Köster, Sarah

[["dc.bibliographiccitation.firstpage","705"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Acta crystallographica. Section D, Structural biology"],["dc.bibliographiccitation.lastpage","717"],["dc.bibliographiccitation.volume","72"],["dc.contributor.author","Tauchert, Marcel J."],["dc.contributor.author","Hémonnot, Clément"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Dickmanns, Achim"],["dc.date.accessioned","2020-12-10T18:26:04Z"],["dc.date.available","2020-12-10T18:26:04Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotic cells, the exchange of macromolecules between the nucleus and cytoplasm is highly selective and requires specialized soluble transport factors. Many of them belong to the importin-beta superfamily, the members of which share an overall superhelical structure owing to the tandem arrangement of a specific motif, the HEAT repeat. This structural organization leads to great intrinsic flexibility, which in turn is a prerequisite for the interaction with a variety of proteins and for its transport function. During the passage from the aqueous cytosol into the nucleus, the receptor passes the gated channel of the nuclear pore complex filled with a protein meshwork of unknown organization, which seems to be highly selective owing to the presence of FG-repeats, which are peptides with hydrophobic patches. Here, the structural changes of free importin-beta from a single organism, crystallized in polar (salt) or apolar (PEG) buffer conditions, are reported. This allowed analysis of the structural changes, which are attributable to the surrounding milieu and are not affected by bound interaction partners. The importin-beta structures obtained exhibit significant conformational changes and suggest an influence of the polarity of the environment, resulting in an extended conformation in the PEG condition. The significance of this observation is supported by SAXS experiments and the analysis of other crystal structures of importin-beta deposited in the Protein Data Bank."],["dc.identifier.doi","10.1107/S2059798316004940"],["dc.identifier.fs","622294"],["dc.identifier.gro","3141673"],["dc.identifier.isi","000379911500002"],["dc.identifier.issn","2059-7983"],["dc.identifier.pmid","27303791"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75940"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2059-7983"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of the crystallization condition on importin-β conformation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2059"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","2068"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Brennich, Martha Elisabeth"],["dc.contributor.author","Bauch, Susanne"],["dc.contributor.author","Vainio, Ulla"],["dc.contributor.author","Wedig, Tatjana"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:46:55Z"],["dc.date.available","2017-09-07T11:46:55Z"],["dc.date.issued","2014"],["dc.description.abstract","The assembly kinetics of intermediate filament (IF) proteins from tetrameric complexes to single filaments and networks depends on the protein concentration, temperature and the ionic composition of their environment. We systematically investigate how changes in the concentration of monovalent potassium and divalent magnesium ions affect the internal organization of the resulting filaments. Small angle X-ray scattering (SAXS) is very sensitive to changes in the filament cross-section such as diameter or compactness. Our measurements reveal that filaments formed in the presence of magnesium chloride differ distinctly from filaments formed in the presence of potassium chloride. The principle multi-step assembly mechanism from tetramers via unit-length filaments (ULF) to elongated filaments is not changed by the valency of ions. However, the observed differences indicate that the magnesium ions free the head domains of tetramers from unproductive interactions to allow assembly but at the same time mediate strong inter-tetrameric interactions that impede longitudinal annealing of unit-length filaments considerably, thus slowing down filament growth."],["dc.identifier.doi","10.1039/c3sm52532e"],["dc.identifier.gro","3142216"],["dc.identifier.isi","000332463300021"],["dc.identifier.pmid","24800271"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5821"],["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","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Impact of ion valency on the assembly of vimentin studied by quantitative small angle X-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["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.firstpage","3313"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biomacromolecules"],["dc.bibliographiccitation.lastpage","3321"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Hémonnot, Clément Y. J."],["dc.contributor.author","Mauermann, Monika"],["dc.contributor.author","Herrmann, Harald"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:43:30Z"],["dc.date.available","2017-09-07T11:43:30Z"],["dc.date.issued","2015"],["dc.description.abstract","The intermediate filament proteins keratin K8 and K18 constitute an essential part of the cytoskeleton in simple epithelial cell layers, structurally enforcing their mechanical resistance. K8/K18 heterodimers form extended filaments and higher-order structures including bundles and networks that bind to cell junctions. We study the assembly of these proteins in the presence of monovalent or divalent ions by small-angle X-ray scattering. We find that both ion species cause an increase of the filament diameter when their concentration is increased; albeit, much higher values are needed for the monovalent compared to the divalent ions for the same effect. Bundling occurs also for monovalent ions and at comparatively low concentrations of divalent ions, very different from vimentin intermediate filaments, a fibroblast-specific cytoskeleton component. We explain these differences by variations in charge and hydrophobicity patterns of the proteins. These differences may reflect the respective physiological situation in stationary cell layers versus single migrating fibroblasts."],["dc.identifier.doi","10.1021/acs.biomac.5b00965"],["dc.identifier.gro","3141817"],["dc.identifier.isi","000362863500025"],["dc.identifier.pmid","26327161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1401"],["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","1526-4602"],["dc.relation.issn","1525-7797"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Assembly of Simple Epithelial Keratin Filaments: Deciphering the Ion Dependence in Filament Organization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2167"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biomacromolecules"],["dc.bibliographiccitation.lastpage","2172"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Pfohl, Thomas"],["dc.contributor.author","Otten, Alexander"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Dootz, Rolf"],["dc.contributor.author","Struth, Bernd"],["dc.contributor.author","Evans, Heather M."],["dc.date.accessioned","2017-09-07T11:49:28Z"],["dc.date.available","2017-09-07T11:49:28Z"],["dc.date.issued","2007"],["dc.description.abstract","DNA condensation in vivo usually requires proteins and/or multivalent salts. Here, we explore the in vitro compaction of DNA by cationic dendrimers having an intermediate size and charge. The dynamic assembly of DNA-dendrimer mesophases is discernible due to the laminar flow in a specially designed X-ray compatible microfluidic device. The setup ensures a nonequilibrium ascent of reactant concentration, and the resulting progression of DNA compaction was detected online using microfocused small-angle X-ray diffraction. The evolution of a DNA-dendrimer columnar square mesophase as a function of increasing dendrimer content is described. Additionally, in regions of maximum shear, an unexpected high-level perpendicular ordering of this phase is recorded. Furthermore, these assemblies are found to be in coexistence with a densely packed DNA-only mesophase in regions of excess DNA. The latter is reminiscent of dense packing found in bacteriophage and chromosomes, although surprisingly, it is not stabilized by direct dendrimer contact."],["dc.identifier.doi","10.1021/bm070317s"],["dc.identifier.gro","3143474"],["dc.identifier.isi","000247820000019"],["dc.identifier.pmid","17579478"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/992"],["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","1525-7797"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Highly packed and oriented DNA mesophases identified using in situ microfluidic X-ray microdiffraction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8445"],["dc.bibliographiccitation.issue","42"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","8454"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Saldanha, Oliva"],["dc.contributor.author","Aufderhorst-Roberts, Anders"],["dc.contributor.author","Martinez-Torres, Cristina"],["dc.contributor.author","Kuijs, Merel"],["dc.contributor.author","Koenderink, Gijsje H."],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Huber, Klaus"],["dc.contributor.author","Lopez, Carlos G."],["dc.date.accessioned","2020-12-10T18:11:25Z"],["dc.date.available","2020-12-10T18:11:25Z"],["dc.date.issued","2018"],["dc.description.abstract","Intermediate filaments are a major structural element in the cytoskeleton of animal cells that mechanically integrate other cytoskeletal components and absorb externally applied stress. Their role is likely to be linked to their complex molecular architecture which is the product of a multi-step assembly pathway. Intermediate filaments form tetrameric subunits which assemble in the presence of monovalent salts to form unit length filaments that subsequently elongate by end-to-end annealing. The present work characterizes this complex assembly process using reconstituted vimentin intermediate filaments with monovalent salts as an assembly trigger. A multi-scale approach is used, comprising static light scattering, dynamic light scattering and quantitative scanning transmission electron microscopy (STEM) mass measurements. Light scattering reveals the radius of gyration (Rg), molecular weight (Mw) and diffusion coefficient (D) of the assembling filaments as a function of time and salt concentration (cS) for the given protein concentration of 0.07 g L−1. At low cS (10 mM KCl) no lateral or elongational growth is observed, whereas at cS = 50–200 mM, the hydrodynamic cross-sectional radius and the elongation rate increases with cS. Rgversus Mw plots suggest that the mass per unit length increases with increasing salt content, which is confirmed by STEM mass measurements. A kinetic model based on rate equations for a two step process is able to accurately describe the variation of mass, length and diffusion coefficient of the filaments with time and provides a consistent description of the elongation accelerated by increasing cS."],["dc.identifier.doi","10.1039/C8SM01007B"],["dc.identifier.eissn","1744-6848"],["dc.identifier.issn","1744-683X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74005"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation.eissn","1744-6848"],["dc.relation.issn","1744-683X"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Effect of ionic strength on the structure and elongational kinetics of vimentin filaments"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","745"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Synchrotron Radiation"],["dc.bibliographiccitation.lastpage","750"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Otten, Alexander"],["dc.contributor.author","Köster, Sarah"],["dc.contributor.author","Struth, Bernd"],["dc.contributor.author","Snigirev, Anatoly"],["dc.contributor.author","Pfohl, Thomas"],["dc.date.accessioned","2017-09-07T11:53:40Z"],["dc.date.available","2017-09-07T11:53:40Z"],["dc.date.issued","2005"],["dc.description.abstract","The combination of X- ray microdiffraction and microfluidics is used to investigate the dynamic behaviour of soft materials. A microfocused X- ray beam enables the observation of the influence of droplet formation on the nanostructure of a smectic liquid crystal in water. Using a hydrodynamic focusing device, the evolution of the intercalation of DNA into multilamellar membranes can be studied. Owing to the elongational flow at the centre of this device, alignment of the material is induced which allows for an improved structural characterization. Furthermore, the influence of strain applied to these materials can be tested."],["dc.identifier.doi","10.1107/S0909049505013580"],["dc.identifier.gro","3143792"],["dc.identifier.isi","000232619300009"],["dc.identifier.pmid","16239743"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1344"],["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","0909-0495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","molecular biophysics"],["dc.subject.gro","microfluidics"],["dc.title","Microfluidics of soft matter investigated by small-angle X-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","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.firstpage","11152"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","11157"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Lopez, Carlos G."],["dc.contributor.author","Saldanha, Oliva"],["dc.contributor.author","Huber, Klaus"],["dc.contributor.author","Köster, Sarah"],["dc.date.accessioned","2017-09-07T11:44:34Z"],["dc.date.available","2017-09-07T11:44:34Z"],["dc.date.issued","2016"],["dc.description.abstract","Vimentin intermediate filaments (IFs) are part of a family of proteins that constitute one of the three filament systems in the cytoskeleton, a major contributor to cell mechanics. One property that distinguishes IFs from the other cytoskeletal filament types, actin filaments and microtubules, is their highly hierarchical assembly pathway, where a lateral association step is followed by elongation. Here we present an innovative technique to follow the elongation reaction in solution and in situ by time-resolved static and dynamic light scattering, thereby precisely capturing the relevant time and length scales of seconds to minutes and 60-600 nm, respectively. We apply a quantitative model to our data and succeed in consistently describing the entire set of data, including particle mass, radius of gyration, and hydrodynamic radius during longitudinal association."],["dc.identifier.doi","10.1073/pnas.1606372113"],["dc.identifier.gro","3141606"],["dc.identifier.isi","000384528900047"],["dc.identifier.pmid","27655889"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/457"],["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","0027-8424"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Köster (Cellular Biophysics)"],["dc.subject.gro","cytoskeleton"],["dc.subject.gro","molecular biophysics"],["dc.title","Lateral association and elongation of vimentin intermediate filament proteins: A time-resolved light-scattering study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]