Köster, Sarah

[["dc.bibliographiccitation.artnumber","188102"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Lorenz, Charlotta"],["dc.contributor.author","Forsting, Johanna"],["dc.contributor.author","Schepers, Anna V."],["dc.contributor.author","Kraxner, Julia"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Witt, Hannes"],["dc.contributor.author","Klumpp, Stefan"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2020-12-10T18:25:50Z"],["dc.date.available","2020-12-10T18:25:50Z"],["dc.date.issued","2019"],["dc.description.abstract","The cytoskeleton is a composite network of three types of protein filaments, among which intermediate filaments (IFs) are the most extensible ones. Two very important IFs are keratin and vimentin, which have similar molecular architectures but different mechanical behaviors. Here we compare the mechanical response of single keratin and vimentin filaments using optical tweezers. We show that the mechanics of vimentin strongly depends on the ionic strength of the buffer and that its force-strain curve suggests a high degree of cooperativity between subunits. Indeed, a computational model indicates that in contrast to keratin, vimentin is characterized by strong lateral subunit coupling of its charged monomers during unfolding of α helices. We conclude that cells can tune their mechanics by differential use of keratin versus vimentin."],["dc.identifier.doi","10.1103/PhysRevLett.123.188102"],["dc.identifier.eissn","1079-7114"],["dc.identifier.issn","0031-9007"],["dc.identifier.pmid","31763918"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75854"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","info:eu-repo/grantAgreement/EC/H2020/724932/EU//MECHANICS"],["dc.relation.eissn","1079-7114"],["dc.relation.issn","0031-9007"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.access","openAccess"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.subject","intermediate filaments; optical tweezers; atomic force microscopy; cytoskeleton; biomechanics; Monte Carlo simulation"],["dc.subject.ddc","530"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Lateral Subunit Coupling Determines Intermediate Filament Mechanics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9104-9115"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Nanoscale"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Meyer, Daniel"],["dc.contributor.author","Telele, Saba"],["dc.contributor.author","Zelená, Anna"],["dc.contributor.author","Gillen, Alice J."],["dc.contributor.author","Antonucci, Alessandra"],["dc.contributor.author","Neubert, Elsa"],["dc.contributor.author","Nißler, Robert"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Boghossian, Ardemis A."],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2020-06-26T11:13:39Z"],["dc.date.available","2020-06-26T11:13:39Z"],["dc.date.issued","2020"],["dc.description.abstract","Cells can take up nanoscale materials, which has important implications for understanding cellular functions, biocompatibility as well as biomedical applications. Controlled uptake, transport and triggered release of nanoscale cargo is one of the great challenges in biomedical applications of nanomaterials. Here, we study how human immune cells (neutrophilic granulocytes, neutrophils) take up nanomaterials and program them to release this cargo after a certain time period. For this purpose, we let neutrophils phagocytose DNA-functionalized single-walled carbon nanotubes (SWCNTs) in vitro that fluoresce in the near infrared (980 nm) and serve as sensors for small molecules. Cells still migrate, follow chemical gradients and respond to inflammatory signals after uptake of the cargo. To program release, we make use of neutrophil extracellular trap formation (NETosis), a novel cell death mechanism that leads to chromatin swelling, subsequent rupture of the cellular membrane and release of the cell's whole content. By using the process of NETosis, we can program the time point of cargo release via the initial concentration of stimuli such as phorbol 12-myristate-13-acetate (PMA) or lipopolysaccharide (LPS). At intermediate stimulation, cells continue to migrate, follow gradients and surface cues for around 30 minutes and up to several hundred micrometers until they stop and release the SWCNTs. The transported and released SWCNT sensors are still functional as shown by subsequent detection of the neurotransmitter dopamine and reactive oxygen species (H2O2). In summary, we hijack a biological process (NETosis) and demonstrate how neutrophils transport and release functional nanomaterials."],["dc.identifier.doi","10.1039/d0nr00864h"],["dc.identifier.pmid","32286598"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/66755"],["dc.language.iso","en"],["dc.relation.eissn","2040-3372"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cellular biophysics"],["dc.title","Transport and programmed release of nanoscale cargo from cells by using NETosis"],["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","500"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","507"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Nisenholz, Noam"],["dc.contributor.author","Paknikar, Aishwarya"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Zemel, Assaf"],["dc.date.accessioned","2017-09-07T11:54:46Z"],["dc.date.available","2017-09-07T11:54:46Z"],["dc.date.issued","2016"],["dc.description.abstract","Myosin II activity and actin polymerization at the leading edge of the cell are known to be essential sources of cellular stress. However, a quantitative account of their separate contributions is still lacking; so is the influence of the coupling between the two phenomena on cell spreading dynamics. We present a simple analytic elastic theory of cell spreading dynamics that quantitatively demonstrates how actin polymerization and myosin activity cooperate in the generation of cellular stress during spreading. Consistent with experiments, myosin activity is assumed to polarize in response to the stresses generated during spreading. The characteristic response time and the overall spreading time are predicted to determine different evolution profiles of cell spreading dynamics. These include, a (regular) monotonic increase of cell projected area with time, a non-monotonic (overshooting) profile with a maximum, and damped oscillatory modes. In addition, two populations of myosin II motors are distinguished based on their location in the lamella; those located above the major adhesion zone at the cell periphery are shown to facilitate spreading whereas those in deeper regions of the lamella are shown to oppose spreading. We demonstrate that the attenuation of myosin activity in the two regions may result in reciprocal effects on spreading. These findings provide important new insight into the function of myosin II motors in the course of spreading."],["dc.identifier.doi","10.1039/c5sm01733e"],["dc.identifier.gro","3141761"],["dc.identifier.isi","000367259700021"],["dc.identifier.pmid","26481613"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12538"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/779"],["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.eissn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cellular biophysics"],["dc.title","Contribution of myosin II activity to cell spreading dynamics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2000595"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Macromolecular Materials and Engineering"],["dc.bibliographiccitation.volume","306"],["dc.contributor.author","Rauschendorfer, Judith Elisabeth"],["dc.contributor.author","Thien, Katharina Maria"],["dc.contributor.author","Denz, Manuela"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Ehlers, Florian"],["dc.contributor.author","Vana, Philipp"],["dc.date.accessioned","2021-04-14T08:30:55Z"],["dc.date.available","2021-04-14T08:30:55Z"],["dc.date.issued","2020"],["dc.description.abstract","Abstract Polymer layered silicate nanocomposites (PLSNs) made of montmorillonite (MMT) nanosheets and poly(methyl acrylate) (PMA) are synthesized and systematically characterized. MMT is first modified with a surface‐bound monomer and then functionalized with PMA via radical addition–fragmentation chain transfer (RAFT) polymerization using a grafting through approach. PMA‐modified MMT nanosheets with grafted polymer chains of variable length are obtained. The successful surface modification is demonstrated by near‐field scanning optical microscopy, thermogravimetric analysis, attenuated total reflection Fourier transform infrared spectroscopy, small‐angle X‐ray scattering, and size‐exclusion chromatography. The mechanical properties of various nanocomposites are evaluated via tensile testing. It can be shown that the mechanical properties (Young's modulus, tensile strength, toughness, and ductility) of these PLSNs can be fully controlled by using two major strategies, i.e., by the variation of the overall content of polymer‐modified MMT and by the variation of the chain length of the surface‐grafted polymer."],["dc.description.abstract","The mechanical properties of nanocomposites of poly(methyl acrylate) and surface‐functionalized montmorillonite nanosheets are explored. Polymer functionalization is achieved using radical addition–fragmentation chain transfer polymerization. Young's modulus, tensile strength, ductility, and toughness are investigated using tensile testing and can be specifically tailored by variation of filler content and surface‐grafted polymer chain length. image"],["dc.identifier.doi","10.1002/mame.202000595"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83411"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1439-2054"],["dc.relation.issn","1438-7492"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited."],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Tuning the Mechanical Properties of Poly(Methyl Acrylate) via Surface‐Functionalized Montmorillonite Nanosheets"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","735"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Lab on a Chip"],["dc.bibliographiccitation.lastpage","745"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Perego, Eleonora"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2021-04-14T08:28:33Z"],["dc.date.available","2021-04-14T08:28:33Z"],["dc.date.issued","2021"],["dc.description.abstract","Despite the importance for cellular processes, the dynamics of molecular assembly, especially on fast time scales, is not yet fully understood. To this end, we present a multi-layer microfluidic device and combine it with fluorescence fluctuation spectroscopy. We apply this innovative combination of methods to investigate the early steps in assembly of vimentin intermediate filaments (IFs). These filaments, together with actin filaments and microtubules, constitute the cytoskeleton of cells of mesenchymal origin and greatly influence their mechanical properties. We are able to directly follow the two-step assembly process of vimentin IFs and quantify the time scale of the first lateral step to tens of ms with a lag time of below 3 ms. Although demonstrated for a specific biomolecular system here, our method may potentially be employed for a wide range of fast molecular reactions in biological or, more generally, soft matter systems, as it allows for a precise quantification of the kinetics underlying the aggregation and assembly."],["dc.identifier.doi","10.1039/d0lc00985g"],["dc.identifier.pmid","33491697"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82646"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/116"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/89"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B02: Ein in vitro-Verfahren zum Verständnis der struktur-organisierenden Rolle des Vesikel-Clusters"],["dc.relation.eissn","1473-0189"],["dc.relation.issn","1473-0197"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Exploring early time points of vimentin assembly in flow by fluorescence fluctuation spectroscopy"],["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","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.firstpage","2693"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2699"],["dc.bibliographiccitation.volume","107"],["dc.contributor.author","Nolting, Jens-Friedrich"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:45:22Z"],["dc.date.available","2017-09-07T11:45:22Z"],["dc.date.issued","2014"],["dc.description.abstract","Along with microtubules and microfilaments, intermediate filaments are a major component of the eukaryotic cytoskeleton and play a key role in cell mechanics. In cells, keratin intermediate filaments form networks of bundles that are sparser in structure and have lower connectivity than, for example, actin networks. Because of this, bending and buckling play an important role in these networks. Buckling events, which occur due to compressive intracellular forces and cross-talk between the keratin network and other cytoskeletal components, are measured here in situ. By applying a mechanical model for the bundled filaments, we can access the mechanical properties of both the keratin bundles themselves and the surrounding cytosol. Bundling is characterized by a coupling parameter that describes the strength of the linkage between the individual filaments within a bundle. Our findings suggest that coupling between the filaments is mostly complete, although it becomes weaker for thicker bundles, with some relative movement allowed."],["dc.identifier.doi","10.1016/j.bpj.2014.10.039"],["dc.identifier.gro","3142001"],["dc.identifier.isi","000345859500029"],["dc.identifier.pmid","25468348"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3445"],["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","1542-0086"],["dc.relation.issn","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY-NC-ND 3.0"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","cellular biophysics"],["dc.title","Mechanics of Individual Keratin Bundles in Living Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3641"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Bernhardt, M."],["dc.contributor.author","Nicolas, J.-D."],["dc.contributor.author","Osterhoff, Markus"],["dc.contributor.author","Mittelstädt, H."],["dc.contributor.author","Reuß, Bernhard M."],["dc.contributor.author","Harke, B."],["dc.contributor.author","Wittmeier, A."],["dc.contributor.author","Sprung, M."],["dc.contributor.author","Köster, S."],["dc.contributor.author","Salditt, T."],["dc.date.accessioned","2020-03-10T11:45:32Z"],["dc.date.available","2020-03-10T11:45:32Z"],["dc.date.issued","2018"],["dc.description.abstract","We present a correlative microscopy approach for biology based on holographic X-ray imaging, X-ray scanning diffraction, and stimulated emission depletion (STED) microscopy. All modalities are combined into the same synchrotron endstation. In this way, labeled and unlabeled structures in cells are visualized in a complementary manner. We map out the fluorescently labeled actin cytoskeleton in heart tissue cells and superimpose the data with phase maps from X-ray holography. Furthermore, an array of local far-field diffraction patterns is recorded in the regime of small-angle X-ray scattering (scanning SAXS), which can be interpreted in terms of biomolecular shape and spatial correlations of all contributing scattering constituents. We find that principal directions of anisotropic diffraction patterns coincide to a certain degree with the actin fiber directions and that actin stands out in the phase maps from holographic recordings. In situ STED recordings are proposed to formulate models for diffraction data based on co-localization constraints."],["dc.identifier.doi","10.1038/s41467-018-05885-z"],["dc.identifier.pmid","30194418"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15331"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63281"],["dc.language.iso","en"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.subject.ddc","530"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cellular biophysics"],["dc.title","Correlative microscopy approach for biology using X-ray holography, X-ray scanning diffraction and STED microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Reshetniak, Sofiia"],["dc.contributor.author","Ußling, Jan‐Eike"],["dc.contributor.author","Perego, Eleonora"],["dc.contributor.author","Rammner, Burkhard"],["dc.contributor.author","Schikorski, Thomas"],["dc.contributor.author","Fornasiero, Eugenio F."],["dc.contributor.author","Truckenbrodt, Sven"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Rizzoli, Silvio O."],["dc.date.accessioned","2021-04-14T08:23:53Z"],["dc.date.available","2021-04-14T08:23:53Z"],["dc.date.issued","2020"],["dc.description.abstract","Abstract Many proteins involved in synaptic transmission are well known, and their features, as their abundance or spatial distribution, have been analyzed in systematic studies. This has not been the case, however, for their mobility. To solve this, we analyzed the motion of 45 GFP‐tagged synaptic proteins expressed in cultured hippocampal neurons, using fluorescence recovery after photobleaching, particle tracking, and modeling. We compared synaptic vesicle proteins, endo‐ and exocytosis cofactors, cytoskeleton components, and trafficking proteins. We found that movement was influenced by the protein association with synaptic vesicles, especially for membrane proteins. Surprisingly, protein mobility also correlated significantly with parameters as the protein lifetimes, or the nucleotide composition of their mRNAs. We then analyzed protein movement thoroughly, taking into account the spatial characteristics of the system. This resulted in a first visualization of overall protein motion in the synapse, which should enable future modeling studies of synaptic physiology."],["dc.description.abstract","Synopsis image Live imaging reveals global protein dynamics in the synaptic bouton, providing a first visualization of overall protein motion in the synapse and showing connections between various protein characteristics and mobility in vivo. Membrane proteins display lower mobility rates than soluble proteins. Proteins are less mobile in synaptic boutons than in axons. Protein mobility is strongly influenced by the protein association with synaptic vesicles. Amino acid composition, mRNA nucleotide composition, and protein lifetimes correlate with mobility parameters. Provided diffusion coefficients for 45 synaptic proteins can be used to generate models of synaptic physiology."],["dc.description.abstract","Live imaging reveals global protein dynamics in the synaptic bouton, providing a first visualization of overall protein motion in the synapse and showing connections between protein characteristics and mobility in vivo. image"],["dc.description.sponsorship","European Research Council http://dx.doi.org/10.13039/100010663"],["dc.description.sponsorship","Germany's Excellence Strategy"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.identifier.doi","10.15252/embj.2020104596"],["dc.identifier.pmid","32627850"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81086"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/54"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/117"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/55"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P09: Proteinsortierung in der Synapse: Prinzipien und molekulare Organisation"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | B02: Ein in vitro-Verfahren zum Verständnis der struktur-organisierenden Rolle des Vesikel-Clusters"],["dc.relation","SFB 1286 | Z02: Integrative Datenanalyse und -interpretation. Generierung einer synaptisch-integrativen Datenstrategie (SynIDs)"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.relation.workinggroup","RG Rizzoli (Quantitative Synaptology in Space and Time)"],["dc.relation.workinggroup","RG Bonn"],["dc.rights","This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited."],["dc.subject.gro","neuro biophysics"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","cellular biophysics"],["dc.title","A comparative analysis of the mobility of 45 proteins in the synaptic bouton"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","22357"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.lastpage","11"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Sandmann, Rabea"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","Blood platelets are instrumental in blood clotting and are thus heavily involved in early wound closure. After adhering to a substrate they spread by forming protrusions like lamellipodia and filopodia. However, the interaction of these protrusions with the physical environment of platelets while spreading is not fully understood. Here we dynamically image platelets during this spreading process and compare their behavior on smooth and on structured substrates. In particular we analyze the temporal evolution of the spread area, the cell morphology and the dynamics of individual filopodia. Interestingly, the topographic cues enable us to distinguish two spreading mechanisms, one that is based on numerous persistent filopodia and one that rather involves lamellipodia. Filopodia-driven spreading coincides with a strong response of platelet morphology to the substrate topography during spreading, whereas lamellipodia-driven spreading does not. Thus, we quantify different degrees of filopodia formation in platelets and the influence of filopodia in spreading on structured substrates."],["dc.identifier.doi","10.1038/srep22357"],["dc.identifier.gro","3141715"],["dc.identifier.isi","000371224600001"],["dc.identifier.pmid","26934830"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13186"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/269"],["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","2045-2322"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.rights","CC BY 4.0"],["dc.subject.gro","cellular biophysics"],["dc.title","Topographic Cues Reveal Two Distinct Spreading Mechanisms in Blood Platelets"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]