2.50
Hdl Handle:
http://hdl.handle.net/10033/620748
Title:
Archazolid and apicularen: novel specific V-ATPase inhibitors.
Authors:
Huss, Markus; Sasse, Florenz; Kunze, Brigitte; Jansen, Rolf; Steinmetz, Heinrich; Ingenhorst, Gudrun; Zeeck, Axel; Wieczorek, Helmut
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.
Affiliation:
Helmholtz Centre for infection research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
Archazolid and apicularen: novel specific V-ATPase inhibitors. 2005, 6:13 BMC Biochem.
Journal:
BMC biochemistry
Issue Date:
4-Aug-2005
URI:
http://hdl.handle.net/10033/620748
DOI:
10.1186/1471-2091-6-13
PubMed ID:
16080788
Type:
Article
Language:
en
ISSN:
1471-2091
Appears in Collections:
Publications of the research group Chemical Biology (CBIO)

Full metadata record

DC FieldValue Language
dc.contributor.authorHuss, Markusen
dc.contributor.authorSasse, Florenzen
dc.contributor.authorKunze, Brigitteen
dc.contributor.authorJansen, Rolfen
dc.contributor.authorSteinmetz, Heinrichen
dc.contributor.authorIngenhorst, Gudrunen
dc.contributor.authorZeeck, Axelen
dc.contributor.authorWieczorek, Helmuten
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.en
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

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