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

Protein structures with complex topologies can be designed by recombining small independently folded domains.

The alpha-synuclein fibril structure reported here buries residues 50-57 at the interface between its two protofilaments, suggesting that familial Parkinson's disease associated mutations in these residues lead to a structure not compatible with the one presented here.

Two new polymorphic structures of recombinant human alpha-synuclein fibrils show striking differences to previous structures, while familial PD mutation sites remain crucial for protofilament interaction and fibril stability.

The crystal structure of Pur-alpha in complex with DNA reveals its molecular mechanisms of nucleic-acid binding and unwinding, allowing for a better understanding of its essential role in neurons.

A buried mutation in αβ-tubulin reveals an allosteric response to GDP in the lattice that dictates microtubule catastrophe and shrinking.

Integrin- and ERK signaling stimulates mammary epithelial cell proliferation when extracellular collagen condenses, causing asymmetric growth of multicellular aggregates that is necessary for elongation during branching morphogenesis.

Demonstrating the tricuspid valve maladapts is critical, and understanding its regurgitation may aid in developing better treatment strategies.

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.