Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of
the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both …

Oligomers and amyloid fibrils formed at different stages of protein aggregation are important
biomarkers for a variety of neurodegenerative diseases including Alzheimer's and …

Alzheimer's disease (AD) and type 2 diabetes (T2D) are two common protein misfolding
diseases. Increasing evidence suggests that these two diseases may be correlated with …

Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the
pathogenesis of a number of common age-related diseases. Although accumulating …

Expansions of polyglutamine (polyQ) tracts in nine different proteins cause a family of
neurodegenerative disorders called polyQ diseases. Because polyQ tracts are potential …

The propensity of protein molecules to self-assemble into highly ordered, fibrillar aggregates
lies at the heart of understanding many disorders ranging from Alzheimer's disease to …

Paramagnetic relaxation enhancement (PRE) is a powerful technique for studying transient
tertiary organizations of unfolded and partially folded proteins. The heterogeneous and …

The 25–35 fragment of the amyloid β (Aβ) peptide is a naturally occurring proteolytic by‐
product that retains the pathophysiology of its larger parent molecule, whose deposition has …

Studies of folded-to-misfolded transitions using model protein systems reveal a range of
unfolding needed for exposure of amyloid-prone regions for subsequent fibrillization. Here …

Protein aggregates are both associated with disease and function. Because a variety of
factors induce protein aggregation, a given protein can aggregate into different states. Here …