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Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains

Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains

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SCHNEIDER, Tatjana, Daniel SCHNEIDER, Daniel RÖSNER, Saurav MALHOTRA, Franziska MORTENSEN, Thomas U. MAYER, Martin SCHEFFNER, Andreas MARX, 2014. Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains. In: Angewandte Chemie International Edition. 53(47), pp. 12925-12929. ISSN 1433-7851. eISSN 1521-3773

@article{Schneider2014-11-17Disse-28979, title={Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains}, year={2014}, doi={10.1002/anie.201407192}, number={47}, volume={53}, issn={1433-7851}, journal={Angewandte Chemie International Edition}, pages={12925--12929}, author={Schneider, Tatjana and Schneider, Daniel and Rösner, Daniel and Malhotra, Saurav and Mortensen, Franziska and Mayer, Thomas U. and Scheffner, Martin and Marx, Andreas} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/28979"> <dc:contributor>Mortensen, Franziska</dc:contributor> <dc:creator>Malhotra, Saurav</dc:creator> <dc:contributor>Marx, Andreas</dc:contributor> <dcterms:issued>2014-11-17</dcterms:issued> <dc:creator>Schneider, Tatjana</dc:creator> <dc:creator>Scheffner, Martin</dc:creator> <dc:contributor>Schneider, Tatjana</dc:contributor> <dc:contributor>Schneider, Daniel</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-09-19T09:18:06Z</dcterms:available> <dc:creator>Mortensen, Franziska</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Rösner, Daniel</dc:contributor> <dcterms:abstract xml:lang="eng">Ubiquitylation is a complex posttranslational protein modification and deregulation of this pathway has been associated with different human disorders. Ubiquitylation comes in different flavors: Besides mono-ubiquitylation, ubiquitin chains of various topologies are formed on substrate proteins. The fate of ubiquitylated proteins is determined by the linkage-type of the attached ubiquitin chains, however, the underlying mechanism is poorly characterized. Herein, we describe a new method based on codon expansion and click-chemistry-based polymerization to generate linkage-defined ubiquitin chains that are resistant to ubiquitin-specific proteases and adopt native-like functions. The potential of these artificial chains for analyzing ubiquitin signaling is demonstrated by linkage-specific effects on cell-cycle progression.</dcterms:abstract> <dcterms:title>Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains</dcterms:title> <dc:creator>Rösner, Daniel</dc:creator> <dcterms:rights rdf:resource="http://nbn-resolving.org/urn:nbn:de:bsz:352-20140905103605204-4002607-1"/> <dc:contributor>Mayer, Thomas U.</dc:contributor> <dc:creator>Schneider, Daniel</dc:creator> <dc:contributor>Scheffner, Martin</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/28979"/> <dc:rights>deposit-license</dc:rights> <dc:creator>Marx, Andreas</dc:creator> <dc:contributor>Malhotra, Saurav</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2014-09-19T09:18:06Z</dc:date> <dc:creator>Mayer, Thomas U.</dc:creator> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 01.10.2014 (Informationen über die Zugriffsstatistik)

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