Recent progress has improved our knowledge of how proteins form amyloid fibrils. Both
'natively unfolded'and globular proteins have been shown to initiate fibrillization by adopting …

The data reported in the past 5 years have highlighted new aspects of protein misfolding
and aggregation. Firstly, it appears that protein aggregation may be a generic property of …

Amyloid fibril formation is assumed to be the molecular basis for a variety of diseases of
unrelated origin. Despite its fundamental clinical importance, the mechanism of amyloid …

The molecular structure of the amyloid fibril has remained elusive because of the difficulty of
growing well diffracting crystals. By using a sequence-designed polypeptide, we have …

Based on the crystal structure of the cross-β spine formed by the peptide NNQQNY, we have
developed a computational approach for identifying those segments of amyloidogenic …

Elastin provides extensible tissues, including arteries and skin, with the propensity for elastic
recoil, whereas amyloid fibrils are associated with tissue-degenerative diseases, such as …

Arterial aging is the major contributing factor to increases in the incidence and prevalence of
cardiovascular disease, due mainly to the presence of chronic, low-grade,'sterile'arterial …

The development of type II diabetes was shown to be associated with the formation of
amyloid fibrils consisted of the islet amyloid polypeptide (IAPP or amylin). Recently, a short …

Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril
formation. Thioflavin T (ThT) is a reagent known to become strongly fluorescent upon …

The process of amyloid fibril formation by the human calcitonin hormone is associated with
medullary thyroid carcinoma. Based on the effect of pH on the fibrillization of human …