eMags is an engineered photodimerizer pair for optogenetic modulation in mammalian cells that is especially suited for the manipulation of intracellular processes occurring in small volumes or subcellular organelles.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Cryo-EM structures capture different conformational states of chromatin remodeler-nucleosome complexes.

A new structure reveals two Arf-GEF regulatory domains form a single structural unit that stimulates Arf-GEF activity.

Exploring natural Hsp104 variation reveals unexpected tuning of a passive activity that inhibits aggregation of specific substrates to selectively counter TDP-43 or alpha-synuclein proteotoxicity connected to neurodegenerative disease.

Protocols that greatly simplify the use of nanobodies in fluorescence imaging and affinity purification have been developed.

Codon optimization through biased synonymous substitutions is a characteristic feature of the genomes of generalist fungal parasites and is associated with the colonization of multiple hosts.