scholarly article | Q13442814 |
P819 | ADS bibcode | 2020NatCo..11.4948G |
P356 | DOI | 10.1038/S41467-020-18770-5 |
P932 | PMC publication ID | 7532149 |
P698 | PubMed publication ID | 33009415 |
P50 | author | Marie Glavier | Q91732216 |
Isabelle Broutin | Q92815332 | ||
Dhenesh Puvanendran | Q100428019 | ||
Gilles Phan | Q100428020 | ||
Olivier Lambert | Q100428021 | ||
Guy Schoehn | Q37372598 | ||
Elisa Frezza | Q47892491 | ||
P2093 | author name string | Martin Picard | |
Marion Decossas | |||
Jean-Christophe Taveau | |||
Laetitia Daury | |||
Cyril Garnier | |||
Quentin Cece | |||
Dimitri Salvador | |||
P2860 | cites work | DelPhi: a comprehensive suite for DelPhi software and associated resources | Q21195848 |
Multidrug resistance in bacteria | Q22255652 | ||
PHENIX: a comprehensive Python-based system for macromolecular structure solution | Q24654617 | ||
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids | Q24684673 | ||
The ensemble nature of allostery | Q26862004 | ||
Functional rotation of the transporter AcrB: insights into drug extrusion from simulations | Q27334906 | ||
Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors | Q27334925 | ||
Crystal structure of bacterial multidrug efflux transporter AcrB | Q27639761 | ||
The assembled structure of a complete tripartite bacterial multidrug efflux pump | Q27654543 | ||
Crystal structure of the multidrug exporter MexB from Pseudomonas aeruginosa | Q27654653 | ||
Structural and dynamical insights into the opening mechanism of P. aeruginosa OprM channel | Q27660577 | ||
Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport | Q27664655 | ||
Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli | Q27667059 | ||
Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket | Q27675850 | ||
Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. | Q27677990 | ||
Transport of drugs by the multidrug transporter AcrB involves an access and a deep binding pocket that are separated by a switch-loop | Q27678230 | ||
Structures of intermediate transport states of ZneA, a Zn(II)/proton antiporter | Q27680487 | ||
UCSF Chimera--a visualization system for exploratory research and analysis | Q27860666 | ||
Principles of protein-protein interactions | Q27860855 | ||
Features and development of Coot | Q27861079 | ||
Structural basis of RND-type multidrug exporters | Q28085595 | ||
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Multidrug efflux pumps: structure, function and regulation | Q57722260 | ||
Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism | Q64081670 | ||
Use of fluorescence probes to monitor function of the subunit proteins of the MexA-MexB-oprM drug extrusion machinery in Pseudomonas aeruginosa | Q73617925 | ||
Cryo-Electron Microscopy Structure of an Acinetobacter baumannii Multidrug Efflux Pump | Q91563926 | ||
Identification and characterization of carbapenem binding sites within the RND-transporter AcrB | Q92985142 | ||
Substrate-dependent transport mechanism in AcrB of multidrug resistant bacteria | Q93056725 | ||
SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions | Q29615882 | ||
Genetic assessment of the role of AcrB β-hairpins in the assembly of the TolC-AcrAB multidrug efflux pump of Escherichia coli | Q30153455 | ||
Conformational flexibility in the multidrug efflux system protein AcrA. | Q30159879 | ||
Engineered disulfide bonds support the functional rotation mechanism of multidrug efflux pump AcrB. | Q30268355 | ||
Drug export and allosteric coupling in a multidrug transporter revealed by molecular simulations | Q30499194 | ||
Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli | Q33714535 | ||
Crystal structure of the Neisseria gonorrhoeae MtrD inner membrane multidrug efflux pump | Q33716579 | ||
The challenge of efflux-mediated antibiotic resistance in Gram-negative bacteria | Q35482558 | ||
Bypassing the periplasm: reconstitution of the AcrAB multidrug efflux pump of Escherichia coli | Q36390365 | ||
Non-equivalent roles of two periplasmic subunits in the function and assembly of triclosan pump TriABC from Pseudomonas aeruginosa | Q36403070 | ||
Tripartite assembly of RND multidrug efflux pumps. | Q36582301 | ||
ff14SB: Improving the Accuracy of Protein Side Chain and Backbone Parameters from ff99SB. | Q36766916 | ||
Drug transport mechanism of the AcrB efflux pump | Q37376556 | ||
Antibacterial drug discovery in the resistance era. | Q38704810 | ||
Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB. | Q39498459 | ||
Structures and transport dynamics of a Campylobacter jejuni multidrug efflux pump. | Q41192285 | ||
In vitro transport activity of the fully assembled MexAB-OprM efflux pump from Pseudomonas aeruginosa. | Q41297505 | ||
Gctf: Real-time CTF determination and correction | Q41603517 | ||
Flexibility in a drug transport accessory protein: molecular dynamics simulations of MexA. | Q41667323 | ||
Photo-induced proton gradients for the in vitro investigation of bacterial efflux pumps | Q41853720 | ||
Assembly of the MexAB-OprM multidrug pump of Pseudomonas aeruginosa: component interactions defined by the study of pump mutant suppressors | Q41908269 | ||
Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa | Q43003288 | ||
Membrane topology of a multidrug efflux transporter, AcrB, in Escherichia coli | Q43832054 | ||
Linkage of the efflux-pump expression level with substrate extrusion rate in the MexAB-OprM efflux pump of Pseudomonas aeruginosa | Q44555516 | ||
Dynamics of Intact MexAB-OprM Efflux Pump: Focusing on the MexA-OprM Interface | Q47133688 | ||
Water-mediated interactions enable smooth substrate transport in a bacterial efflux pump | Q47714372 | ||
Discovery, research, and development of new antibiotics: the WHO priority list of antibiotic-resistant bacteria and tuberculosis. | Q47765000 | ||
Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. | Q48919839 | ||
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. | Q50104608 | ||
Highly accurate biomolecular electrostatics in continuum dielectric environments. | Q51914380 | ||
Resmap: automated representation of macromolecular interfaces as two-dimensional networks. | Q51972918 | ||
Understanding transport by the major facilitator superfamily (MFS): structures pave the way. | Q53211992 | ||
Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli. | Q53882432 | ||
Functional rotation induced by alternating protonation states in the multidrug transporter AcrB: all-atom molecular dynamics simulations. | Q54302997 | ||
Role of water during the extrusion of substrates by the efflux transporter AcrB. | Q54359686 | ||
Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. | Q54457560 | ||
Real-space refinement in PHENIX for cryo-EM and crystallography | Q54691589 | ||
Statistical thermodynamics for functionally rotating mechanism of the multidrug efflux transporter AcrB. | Q55068360 | ||
Molecular mechanisms of AcrB-mediated multidrug export | Q57118924 | ||
P433 | issue | 1 | |
P304 | page(s) | 4948 | |
P577 | publication date | 2020-10-02 | |
P1433 | published in | Nature Communications | Q573880 |
P1476 | title | Antibiotic export by MexB multidrug efflux transporter is allosterically controlled by a MexA-OprM chaperone-like complex | |
P478 | volume | 11 |
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