Publikation: Formation of ubiquitin dimers via azide-alkyne click reaction
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2012
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DOHMEN, R. Jürgen, ed., Martin SCHEFFNER, ed.. Ubiquitin Family Modifiers and the Proteasome. Totowa, NJ: Humana Press, 2012, pp. 589-596. Methods in Molecular Biology. 832. ISBN 978-1-61779-473-5. Available under: doi: 10.1007/978-1-61779-474-2_41
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The conjugation of poly-ubiquitin chains is a widespread post-translational modification of proteins that plays a role in many different cellular processes. Notably, the biological function of the attached ubiquitin chain depends on which lysine residue is used for chain formation. Here, we report a method for the modular synthesis of site-specifically linked ubiquitin dimers, which is based on click reaction between two artificial amino acids. In this way, it is possible to synthesize all seven naturally occurring ubiquitin connectivities, thus giving access to all ubiquitin dimers. Furthermore, this method can be generally applied to link ubiquitin to any substrate protein or even to link any two proteins site specifically.
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EGER, Silvia, Martin SCHEFFNER, Andreas MARX, Marina RUBINI, 2012. Formation of ubiquitin dimers via azide-alkyne click reaction. In: DOHMEN, R. Jürgen, ed., Martin SCHEFFNER, ed.. Ubiquitin Family Modifiers and the Proteasome. Totowa, NJ: Humana Press, 2012, pp. 589-596. Methods in Molecular Biology. 832. ISBN 978-1-61779-473-5. Available under: doi: 10.1007/978-1-61779-474-2_41BibTex
@incollection{Eger2012Forma-21932,
year={2012},
doi={10.1007/978-1-61779-474-2_41},
title={Formation of ubiquitin dimers via azide-alkyne click reaction},
number={832},
isbn={978-1-61779-473-5},
publisher={Humana Press},
address={Totowa, NJ},
series={Methods in Molecular Biology},
booktitle={Ubiquitin Family Modifiers and the Proteasome},
pages={589--596},
editor={Dohmen, R. Jürgen and Scheffner, Martin},
author={Eger, Silvia and Scheffner, Martin and Marx, Andreas and Rubini, Marina}
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<dcterms:abstract xml:lang="eng">The conjugation of poly-ubiquitin chains is a widespread post-translational modification of proteins that plays a role in many different cellular processes. Notably, the biological function of the attached ubiquitin chain depends on which lysine residue is used for chain formation. Here, we report a method for the modular synthesis of site-specifically linked ubiquitin dimers, which is based on click reaction between two artificial amino acids. In this way, it is possible to synthesize all seven naturally occurring ubiquitin connectivities, thus giving access to all ubiquitin dimers. Furthermore, this method can be generally applied to link ubiquitin to any substrate protein or even to link any two proteins site specifically.</dcterms:abstract>
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