See our full publication list Publications

  1. Bernatchez, J. A.; Coste, M.; Beck, S.; Wells, G. S.; Luna, L. A.; Clark, A. E.; Zhu, Z.; Sohl, C. D.*; Purse, B. W.*; Siqueira-Neto, J. L.* (2019) Viruses, in press. “Activity of selected nucleoside analogue ProTides against Zika virus in human neural stem cells.” (*co-corresponding authors).
  2. Kennedy, M. A.; Xu, Z.; Wu, Y.; and Sohl, C. D. (2019) Biochem Biophys Res Commun 509, 898-902. A Tie2 kinase mutation causing venous malformations increases phosphorylation rates and enhances cooperativity. PMID:30638931
  3. Ryan, M. R.; Sohl, C. D.; Luo, B.; and Anderson, K. A. (2019) Mol Cancer Res 17, 532-543. The FGFR1 V561M gatekeeper mutation drives AZD4547 resistance through STAT3 activation and EMT. PMID30257990.
  4. Matteo, D. A.; Wells, G. A.; Luna, L. A.; Grunseth, A. J.; Zagnitko, O.; Scott, D. A.; Hoang, A.; Luthra, A.; Swairjo, M. A.; Schiffer, J. A.; and Sohl, C. D. (2018) Biochem J 475, 3221-3238. Inhibitor potency varies widely among tumor relevant human isocitrate dehydrogenase 1 mutants. PMID30257990
  5. Bernatchez, J. A., Coste, Yang, Z., Coste, M., Li, J., Beck, S., Liu, Y., Clark, A. E., Zhu, Z., Luna, L. A., Sohl, C. D., Purse, B. W., Li, R., and Siqueira-Neto, J. L. (2018) Antimicrob Agents Chemother 62, e00725-18. “Development of a phenotypic high-content imaging assay for assessing the antiviral activity of small-molecule inhibitors targeting the Zika virus.” PMID30257990.
  6. Matteo, D. M.*, Grunseth, A. J.*, Gonzalez, E. R., Anselmo, S. L., Kennedy, M. A., Moman, P., Scott, D. A., Hoang, A., and Sohl, C. D. (2017) J Biol Chem 292, 7971-83. “Molecular mechanisms of isocitrate dehydrogenase 1 (IDH1) mutations identified in tumors: the role of size and hydrophobicity at residue 132 on catalytic efficiency.” (*co-first author). PMID:28330869
  7. Sohl, C. D., Ryan, M. R., Luo, B., Frey, K. M., and Anderson, K. S. (2015) ACS Chem Biol 10, 1319-29. “Illuminating the molecular mechanism of tyrosine kinase inhibitor resistance for the FGFR1 gatekeeper mutation: the Achilles’ heel of targeted therapy.”
  8. Sohl, C. D.*, Szymanski, M. R.*, Mislak, A. C., Shumate, C. K., Amiralaei, S., Schinazi, R. F., Anderson, K. S., and Yin, Y. W. (2015) Proc Natl Acad Sci USA 112, 8596-601. “Probing the structural and molecular basis of nucleotide selectivity by human mitochondrial DNA polymerase g.” (*co-first author).
  9. Sohl, C. D.*, Ray, S., and Sweasy, J. B. (2015) Proc Natl Acad Sci USA 112, 5864-5. “Pools and pols: mechanism of a mutator phenotype. (*co-first author)
  10. Towle-Weicksel, J. B., Dalal, S., Sohl, C. D., Doublie, S., Anderson, K. S., Sweasy, J. B. (2014) J Biol Chem 289, 16541-50. “Fluorescence resonance energy transfer studies of DNA polymerase ß: the critical role of fingers domain movements and a novel non-covalent step during nucleotide selection.”
  11. Muftuoglu, Y.*, Sohl, C. D.*, Mislak, A. C., Mitsuya, H., Sarafianos, S. G., and Anderson, K. S. (2014) Antiviral Res 106, 1-4. “Probing the molecular mechanism of action of the HIV-1 reverse transcriptase inhibitor 4’-ethynyl-2-fluoro-2’-deoxyadenosine (EFdA) using pre-steady-state kinetics.” (*co-first author)
  12. Sohl, C. D., Kasiviswanathan, R., Copeland, W. C., and Anderson, K. S. (2013) Hum Mol Genet 22, 1074-85. “Mutations in human DNA polymerase g confer unique mechanisms of catalytic deficiency that mirror the disease severity in mitochondrial disorder patients.”
  13. Cheng, Q., Sohl, C. D., Yoshimoto, F. K., and Guengerich, F. P. (2012) J Biol Chem 287, 59554-67. “Oxidation of dihydrotestosterone by human cytochromes P450s 19A1 and 3A4.”
  14. Sohl, C. D., Kasiviswanathan, R., Kim, J., Pradere, U., Schinazi, R. F., Copeland, W. C., Mitsuya, H., Baba, M., and Anderson, K. (2012) Mol Pharmacol 82, 125-33. “Balancing antiviral potency and host toxicity: identifying a nucleotide inhibitor with an optimal kinetic phenotype for HIV-1 reverse transcriptase.”
  15. Sohl, C. D., Singh, K., Kasiviswanathan, R., Copeland, W. C., Mitsuya, H., Sarafianos, S., and Anderson, K. (2012) Antimicrob Agents Chemother 56, 1630-4. “Mechanism of interaction of human mitochondrial DNA polymerase γ with the novel nucleoside reverse transcriptase inhibitor 4’-ethynyl-2-fluoro-2’-deoxyadenosine indicates a low potential for host toxicity.”
  16. Guengerich, F. P., Sohl, C. D., and Chowdhury, G. (2011) Arch Biochem Biophys 507, 126-34. “Multi-step oxidations catalyzed by cytochrome P450 enzymes: processive distributive kinetics and the issue of carbonyl oxidation in chemical mechanisms.”
  17. Sohl, C. D., and Guengerich, F. P. (2010) J Biol Chem 285, 17734-17743. “Kinetic analysis of the three-step steroid aromatase reaction of human cytochrome P450 19A1.”
  18. Cheng, Q., Sohl, C. D., and Guengerich, F. P., (2009) Nat Protoc 4, 1258-61. “High-throughput fluorescence assay of cytochrome P450 3A4.”
  19. Sohl, C. D., Cheng, Q., and Guengerich, F. P. (2009) Nat Protoc 4, 1252-7. “Chromatographic assays of drug oxidation by human cytochrome P450 3A4.”
  20. Guengerich, F. P., Martin, M. V., Sohl, C. D., and Cheng, Q. (2009) Nat Protoc 4, 1245-51. “Measurement of cytochrome P450 and NADPH-cytochrome P450 reductase.”
  21. Sohl, C. D., Isin, E. M., Eoff, R. L., Marsch, G. A., Stec, D. F., and Guengerich, F. P. (2008) J Biol Chem 283, 7293-7308. “Cooperativity in oxidation reactions catalyzed by cytochrome P450 1A2. Highly cooperative pyrene hydroxylation and multiphasic kinetics of ligand binding.”
  22. Isin, E. M.*, Sohl, C. D.*, Eoff, R. L., and Guengerich, F. P. (2008) Arch Biochem Biophys 473, 69-75. “Cooperativity of cytochrome P450 1A2: interaction of 1,4-phenylene diisocyanide and 1-alkoxy-4-nitrobenzenes.”  (*co-first author)
  23. Wu, Z-L., Sohl, C. D., Shimada, T., and Guengerich, F. P. (2006) Mol Pharmacol 69, 2007-2014. “Recombinant enzymes over-expressed in bacteria show broad catalytic specificity of human cytochrome P450 2W1 and limited activity of human cytochrome P450 2S1.”
  24. Sohl, C. D., Lee, J., Alguindigue, S. S., Khan, M. A., and Richter-Addo, G. B. (2004) J Inorg Biochem 98, 1238-46. “Synthesis and solid-state molecular structures of nitrosoalkane complexes of iron porphyrins containing methanol, pyridine, and 1-methylimidazole ligands.”