Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Drug Discovery,Biochemistry,Biotechnology
Link
http://link.springer.com/content/pdf/10.1007/s13238-010-0011-4.pdf
Reference42 articles.
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2. Anand, K., Ziebuhr, J., Wadhwani, P., Mesters, J.R., and Hilgenfeld, R. (2003). Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs. Science 300, 1763–1767.
3. Barrila, J., Bacha, U., and Freire, E. (2006). Long-range cooperative interactions modulate dimerization in SARS 3CLpro. Biochemistry 45, 14908–14916.
4. Chen, S., Chen, L., Tan, J., Chen, J., Du, L., Sun, T., Shen, J., Chen, K., Jiang, H., and Shen, X. (2005). Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations. J Biol Chem 280, 164–173.
5. Chen, S., Hu, T., Zhang, J., Chen, J., Chen, K., Ding, J., Jiang, H., and Shen, X. (2008a). Mutation of Gly-11 on the dimer interface results in the complete crystallographic dimer dissociation of severe acute respiratory syndrome coronavirus 3C-like protease: crystal structure with molecular dynamics simulations. J Biol Chem 283, 554–564.
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