Regular ArticleAn ABC-type multidrug transporter of Lactococcus lactis possesses an exceptionally broad substrate specificity
References (33)
- et al.
The Lactococcal lmrP gene encodes a proton motive force-dependent drug transporter
J Biol Chem
(1995) - et al.
Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis
J Biol Chem
(1997) - et al.
Determining the structure and mechanism of the human multidrug resistance P-glycoprotein using cysteine scanning mutagenesis and thiol-modification techniques
Biochim Biophys Acta
(1999) - et al.
Fluorescent cellular indicators are extruded by the multidrug resistance protein
J Biol Chem
(1993) - et al.
Disruption of the mouse mdrla P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs
Cell
(1994) - et al.
ABC transporters in lipid transport
Biochim Biophys Acta
(2000) - et al.
Photosensitized labeling of a functional multidrug transporter in living drug resistant tumor cells
J Biol Chem
(1990) - et al.
Is the multidrug transporter a flippase?
Trends Biochem Sci
(1992) Major photoaffinity drug labeling sites for iodoaryl azidoprazosin in P-glycoprotein are within, or immediately C-terminal to, transmembrane domains 6 and 12
J Biol Chem
(1993)- et al.
The catalytic cycle of P-glycoprotein
FEBS Lett
(1995)
Secondary and tertiary structure changes of reconstituted P-glycoprotein
J Biol Chem
Ligand-mediated tertiary structure changes of reconstituted P-glycoprotein
J Biol Chem
Secondary and tertiary changes of reconstituted LmrA induced by nucleotide binding or hydrolysis
J Biol Chem
Prevention of drug access to bacterial targets: permeability barriers and active efflux
Science
How cancer cells evade chemotherapy
Cancer Res
Molecular properties of bacterial multidrug transporters
Microbiol Mol Biol Rev
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Efflux pump as alternate mechanism for drug resistance in Mycobacterium tuberculosis
2019, Indian Journal of TuberculosisCitation Excerpt :The mechanisms for the expression and regulation of these efflux pumps are not yet fully understood. Moreover, their role in drug resistance needs to be understood.15 In Mycobacterium smegmatis as well as in other mycobacteria, the cell wall, rich in mycolic acids, functions as an efficient barrier preventing the access of several molecules including antibiotics.
Single nucleotide polymorphisms in efflux pumps genes in extensively drug resistant Mycobacterium tuberculosis isolates from Pakistan
2017, TuberculosisCitation Excerpt :The mechanisms for the expression and regulation of these efflux pumps are not yet fully understood. Moreover, their role in drug resistance needs to be understood [9]. Although efflux mechanisms have been studied in several mycobacteria [10–12] mostly, M. smegmatis has been used to study heterologous putative efflux pump genes [13–16].
ATP hydrolysis and pristinamycin IIA inhibition of the Staphylococcus aureus Vga(A), a dual ABC protein involved in streptogramin A resistance
2008, Journal of Biological ChemistryMicrobial export of lactic and 3-hydroxypropanoic acid: Implications for industrial fermentation processes
2004, Metabolic EngineeringCitation Excerpt :The transport proteins involved often belong to the ATP-Binding-Cassette (ABC) transporter family (Higgins, 1992). ABC transporters have been found for the export of a wide variety of substrates, ranging from antibiotics to weak organic acids and proteins (Braibant et al., 2000; Higgins, 1992; Poelarends et al., 2000). For instance, in yeast, the ABC transporter PDR12 has been directly shown to lower the intracellular levels of benzoate by catalyzing an active efflux from the cell (Piper et al., 1998).
ABC-transporters: Implications on drug resistance from microorganisms to human cancers
2003, International Journal of Antimicrobial AgentsThe transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within the membrane
2002, Journal of Biological Chemistry