Crucial role of Asp408 in the proton translocation pathway of multidrug transporter AcrB: evidence from site- directed mutagenesis and carbodiimide labeling. Biochemistry.
Trinity revealed: Stoichiometric complex assembly of a bacterial multidrug efflux pump. Proc Natl Acad Sci U S A.
Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. Gastroenterology.
Site- directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB. J Bacteriol.
The AcrB efflux pump: conformational cycling and peristalsis lead to multidrug resistance. Curr Drug Targets.
Molecular analysis of BcrR, a membrane-bound bacitracin sensor and DNA-binding protein from Enterococcus faecalis. J Biol Chem.
Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB. Nat Struct Mol Biol.
Recycling of aromatic amino acids via TAT1 allows efflux of neutral amino acids via LAT2-4F2hc exchanger. Pflugers Arch.