Structural basis for the mechanism of ABC transporters.
Biochem Soc Trans
; 43(5): 889-93, 2015 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-26517899
Yeast and human P4-ATPases transport glycosphingolipids using conserved structural motifs.
Rv2477c is an antibiotic-sensitive manganese-dependent ABC-F ATPase in Mycobacterium tuberculosis.
Quaternary structure and functional unit of energy coupling factor (ECF)-type transporters.
Evidence for a molecular diode-based mechanism in a multispecific ATP-binding cassette (ABC) exporter: SER-1368 as a gatekeeping residue in the yeast multidrug transporter Pdr5.
Transmitting the energy: interdomain cross-talk in Pdr5.
Structures of ABCB10, a human ATP-binding cassette transporter in apo- and nucleotide-bound states.
The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters.
Structure and function of the bacterial heterodimeric ABC transporter CydDC: stimulation of ATPase activity by thiol and heme compounds.
Quantification of volume and lipid filling of intracellular vesicles carrying the ABCA3 transporter.
Interdomain regulation of the ATPase activity of the ABC transporter haemolysin B from Escherichia coli.