A massively parallel analysis of the effects of mutations on amyloid beta nucleation provide the first comprehensive atlas of how mutations alter the formation of amyloid fibrils.

Co-aggregation, amyloid formation, and unidirectional cross-seeding of prolactin and galanin for their efficient storage in secretory granules of pituitary and subsequent functional hormone release.

Ex vivo characterization of the interaction of human sperm with semen factors reveals that semen amyloids, previously discovered due to their ability to enhance HIV infection, serve a physiological function by promoting disposal of the defective sperm.

The role of amyloid-β-aggregation sequence and of the various domains in the physiological function of the FLO11-encoded adhesin in the yeast Saccharomyces cerevisiae are disclosed in this report.

Solution NMR provides structural and kinetic information about oligomers on pathway to amyloid fibrils that are precisely structured but not cytotoxic.

SINE RNAs are implicated in amyloid beta molecular pathology in hippocampus.

Serum amyloid A proteins bind retinol with nanomolar affinity, and do so by forming oligomers that create a hydrophobic pocket that shields retinol from the aqueous environment.

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.

Inter-molecular cross-seeding between phenol-soluble modulins facilitates rapid and efficient self-assembly in Staphylococcus aureus biofilms revealing a complex molecular interplay between distinct phenol-soluble modulins orchestrating functional amyloid formation.

Aβ inhibitors effectively block its aggregation, while also reducing seeding of tau aggregation from Aβ, tau, and AD derived fibrils, suggesting the two share a structurally related disease relevant interface.