@article{Schneider2014-11-17Disse-28979,
  year={2014},
  doi={10.1002/anie.201407192},
  title={Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains},
  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}
}

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    <dc:contributor>Malhotra, Saurav</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>
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    <dc:contributor>Rösner, Daniel</dc:contributor>
    <dcterms:title>Dissecting Ubiquitin Signaling with Linkage-defined and Protease Resistant Ubiquitin Chains</dcterms:title>
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    <dc:creator>Mayer, Thomas U.</dc:creator>
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    <dc:contributor>Mortensen, Franziska</dc:contributor>
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    <dc:contributor>Schneider, Daniel</dc:contributor>
    <dc:contributor>Mayer, Thomas U.</dc:contributor>
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    <dc:contributor>Schneider, Tatjana</dc:contributor>
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