Schaap, Iwan A. T.

[["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","5656"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nano Letters"],["dc.bibliographiccitation.lastpage","5661"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Ghosh, Siddharth"],["dc.contributor.author","Chizhik, Anna M."],["dc.contributor.author","Karedla, Narain"],["dc.contributor.author","Dekaliuk, Mariia O."],["dc.contributor.author","Gregor, Ingo"],["dc.contributor.author","Schuhmann, Henning"],["dc.contributor.author","Seibt, Michael"],["dc.contributor.author","Bodensiek, Kai"],["dc.contributor.author","Schaap, Iwan A. T."],["dc.contributor.author","Schulz, Olaf"],["dc.contributor.author","Demchenko, Alexander P."],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Chizhik, Alexey I."],["dc.date.accessioned","2018-04-23T11:49:26Z"],["dc.date.available","2018-04-23T11:49:26Z"],["dc.date.issued","2014"],["dc.description.abstract","Inorganic carbon nanomaterials, also called carbon nanodots, exhibit a strong photoluminescence with unusual properties and, thus, have been the focus of intense research. Nonetheless, the origin of their photoluminescence is still unclear and the subject of scientific debates. Here, we present a single particle comprehensive study of carbon nanodot photoluminescence, which combines emission and lifetime spectroscopy, defocused emission dipole imaging, azimuthally polarized excitation dipole scanning, nanocavity-based quantum yield measurements, high resolution transmission electron microscopy, and atomic force microscopy. We find that photoluminescent carbon nanodots behave as electric dipoles, both in absorption and emission, and that their emission originates from the recombination of photogenerated charges on defect centers involving a strong coupling between the electronic transition and collective vibrations of the lattice structure."],["dc.identifier.doi","10.1021/nl502372x"],["dc.identifier.gro","3142116"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13696"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1530-6984"],["dc.title","Photoluminescence of Carbon Nanodots: Dipole Emission Centers and Electron–Phonon Coupling"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]