Ubiquitin Recognition by the Ubiquitin-associated Domain of p62 Involves a Novel Conformational Switch
Open Access
- 1 February 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (9) , 5427-5440
- https://doi.org/10.1074/jbc.m704973200
Abstract
No abstract availableKeywords
This publication has 64 references indexed in Scilit:
- Conformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domainProceedings of the National Academy of Sciences, 2007
- Retinol Modulates Site-Specific Mobility of Apo-Cellular Retinol-Binding Protein to Promote Ligand BindingJournal of the American Chemical Society, 2006
- Loss of Ubiquitin-Binding Associated With Paget's Disease of Bone p62 (SQSTM1) MutationsJournal of Bone and Mineral Research, 2005
- Two Novel Mutations at Exon 8 of the Sequestosome 1 (SQSTM1) Gene in an Italian Series of Patients Affected by Paget's Disease of Bone (PDB)Journal of Bone and Mineral Research, 2004
- Three Novel Mutations in SQSTM1 Identified in Familial Paget's Disease of BoneJournal of Bone and Mineral Research, 2003
- Polyglutamine protein aggregates are dynamicNature Cell Biology, 2002
- Solution Structures of UBA Domains Reveal a Conserved Hydrophobic Surface for Protein–Protein InteractionsJournal of Molecular Biology, 2002
- Distinct Functional Surface Regions on UbiquitinJournal of Biological Chemistry, 2001
- Measurement ofJand Dipolar Couplings from Simplified Two-Dimensional NMR SpectraJournal of Magnetic Resonance, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995