Structural basis for the drug extrusion mechanism by a MATE multidrug transporter-Reference-Cited by-同舟云学术

Structural basis for the drug extrusion mechanism by a MATE multidrug transporter

Published:2013-03-27 Issue:7444 Volume:496 Page:247-251
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Tanaka Yoshiki,Hipolito Christopher J.,Maturana Andrés D.,Ito Koichi,Kuroda Teruo,Higuchi Takashi,Katoh Takayuki,Kato Hideaki E.,Hattori Motoyuki,Kumazaki Kaoru,Tsukazaki Tomoya,Ishitani Ryuichiro,Suga Hiroaki,Nureki Osamu

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature12014.pdf

Reference42 articles.

1. Brown, M. H., Paulsen, I. T. & Skurray, R. A. The multidrug efflux protein NorM is a prototype of a new family of transporters. Mol. Microbiol. 31, 394–395 (1999)

2. He, G. X. et al. An H+-coupled multidrug efflux pump, PmpM, a member of the MATE family of transporters, from Pseudomonas aeruginosa. J. Bacteriol. 186, 262–265 (2004)

3. Kaatz, G. W., McAleese, F. & Seo, S. M. Multidrug resistance in Staphylococcus aureus due to overexpression of a novel multidrug and toxin extrusion (MATE) transport protein. Antimicrob. Agents Chemother. 49, 1857–1864 (2005)

4. McAleese, F. et al. A novel MATE family efflux pump contributes to the reduced susceptibility of laboratory-derived Staphylococcus aureus mutants to tigecycline. Antimicrob. Agents Chemother. 49, 1865–1871 (2005)

5. Tsuda, M. et al. Oppositely directed H+ gradient functions as a driving force of rat H+/organic cation antiporter MATE1. Am. J. Physiol. 292, F593–F598 (2007)

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