular
deposition of monoclonal immunoglobulin light chain variable domains in the form of …

Cryoelectron microscopy (cryo-EM) has provided unprecedented insights into amyloid fibril
structures, including those associated with disease. However, these structures represent the …

Amyloid fibrils with an ordered cross-β structure are one form of protein aberrant aggregates.
Fibrils themselves and on-pathway small aggregates are involved in many …

The aggregation of the α/β protein acylphosphatase from Sulfolobus solfataricus has been
studied under conditions in which the protein maintains a native-like, although destabilised …

Understanding the process of amyloidogenesis is important for the future treatment of
misfolding-based diseases, such as Alzheimer's, spongiform encephalopathies, and other …

The aggregation of proteins into amyloid fibrils is a complex and fascinating process
associated with debilitating clinical disorders such as Alzheimer's and Parkinson's diseases …

Amyloid fibrils are ordered protein aggregates and a hallmark of many severe
neurodegenerative diseases. Amyloid fibrils form through primary nucleation from …

Amyloid deposits are proteinaceous extra-cellular aggregates associated with a diverse
range of disease states. These deposits are composed predominantly of amyloid fibrils, the …

Protofibrils are transient structures observed during in vitro formation of mature amyloid
fibrils and have been implicated as the toxic species responsible for cell dysfunction and …