Self-assembled peptide and protein amyloid nanostructures have traditionally been
considered only as pathological aggregates implicated in human neurodegenerative …

The conversion of proteins from their soluble states into well-organized fibrillar aggregates is
associated with a wide range of pathological conditions, including neurodegenerative …

Aggregation of human α-synuclein (αSyn) is linked to Parkinson's disease (PD) pathology.
The central region of the αSyn sequence contains the non-amyloid β-component (NAC) …

Objective: This review focuses on the current knowledge on the implication and significance
of beta 2 microglobulin (β2M), a conservative immune molecule in vertebrate. Data Sources …

All amyloid fibrils contain a cross-β fold. How this structure differs in fibrils formed from
proteins associated with different diseases remains unclear. Here, we combine cryo-EM and …

Amyloid proteins are involved in many neurodegenerative disorders such as Alzheimer's
disease [Tau, Amyloid β (Aβ)], Parkinson's disease [alpha-synuclein (αSyn)], and …

Although most proteins can assemble into amyloid-like fibrils in vitro under extreme
conditions, how proteins form amyloid fibrils in vivo remains unresolved. Identifying rare …

Understanding the mechanisms underlying protein misfolding and aggregation has become
a central issue in biology and medicine. Compelling evidence show that the formation of …

AL amyloidosis is caused by deposition in target tissue of amyloid fibrils constituted by
monoclonal immunoglobulin light chains. The amyloidogenic plasma cells derive from a …

Numerous studies of amyloid assembly have indicated that partially folded protein species
are responsible for initiating aggregation. Despite their importance, the structural and …