Morick, Daniela

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Kramer, C."],["dc.contributor.author","Morick, Daniela"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:22:33Z"],["dc.date.available","2018-11-07T09:22:33Z"],["dc.date.issued","2013"],["dc.format.extent","S152"],["dc.identifier.isi","000330215300448"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29370"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Lisbon, Portugal"],["dc.relation.issn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Cytoskeletal interaction forces characterized by means of atomic force microscopy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14204"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","14213"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Braunger, Julia A."],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Morick, Daniela"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:47:02Z"],["dc.date.available","2017-09-07T11:47:02Z"],["dc.date.issued","2013"],["dc.description.abstract","Phosphoinositides and in particular L-alpha-phosphatidylinositol-4,5-bisphosphate (PIP2) are key lipids controlling many cellular events and serve as receptors for a large number of intracellular proteins. To quantitatively analyze protein-PIP2 interactions in vitro in a time-resolved manner, planar membranes on solid substrates are highly desirable. Here, we describe an optimized protocol to form PIP2 containing planar solid supported membranes on silicon surfaces by vesicle spreading. Supported lipid bilayers (SLBs) were obtained by spreading POPC/PIP2 (92:8) small unilamellar vesicles onto hydrophilic silicon substrates at a low pH of 4.8. These membranes were capable of binding ezrin, resulting in large protein coverage as concluded from reflectometric interference spectroscopy and fluorescence microscopy. As deduced from fluorescence microscopy, only under low pH conditions, a homogeneously appearing distribution of fluorescently labeled PIP2 molecules in the membrane was achieved. Fluorescence recovery after photobleaching experiments revealed that PIP2 is not mobile in the bottom layer of the SLBs, while PIP2 is fully mobile in the top layer with diffusion coefficients of about 3 mu m(2)/s. This diffusion coefficient was considerably reduced by a factor of about 3 if ezrin has been bound to PIP2 in the membrane."],["dc.identifier.doi","10.1021/la402646k"],["dc.identifier.gro","3142249"],["dc.identifier.isi","000330144100026"],["dc.identifier.pmid","24199623"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6187"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [STE 884/11-1]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Solid Supported Membranes Doped with PIP2: Influence of Ionic Strength and pH on Bilayer Formation and Membrane Organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","532"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","537"],["dc.bibliographiccitation.volume","437"],["dc.contributor.author","Morick, Daniela"],["dc.contributor.author","Schatz, Michaela"],["dc.contributor.author","Hubrich, Raphael"],["dc.contributor.author","Hoffmeister, Helen"],["dc.contributor.author","Krefft, Anya"],["dc.contributor.author","Witzgall, Ralph"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:47:38Z"],["dc.date.available","2017-09-07T11:47:38Z"],["dc.date.issued","2013"],["dc.description.abstract","Polycystin-2 (PC2) trafficking has been proposed to be a result of the interaction of PIGEA14 with PC2 as a function of the phosphorylation state of PC2. Here, we investigated the interaction of PIGEA14 with the C-terminal part of polycystin-2 wild type (cPC2wt) and the pseudophosphorylated mutant (cPC2S812D) to first, quantify the binding affinity between cPC2 and PIGEA14 and second, to elucidate the influence of PC2 phosphorylation on PIGEA14 binding. Solid supported membranes composed of octanethiol/1,2-dioleoyl-sn-glycero-3-phosphocholine doped with the receptor lipid DOGS-NTA-Ni were used to attach PIGEA14 to the membrane via its hexahistidine tag. By means of the quartz crystal microbalance technique, binding affinities as well as kinetic constants of the interaction were extracted in a label-free manner by applying the scaled particle theory. The results show that the dissociation constant of cPC2 to PIGEA14 is in the 10 nM regime providing strong evidence of a very specific interaction of cPC2 with PIGEA14. The interaction of cPC2wt is twofold larger than that of cPC2S812D. The moderate higher binding affinity of cPC2wt to PIGEA14 is discussed in light of PC2 trafficking to the plasma membrane. (C) 2013 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.bbrc.2013.06.105"],["dc.identifier.gro","3142309"],["dc.identifier.isi","000323584400007"],["dc.identifier.pmid","23838289"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6853"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Dorothea Schlozer Program of the University of Gottingen"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-291X"],["dc.title","Phosphorylation of C-terminal polycystin-2 influences the interaction with PIGEA14: A QCM study based on solid supported membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","106"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Morick, Daniela"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2018-11-07T09:44:57Z"],["dc.date.available","2018-11-07T09:44:57Z"],["dc.date.issued","2014"],["dc.format.extent","500A"],["dc.identifier.isi","000337000402769"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34511"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","San Francisco, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Mechanics of F-Actin-Membrane Composites Investigated by Atomic Force Microscopy"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]