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dc.contributor.authorHuss, Markus
dc.contributor.authorSasse, Florenz
dc.contributor.authorKunze, Brigitte
dc.contributor.authorJansen, Rolf
dc.contributor.authorSteinmetz, Heinrich
dc.contributor.authorIngenhorst, Gudrun
dc.contributor.authorZeeck, Axel
dc.contributor.authorWieczorek, Helmut
dc.date.accessioned2017-01-26T09:43:29Z
dc.date.available2017-01-26T09:43:29Z
dc.date.issued2005-08-04
dc.identifier.citationArchazolid and apicularen: novel specific V-ATPase inhibitors. 2005, 6:13 BMC Biochem.en
dc.identifier.issn1471-2091
dc.identifier.pmid16080788
dc.identifier.doi10.1186/1471-2091-6-13
dc.identifier.urihttp://hdl.handle.net/10033/620748
dc.description.abstractV-ATPases constitute a ubiquitous family of heteromultimeric, proton translocating proteins. According to their localization in a multitude of eukaryotic membranes, they energize many different transport processes. Since their malfunction is correlated with various diseases in humans, the elucidation of the properties of this enzyme for the development of selective inhibitors and drugs is one of the challenges in V-ATPase research.
dc.language.isoenen
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subject.meshAnimalsen
dc.subject.meshBridged Bicyclo Compounds, Heterocyclicen
dc.subject.meshCattleen
dc.subject.meshCell Lineen
dc.subject.meshMacrolidesen
dc.subject.meshManducaen
dc.subject.meshMiceen
dc.subject.meshProtease Inhibitorsen
dc.subject.meshSubstrate Specificityen
dc.subject.meshSwineen
dc.subject.meshVacuolar Proton-Translocating ATPasesen
dc.titleArchazolid and apicularen: novel specific V-ATPase inhibitors.en
dc.typeArticleen
dc.contributor.departmentHelmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalBMC biochemistryen
refterms.dateFOA2018-06-13T19:41:48Z
html.description.abstractV-ATPases constitute a ubiquitous family of heteromultimeric, proton translocating proteins. According to their localization in a multitude of eukaryotic membranes, they energize many different transport processes. Since their malfunction is correlated with various diseases in humans, the elucidation of the properties of this enzyme for the development of selective inhibitors and drugs is one of the challenges in V-ATPase research.


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