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","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"]]