title: Lingering mysteries of ubiquitin-chain assembly.
abstract: The small protein ubiquitin is often linked to substrates as a polymer. Such polymers vary in both linkage and length, which has important consequences for their function. Surprisingly, the mechanisms of ubiquitin-chain assembly are still not known. Deciphering them will shed light on why substrates differ in the extent and timing of polyubiquitin modification and how ancillary ubiquitination factors function.
authors.affiliation: Yale University, Department of Molecular Biophysics & Biochemistry, New Haven, CT 06520, USA. mark.hochstrasser@yale.edu
authors.forename: Mark
authors.initials: M
authors.lastname: Hochstrasser
mesh_terms: D001665:Binding Sites / Q000502:physiology; D008958:Models, Molecular; D025801:Ubiquitin / Q000096:biosynthesis* / Q000737:chemistry / Q000502:physiology; D043743:Ubiquitin-Protein Ligase Complexes / Q000737:chemistry / Q000502:physiology
chemical_list: D025801:Ubiquitin; D043743:Ubiquitin-Protein Ligase Complexes