Publikation:

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

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Schneider_289791.pdf
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2014

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http://nbn-resolving.de/urn:nbn:de:bsz:352-289791
DOI (zitierfähiger Link)
https://doi.org/10.1002/anie.201407192
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Angewandte Chemie International Edition. 2014, 53(47), pp. 12925-12929. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201407192

Zusammenfassung

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.

Zusammenfassung in einer weiteren Sprache

Fachgebiet (DDC)
540 Chemie

Schlagwörter

click chemistry, codon expansion, posttranslational modification, ubiquitin chains, unnatural amino acids

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ISO 690SCHNEIDER, 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. 2014, 53(47), pp. 12925-12929. ISSN 1433-7851. eISSN 1521-3773. Available under: doi: 10.1002/anie.201407192
BibTex
@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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