Drug-Induced Conformational Changes in Multidrug Efflux Transporter AcrB from Haemophilus influenzae
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019
2. Microcide Pharmaceuticals, Mountain View, California
3. Mpex Pharmaceuticals, San Diego, California 92109
Abstract
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JB.00471-07
Reference27 articles.
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2. Aminoglycosides Are Captured from both Periplasm and Cytoplasm by the AcrD Multidrug Efflux Transporter of Escherichia coli
3. Borges-Walmsley, M. I., J. Beauchamp, S. M. Kelly, K. Jumel, D. Candlish, S. E. Harding, N. C. Price, and A. R. Walmsley. 2003. Identification of oligomerization and drug-binding domains of the membrane fusion protein EmrA. J. Biol. Chem. 278 : 12903-12912.
4. Dodd, J. R., and D. L. Christie. 2005. Substituted cysteine accessibility of the third transmembrane domain of the creatine transporter: defining a transport pathway. J. Biol. Chem. 280 : 32649-32654.
5. Substrate Specificity of the RND-Type Multidrug Efflux Pumps AcrB and AcrD of Escherichia coli Is Determined Predominately by Two Large Periplasmic Loops
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