Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT Domain E3 Ligase
Open Access
- 1 January 2003
- journal article
- Published by Elsevier
- Vol. 11 (1) , 249-259
- https://doi.org/10.1016/s1097-2765(02)00774-8
Abstract
No abstract availableKeywords
This publication has 49 references indexed in Scilit:
- Alternative Splicing Determines the Domain Structure of WWP1, a Nedd4 Family ProteinBiochemical and Biophysical Research Communications, 2002
- Molecular Insights into Polyubiquitin Chain AssemblyCell, 2001
- A HECT Domain E3 Enzyme Assembles Novel Polyubiquitin ChainsJournal of Biological Chemistry, 2001
- Structure of an E6AP-UbcH7 Complex: Insights into Ubiquitination by the E2-E3 Enzyme CascadeScience, 1999
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Methods used in the structure determination of bovine mitochondrial F1 ATPaseActa Crystallographica Section D-Biological Crystallography, 1996
- A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase.Proceedings of the National Academy of Sciences, 1995
- A visual protein crystallographic software system for X11/XviewJournal of Molecular Graphics, 1992
- Determination of Macromolecular Structures from Anomalous Diffraction of Synchrotron RadiationScience, 1991
- The MIDAS display systemJournal of Molecular Graphics, 1988