The Intrinsic Affinity between E2 and the Cys Domain of E1 in Ubiquitin-like Modifications
- 20 July 2007
- journal article
- Published by Elsevier BV in Molecular Cell
- Vol. 27 (2), 228-237
- https://doi.org/10.1016/j.molcel.2007.05.023
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (CA094595, GM074748)
This publication has 31 references indexed in Scilit:
- Basis for a ubiquitin-like protein thioester switch toggling E1–E2 affinityNature, 2007
- The Mechanisms of PML-Nuclear Body FormationMolecular Cell, 2006
- Insights into E3 ligase activity revealed by a SUMO–RanGAP1–Ubc9–Nup358 complexNature, 2005
- Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1The EMBO Journal, 2005
- Insights into the ubiquitin transfer cascade from the structure of the activating enzyme for NEDD8Nature, 2003
- HADDOCK: A Protein−Protein Docking Approach Based on Biochemical or Biophysical InformationJournal of the American Chemical Society, 2003
- Structural Basis for E2-Mediated SUMO Conjugation Revealed by a Complex between Ubiquitin-Conjugating Enzyme Ubc9 and RanGAP1Cell, 2002
- Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. distance restraints from paramagnetic relaxation and calculation of an ensemble of structuresJournal of Molecular Biology, 1997
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Comparative Protein Modelling by Satisfaction of Spatial RestraintsJournal of Molecular Biology, 1993