Atomic structures of hIAPP fibrillar segments, determined using the cryo electron microscopy method MicroED, reveal that strong, stable intermolecular interactions are important features of cytotoxic amyloid proteins.

Toxic IAPP intermediates have some molecular features that are similar to, and others that are distinct from, toxic species reported for other amyloidogenic polypeptides.

The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

CLR01 is a small molecule that could be an effective topical microbicide to eliminate HIV (and other enveloped viruses), and to antagonize host-encoded amyloid fibrils that promote HIV infection.

Insulin secreting cells harbor distinct subpopulations of insulin granules and loss of one or the other correlates strongly with secretory deficiencies characterizing type-1 or type-2 diabetes.

Cells from the human pancreatic duct can be grown in culture and triggered to become insulin-producing cells, which could potentially be transplanted into patients with diabetes.

Novel designed alpha-sheet peptides inhibit amyloidosis in two different systems and preferentially bind the toxic oligomer.

Production of an amyloid protein by bacteria within the gut microbiome can influence the pathophysiology of a mouse model of synucleinopathy.

A theoretical basis for the spatial regulation of protein aggregation shows how aggregates can partition preferentially into intracellular liquid compartments.

A systematic survey of the epididymis identifies the cell types involved in post-testicular maturation of sperm.