Biochemical, biophysical, and structural approach to determine the molecular basis of the calcium-sensitive regulation of the Gα chaperone and guanine exchange factor Ric-8A by the neuronal calcium sensor NCS-1.

Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

The glideosome-associated connector protein transitions between open and closed states, and this regulates its assembly and function during apicomplexan parasite motility.

A novel co-translational mechanism continuously adjusts the expression levels of ribosomal proteins Rpl3 and Rpl4 to their consumption during ribosome synthesis by regulating the abundance of their mRNAs.

Challenging a widespread model, biophysical and electrophysiological experiments suggest a new mechanism whereby complexins inhibit neurotransmitter release through electrostatic repulsion between their accessory helix and the membranes.

A heterodimeric exporter exhibits conformational equilibria in the presence of nucleotides, suggesting a unified mechanistic model for the conformational cycle of ABC exporters.

SNAP25 disease mutations within the synaptotagmin interface impair vesicle priming and cause uncontrolled spontaneous release due to enhanced SNARE:SNARE interactions, whereas a mutation within the SNARE-bundle increases the fusion energy barrier.

The glycine T-box riboswitch recognizes tRNAgly and senses its aminoacylation state by first interacting with the anticodon region and subsequently probing the 3' end of the ligand using both specific structural elements and conformational dynamics.

In an unusual complex that is not dissociated by RanGTP alone, Importin-9 sequesters the H2A-H2B core from promiscuous interactions.