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Keywords
- Severe Acute Respiratory Syndrome
- Active Conformation
- Severe Acute Respiratory Syndrome
- Conformational Rearrangement
- Inactive Conformation
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
References
D. A. Groneberg, R. Hilgenfeld, and P. Zabel, Molecular mechanisms of severe acute respiratory syndrome (SARS), Respir. Res. 6, 8-23 (2005).
V. Thiel, K. A. Ivanov, A. Putics, et al. , Mechanisms and enzymes involved in SARS coronavirus genome expression, J. Gen. Virol. 84, 2305-2315 (2003).
A. E. Gorbalenya, E. V. Koonin, A. P. Donchenko, and V. M. Blinov, Coronavirus genome: prediction of putative functional domains in the non-structural polyprotein by comparative amino acid analysis, Nucl. Acids Res. 17, 4847-4861 (1989).
K. Anand, J. Ziebuhr, P. Wadhwani, J. R. Mesters, and R. Hilgenfeld, Coronavirus main proteinase (3CLpro) structure: basis for design of anti-SARS drugs, Science 300, 1763-1767 (2003).
B. Xiong, C. S. Gui, X. Y. Xu, et al. , A 3D model of SARS-CoV 3CL proteinase and its inhibitors design by virtual screening, Acta Pharmacol. Sin. 24, 497-504 (2003).
K. Anand, H. Yang, M. Bartlam, Z. Rao, and R. Hilgenfeld, in: Coronaviruses with Special Emphasis on First Insights Concerning SARS, edited by A. Schmidt, M. H. Wolff, and O. Weber (Birkhäuser, Basel, 2005), pp. 173-199.
H. Yang, W. Xie, X. Xue, et al. , Design of wide-spectrum inhibitors targeting coronavirus main proteinases, PLoS Biology 3, e324 (2005).
K. Anand, G. J. Palm, J. R. Mesters, et al. , Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra α-helical domain, EMBO J. 21, 3213-3224 (2002).
H. Yang, M. Yang, Y. Ding, et al. , The crystal structures of severe acute respiratory syndrome virus main protease and its complex with an inhibitor, Proc. Natl. Acad. Sci. USA 100, 13190-13195 (2003).
J. Tan, K. H. G. Verschueren, K. Anand, et al. , pH-Dependent conformational flexibility of the SARS-CoV main proteinase (Mpro ) dimer: Molecular dynamics simulations and multiple X-ray structure analyses, J. Mol. Biol. 354, 25-40 (2005).
M. -F. Hsu, C. -J. Kuo, K. -T. Chang, et al. , Mechanism of the maturation process of SARS-CoV 3CL protease, J. Biol. Chem. 280, 31257-31266 (2005).
C. -Y. Chou, H. -C. Chang, W. -C. Hsu, et al. , Quarternary structure of the severe acute respiratory syndrome (SARS) coronavirus main protease, Biochemistry 43, 14958-14970 (2004).
J. Shi, Z. Wei, and J. Song, Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme: Defining the extra domain as a new target for design of highly specific protease inhibitors, J. Biol. Chem. 279, 24765-24773 (2004).
K. Fan, P. Wei, Q. Feng, et al. , Biosynthesis, purification, and substrate specificity of severe acute respiratory syndrome coronavirus 3C-like proteinase, J. Biol. Chem. 279, 1637-1642 (2004).
A. Hegyi, A. Friebe, A. E. Gorbalenya, and J. Ziebuhr, Mutational analysis of the active centre of coronavirus 3C-like proteases, J. Gen. Virol. 83, 581-593 (2002).
J. Ziebuhr, E. J. Snijder, and A. E. Gorbalenya, Virus-encoded proteinases and proteolytic processing in the Nidovirales. J. Gen. Virol. 81, 853-879 (2000).
J. Yang, M. Yu, Y. N. Jan, and L. Y. Jan, Stabilization of ion selectivity filter by pore loop ion pairs in an inwardly rectifying potassium channel, Proc. Natl. Acad. Sci. USA 94, 1568-1572 (1997).
S. Chen, L. Chen, J. Tan, et al. , 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 (2005).
W. -C. Hsu, H. -C. Chang, C. -Y. Chou, P. -J. Tsai, P. -I. Lin, and G. -G. Chang, Critical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease, J. Biol. Chem. 280, 22741-22748 (2005).
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Hilgenfeld, R. et al. (2006). Structure and Dynamics of Sars Coronavirus Main Proteinase (MPRO). In: Perlman, S., Holmes, K.V. (eds) The Nidoviruses. Advances in Experimental Medicine and Biology, vol 581. Springer, Boston, MA. https://doi.org/10.1007/978-0-387-33012-9_106
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