title: Methods for the purification of ubiquitinated proteins.
abstract: Post-translational protein modification by the covalent conjugation of ubiquitin, originally implicated as a signal for proteolytic degradation by 26S proteasome, has now been realised to play important roles in the regulation of almost all biological processes in eukaryotes. In order to understand these processes in greater detail there is a requirement for techniques that can purify mixtures of ubiquitin-conjugated proteins, as a prerequisite to their identification and characterisation. Here we review the methods that have been applied to the bulk purification of ubiquitinated proteins and discuss their applications in proteomic analyses of the 'ubiquitome'.
authors.affiliation: School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK.
authors.forename: Emma
authors.initials: E
authors.lastname: Tomlinson
authors.forename: Naaventhan
authors.initials: N
authors.lastname: Palaniyappan
authors.forename: David
authors.initials: D
authors.lastname: Tooth
authors.forename: Robert
authors.initials: R
authors.lastname: Layfield
mesh_terms: D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*
chemical_list: D011506:Proteins; D025801:Ubiquitin