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The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion

dc.contributor.authorSchulte, Kathrin
dc.contributor.authorPawlowski, Nikolaus
dc.contributor.authorFaelber, Katja
dc.contributor.authorFröhlich, Chris
dc.contributor.authorHoward, Jonathan
dc.contributor.authorDaumke, Oliver
dc.date.accessioned2016-03-07T12:37:50Z
dc.date.available2016-03-07T12:37:50Z
dc.date.issued2016-03-02
dc.description.abstractThe immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens. Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation. Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.pt_PT
dc.description.sponsorshipLeibniz Graduate School grants: (SFB958, SFB635).pt_PT
dc.identifier.doi10.1186/s12915-016-0236-7pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/555
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherBioMed Centralpt_PT
dc.relation.publisherversionhttp://bmcbiol.biomedcentral.com/articles/10.1186/s12915-016-0236-7pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectInnate immunitypt_PT
dc.subjectIRG proteinspt_PT
dc.subjectGTPasept_PT
dc.subjectDynamin superfamilypt_PT
dc.subjectDimerizationpt_PT
dc.subjectOligomerizationpt_PT
dc.titleThe immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashionpt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage8pt_PT
oaire.citation.issue1pt_PT
oaire.citation.startPage1pt_PT
oaire.citation.titleBMC Biologypt_PT
oaire.citation.volume14pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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