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In human cell lines, neither P\u2010glycoprotein overexpression nor the use of efflux pump inhibitors significantly modulated mycalamide A toxicity in the systems tested. In <jats:italic>Saccharomyces cerevisiae,<\/jats:italic> it appears that mycalamide A is subject to efflux by the principle mediator of xenobiotic efflux, Pdr5p along with the major facilitator superfamily pump Tpo1p. Mycalamide E showed a similar efflux profile. These results suggest that future drugs based on the mycalamides are likely to be valuable in situations where efflux pump\u2013based resistance leads to failure of other chemotherapeutic approaches, although efflux may be a mediator of resistance in antifungal applications. \u00a9 2012 Wiley Periodicals, Inc. J Biochem Mol Toxicol 26:94\u2013100, 2012; View this article online at <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"wileyonlinelibrary.com\">wileyonlinelibrary.com<\/jats:ext-link>. DOI 10.1002\/jbt.20414<\/jats:p>","DOI":"10.1002\/jbt.20414","type":"journal-article","created":{"date-parts":[[2011,12,8]],"date-time":"2011-12-08T15:22:14Z","timestamp":1323357734000},"page":"94-100","source":"Crossref","is-referenced-by-count":9,"title":["The protein synthesis inhibitors mycalamides A and E have limited susceptibility toward the drug efflux network"],"prefix":"10.1002","volume":"26","author":[{"given":"Veronica","family":"Venturi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carolina","family":"Davies","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A. 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