Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

The import of proteins into the intermembrane space of mitochondria is driven by binding to the trans-site receptor Mia40 and not by the oxidation of cysteine residues.

Mechanistic insight into the chaperone-like activity of NMNAT to phosphorylated Tau reveals a connection between NAD⁺metabolism and Tau homeostasis.

Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

Structure of the dimeric Haemophilus influenzae TRAP transporter (SiaQM) reveals two Na⁺ sites, the substrate-binding site and lipid-binding sites, and weak but promiscuous binding of SiaP to SiaQM.

The GEF activity of Rabex-5 is weakly autoinhibited by its CC domain and activated by Rabaptin-5 and the two proteins work concertedly to activate Rab5.

Multiple chaperone binding sites on substrates suggest a mechanism by which the Hsp70 chaperone can circumvent kinetic traps in protein folding.

Crystal structures of an archaeal homologue of mammalian glutamate transporters in apo and ion-only bound outward- and inward-facing states reveal ion-coupled conformational changes supporting mechanisms of coupling, gating, and transport.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

Theoretical study shows how enzymes can achieve substrate proofreading by taking advantage of existing molecular gradients in the cell while not being endowed with structural features typically required for proofreading.