Mitochondrial anti-viral signaling proteins form three-stranded helical filaments in launching innate immune responses against RNA viruses.

While electron microscopic helical reconstruction is a powerful technique in structural biology, mistakes can be made in determining the helical symmetry, leading to structures that are artifactual.

Computational analyses and biochemical measurements redefine the mechanisms by which pyrin-only-proteins specifically target and regulate the assembly of inflammasomes.

Tau protein exists as two conformational ensembles, one inert, and another that has intrinsic properties of self-association, triggers seeding in cells and in vitro, and is associated with Alzheimer's disease.

Laboratory-based methods are presented that produce filamentous tau aggregates with the same structures as those observed in neurodegenerative disease.

Switches in cell state downstream of pathogen exposure are driven by a deeply conserved disorder-to-order phase transition in an immunity signaling network.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Tau monomer from aggregate-containing cell models and tauopathy brains adopts discrete structures that act as templates, dictating the conformation of distinct strains that result from its seeding activity.