title: Isolation of ubiquitylated proteins using tandem ubiquitin-binding entities.
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.
authors.affiliation: Proteomics Unit, CIC bioGUNE, CIBERehd, Technology Park of Bizkaia, Derio, Spain.
authors.forename: Fabienne
authors.initials: F
authors.lastname: Aillet
authors.forename: Fernando
authors.initials: F
authors.lastname: Lopitz-Otsoa
authors.forename: Roland
authors.initials: R
authors.lastname: Hjerpe
authors.forename: Mónica
authors.initials: M
authors.lastname: Torres-Ramos
authors.forename: Valérie
authors.initials: V
authors.lastname: Lang
authors.forename: Manuel S
authors.initials: MS
authors.lastname: Rodríguez
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods*; D025821:Polyubiquitin / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D054875:Ubiquitination
chemical_list: D025821:Polyubiquitin