Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding(505 views) Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2007; 46(42): 7993-7995.
Keywords: Copper, Neurodegenerative Diseases, Nmr Spectroscopy, Ubiquitin, Binding Sites, Ligands, Metal Ions, Nitrogen, Nuclear Magnetic Resonance Spectroscopy, Proteins, Neurodegenerative Disorders, Oxygen Donor Ligands, Tetragonal Geometry, Ubiquitin Stability, Toxic Materials, Lysine, Polyubiquitin, Article, Chemical Structure, Chemistry, Differential Scanning Calorimetry, Human, Methodology, Protein Conformation, Protein Tertiary Structure, Solution And Solubility, Ubiquitination, Models, Molecular, Protein Structure, Differential Scanning Methods, Copper Chemistry, Lysine Chemistry, Magnetic Resonance Spectroscopy Methods, Polyubiquitin Chemistry, Solutions Chemistry,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini-CNR, V.le A. Doria 6, 95125 Catania, Italy.
Dipartimento Farmaco-Chimico, University of Bari, Via E. Orabona 4, 70125 Bari, Italy
Dipartimento di Scienze Chimiche, University of Catania, V.le A. Doria 6, 95125 Catania, Italy
References: Not available.
Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding