title: A Billion Ubiquitin Variants to Probe and Modulate the UPS.
abstract: Low-affinity but highly specific protein-protein interactions abound within the ubiquitin-proteasome system (UPS). Selection for ubiquitin variants (UbVs) that bind tightly to HECT ubiquitin ligases proved remarkably useful for probing enzyme mechanism and modulating E3 activities in cells.
authors.affiliation: Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA.
authors.forename: Larissa A
authors.initials: LA
authors.lastname: Canadeo
authors.affiliation: Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: huibregtse@austin.utexas.edu.
authors.forename: Jon M
authors.initials: JM
authors.lastname: Huibregtse
mesh_terms: D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism
chemical_list: D025801:Ubiquitin; D044767:Ubiquitin-Protein Ligases; D046988:Proteasome Endopeptidase Complex