| Proximal Binding Pocket Arg717 Substitutions in Escherichia coli AcrB Cause Clinically Relevant Divergencies in Resistance Profiles. | Proximal Binding Pocket Arg717 Substitutions in Escherichia coli AcrB Cause Clinically Relevant Divergencies in Resistance Profiles.
Zwama M, Nishino K., Free PMC Article | 04/30/2022 |
| In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution. | In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution.
Chen M, Shi X, Yu Z, Fan G, Serysheva II, Baker ML, Luisi BF, Ludtke SJ, Wang Z., Free PMC Article | 03/26/2022 |
| Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps. | Pyridylpiperazine-based allosteric inhibitors of RND-type multidrug efflux pumps.
Plé C, Tam HK, Vieira Da Cruz A, Compagne N, Jiménez-Castellanos JC, Müller RT, Pradel E, Foong WE, Malloci G, Ballée A, Kirchner MA, Moshfegh P, Herledan A, Herrmann A, Deprez B, Willand N, Vargiu AV, Pos KM, Flipo M, Hartkoorn RC., Free PMC Article | 01/29/2022 |
| Metabolomics Reveal Potential Natural Substrates of AcrB in Escherichia coli and Salmonella enterica Serovar Typhimurium. | Metabolomics Reveal Potential Natural Substrates of AcrB in Escherichia coli and Salmonella enterica Serovar Typhimurium.
Wang-Kan X, Rodríguez-Blanco G, Southam AD, Winder CL, Dunn WB, Ivens A, Piddock LJV., Free PMC Article | 10/16/2021 |
| Allosteric drug transport mechanism of multidrug transporter AcrB. | Allosteric drug transport mechanism of multidrug transporter AcrB.
Tam HK, Foong WE, Oswald C, Herrmann A, Zeng H, Pos KM., Free PMC Article | 07/17/2021 |
| Studying dynamics without explicit dynamics: A structure-based study of the export mechanism by AcrB. | Studying dynamics without explicit dynamics: A structure-based study of the export mechanism by AcrB.
Simsir M, Broutin I, Mus-Veteau I, Cazals F. | 07/17/2021 |
| Interactions of a Bacterial RND Transporter with a Transmembrane Small Protein in a Lipid Environment. | Interactions of a Bacterial RND Transporter with a Transmembrane Small Protein in a Lipid Environment.
Du D, Neuberger A, Orr MW, Newman CE, Hsu PC, Samsudin F, Szewczak-Harris A, Ramos LM, Debela M, Khalid S, Storz G, Luisi BF., Free PMC Article | 05/1/2021 |
| Substrate-dependent transport mechanism in AcrB of multidrug resistant bacteria. | Substrate-dependent transport mechanism in AcrB of multidrug resistant bacteria.
Jewel Y, Van Dinh Q, Liu J, Dutta P., Free PMC Article | 01/9/2021 |
| Discovery of multidrug efflux pump inhibitors with a novel chemical scaffold. | Discovery of multidrug efflux pump inhibitors with a novel chemical scaffold.
Green AT, Moniruzzaman M, Cooper CJ, Walker JK, Smith JC, Parks JM, Zgurskaya HI., Free PMC Article | 10/24/2020 |
| Cryo-EM analysis of a membrane protein embedded in the liposome. | Cryo-EM analysis of a membrane protein embedded in the liposome.
Yao X, Fan X, Yan N., Free PMC Article | 10/3/2020 |
| AcrA, the membrane fusion protein, connects the inner-membrane-bound AcrB to the outer-membrane-bound TolC to form the multidrug efflux pump. | Conformational Dynamics of AcrA Govern Multidrug Efflux Pump Assembly.
Hazel AJ, Abdali N, Leus IV, Parks JM, Smith JC, Zgurskaya HI, Gumbart JC., Free PMC Article | 07/11/2020 |
| In the presence of translation-inhibiting antibiotics, resistance acquisition depends on the AcrAB-TolC multidrug efflux pump, because it reduces tetracycline concentrations in the cell. | Role of AcrAB-TolC multidrug efflux pump in drug-resistance acquisition by plasmid transfer.
Nolivos S, Cayron J, Dedieu A, Page A, Delolme F, Lesterlin C. | 12/21/2019 |
| dynamics of the active AcrB transporter is different in a substrate-bound state compared to an inhibitor-bound state | Mapping the Dynamic Functions and Structural Features of AcrB Efflux Pump Transporter Using Accelerated Molecular Dynamics Simulations.
Jamshidi S, Sutton JM, Rahman KM., Free PMC Article | 10/26/2019 |
| analysis of how physico-chemical properties of carbapenem compounds reflect on their interactions with AcrB | Identification and characterization of carbapenem binding sites within the RND-transporter AcrB.
Atzori A, Malviya VN, Malloci G, Dreier J, Pos KM, Vargiu AV, Ruggerone P. | 08/24/2019 |
| The conformational pathway identifies vertical shear motions among several transmembrane helices, which regulate alternate access of water in the transmembrane as well as peristaltic motions that pump drugs in the periplasm. | Energetics and conformational pathways of functional rotation in the multidrug transporter AcrB.
Matsunaga Y, Yamane T, Terada T, Moritsugu K, Fujisaki H, Murakami S, Ikeguchi M, Kidera A., Free PMC Article | 07/13/2019 |
| It has been demonstrated that an intact AcrAB-TolC efflux pump is crucial to the development of bacterial quinolone resistance. Its activity is complemented by expression of the alternative AcrEF efflux pump. | Upregulation of AcrEF in Quinolone Resistance Development in Escherichia coli When AcrAB-TolC Function Is Impaired.
Zhang CZ, Chang MX, Yang L, Liu YY, Chen PX, Jiang HX. | 08/11/2018 |
| Data show that the conformational changes occurring in multidrug resistance-associated protein AcrB enable the formation of a layer of structured waters on the internal surface of the transport channel. | Water-mediated interactions enable smooth substrate transport in a bacterial efflux pump.
Vargiu AV, Ramaswamy VK, Malvacio I, Malloci G, Kleinekathöfer U, Ruggerone P. | 04/28/2018 |
| the gate loop mutations effects on AcrB solution energetics (fold, stability, molecular dynamics) and on the in vivo efflux of Erythromycin and Doxorubicin. Finally, we discuss the efflux and the discrepancy between the structural and the functional experiments for Erythromycin in these gate loop mutants. | New insights into the structural and functional involvement of the gate loop in AcrB export activity.
Ababou A. | 04/21/2018 |
| The T37W/A100W double mutant AcrB exports ethidium bromide (EtBr) more actively than wild-type AcrB. | Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition.
Zwama M, Yamasaki S, Nakashima R, Sakurai K, Nishino K, Yamaguchi A., Free PMC Article | 03/3/2018 |
| Energy-coupling mechanism of the multidrug resistance transporter AcrB: Evidence for membrane potential-driving hypothesis through mutagenic analysis. | Energy-coupling mechanism of the multidrug resistance transporter AcrB: Evidence for membrane potential-driving hypothesis through mutagenic analysis.
Liu M, Zhang XC., Free PMC Article | 03/3/2018 |
| Ten phosphorus ylides were compared in multidrug efflux pump system consisting of the subunits acridine-resistance proteins A and B (AcrA and AcrB) and the multidrug efflux pump outer membrane factor TolC (TolC) and in AcrAB-TolC-deletion. | Fluorinated Beta-diketo Phosphorus Ylides Are Novel Efflux Pump Inhibitors in Bacteria.
Kincses A, Szabó ÁM, Saijo R, Watanabe G, Kawase M, Molnár J, Spengler G. | 02/3/2018 |
| Data show that CsrA binds directly to the 5' end of the transcript encoding AcrAB. | CsrA maximizes expression of the AcrAB multidrug resistance transporter.
Ricci V, Attah V, Overton T, Grainger DC, Piddock LJV., Free PMC Article | 01/20/2018 |
| It has been found that both AcrA and AcrB lasted for approximately 6 days in live E. coli cells, and the stability of AcrB depended on the presence of AcrA but not on active antibiotic efflux. | Study of the degradation of a multidrug transporter using a non-radioactive pulse chase method.
Chai Q, Webb SR, Wang Z, Dutch RE, Wei Y., Free PMC Article | 01/20/2018 |
| Two phenylalanine residues located adjacent to the substitution sensitive glycine residues of acrB play a role in blocking the pathway upon rigidification of the loop, since the removal of the phenyl rings from the rigid loop restores drug transport activity | Switch Loop Flexibility Affects Substrate Transport of the AcrB Efflux Pump.
Müller RT, Travers T, Cha HJ, Phillips JL, Gnanakaran S, Pos KM. | 12/9/2017 |
| Our data show for the first time effects of various substrate-binding pocket mutations on the kinetics of efflux of two substrates by the AcrB pump. They also confirm interactions between substrates and drugs predicted by MD simulation studies, and also reveal areas that need future research. | Effect of site-directed mutations in multidrug efflux pump AcrB examined by quantitative efflux assays.
Kinana AD, Vargiu AV, Nikaido H., Free PMC Article | 06/3/2017 |