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.

Interaction of small molecule expands the conformational ensemble of alpha synuclein.

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.

First high-resolution structure of HGSNAT-acetyl-CoA complex, that describes the architecture of a novel transmembrane N-acetyltransferase fold and provides a molecular basis for MPS IIIC causing mutation induced destabilization of HGSNAT.

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