title: Peeling away the layers of ubiquitin signaling complexities with synthetic ubiquitin-protein conjugates.
abstract: Covalent attachment of ubiquitin, a process termed ubiquitination, affects the location, function, and stability of modified proteins. Significant advances have been made in building synthetic ubiquitin-protein conjugates that can be used to investigate how ubiquitin regulates diverse biological processes. Herein we describe recent advances and discuss how chemical methods have been implemented to address the molecular underpinnings of ubiquitin-dependent cellular signaling.
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States.
authors.forename: Grace H
authors.initials: GH
authors.lastname: Pham
authors.affiliation: Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States. Electronic address: strieter@chem.wisc.edu.
authors.forename: Eric R
authors.initials: ER
authors.lastname: Strieter
mesh_terms: D000818:Animals; D006801:Humans; D008958:Models, Molecular; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D011506:Proteins; D025801:Ubiquitin