000307378 001__ 307378
000307378 005__ 20240928181418.0
000307378 0247_ $$aG:(GEPRIS)13122596$$d13122596
000307378 035__ $$aG:(GEPRIS)13122596
000307378 040__ $$aGEPRIS$$chttp://gepris.its.kfa-juelich.de
000307378 150__ $$aStructural characterization of EXCRT-III assemblies$$y2005 - 2013
000307378 371__ $$aProfessor Dr. Winfried Weissenhorn
000307378 450__ $$aDFG project G:(GEPRIS)13122596$$wd$$y2005 - 2013
000307378 5101_ $$0I:(DE-588b)2007744-0$$aDeutsche Forschungsgemeinschaft$$bDFG
000307378 550__ $$0G:(GEPRIS)5472160$$aSPP 1175: Dynamics of Cellular Membranes and their Exploitation by Viruses$$wt
000307378 680__ $$aEnveloped viruses such as HIV and Ebola assemble at and pinch off from cellular membranes as newly formed infectious particles. This process is largely mediated by the retroviral polyprotein Gag and the filovirus matrix protein VP40, which contain late domain sequence motifs that help to recruit cellular factors that normally act at endosomal membranes in the sorting of ubiquitylated cargo into vesicles that bud into endosomes giving rise to multi-vesicular bodies. The latter process is morphologically similar to enveloped virus budding and the interference with the protein machinery identified in multivesicular body formation leads to a defect in the pinching off of retroviral particles. Our goal is to understand the structural requirements of a late step in budding, which involves CHMP family protein assembly. We will use X-ray crystallography and biochemical approaches to analyze the structure of central CHMP family members, to study their activation and assembly mechanism, to elucidate their membrane binding properties and to obtain atomic details of their interactions with regulatory partners involved in the budding process.
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000307378 909CO $$ooai:juser.fz-juelich.de:974253
000307378 980__ $$aG
000307378 980__ $$aAUTHORITY