Inhibitors of V-ATPases: old and new players

DC FieldValueLanguage
dc.contributor.authorHuss, Markus
dc.contributor.authorWieczorek, Helmut
dc.date.accessioned2021-12-23T16:03:35Z-
dc.date.available2021-12-23T16:03:35Z-
dc.date.issued2009
dc.identifier.issn00220949
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/6071-
dc.description.abstractV-ATPases constitute a ubiquitous family of heteromultimeric, proton translocating proteins. According to their localization in a multitude of eukaryotic endomembranes and plasma membranes, they energize many different transport processes. Currently, a handful of specific inhibitors of the V-ATPase are known, which represent valuable tools for the characterization of transport processes on the level of tissues, single cells or even purified proteins. 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.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 431]; VolkswagenStiftungVolkswagen; Supported by the Deutsche Forschungsgemeinschaft (SFB 431) and the VolkswagenStiftung (Funding Initiative. Interplay between Molecular Conformations and Biological Function'). Supply with apicularen derivatives by Martin E. Maier ( University of Tubingen) is gratefully acknowledged.
dc.language.isoen
dc.publisherCOMPANY BIOLOGISTS LTD
dc.relation.ispartofJOURNAL OF EXPERIMENTAL BIOLOGY
dc.subjectantibiotic inhibitors
dc.subjectBAFILOMYCIN A(1)
dc.subjectBAFILOMYCIN/CONCANAMYCIN-BINDING-SITE
dc.subjectbenzolactone enamides
dc.subjectBiology
dc.subjectCONCANAMYCIN-A
dc.subjectCYTOTOXIC MACROLIDES
dc.subjectH+-translocating vacuolar-type ATPase
dc.subjectindolyls
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectmacrolactones
dc.subjectP-TYPE
dc.subjectplecomacrolides
dc.subjectPOTENT
dc.subjectSELECTIVE INHIBITOR
dc.subjectSTRUCTURAL ELUCIDATION
dc.subjectSUBUNIT-C
dc.subjectV-ATPase
dc.subjectVACUOLAR-H+-ATPASE
dc.titleInhibitors of V-ATPases: old and new players
dc.typereview
dc.identifier.doi10.1242/jeb.024067
dc.identifier.isiISI:000262581900009
dc.description.volume212
dc.description.issue3
dc.description.startpage341
dc.description.endpage346
dc.identifier.eissn14779145
dc.publisher.placeBIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND
dcterms.isPartOf.abbreviationJ. Exp. Biol.
dcterms.oaStatusBronze
crisitem.author.deptUniversität Osnabrück-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidHuMa001-
crisitem.author.netidWiHe990-
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