title: Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain.
authors.affiliation: ICREA and the Biomedical Research Institute of Barcelona, Barcelona Science Park, Barcelona, Spain.
authors.forename: Alison Z
authors.initials: AZ
authors.lastname: Shaw
authors.forename: Pau
authors.initials: P
authors.lastname: Martin-Malpartida
authors.forename: Begoña
authors.initials: B
authors.lastname: Morales
authors.forename: Francesc
authors.initials: F
authors.lastname: Yraola
authors.forename: Miriam
authors.initials: M
authors.lastname: Royo
authors.forename: Maria J
authors.initials: MJ
authors.lastname: Macias
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001703:Biophysics / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D040901:Proteomics / Q000379:methods*; D012694:Serine / Q000737:chemistry*; D013912:Threonine / Q000737:chemistry*; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry*
chemical_list: D013912:Threonine; D012694:Serine; D044767:Ubiquitin-Protein Ligases