Steinem, Claudia

[["dc.bibliographiccitation.firstpage","141"],["dc.bibliographiccitation.lastpage","182"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.editor","Grandin, H. Michelle"],["dc.contributor.editor","Textor, Marcus"],["dc.date.accessioned","2017-09-07T11:54:18Z"],["dc.date.available","2017-09-07T11:54:18Z"],["dc.date.issued","2012"],["dc.identifier.doi","10.1002/9781118181249.ch5"],["dc.identifier.gro","3145143"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2847"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","public"],["dc.notes.status","final"],["dc.publisher","Wiley-Blackwell"],["dc.relation.isbn","978-0-470-53650-6"],["dc.relation.ispartof","Intelligent Surfaces in Biotechnology: Scientific and Engineering Concepts, Enabling Technologies, and Translation to Bio-Oriented Applications"],["dc.title","Supported Lipid Bilayers: Intelligent Surfaces for Ion Channel Recordings"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1816"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","1823"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Reiss, Björn"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Seebach, Jochen"],["dc.contributor.author","Wegener, Joachim"],["dc.date.accessioned","2017-09-07T11:45:04Z"],["dc.date.available","2017-09-07T11:45:04Z"],["dc.date.issued","2003"],["dc.description.abstract","The suitability of the quartz crystal microbalance technique (QCM) to monitor the formation and modulation of cell- substrate contacts in real time has recently been established. A more detailed analysis of the QCM response when living cells attach and spread on the resonator surfaces is, however, hampered by the chemical and mechanical complexity of cellular systems and the experimental difficulties to control one single parameter of cell-substrate contacts in a predictable way. In this study, we made use of liposomes as simple cell models and studied the interactions of these liposomes with the resonator surface. To mimic the specific interactions between cell and protein-coated substrate as given in cell culture experiments, we incorporated biotin-labeled lipids as \"receptors\" in the liposome shell and preadsorbed avidin on the resonator surface. The dissipational QCM (D-QCM) technology was applied to monitor the shifts in resonance frequency and energy dissipation during the adsorption of liposomes prepared with increasing amounts of biotin-labeled lipids. We also studied the adsorption kinetics of liposomes doped with biotin moieties that were attached to the lipid core by an alkyl spacer in order to increase the distance between liposome shell and resonator surface. A comparison of these data with the adhesion kinetics of mammalian cells as monitored by D-QCM is presented and discussed. Although the shifts in resonance frequency are very similar for intact liposomes and mammalian cells, the viscous energy dissipation is significantly higher when cells attach and spread on the resonator surface."],["dc.identifier.doi","10.1021/la0261747"],["dc.identifier.gro","3144124"],["dc.identifier.isi","000181309600049"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1714"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Adhesion kinetics of functionalized vesicles and mammalian cells: A comparative study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2287"],["dc.bibliographiccitation.issue","13-14"],["dc.bibliographiccitation.journal","Journal of Adhesion Science and Technology"],["dc.bibliographiccitation.lastpage","2300"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Lorenz, Bärbel"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Fine, Tamir"],["dc.contributor.author","Tarantola, Marco"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Wegener, Joachim"],["dc.date.accessioned","2017-09-07T11:46:42Z"],["dc.date.available","2017-09-07T11:46:42Z"],["dc.date.issued","2010"],["dc.description.abstract","The adhesion of MDCK II cells to porous and non-porous silicon substrates has been investigated by means of fluorescence and atomic force microscopy. The MDCK II cell density and the average height of the cells were increased on porous silicon substrates with regular 1.2 mu m pores as compared to flat, non-porous surfaces. In addition, we found a substantially reduced actin cytoskeleton within confluent cells cultured on the macroporous substrate compared to flat surfaces. The perturbation of the cytoskeleton relates to a significantly reduced expression of integrins on the porous area. The loss of stress fibers and cortical actin is accompanied by a dramatically reduced Young's modulus of 0.15 kPa compared to 6 kPa on flat surfaces as revealed by site-specific force-indentation experiments. (C) Koninklijke Brill NV, Leiden, 2010"],["dc.identifier.doi","10.1163/016942410X508028"],["dc.identifier.gro","3142996"],["dc.identifier.isi","000284152300013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/462"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0169-4243"],["dc.title","Cell Adhesion to Ordered Pores: Consequences for Cellular Elasticity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","126a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Schön, Markus"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Noeding, Helen"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2020-12-10T14:22:43Z"],["dc.date.available","2020-12-10T14:22:43Z"],["dc.date.issued","2016"],["dc.format.extent","126A"],["dc.identifier.doi","10.1016/j.bpj.2015.11.727"],["dc.identifier.isi","000375093800128"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71703"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.publisher.place","Cambridge"],["dc.relation.eventlocation","Los Angeles, CA"],["dc.relation.issn","1542-0086"],["dc.relation.issn","0006-3495"],["dc.title","Self-Organization of Actomyosin Networks Attached to Artificial Membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8186"],["dc.bibliographiccitation.issue","27"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","8192"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Kuhlmann, Jan W."],["dc.contributor.author","Mey, Ingo P."],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:45:42Z"],["dc.date.available","2017-09-07T11:45:42Z"],["dc.date.issued","2014"],["dc.description.abstract","The plasma membrane of animal cells is attached to the cytoskeleton, which significantly contributes to the lateral tension of the membrane. Lateral membrane tension has been shown to be an important physical regulator of cellular processes such as cell motility and morphology as well as exo- and endocytosis. Here, we report on lipid bilayers spanning highly ordered pore arrays, where we can control the lateral membrane tension by chemically varying the surface functionalization of the porous substrate. Surface functionalization was achieved by a gold coating on top of the pore rims of the hexagonal array of pores in silicon nitride substrates with pore radii of 600 nm followed by subsequent incubation with various n-propanolic mixtures of 6-mercapto-1-hexanol (6MH) and O-cholesteryl N-(8'-mercapto-3',6'-dioxaoctyl)carbamate (CPEO3). Pore-spanning membranes composed of 1,2-diphytanoyl-sn-glycero-3-phosphocholine were prepared by spreading giant unilarnellar vesicles on these functionalized porous silicon nitride substrates. Different mixtures of 6MH and CPEO3 provided self-assembled monolayers (SAMs) with different compositions as analyzed by contact angle and PM-IRRAS measurements. Site specific force-indentation experiments on the pore-spanning membranes attached to the different SAMs revealed a clear dependence of the amount of CPEO3 in the monolayer on the lateral membrane tension. While bilayers on pure 6MH monolayers show an average lateral membrane tension of 1.4 mN m(-1), a mixed monolayer of CPEO3 and 6MH obtained from a solution with 9.1 mol % CPEO3 exhibits a lateral tension of 5.0 mN m(-1). From contact angle and PM-IRRAS results, the mole fraction of CPEO3 in solution can be roughly translated into a CPEO3 surface concentration of 40 mol %. Our results clearly demonstrate that the free energy difference between the supported and freestanding part of the membrane depends on the chemical composition of the SAM, which controls the lateral membrane tension."],["dc.identifier.doi","10.1021/la5019086"],["dc.identifier.gro","3142088"],["dc.identifier.isi","000339229000031"],["dc.identifier.pmid","24950370"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4411"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 803]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["dc.title","Modulating the Lateral Tension of Solvent-Free Pore-Spanning Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11245"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry B"],["dc.bibliographiccitation.lastpage","11254"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Drexler, Janine"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:44:14Z"],["dc.date.available","2017-09-07T11:44:14Z"],["dc.date.issued","2003"],["dc.description.abstract","Nonordered and ordered porous alumina substrates with pore diameters of 20 and 50 nm, respectively, were utilized to immobilize lipid membranes spanning the pores of the porous material. The substrates were characterized by means of interferometry and electrical impedance spectroscopy. For impedance data reduction, an equivalent circuit representing the electrical behavior of porous alumina was developed on the basis of the parallel layer model. It turned out that the electrical parameters of the as prepared alumina substrates prevent a sensitive monitoring of the formation of immobilized lipid membranes. Thus, we established a technique to modify the substrates with respect to their electrical properties, leading to a significantly increased capacitance of porous alumina, which allowed for a sensitive detection of pore-spanning lipid bilayers by impedance spectroscopy. Two different membrane preparation techniques based on vesicle spreading were investigated. First, negatively charged giant liposomes were spread onto the porous alumina surface under an applied dc voltage of +100 mV. Second, large unilamellar vesicles containing lipids bearing a thiol anchor were used to chemisorb on gold functionalized porous alumina substrates and subsequently rupture to form planar pore-spanning membranes. For both techniques, impedance spectra were obtained, which indicate the formation of lipid bilayers on top of the porous alumina substrates."],["dc.identifier.doi","10.1021/jp030762r"],["dc.identifier.gro","3144048"],["dc.identifier.isi","000185756900038"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1629"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1520-6106"],["dc.title","Pore-suspending lipid bilayers on porous alumina investigated by electrical impedance spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1865"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Measurement Science and Technology"],["dc.bibliographiccitation.lastpage","1875"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Lüthgens, Eike"],["dc.contributor.author","Herrig, Alexander"],["dc.contributor.author","Kastl, Katja"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Reiss, Björn"],["dc.contributor.author","Wegener, Joachim"],["dc.contributor.author","Pignataro, Bruno"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:44:09Z"],["dc.date.available","2017-09-07T11:44:09Z"],["dc.date.issued","2003"],["dc.description.abstract","Three different systems are presented, exploring the adhesion of liposomes mediated by electrostatic and lipid-protein interactions as well as molecular recognition of ligand receptor pairs. Liposomes are frequently used to gain insight into the complicated processes involving adhesion and subsequent events such as fusion and fission mainly triggered by specific proteins. We combined liposome technology with the quartz crystal microbalance (QCM) technique as a powerful tool to study the hidden interface between the membrane and functionalized surface. Electrostatic attraction and molecular recognition were employed to bind liposomes to the functionalized quartz crystal. The QCM was used to distinguish between adsorption of vesicles and rupture due to strong adhesive forces. Intact vesicles display viscoelastic behaviour, while planar lipid bilayers as a result of vesicle rupture can be modelled by a thin rigid film. Furthermore, the adhesion of cells was modelled successfully by receptor bearing liposomes. Scanning force microscopy was used to confirm the results obtained by QCM measurements."],["dc.identifier.doi","10.1088/0957-0233/14/11/003"],["dc.identifier.gro","3144042"],["dc.identifier.isi","000187238900004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1622"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1361-6501"],["dc.relation.issn","0957-0233"],["dc.title","Adhesion of liposomes: a quartz crystal microbalance study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","eabg2174"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Science Advances"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Antonschmidt, Leif"],["dc.contributor.author","Dervişoğlu, Rıza"],["dc.contributor.author","Sant, Vrinda"],["dc.contributor.author","Tekwani Movellan, Kumar"],["dc.contributor.author","Mey, Ingo P."],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Becker, Stefan T."],["dc.contributor.author","Andreas, Loren B."],["dc.contributor.author","Griesinger, Christian"],["dc.date.accessioned","2021-06-01T09:42:06Z"],["dc.date.available","2021-06-01T09:42:06Z"],["dc.date.issued","2021"],["dc.description.abstract","Recent advances in the structural biology of disease-relevant α-synuclein fibrils have revealed a variety of structures, yet little is known about the process of fibril aggregate formation. Characterization of intermediate species that form during aggregation is crucial; however, this has proven very challenging because of their transient nature, heterogeneity, and low population. Here, we investigate the aggregation of α-synuclein bound to negatively charged phospholipid small unilamellar vesicles. Through a combination of kinetic and structural studies, we identify key time points in the aggregation process that enable targeted isolation of prefibrillar and early fibrillar intermediates. By using solid-state nuclear magnetic resonance, we show the gradual buildup of structural features in an α-synuclein fibril filament, revealing a segmental folding process. We identify distinct membrane-binding domains in α-synuclein aggregates, and the combined data are used to present a comprehensive mechanism of the folding of α-synuclein on lipid membranes."],["dc.identifier.doi","10.1126/sciadv.abg2174"],["dc.identifier.pmid","33990334"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85143"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/259"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","2375-2548"],["dc.relation.workinggroup","RG Griesinger"],["dc.relation.workinggroup","RG Steinem (Biomolecular Chemistry)"],["dc.rights","CC BY-NC 4.0"],["dc.title","Insights into the molecular mechanism of amyloid filament formation: Segmental folding of α-synuclein on lipid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","18604"],["dc.bibliographiccitation.issue","52"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","18613"],["dc.bibliographiccitation.volume","295"],["dc.contributor.author","Schäfer, Jonas"],["dc.contributor.author","Förster, Lucas"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Papadopoulos, Theofilos"],["dc.contributor.author","Brose, Nils"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2021-04-14T08:25:50Z"],["dc.date.available","2021-04-14T08:25:50Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1074/jbc.RA120.015347"],["dc.identifier.pmid","33127642"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81745"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/62"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A09: SUMOylation und Neddylation in Synapsen"],["dc.relation","SFB 1286 | B04: In vitro Rekonstitution von inhibitorischen GABAergen Postsynapsen"],["dc.relation.issn","0021-9258"],["dc.relation.workinggroup","RG Brose"],["dc.relation.workinggroup","RG Steinem (Biomolecular Chemistry)"],["dc.rights","CC BY 4.0"],["dc.title","Neuroligin-2 dependent conformational activation of collybistin reconstituted in supported hybrid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","213"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Bioelectrochemistry and Bioenergetics"],["dc.bibliographiccitation.lastpage","220"],["dc.bibliographiccitation.volume","42"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.contributor.author","Sieber, Manfred"],["dc.date.accessioned","2017-09-07T11:50:58Z"],["dc.date.available","2017-09-07T11:50:58Z"],["dc.date.issued","1997"],["dc.description.abstract","The topic of this study is a solid supported lipid bilayer consisting of dimethyldioctadecylammoniumbromide (DODAB) and the channel-forming polypeptide, gramicidin D, from Bacillus brevis immobilized on gold electrodes. The peptide was reconstituted into large unilamellar vesicles of DODAB which were fused on a negatively charged monolayer of 3-mercaptopropionic acid. The peptide forms a pore of 4 Angstrom diameter, selective for monovalent cations. The sequence of conductivity of monovalent alkaline cations is Cs+ > K+ > Na+ > Li+. The transport of these monovalent cations through this supported lipid bilayer via the gramicidin dimer was observed by a.c. impedance spectroscopy as an integral electrochemical method. Only a single bilayer preparation was necessary to perform the whole measurement. The obtained data were analysed with an equivalent circuit based on the theory developed by de Levie. We succeeded in confirming the sequence of the conductivity by impedance spectroscopy. The conductance of the membrane shows a linear dependence on the concentration of the cations in the bulk phase. This system is therefore recommended for biosensor devices based on ion transport through solid supported membranes. (C) 1997 Elsevier Science S.A."],["dc.identifier.doi","10.1016/S0302-4598(96)05113-6"],["dc.identifier.gro","3144603"],["dc.identifier.isi","A1997XM00500016"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2246"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0302-4598"],["dc.title","Impedance analysis of ion transport through gramicidin channels incorporated in solid supported lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]