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Comparative studies on regulation of SNARE complex formation by the SM protein Sly1p

dc.contributor.advisorFasshauer, Dirk Prof. Dr.de
dc.contributor.authorDemircioglu, Fatma Esrade
dc.date.accessioned2012-06-11T18:35:13Zde
dc.date.accessioned2013-01-18T14:27:01Zde
dc.date.available2013-10-31T23:50:04Z
dc.date.issued2012-06-11de
dc.identifier.urihttp://hdl.handle.net/11858/00-1735-0000-000D-F0B7-2de
dc.identifier.urihttp://dx.doi.org/10.53846/goediss-3262
dc.identifier.urihttp://dx.doi.org/10.53846/goediss-3262
dc.identifier.urihttp://dx.doi.org/10.53846/goediss-3262
dc.format.mimetypeapplication/pdfde
dc.language.isoengde
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/de
dc.titleComparative studies on regulation of SNARE complex formation by the SM protein Sly1pde
dc.typedoctoralThesisde
dc.title.translatedVergleichende Studien zur Regulation der SNARE Komplex Bildung durch das SM protein Sly1pde
dc.contributor.refereeFasshauer, Dirk Prof. Dr.de
dc.date.examination2011-11-01de
dc.subject.dnb570 Biowissenschaftende
dc.subject.dnbBiologiede
dc.subject.gokWF 200de
dc.subject.gokSX 000de
dc.description.abstractengSec1/ Munc18 (SM) proteins are indispensible regulators of intracellular membrane fusion. In general, the high-affinity binding partners of SM proteins are Qa-SNAREs (syntaxins). Despite the high structural homology among SM proteins, different modes are proposed for their association with syntaxins. Neuronal Munc18a binds to a ‟closed conformationde
dc.contributor.coRefereeWahl, Markus Prof. Dr.de
dc.contributor.thirdRefereeEimer, Stefan Prof. Dr.de
dc.subject.topicGöttingen Graduate School for Neurosciences and Molecular Biosciences (GGNB)de
dc.subject.gerMembranfusionde
dc.subject.gerSly1pde
dc.subject.gerSNAREde
dc.subject.gerSyntaxinde
dc.subject.gerSed5pde
dc.subject.gerERde
dc.subject.gerGolgide
dc.subject.engMembrane fusionde
dc.subject.engSly1pde
dc.subject.engSNAREde
dc.subject.engsyntaxinde
dc.subject.engSed5pde
dc.subject.engERde
dc.subject.engGolgide
dc.subject.bk42.13 Molekularbiologiede
dc.subject.bk42.15 Zellbiologiede
dc.subject.bk35.70 Biochemie: Allgemeinesde
dc.identifier.urnurn:nbn:de:gbv:7-webdoc-3550-4de
dc.identifier.purlwebdoc-3550de
dc.affiliation.instituteGöttinger Graduiertenschule für Neurowissenschaften und Molekulare Biowissenschaften (GGNB)de
dc.description.embargoed2013-10-31de
dc.identifier.ppn773529144


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