Abstract
Studying postubiquitylation events has always been a difficult task due to the labile nature of these posttranslational modifications. When utilized in tandem, ubiquitin-binding entities (TUBEs) not only increase up to thousand times the affinity for poly-ubiquitin chains but also protect ubiquitylated proteins from the action of the proteasome and de-ubiquitylating enzymes.
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Acknowledgments
We would like to thank Seth Goldenberg for the critical reading of this document. This work was funded by the Ramón y Cajal Program, Ministerio de Educación y Ciencia grant BFU2006-12991 and BFU2008-01108/BMC, Fondo de Investigaciones Sanitarias (FIS) CIBERhed, Government of the Autonomous Community of the Basque Country grant PI09-05, Department of Industry, Tourism and Trade of the Government of the Autonomous Community of the Basque Country (Etortek Research Programs 2008/2009), and from the Innovation Technology Department of the Bizkaia County.
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Aillet, F., Lopitz-Otsoa, F., Hjerpe, R., Torres-Ramos, M., Lang, V., Rodríguez, M.S. (2012). Isolation of Ubiquitylated Proteins Using Tandem Ubiquitin-Binding Entities. In: Dohmen, R., Scheffner, M. (eds) Ubiquitin Family Modifiers and the Proteasome. Methods in Molecular Biology, vol 832. Humana Press. https://doi.org/10.1007/978-1-61779-474-2_12
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DOI: https://doi.org/10.1007/978-1-61779-474-2_12
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