Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure
- 5 June 2009
- journal article
- Published by Elsevier BV in Virology
- Vol. 388 (2), 324-334
- https://doi.org/10.1016/j.virol.2009.03.034
Abstract
No abstract availableKeywords
This publication has 51 references indexed in Scilit:
- Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like ProteaseJournal of Virology, 2008
- Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal DomainJournal of Virology, 2008
- Regulation of IRF-3-dependent Innate Immunity by the Papain-like Protease Domain of the Severe Acute Respiratory Syndrome CoronavirusOnline Journal of Public Health Informatics, 2007
- Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium ChlorideBiophysical Journal, 2007
- Long-Range Cooperative Interactions Modulate Dimerization in SARS 3CLproBiochemistry, 2006
- SARS: Systematic Review of Treatment EffectsPLoS Medicine, 2006
- Severe acute respiratory syndrome coronavirus papain-like protease: Structure of a viral deubiquitinating enzymeProceedings of the National Academy of Sciences of the United States of America, 2006
- Coot: model-building tools for molecular graphicsActa crystallographica. Section D, Structural biology, 2004
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa crystallographica. Section D, Structural biology, 1997
- The CCP4 suite: programs for protein crystallographyActa crystallographica. Section D, Structural biology, 1994