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The understanding of how these inhibitors function may provide a basis to develop new drugs for the benefit of patients suffering from diseases such as osteoporosis or cancer. For this purpose, it appears absolutely essential to determine the exact inhibitor binding site in a target protein on the one side and to uncover the crucial structural elements of an inhibitor on the other side. However, even for some of the most popular and long known V-ATPase inhibitors, such as bafilomycin or concanamycin, the authentic structures of their binding sites are elusive. The aim of this review is to summarize the recent advances for the old players in the inhibition game, the plecomacrolides bafilomycin and concanamycin, and to introduce some of the new players, the macrolacton archazolid, the benzolactone enamides salicylihalamide, lobatamide, apicularen, oximidine and cruentaren, and the indolyls.<\/jats:p>","DOI":"10.1242\/jeb.024067","type":"journal-article","created":{"date-parts":[[2009,1,16]],"date-time":"2009-01-16T18:33:24Z","timestamp":1232130804000},"page":"341-346","source":"Crossref","is-referenced-by-count":189,"title":["Inhibitors of V-ATPases: old and new players"],"prefix":"10.1242","volume":"212","author":[{"given":"Markus","family":"Huss","sequence":"first","affiliation":[{"name":"Department of Biology\/Chemistry, University of Osnabru\u0308ck, 49069 Osnabru\u0308ck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Helmut","family":"Wieczorek","sequence":"additional","affiliation":[{"name":"Department of Biology\/Chemistry, University of Osnabru\u0308ck, 49069 Osnabru\u0308ck, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042505435826800_REF1","doi-asserted-by":"crossref","unstructured":"Bender, T., Huss, M., Wieczorek, H., Grond, S. and von Zezschwitz, P. 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