Janshoff, Andreas

[["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.artnumber","140046"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Open Biology"],["dc.bibliographiccitation.lastpage","7"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Rother, Jan"],["dc.contributor.author","Nöding, Helen"],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2019-07-09T11:41:15Z"],["dc.date.available","2019-07-09T11:41:15Z"],["dc.date.issued","2014-05-01"],["dc.description.abstract","Mechanical phenotyping of cells by atomic force microscopy (AFM) was proposed as a novel tool in cancer cell research as cancer cells undergo massive structural changes, comprising remodelling of the cytoskeleton and changes of their adhesive properties. In this work, we focused on the mechanical properties of human breast cell lines with different metastatic potential by AFM-based microrheology experiments. Using this technique, we are not only able to quantify the mechanical properties of living cells in the context of malignancy, but we also obtain a descriptor, namely the loss tangent, which provides model-independent information about the metastatic potential of the cell line. Including also other cell lines from different organs shows that the loss tangent (G″/G') increases generally with the metastatic potential from MCF-10A representing benign cells to highly malignant MDA-MB-231 cells."],["dc.identifier.doi","10.1098/rsob.140046"],["dc.identifier.fs","609535"],["dc.identifier.pmid","24850913"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11878"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58382"],["dc.language.iso","en"],["dc.relation.issn","2046-2441"],["dc.rights.access","openAccess"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Breast Neoplasms"],["dc.subject.mesh","Cell Line"],["dc.subject.mesh","Dogs"],["dc.subject.mesh","Elasticity"],["dc.subject.mesh","Female"],["dc.subject.mesh","Humans"],["dc.subject.mesh","MCF-7 Cells"],["dc.subject.mesh","Mice"],["dc.subject.mesh","Microscopy, Atomic Force"],["dc.subject.mesh","Models, Biological"],["dc.subject.mesh","NIH 3T3 Cells"],["dc.subject.mesh","Neoplasm Metastasis"],["dc.title","Atomic force microscopy-based microrheology reveals significant differences in the viscoelastic response between malign and benign cell lines."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5624"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Analytical Chemistry"],["dc.bibliographiccitation.lastpage","5630"],["dc.bibliographiccitation.volume","83"],["dc.contributor.author","Lazzara, Thomas D."],["dc.contributor.author","Mey, Ingo"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:44:07Z"],["dc.date.available","2017-09-07T11:44:07Z"],["dc.date.issued","2011"],["dc.description.abstract","Porous substrates have gained widespread interest for biosensor applications based on molecular recognition. Thus, there is a great demand to systematically investigate the parameters that limit the transport of molecules toward and within the porous matrix as a function of pore geometry. Finite element simulations (FES) and time-resolved optical waveguide spectroscopy (OWS) experiments were used to systematically study the transport of molecules and their binding on ism the inner surface of a porous material. OWS allowed us to measure the kinetics of protein adsorption within porous anodic aluminum oxide membranes composed of parallel-aligned, cylindrical pores with pore radii of 10-40 nm and pore depths of 0.8-9.6 mu m. FES showed that protein adsorption on the inner surface of a porous matrix is almost exclusively governed by the flux into the pores. The pore-interior surface nearly acts as a perfect sink for the macromolecules. Neither diffusion within the pores nor adsorption on the surface are rate limiting steps, except for very low rate constants of adsorption. While adsorption on the pore walls is mainly governed by the stationary flux into the pores, desorption from the inner pore walls involves the rate constants of desorption and adsorption, essentially representing the protein surface interaction potential. FES captured the essential features of the OWS experiments such as the initial linear slopes of the adsorption kinetics, which are inversely proportional to the pore depth and linearly proportional to protein concentration. We show that protein adsorption kinetics allows for an accurate determination of protein concentration, while desorption kinetics could be used to capture the interaction potential of the macromolecules with the pore walls."],["dc.identifier.doi","10.1021/ac200725y"],["dc.identifier.gro","3142695"],["dc.identifier.isi","000292892000021"],["dc.identifier.pmid","21651041"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9415"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/128"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0003-2700"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Benefits and Limitations of Porous Substrates as Biosensors for Protein Adsorption"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1001577"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Aggarwal, Shweta"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Paehler, Gesa"],["dc.contributor.author","Frey, Steffen"],["dc.contributor.author","Sanchez, Paula"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Schaap, Iwan Alexander Taco"],["dc.contributor.author","Goerlich, Dirk"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:23:52Z"],["dc.date.available","2018-11-07T09:23:52Z"],["dc.date.issued","2013"],["dc.description.abstract","Rapid conduction of nerve impulses requires coating of axons by myelin. To function as an electrical insulator, myelin is generated as a tightly packed, lipid-rich multilayered membrane sheath. Knowledge about the mechanisms that govern myelin membrane biogenesis is required to understand myelin disassembly as it occurs in diseases such as multiple sclerosis. Here, we show that myelin basic protein drives myelin biogenesis using weak forces arising from its inherent capacity to phase separate. The association of myelin basic protein molecules to the inner leaflet of the membrane bilayer induces a phase transition into a cohesive mesh-like protein network. The formation of this protein network shares features with amyloid fibril formation. The process is driven by phenylalanine-mediated hydrophobic and amyloid-like interactions that provide the molecular basis for protein extrusion and myelin membrane zippering. These findings uncover a physicochemical mechanism of how a cytosolic protein regulates the morphology of a complex membrane architecture. These results provide a key mechanism in myelin membrane biogenesis with implications for disabling demyelinating diseases of the central nervous system."],["dc.description.sponsorship","ERC Starting Grant; German Research Foundation [SI 746/9-1, TRR43]"],["dc.identifier.doi","10.1371/journal.pbio.1001577"],["dc.identifier.fs","600727"],["dc.identifier.isi","000321042900005"],["dc.identifier.pmid","23762018"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29688"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1545-7885"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/3.0/"],["dc.title","Myelin Membrane Assembly Is Driven by a Phase Transition of Myelin Basic Proteins Into a Cohesive Protein Meshwork"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4487"],["dc.bibliographiccitation.issue","22"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","4495"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Schaefer, Edith"],["dc.contributor.author","Vache, Marian"],["dc.contributor.author","Kliesch, Torben-Tobias"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T10:03:13Z"],["dc.date.available","2018-11-07T10:03:13Z"],["dc.date.issued","2015"],["dc.description.abstract","Indentation of giant liposomes with a conical indenter is described by means of a tension-based membrane model. We found that nonlinear membrane theory neglecting the impact of bending sufficiently describes the mechanical response of liposomes to indentation as measured by atomic force microscopy. Giant vesicles are gently adsorbed on glassy surfaces via avidin-biotin linkages and indented centrally using an atomic force microscope equipped with conventional sharp tips mounted on top of an inverted microscope. Force indentation curves display a nonlinear response that allows to extract pre-stress of the bilayer T-0 and the area compressibility modulus K-A by computing the contour of the vesicle at a given force. The values for K-A of fluid membranes correspond well to what is known from micropipet suction experiments and inferred from membrane undulation monitoring. Assembly of actin shells inside the liposome considerably stiffens the vesicles resulting in significantly larger area compressibility modules. The analysis can be easily extended to different indenter geometries with rotational symmetry."],["dc.description.sponsorship","[SFB 803 (B08)]"],["dc.identifier.doi","10.1039/c5sm00191a"],["dc.identifier.isi","000355555100018"],["dc.identifier.pmid","25946988"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12612"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38409"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.rights.access","openAccess"],["dc.title","Mechanical response of adherent giant liposomes to indentation with a conical AFM-tip"],["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.artnumber","eaat1161"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Science Advances"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Block, Johanna"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Candelli, Andrea"],["dc.contributor.author","Danes, Jordi Cabanas"],["dc.contributor.author","Peterman, Erwin J. G."],["dc.contributor.author","Wuite, Gijs J. L."],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2019-07-09T11:45:54Z"],["dc.date.available","2019-07-09T11:45:54Z"],["dc.date.issued","2018"],["dc.description.abstract","Structure and dynamics of living matter rely on design principles fundamentally different from concepts of traditional material science. Specialized intracellular filaments in the cytoskeleton permit living systems to divide, migrate, and growwith a high degree of variability and durability. Among the three filament systems,microfilaments,microtubules, and intermediate filaments (IFs), the physical properties of IFs and their role in cellular mechanics are the least well understood. We use optical trapping of individual vimentin filaments to investigate energy dissipation, strain history dependence, and creep behavior of stretched filaments. By stochastic and numerical modeling, we link our experimental observations to the peculiar molecular architecture of IFs. We find that individual vimentin filaments display tensile memory and are able to dissipate more than 70% of the input energy.We attribute these phenomena to distinct nonequilibrium folding and unfolding of a helices in the vimentin monomers constituting the filaments."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2018"],["dc.identifier.doi","10.1126/sciadv.aat1161"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15341"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59334"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2375-2548"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","530"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Viscoelastic properties of vimentin originate from nonequilibrium conformational changes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","130084"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Open Biology"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Pietuch, Anna"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2018-11-07T09:22:39Z"],["dc.date.available","2018-11-07T09:22:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Cellular adhesion and motility are fundamental processes in biological systems such as morphogenesis and tissue homeostasis. During these processes, cells heavily rely on the ability to deform and supply plasma membrane from pre-existing membrane reservoirs, allowing the cell to cope with substantial morphological changes. While morphological changes during single cell adhesion and spreading are well characterized, the accompanying alterations in cellular mechanics are scarcely addressed. Using the atomic force microscope, we measured changes in cortical and plasma membrane mechanics during the transition from early adhesion to a fully spread cell. During the initial adhesion step, we found that tremendous changes occur in cortical and membrane tension as well as in membrane area. Monitoring the spreading progress by means of force measurements over 2.5 h reveals that cortical and membrane tension become constant at the expense of excess membrane area. This was confirmed by fluorescence microscopy, which shows a rougher plasma membrane of cells in suspension compared with spread ones, allowing the cell to draw excess membrane from reservoirs such as invaginations or protrusions while attaching to the substrate and forming a first contact zone. Concretely, we found that cell spreading is initiated by a transient drop in tension, which is compensated by a decrease in excess area. Finally, all mechanical parameters become almost constant although morphological changes continue. Our study shows how a single cell responds to alterations in membrane tension by adjusting its overall membrane area. Interference with cytoskeletal integrity, membrane tension and excess surface area by administration of corresponding small molecular inhibitors leads to perturbations of the spreading process."],["dc.identifier.doi","10.1098/rsob.130084"],["dc.identifier.isi","000325975300004"],["dc.identifier.pmid","23864554"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29396"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc"],["dc.relation.issn","2046-2441"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Mechanics of spreading cells probed by atomic force microscopy"],["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","1987"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Analyst"],["dc.bibliographiccitation.lastpage","1992"],["dc.bibliographiccitation.volume","139"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Kramer, Corinna"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","Small molecule sensing is of great importance in pharmaceutical research. While there exist well established screening methods such as EMSA (electrophoretic motility shift assay) or biointeraction chromatography to report on successful binding interactions, there are only a few techniques that allow studying and quantifying the interaction of low molecular weight analytes with a binding partner directly. We report on a binding assay for small molecules based on the reflectivity change of a porous transparent film upon immobilisation of an absorbing substance on the pore walls. The porous matrix acts as a thin optical transparent film to produce interference fringes and accumulates molecules at the inner wall to amplify the sensor response. The benefits and limits of the assay are demonstrated by investigating the binding of biotin labelled with an atto dye to avidin physisorbed within an anodic aluminium oxide membrane."],["dc.identifier.doi","10.1039/c4an00009a"],["dc.identifier.fs","604886"],["dc.identifier.gro","3142213"],["dc.identifier.isi","000333081800024"],["dc.identifier.pmid","24599267"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5788"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: DFG [SFB 937 (A08)]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1364-5528"],["dc.relation.issn","0003-2654"],["dc.rights.access","openAccess"],["dc.title","Binding assay for low molecular weight analytes based on reflectometry of absorbing molecules in porous substrates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1068"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","ACS Applied Materials & Interfaces"],["dc.bibliographiccitation.lastpage","1076"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Lazzara, Thomas D."],["dc.contributor.author","Kliesch, Torben-Tobias"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Steinem, Claudia"],["dc.date.accessioned","2017-09-07T11:44:17Z"],["dc.date.available","2017-09-07T11:44:17Z"],["dc.date.issued","2011"],["dc.description.abstract","Anodic aluminum oxide (AAO) membranes with aligned, cylindrical, nonintersecting pores were selectively fiinctionalized in order to create dual-functionality substrates with different pore-rim and pore-interior surface functionalities, using silane chemistry. We used a two-step process involving an evaporated thin gold film to protect the underlying surface functionality of the pore rims. Subsequent treatment with oxygen plasma of the modified AAO membrane removed the unprotected organic functional groups, i.e., the pore-interior surface. After gold removal, the substrate became optically transparent, and displayed two distinct surface functionalities, one at the pore-rim surface and another at the pore-interior surface. We achieved a selective hydrophobic functionalization with dodecyl-trichlorosilane of either the pore rims or the pore interiors. The deposition of planar lipid membranes on the functionalized areas by addition of small unilamellar vesicles occurred in a predetermined fashion. Small unilamellar vesicles only ruptured upon contact with the hydrophobic substrate regions forming solid supported hybrid bilayers. In addition, pore-rim functionalization with dodecyl-trichlorosilane allowed the formation of pore-spanning hybrid lipid membranes as a result of giant unilamellar vesicle rupture. Confocal laser scanning microscopy was employed to identify the selective spatial localization of the adsorbed fluorescently labeled lipids. The corresponding increase in the AAO refractive index due to lipid adsorption on the hydrophobic regions was monitored by optical waveguide spectroscopy. This simple orthogonal functionalization route is a promising method to control the three-dimensional surface functionality of nanoporous films."],["dc.identifier.doi","10.1021/am101212h"],["dc.identifier.gro","3142745"],["dc.identifier.isi","000289762400021"],["dc.identifier.pmid","21370818"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9425"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/183"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1944-8244"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Orthogonal Functionalization of Nanoporous Substrates: Control of 3D Surface Functionality"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2100478"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Advanced Science"],["dc.bibliographiccitation.volume","8"],["dc.contributor.affiliation","Skamrahl, Mark; 1\r\nInstitute of Physical Chemistry\r\nUniversity of Göttingen\r\nTammannstr. 6 Göttingen 37077 Germany"],["dc.contributor.affiliation","Pang, Hongtao; 1\r\nInstitute of Physical Chemistry\r\nUniversity of Göttingen\r\nTammannstr. 6 Göttingen 37077 Germany"],["dc.contributor.affiliation","Ferle, Maximilian; 1\r\nInstitute of Physical Chemistry\r\nUniversity of Göttingen\r\nTammannstr. 6 Göttingen 37077 Germany"],["dc.contributor.affiliation","Gottwald, Jannis; 1\r\nInstitute of Physical Chemistry\r\nUniversity of Göttingen\r\nTammannstr. 6 Göttingen 37077 Germany"],["dc.contributor.affiliation","Rübeling, Angela; 2\r\nInstitute of Organic and Biomolecular Chemistry\r\nUniversity of Göttingen\r\nTammannstr. 2 Göttingen 37077 Germany"],["dc.contributor.affiliation","Maraspini, Riccardo; 3\r\nMax Planck Institute of Molecular Cell Biology and Genetics\r\nPfotenhauerstraße 108 Dresden 01307 Germany"],["dc.contributor.affiliation","Honigmann, Alf; 3\r\nMax Planck Institute of Molecular Cell Biology and Genetics\r\nPfotenhauerstraße 108 Dresden 01307 Germany"],["dc.contributor.author","Skamrahl, Mark"],["dc.contributor.author","Pang, Hongtao"],["dc.contributor.author","Ferle, Maximilian"],["dc.contributor.author","Gottwald, Jannis"],["dc.contributor.author","Rübeling, Angela"],["dc.contributor.author","Maraspini, Riccardo"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Oswald, Tabea A."],["dc.contributor.author","Janshoff, Andreas"],["dc.date.accessioned","2021-09-01T06:42:50Z"],["dc.date.available","2021-09-01T06:42:50Z"],["dc.date.issued","2021"],["dc.date.updated","2022-03-20T23:27:43Z"],["dc.description.abstract","Tight junctions (TJs) are essential components of epithelial tissues connecting neighboring cells to provide protective barriers. While their general function to seal compartments is well understood, their role in collective cell migration is largely unexplored. Here, the importance of the TJ zonula occludens (ZO) proteins ZO1 and ZO2 for epithelial migration is investigated employing video microscopy in conjunction with velocimetry, segmentation, cell tracking, and atomic force microscopy/spectroscopy. The results indicate that ZO proteins are necessary for fast and coherent migration. In particular, ZO1 and 2 loss (dKD) induces actomyosin remodeling away from the central cortex towards the periphery of individual cells, resulting in altered viscoelastic properties. A tug‐of‐war emerges between two subpopulations of cells with distinct morphological and mechanical properties: 1) smaller and highly contractile cells with an outward bulging apical membrane, and 2) larger, flattened cells, which, due to tensile stress, display a higher proliferation rate. In response, the cell density increases, leading to crowding‐induced jamming and more small cells over time. Co‐cultures comprising wildtype and dKD cells migrate inefficiently due to phase separation based on differences in contractility rather than differential adhesion. This study shows that ZO proteins are necessary for efficient collective cell migration by maintaining tissue fluidity and controlling proliferation."],["dc.description.sponsorship","DFG http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1002/advs.202100478"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89156"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation.eissn","2198-3844"],["dc.relation.issn","2198-3844"],["dc.rights","CC BY 4.0"],["dc.title","Tight Junction ZO Proteins Maintain Tissue Fluidity, Ensuring Efficient Collective Cell Migration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]