Platen, Mitja

[["dc.bibliographiccitation.firstpage","519"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","533"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Dannhauser, Philip N."],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Boening, Heike"],["dc.contributor.author","Ungewickell, Huberta"],["dc.contributor.author","Schaap, Iwan Alexander Taco"],["dc.contributor.author","Ungewickell, Ernst J."],["dc.date.accessioned","2018-11-07T09:58:02Z"],["dc.date.available","2018-11-07T09:58:02Z"],["dc.date.issued","2015"],["dc.description.abstract","Clathrin-dependent transport processes require the polymerization of clathrin triskelia into polygonal scaffolds. Together with adapter proteins, clathrin collects cargo and induces membrane bud formation. It is not known to what extent clathrin light chains affect the structural and functional properties of clathrin lattices and the ability of clathrin to deform membranes. To address these issues, we have developed a novel procedure for analyzing clathrin lattice formation on rigid surfaces. We found that lattices can form on adaptor-coated convex-, planar- and even shallow concave surfaces, but the rate of formation and resistance to thermal dissociation of the lattice are greatly enhanced on convex surfaces. Atomic force microscopy on planar clathrin lattices demonstrates that the stiffness of the clathrin lattice is strictly dependent on light chains. The reduced stiffness of the lattice also compromised the ability of clathrin to generate coated buds on the surface of rigid liposomal membranes."],["dc.identifier.doi","10.1111/tra.12263"],["dc.identifier.isi","000353461400006"],["dc.identifier.pmid","25652138"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37289"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1600-0854"],["dc.relation.issn","1398-9219"],["dc.title","Effect of Clathrin Light Chains on the Stiffness of Clathrin Lattices and Membrane Budding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nano Letters"],["dc.bibliographiccitation.lastpage","242"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Chizhik, Anna M."],["dc.contributor.author","Stein, Simon"],["dc.contributor.author","Dekaliuk, Mariia O."],["dc.contributor.author","Battle, Christopher"],["dc.contributor.author","Li, Weixing"],["dc.contributor.author","Huss, Anja"],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Demchenko, Alexander P."],["dc.contributor.author","Schmidt, Christoph F."],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Chizhik, Alexey"],["dc.date.accessioned","2017-09-07T11:54:46Z"],["dc.date.available","2017-09-07T11:54:46Z"],["dc.date.issued","2016"],["dc.description.abstract","Success in super-resolution imaging relies on a proper choice of fluorescent probes. Here, we suggest novel easily produced and biocompatible nanoparticles-carbon nanodots-for super-resolution optical fluctuation bioimaging (SOFT). The particles revealed an intrinsic dual-color fluorescence, which corresponds to two subpopulations of particles of different electric charges. The neutral nanoparticles localize to cellular nuclei suggesting their potential use as an inexpensive, easily produced nucleus-specific label. The single particle study revealed that the carbon nanodots possess a unique hybrid combination of fluorescence properties exhibiting characteristics of both dye molecules and semiconductor nanocrystals. The results suggest that charge trapping and redistribution on the surface of the particles triggers their transitions between emissive and dark states. These findings open up new possibilities for the utilization of carbon nanodots in the various super-resolution microscopy methods based on stochastic optical switching."],["dc.identifier.doi","10.1021/acs.nanolett.5b03609"],["dc.identifier.gro","3141754"],["dc.identifier.isi","000368322700038"],["dc.identifier.pmid","26605640"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/702"],["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","1530-6992"],["dc.relation.issn","1530-6984"],["dc.title","Super-Resolution Optical Fluctuation Bio-Imaging with Dual-Color Carbon Nanodots"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7868"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","7876"],["dc.bibliographiccitation.volume","291"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Junius, Meike"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","van den Bogaart, Geert"],["dc.date.accessioned","2020-12-10T18:12:56Z"],["dc.date.available","2020-12-10T18:12:56Z"],["dc.date.issued","2016"],["dc.description.abstract","Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) is a minor component of total plasma membrane lipids, but it has a substantial role in the regulation of many cellular functions, including exo- and endocytosis. Recently, it was shown that PI(4,5)P2and syntaxin 1, a SNARE protein that catalyzes regulated exocytosis, form domains in the plasma membrane that constitute recognition sites for vesicle docking. Also, calcium was shown to promote syntaxin 1 clustering in the plasma membrane, but the molecular mechanism was unknown. Here, using a combination of superresolution stimulated emission depletion microscopy, FRET, and atomic force microscopy, we show that Ca(2+)acts as a charge bridge that specifically and reversibly connects multiple syntaxin 1/PI(4,5)P2complexes into larger mesoscale domains. This transient reorganization of the plasma membrane by physiological Ca(2+)concentrations is likely to be important for Ca(2+)-regulated secretion."],["dc.identifier.doi","10.1074/jbc.M116.716225"],["dc.identifier.eissn","1083-351X"],["dc.identifier.issn","0021-9258"],["dc.identifier.pmid","26884341"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74536"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.relation.eissn","0021-9258"],["dc.rights","Goescholar"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.title","Calcium Promotes the Formation of Syntaxin 1 Mesoscale Domains through Phosphatidylinositol 4,5-Bisphosphate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","954"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Nanotechnology"],["dc.bibliographiccitation.lastpage","U194"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Dannhauser, Philip N."],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Boening, Heike"],["dc.contributor.author","Schaap, I. A. T."],["dc.date.accessioned","2018-11-07T09:49:35Z"],["dc.date.available","2018-11-07T09:49:35Z"],["dc.date.issued","2015"],["dc.description.abstract","Biological molecules that self-assemble and interact with other molecules are attractive building blocks for engineering biological devices. DNA has been widely used for the creation of nanomaterials(1), but the use of proteins remains largely unexplored. Here, we show that clathrin can form homogeneous and extended two-dimensional lattices on a variety of substrates, including glass, metal, carbon and plastic. Clathrin is a threelegged protein complex with unique self-assembling properties and is relevant in the formation of membrane transport vesicles in eukaryotic cells(2,3). We used a fragment of the adaptor protein epsin to immobilize clathrin lattices on the substrates. The lattices span multiple square millimetres with a regular periodicity of 30 nm and can be functionalized via modified subunits of clathrin with either inorganic nanoparticles or active enzymes. The lattices can be stored for months after crosslinking and stabilization with uranyl acetate. They could be dehydrated and rehydrated without loss of function, offering potential applications in sensing and as biosynthetic reactors."],["dc.identifier.doi","10.1038/NNANO.2015.206"],["dc.identifier.isi","000364528300012"],["dc.identifier.pmid","26367107"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35538"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1748-3395"],["dc.relation.issn","1748-3387"],["dc.title","Durable protein lattices of clathrin that can be functionalized with nanoparticles and active biomolecules"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1821"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Analytical Chemistry"],["dc.bibliographiccitation.lastpage","1828"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Wang, Y. U."],["dc.contributor.author","Modena, Mario Matteo"],["dc.contributor.author","Platen, Mitja"],["dc.contributor.author","Schaap, Iwan Alexander Taco"],["dc.contributor.author","Burg, Thomas Peter"],["dc.date.accessioned","2018-11-07T10:01:05Z"],["dc.date.available","2018-11-07T10:01:05Z"],["dc.date.issued","2015"],["dc.description.abstract","Protein aggregation is a widely studied phenomenon that is associated with many human diseases and with the degradation of biotechnological products. Here, we establish a new label-free method for characterizing the aggregation kinetics of proteins into amyloid fibrils by suspended microchannel resonators (SMR). SMR devices are unique in their ability to provide mass-based measurements under reaction-limited conditions in a 10 pL volume. To demonstrate the method, insulin seed fibrils of defined length, characterized by atomic force microscopy (AFM) and transmission electron microscopy (TEM), were covalently immobilized inside microchannels embedded within a micromechanical resonator, and the elongation of these fibrils under a continuous flow of monomer solution (rate similar to 1 nL/s) was measured by monitoring the resonance frequency shift. The kinetics for concentrations below similar to 0.6 mg/mL fits well with an irreversible bimolecular binding model with the rate constant kon = (1.2 +/- 0.1) x103 M-1 s(-1). Rate saturation occurred at higher concentrations. The nonlinear on-rate for monomer concentrations from 0 to 6 mg/mL and for temperatures from 20 to 42 degrees C fit well globally with an energy landscape model characterized by a single activation barrier. Finally, elongation rates were studied under different solution conditions and in the presence of a small molecule inhibitor of amyloid growth. Due to the low volume requirements, high precision, and speed of SMR measurements, the method may become a valuable new tool in the screening for inhibitors and the study of fundamental biophysical mechanisms of protein aggregation processes."],["dc.identifier.doi","10.1021/ac503845f"],["dc.identifier.isi","000349059000056"],["dc.identifier.pmid","25539393"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37940"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1520-6882"],["dc.relation.issn","0003-2700"],["dc.title","Label-Free Measurement of Amyloid Elongation by Suspended Microchannel Resonators"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]