Two thermodynamically distinct transport mechanisms operating within the same binding site explains the remarkable promiscuity of POT family transporters towards peptide and drug ligands.

Peptide and nitrate transporters have been converted into fluorescent reporters of transport activity and have been used to measure various transport properties including the dual affinity of the nitrate transceptor

Structural and biochemical characterization of the protease domain of an ABC transporter demonstrates the basis for recognition of substrate leader peptides.

By random nonstandard peptide integrated discovery, combinatorial macrocyclic peptides were leavaged that target a heterodimeric ABC transport complex and explore fundamental principles of the substrate translocation cycle.

Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.

Single-turnover studies reveal quantitative insights into the inner mechanics and unfold hidden facets in the conformational coupling of ATP binding, hydrolysis, and substrate translocation by ABC transporters.

The manner in which protons control the conformational behaviour of mammalian peptide transporters is revealed through state-of-the-art molecular dynamics simulations supported by cell-based assays.

Phylogenetic and biochemical analyses reveals a shared evolutionary path between biosynthesis and transport of defense metabolites in plants.

Herpes simplex virus evades the immune response by inhibiting the TAP transporter with a peptide inhibitor ICP47 that has an extensive interface at the peptide translocation cavity and locks the transporter in an inactive state.

Cryo-EM structure of a peptidase-containing ABC transporter in complex with its protein substrate reveals a mechanism of coupling substrate cleavage to translocation.