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Washington DC: National Academy Press; 2011."},{"issue":"6","key":"ref30","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/S0966-842X(03)00117-3","article-title":"Antifungal agents: mechanisms of action","volume":"11","author":"FC Odds","year":"2003","journal-title":"Trends Microbiol"},{"issue":"21","key":"ref31","doi-asserted-by":"crossref","first-page":"7972","DOI":"10.1073\/pnas.85.21.7972","article-title":"Bafilomycins: a class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells","volume":"85","author":"EJ Bowman","year":"1988","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"15","key":"ref32","doi-asserted-by":"crossref","first-page":"3902","DOI":"10.1021\/bi00066a008","article-title":"Inhibitory effect of modified bafilomycins and concanamycins on P- and V-type adenosinetriphosphatases","volume":"32","author":"S 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