Archazolid and apicularen: novel specific V-ATPase inhibitors.
dc.contributor.author | Huss, Markus | |
dc.contributor.author | Sasse, Florenz | |
dc.contributor.author | Kunze, Brigitte | |
dc.contributor.author | Jansen, Rolf | |
dc.contributor.author | Steinmetz, Heinrich | |
dc.contributor.author | Ingenhorst, Gudrun | |
dc.contributor.author | Zeeck, Axel | |
dc.contributor.author | Wieczorek, Helmut | |
dc.date.accessioned | 2017-01-26T09:43:29Z | |
dc.date.available | 2017-01-26T09:43:29Z | |
dc.date.issued | 2005-08-04 | |
dc.identifier.citation | Archazolid and apicularen: novel specific V-ATPase inhibitors. 2005, 6:13 BMC Biochem. | en |
dc.identifier.issn | 1471-2091 | |
dc.identifier.pmid | 16080788 | |
dc.identifier.doi | 10.1186/1471-2091-6-13 | |
dc.identifier.uri | http://hdl.handle.net/10033/620748 | |
dc.description.abstract | V-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.iso | en | en |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-sa/4.0/ | * |
dc.subject.mesh | Animals | en |
dc.subject.mesh | Bridged Bicyclo Compounds, Heterocyclic | en |
dc.subject.mesh | Cattle | en |
dc.subject.mesh | Cell Line | en |
dc.subject.mesh | Macrolides | en |
dc.subject.mesh | Manduca | en |
dc.subject.mesh | Mice | en |
dc.subject.mesh | Protease Inhibitors | en |
dc.subject.mesh | Substrate Specificity | en |
dc.subject.mesh | Swine | en |
dc.subject.mesh | Vacuolar Proton-Translocating ATPases | en |
dc.title | Archazolid and apicularen: novel specific V-ATPase inhibitors. | en |
dc.type | Article | en |
dc.contributor.department | Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany. | en |
dc.identifier.journal | BMC biochemistry | en |
refterms.dateFOA | 2018-06-13T19:41:48Z | |
html.description.abstract | V-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. |