Janshoff, Andreas

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T08:53:37Z"],["dc.date.available","2018-11-07T08:53:37Z"],["dc.date.issued","2011"],["dc.format.extent","231"],["dc.identifier.isi","000293637300661"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22462"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["dc.relation.issn","0175-7571"],["dc.title","Enhanced stimulation of Toll-like receptor 9 via immunostimulatory nanoparticles"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.artnumber","e80068"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Schneider, David"],["dc.contributor.author","Baronsky, Thilo"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Oelkers, Marieelen"],["dc.contributor.author","Fichtner, Dagmar"],["dc.contributor.author","Wedlich, Doris"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T09:16:39Z"],["dc.date.available","2018-11-07T09:16:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Structural alterations during epithelial-to-mesenchymal transition (EMT) pose a substantial challenge to the mechanical response of cells and are supposed to be key parameters for an increased malignancy during metastasis. Herein, we report that during EMT, apical tension of the epithelial cell line NMuMG is controlled by cell-cell contacts and the architecture of the underlying actin structures reflecting the mechanistic interplay between cellular structure and mechanics. Using force spectroscopy we find that tension in NMuMG cells slightly increases 24 h after EMT induction, whereas upon reaching the final mesenchymal-like state characterized by a complete loss of intercellular junctions and a concerted down-regulation of the adherens junction protein E-cadherin, the overall tension becomes similar to that of solitary adherent cells and fibroblasts. Interestingly, the contribution of the actin cytoskeleton on apical tension increases significantly upon EMT induction, most likely due to the formation of stable and highly contractile stress fibers which dominate the elastic properties of the cells after the transition. The structural alterations lead to the formation of single, highly motile cells rendering apical tension a good indicator for the cellular state during phenotype switching. In summary, our study paves the way towards a more profound understanding of cellular mechanics governing fundamental morphological programs such as the EMT."],["dc.description.sponsorship","Open-Acces-Publikationsfonds 2013"],["dc.identifier.doi","10.1371/journal.pone.0080068"],["dc.identifier.isi","000328566100009"],["dc.identifier.pmid","24339870"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9505"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27979"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Tension Monitoring during Epithelial-to-Mesenchymal Transition Links the Switch of Phenotype to Expression of Moesin and Cadherins in NMuMG Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","125"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Structural Biology"],["dc.bibliographiccitation.lastpage","136"],["dc.bibliographiccitation.volume","168"],["dc.contributor.author","Schuy, Steffen"],["dc.contributor.author","Schaefer, Edith"],["dc.contributor.author","Yoder, Nicholas C."],["dc.contributor.author","Kumar, Krishna"],["dc.contributor.author","Vogel, Reiner"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T11:23:55Z"],["dc.date.available","2018-11-07T11:23:55Z"],["dc.date.issued","2009"],["dc.description.abstract","We present a universal mimetic approach of the prehairpin intermediate of gp41, which represents the active drug target for fusion inhibitors of HIV (human immunodeficiency virus) and SIV (simian immunodeficiency virus) based on membrane anchored lipopeptides. For this purpose, we have in situ coupled terminal cysteine-modified peptides originating from the NHR of SIV and HIV to a maleimide-functionalized DOPC bilayer and monitored the interactions with potential antagonists of the trimer-of-hairpin conformation C34 and T20 peptides by means of atomic force microscopy and ellipsometry. FT-IR analysis in conjugation with CD-spectroscopy of hydrated N36-lipopeptides, incorporated in multilamellar bilayer stacks was employed to investigate peptide conformation prior to antagonist binding. In contrast to solution studies substantial secondary structure formation of S-N36 after in situ coupling to the bilayer was found. We could show that S-N36-lipopeptide-aggregates in bilayers were selectively able to bind T20 or the corresponding C-peptides (C34) and similar results could be achieved by using H-N36 lipopeptides. It was found that T20 binding to coiled coil S-N36 lipopeptide assemblies was fully reversible at elevated temperatures, while T20 binds irreversibly to H-N36 bundles. (C) 2009 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.jsb.2009.04.006"],["dc.identifier.isi","000274799800013"],["dc.identifier.pmid","19406246"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56289"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1047-8477"],["dc.title","Lipopeptides derived from HIV and SIV mimicking the prehairpin intermediate of gp41 on solid supported lipid bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E2042"],["dc.bibliographiccitation.issue","30"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E2049"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Krick, Roswitha"],["dc.contributor.author","Busse, Ricarda A."],["dc.contributor.author","Scacioc, Andreea"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Thumm, Michael"],["dc.contributor.author","Kuehnel, Karin"],["dc.date.accessioned","2018-11-07T09:08:09Z"],["dc.date.available","2018-11-07T09:08:09Z"],["dc.date.issued","2012"],["dc.description.abstract","beta-propellers that bind polyphosphoinositides (PROPPINs), a eukaryotic WD-40 motif-containing protein family, bind via their predicted beta-propeller fold the polyphosphoinositides PtdIns3P and PtdIns(3,5) P-2 using a conserved FRRG motif. PROPPINs play a key role in macroautophagy in addition to other functions. We present the 3.0-angstrom crystal structure of Kluyveromyces lactis Hsv2, which shares significant sequence homologies with its three Saccharomyces cerevisiae homologs Atg18, Atg21, and Hsv2. It adopts a seven-bladed beta-propeller fold with a rare nonvelcro propeller closure. Remarkably, in the crystal structure, the two arginines of the FRRG motif are part of two distinct basic pockets formed by a set of highly conserved residues. In comprehensive in vivo and in vitro studies of ScAtg18 and ScHsv2, we define within the two pockets a set of conserved residues essential for normal membrane association, phosphoinositide binding, and biological activities. Our experiments show that PROPPINs contain two individual phosphoinositide binding sites. Based on docking studies, we propose a model for phosphoinositide binding of PROPPINs."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.1073/pnas.1205128109"],["dc.identifier.isi","000306992700006"],["dc.identifier.pmid","22753491"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25961"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Structural and functional characterization of the two phosphoinositide binding sites of PROPPINs, a beta-propeller protein family"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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","908"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","912"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Tahir, Muhammad Nawaz"],["dc.contributor.author","Eberhardt, Marc"],["dc.contributor.author","Theato, Patrick"],["dc.contributor.author","Faiß, Simon"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Gorelik, Tatiana"],["dc.contributor.author","Kolb, Ute"],["dc.contributor.author","Tremel, Wolfgang"],["dc.date.accessioned","2022-03-01T11:44:53Z"],["dc.date.available","2022-03-01T11:44:53Z"],["dc.date.issued","2006"],["dc.identifier.doi","10.1002/anie.200502517"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103151"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.title","Reactive Polymers: A Versatile Toolbox for the Immobilization of Functional Molecules on TiO2 Nanoparticles"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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.artnumber","051132"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PHYSICAL REVIEW E"],["dc.bibliographiccitation.volume","82"],["dc.contributor.author","Diezemann, Gregor"],["dc.contributor.author","Schlesier, Thomas"],["dc.contributor.author","Geil, Burkhard"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T08:36:38Z"],["dc.date.available","2018-11-07T08:36:38Z"],["dc.date.issued","2010"],["dc.description.abstract","We present a detailed analysis of two-state trajectories obtained from force-clamp spectroscopy (FCS) of reversibly bonded systems. FCS offers the unique possibility to vary the equilibrium constant in two-state kinetics, for instance, the unfolding and refolding of biomolecules, over many orders of magnitude due to the force dependence of the respective rates. We discuss two different kinds of counting statistics, the event counting usually employed in the statistical analysis of two-state kinetics and additionally the so-called cycle counting. While in the former case all transitions are counted, cycle counting means that we focus on one type of transitions. This might be advantageous in particular if the equilibrium constant is much larger or much smaller than unity because in these situations the temporal resolution of the experimental setup might not allow to capture all transitions of an event-counting analysis. We discuss how an analysis of FCS data for complex systems exhibiting dynamic disorder might be performed yielding information about the detailed force dependence of the transition rates and about the time scale of the dynamic disorder. In addition, the question as to which extent the kinetic scheme can be viewed as a Markovian two-state model is discussed."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 625]"],["dc.identifier.doi","10.1103/PhysRevE.82.051132"],["dc.identifier.isi","000286736200002"],["dc.identifier.pmid","21230462"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18362"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Physical Soc"],["dc.relation.issn","1539-3755"],["dc.title","Statistics of reversible bond dynamics observed in force-clamp spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]