Poly-PR and poly-GR interact with importin β, disrupt importin-cargo loading, and inhibit nuclear import in permeabilized cells in a manner that can be rescued by RNA.

There is a strand-based evolutionary mechanism for the diversification of outer membrane proteins, which has implications for how repeat proteins are created and for how outer membrane proteins fold.

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.

Mutational analysis in cell-based models of C9ORF72 ALS/FTD identifies canonical translation initiation codons (AUG) on the antisense CCCCGG transcript as initiation sites for synthesis of neurotoxic dipeptide repeat proteins.

Zfp106 functions as an RNA binding protein, binds directly to GGGGCC RNA repeats, is required in motor neurons to prevent ALS-like neurodegeneration in mice, and can suppress neurotoxicity in an established fly model of ALS.

Minimal changes allow an ancestral, unfolded peptide to adopt a known fold by repetition, illuminating a possible path for the emergence of folded proteins at the origin of life.

Autism-associated SHANK3 missense mutations result in differential protein folding, stability, and intramolecular dynamics affecting its turnover at the synapse.

The colonization of corals and their relatives by intracellular microalgae is facilitated by immunity proteins in the animal that contain thrombospondin-type-1 repeats, elucidating the inter-partner recognition processes required for the establishment of this ecologically important symbiosis.

Structural promiscuity in PURA protein, induced by patient mutations, impacts nucleic acid binding, unwinding, and subcellular localization, indicating why so many patients display the full disease spectrum of PURA syndrome.

A structure of the ciliary inner junction at 3.6 Å resolution permits atomic modeling of six inner junction proteins and their interactions with acetylated lysine 40 loops of alpha tubulins.