| scholarly article | Q13442814 |
| P50 | author | Jana Shen | Q87827774 |
| P2860 | cites work | Electrostatic lock in the transport cycle of the multidrug resistance transporter EmrE | Q90348471 |
| X-ray structure of EmrE supports dual topology model | Q27649102 | ||
| Multiple molecular mechanisms for multidrug resistance transporters | Q28297705 | ||
| Protonation of a glutamate residue modulates the dynamics of the drug transporter EmrE | Q28604217 | ||
| Intrinsic conformational plasticity of native EmrE provides a pathway for multidrug resistance | Q28657903 | ||
| Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer | Q34053453 | ||
| Antiparallel EmrE exports drugs by exchanging between asymmetric structures | Q34104584 | ||
| Asymmetric protonation of EmrE. | Q36333191 | ||
| Protonation-dependent conformational dynamics of the multidrug transporter EmrE. | Q36563374 | ||
| Small multidrug resistance proteins: a multidrug transporter family that continues to grow. | Q36973879 | ||
| Mechanism of pH-dependent activation of the sodium-proton antiporter NhaA | Q37330506 | ||
| Conformational Activation of a Transmembrane Proton Channel from Constant pH Molecular Dynamics | Q39371217 | ||
| Quasi-symmetry in the cryo-EM structure of EmrE provides the key to modeling its transmembrane domain | Q41625584 | ||
| Direct evidence for substrate-induced proton release in detergent-solubilized EmrE, a multidrug transporter. | Q44710560 | ||
| EmrE, a multidrug transporter from Escherichia coli, transports monovalent and divalent substrates with the same stoichiometry | Q45061745 | ||
| The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric | Q46879457 | ||
| Constant pH Molecular Dynamics Reveals How Proton Release Drives the Conformational Transition of a Transmembrane Efflux Pump | Q47154372 | ||
| New free-exchange model of EmrE transport | Q47428532 | ||
| Energetics and conformational pathways of functional rotation in the multidrug transporter AcrB. | Q53704466 | ||
| Functional rotation induced by alternating protonation states in the multidrug transporter AcrB: all-atom molecular dynamics simulations. | Q54302997 | ||
| Identification of tyrosine residues critical for the function of an ion-coupled multidrug transporter. | Q54465950 | ||
| Predicting Catalytic Proton Donors and Nucleophiles in Enzymes: How Adding Dynamics Helps Elucidate the Structure-Function Relationships | Q87827776 | ||
| P433 | issue | 32 | |
| P1104 | number of pages | 3 | |
| P304 | page(s) | 8060-8062 | |
| P577 | publication date | 2018-07-30 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Zooming in on a small multidrug transporter reveals details of asymmetric protonation | |
| P478 | volume | 115 |
| Q99710728 | Alternative proton-binding site and long-distance coupling in Escherichia coli sodium-proton antiporter NhaA | cites work | P2860 |
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