Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

The possible link between hIAPP accumulation and β-cell death in diabetic patients has
inspired numerous studies focusing on amyloid structures and aggregation pathways of this …

This review will focus on the process of amyloid-type protein aggregation. Amyloid fibrils are
an important hallmark of protein misfolding diseases and therefore have been investigated …

ATTR amyloidosis is caused by the deposition of transthyretin in the form of amyloid fibrils in
virtually every organ of the body, including the heart. This systemic deposition leads to a …

Amyloidosis of human islet amyloid polypeptide (hIAPP) is a pathological hallmark of type II
diabetes (T2D), an epidemic afflicting nearly 10% of the world's population. To visualize …

The use of transgenic mice displaying amyloid-β (Aβ) brain pathology has been essential for
the preclinical assessment of new treatment strategies for Alzheimer's disease. However, the …

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

Aggregation of the peptide hormone amylin into amyloid deposits is a pathological hallmark
of type-2 diabetes (T2D). While no causal link between T2D and amyloid has been …

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

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 …