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 …

In the last two decades, solid-state nuclear magnetic resonance (ssNMR) spectroscopy has
transformed from a spectroscopic technique investigating small molecules and industrial …

The formation of Aβ amyloid fibrils is a neuropathological hallmark of Alzheimer's disease
and cerebral amyloid angiopathy. However, the structure of Aβ amyloid fibrils from brain …

Aggregation of amyloid-β peptides into fibrils or other self-assembled states is central to the
pathogenesis of Alzheimer's disease. Fibrils formed in vitro by 40-and 42-residue amyloid-β …

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 …

Human islet amyloid polypeptide (hIAPP) functions as a glucose-regulating hormone but
deposits as amyloid fibrils in more than 90% of patients with type II diabetes (T2D). Here we …

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 …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

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 …

The amyloid beta (Aβ) fibrillar aggregate is the hallmark of Alzheimer's disease (AD).
Disassembling preformed fibril or inhibiting Aβ aggregation is considered as a therapeutic …