Skip to content

References


References

  1. Malekshah, O. M., Chen, X., Nomani, A., Sarkar, S. & Hatefi, A. Enzyme/Prodrug Systems for Cancer Gene Therapy. en. Current Pharmacology Reports 2, 299–308. ISSN: 2198-641X. http://dx.doi.org/10.1007/ s40495-016-0073-y (Oct. 19, 2016).
  2. Stolworthy, T. S. et al. Yeast Cytosine Deaminase Mutants with Increased Thermostability Impart Sensitivity to 5-Fluorocytosine. en. Journal of Molecular Biology 377, 854–869. ISSN: 0022-2836. http://dx.doi. org/10.1016/j.jmb.2008.01.002 (Mar. 2008).
  3. Rooseboom, M., Commandeur, J. N. & Vermeulen, N. P. Enzyme-catalyzed activation of anticancer prodrugs. Pharmacological reviews 56, 53–102 (2004).
  4. Holldorf, A. W. in Methods of Enzymatic Analysis 1916– 1918 (Elsevier, 1974). http://dx.doi.org/10.1016/B978-0- 12-091304-6.50049-5.
  5. Swietach, P., Vaughan-Jones, R. D., Harris, A. L. & Hulikova, A. The chemistry, physiology and pathology of pH in cancer. en. Philosophical Transactions of the Royal Society B: Biological Sciences 369, 20130099. ISSN: 0962-8436. http://dx.doi.org/10.1098/rstb.2013. 0099 (Mar. 19, 2014).
  6. Fuchita, M. et al. Bacterial Cytosine Deaminase Mutants Created by Molecular Engineering Show Improved 5-Fluorocytosine–Mediated Cell Killing In vitro and In vivo. en. Cancer Research 69, 4791–4799. ISSN: 0008-5472. http://dx.doi.org/10.1158/0008- 5472.CAN-09-0615 (June 1, 2009).
  7. Kievit, E. et al. Superiority of yeast over bacterial cytosine deaminase for enzyme/prodrug gene therapy in colon cancer xenografts. Cancer research 59, 1417– 1421 (1999).
  8. Rostkowski, M., Olsson, M. H., Søndergaard, C. R. & Jensen, J. H. Graphical analysis of pH-dependent properties of proteins predicted using PROPKA. BMC Structural Biology 11. https://doi.org/10.1186/ 1472-6807-11-6 (Jan. 2011).
  9. Gopi, S., Devanshu, D., Krishna, P. & Naganathan, A. N. pStab: prediction of stable mutants, unfolding curves, stability maps and protein electrostatic frustration. en. Bioinformatics 34 (ed Valencia, A.) 875–
  10. ISSN: 1367-4803. http : / / dx . doi . org / 10 . 1093 / bioinformatics/btx697 (Oct. 28, 2017).
  11. Naganathan, A. N. A Rapid, Ensemble and Free Energy Based Method for Engineering Protein Stabilities. The Journal of Physical Chemistry B 117, 4956–4964. https://doi.org/10.1021/jp401588x (Apr. 2013).
  12. Strickler, S. S. et al. Protein Stability and Surface Electrostatics: A Charged Relationship. Biochemistry 45, 2761–2766. https://doi.org/10.1021/bi0600143 (Feb. 2006).
  13. Blacklock, K. M., Yachnin, B. J., Woolley, G. A. & Khare, S. D. Computational Design of a Photocontrolled Cytosine Deaminase. Journal of the American Chemical Society 140, 14–17. https://doi.org/10.1021/ jacs.7b08709 (Dec. 2017).
  14. Wilson, D. S. & Keefe, A. D. Random mutagenesis by PCR. Current protocols in molecular biology 51, 8–3 (2000).
  15. Hefti, M. H., der Toorn, C. J. V. V.-V., Dixon, R. & Vervoort, J. A Novel Purification Method for HistidineTagged Proteins Containing a Thrombin Cleavage Site. Analytical Biochemistry 295, 180–185. https://doi. org/10.1006/abio.2001.5214 (Aug. 2001).
  16. Ko, T.-P. et al. Crystal Structure of Yeast Cytosine Deaminase. Journal of Biological Chemistry 278, 19111–
  17. https://doi.org/10.1074/jbc.m300874200 (May 2003).
  18. Gerlt, J. A., Kreevoy, M. M., Cleland, W. & Frey, P. A. Understanding enzymic catalysis: the importance of short, strong hydrogen bonds. Chemistry &amp Biology 4, 259–267. https://doi.org/10.1016/s1074- 5521(97)90069-7 (Apr. 1997).
  19. Goh, K. M., Hong, G. P., Ng, N. H. C. P., Piaw, C. K. & Rahman, R. N. Z. R. A. Trends and Tips in Protein Engineering, A Review. Jurnal Teknologi 59. https : //doi.org/10.11113/jt.v59.1574 (Sept. 2012)

Supplementary

Supplementary 1: PyMol PDB Files
Supplementary 2: Electrostatic data from pStab