Schaap, Iwan A. T.

[["dc.bibliographiccitation.artnumber","443001"],["dc.bibliographiccitation.issue","44"],["dc.bibliographiccitation.journal","Journal of Physics. D, Applied Physics"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Ando, Toshio"],["dc.contributor.author","Bhamidimarri, Satya Prathyusha"],["dc.contributor.author","Brending, Niklas"],["dc.contributor.author","Colin-York, H."],["dc.contributor.author","Collinson, Lucy"],["dc.contributor.author","De Jonge, Niels"],["dc.contributor.author","de Pablo, P. J."],["dc.contributor.author","Debroye, Elke"],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Franck, Christian"],["dc.contributor.author","Fritzsche, Marco"],["dc.contributor.author","Gerritsen, Hans"],["dc.contributor.author","Giepmans, Ben N. G."],["dc.contributor.author","Grunewald, Kay"],["dc.contributor.author","Hofkens, Johan"],["dc.contributor.author","Hoogenboom, Jacob P."],["dc.contributor.author","Janssen, Kris P. F."],["dc.contributor.author","Kaufman, Rainer"],["dc.contributor.author","Klumpermann, Judith"],["dc.contributor.author","Kurniawan, Nyoman"],["dc.contributor.author","Kusch, Jana"],["dc.contributor.author","Liv, Nalan"],["dc.contributor.author","Parekh, Viha"],["dc.contributor.author","Peckys, Diana B."],["dc.contributor.author","Rehfeldt, Florian"],["dc.contributor.author","Reutens, David C."],["dc.contributor.author","Roeffaers, Maarten B. J."],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Schwarz, Ulrich S."],["dc.contributor.author","Verkade, Paul"],["dc.contributor.author","Vogel, Michael W."],["dc.contributor.author","Wagner, Richard"],["dc.contributor.author","Winterhalter, Mathias"],["dc.contributor.author","Yuan, Haifeng"],["dc.contributor.author","Zifarelli, Giovanni"],["dc.date.accessioned","2020-03-10T15:26:08Z"],["dc.date.available","2020-03-10T15:26:08Z"],["dc.date.issued","2018"],["dc.description.abstract","Developments in microscopy have been instrumental to progress in the life sciences, and many new techniques have been introduced and led to new discoveries throughout the last century. A wide and diverse range of methodologies is now available, including electron microscopy, atomic force microscopy, magnetic resonance imaging, small-angle x-ray scattering and multiple super-resolution fluorescence techniques, and each of these methods provides valuable read-outs to meet the demands set by the samples under study. Yet, the investigation of cell development requires a multi-parametric approach to address both the structure and spatio-temporal organization of organelles, and also the transduction of chemical signals and forces involved in cell-cell interactions. Although the microscopy technologies for observing each of these characteristics are well developed, none of them can offer read-out of all characteristics simultaneously, which limits the information content of a measurement. For example, while electron microscopy is able to disclose the structural layout of cells and the macromolecular arrangement of proteins, it cannot directly follow dynamics in living cells. The latter can be achieved with fluorescence microscopy which, however, requires labelling and lacks spatial resolution. A remedy is to combine and correlate different readouts from the same specimen, which opens new avenues to understand structure-function relations in biomedical research. At the same time, such correlative approaches pose new challenges concerning sample preparation, instrument stability, region of interest retrieval, and data analysis. Because the field of correlative microscopy is relatively young, the capabilities of the various approaches have yet to be fully explored, and uncertainties remain when considering the best choice of strategy and workflow for the correlative experiment. With this in mind, the Journal of Physics D: Applied Physics presents a special roadmap on the correlative microscopy techniques, giving a comprehensive overview from various leading scientists in this field, via a collection of multiple short viewpoints."],["dc.identifier.doi","10.1088/1361-6463/aad055"],["dc.identifier.pmid","30799880"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63287"],["dc.language.iso","en"],["dc.relation.issn","0022-3727"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights","CC BY 4.0"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","other"],["dc.title","The 2018 correlative microscopy techniques roadmap"],["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","7523"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Butkevich, Eugenia"],["dc.contributor.author","Bodensiek, Kai"],["dc.contributor.author","Fakhri, Nikta"],["dc.contributor.author","von Roden, Kerstin"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Majoul, Irina"],["dc.contributor.author","Schmidt, Christoph"],["dc.contributor.author","Klopfenstein, Dieter R."],["dc.date.accessioned","2017-09-07T11:43:42Z"],["dc.date.available","2017-09-07T11:43:42Z"],["dc.date.issued","2015"],["dc.description.abstract","Actin filament organization and stability in the sarcomeres of muscle cells are critical for force generation. Here we identify and functionally characterize a Caenorhabditis elegans drebrin-like protein DBN-1 as a novel constituent of the muscle contraction machinery. In vitro, DBN-1 exhibits actin filament binding and bundling activity. In vivo, DBN-1 is expressed in body wall muscles of C. elegans. During the muscle contraction cycle, DBN-1 alternates location between myosin- and actin-rich regions of the sarcomere. In contracted muscle, DBN-1 is accumulated at I-bands where it likely regulates proper spacing of alpha-actinin and tropomyosin and protects actin filaments from the interaction with ADF/cofilin. DBN-1 loss of function results in the partial depolymerization of F-actin during muscle contraction. Taken together, our data show that DBN-1 organizes the muscle contractile apparatus maintaining the spatial relationship between actin-binding proteins such as alpha-actinin, tropomyosin and ADF/cofilin and possibly strengthening actin filaments by bundling."],["dc.identifier.doi","10.1038/ncomms8523"],["dc.identifier.gro","3141869"],["dc.identifier.isi","000358851600001"],["dc.identifier.pmid","26146072"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1978"],["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.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction"],["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","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"]]