Thompson Lab Publications
1. Travis, S., Green, K.D., Thamban Chandrika, N., Pang, A.H., Frantom, P.A., Tsodikov, O.V., Garneau-Tsodikova, S., and Thompson, M.K. "Identification and analysis of small molecule inhibitors of FosB from Staphylococcus aureus." RSC Med Chem. 2023.
2. Travis, S., Green, K.D., Gilbert, N.C., Tsodikov, O.V., Garneau-Tsodikova, S., and Thompson, M.K. "Inhibition of Fosfomycin Resistance Protein FosB from Gram-Positive Pathogens by Phosphonoformate." Biochemistry. 2023.
3. Wiltsie, V.; Travis, S.; Shay, M. R.; Simmons, Z.; Frantom, P.; Thompson, M. K. "Structural and functional characterization of fosfomycin resistance conferred by FosB from Enterococcus faecium." Protein Science. 2022.
4. Travis, S.; Shay, M.R.; Manabe, S.; Gilbert, N.C.; Frantom, P.A.; Thompson, M.K. "Characterization of the Genomically Encoded Fosfomycin Resistance Enzyme From Mycobacterium abscessus." MedChemComm. 2019.
5. Johnson, C.N.; Potet, F.; Thompson, M.K.; Kroncke, B.M.; Glazer, A.M.; Voehler, M.W.; Knollmann, B.C.; George, A.L; Chazin, W.J. “A Novel Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.” Cell Structure. 2018.
6. Droege, K.D.; Keithly, M.E.; Sanders, C.R.; Armstrong, R.N.; Thompson, M.K. “Structural Dynamics of 15-Lipoxygenase-2 via Hydrogen-Deuterium Exchange.” Biochem. 2017. 56(38), 5065–5074.
- Recommended by F1000
7. O’Brien, E.; Holt, M.E.; Thompson, M.K.; Salay, L.E.; Ehlinger, A.C.; Chazin, W.J.; Barton, J.K. Response to comments on “The [4Fe4S] Cluster Functions as a Redox Switch in Human DNA Primase Using DNA Charge Transport.” Science. 2017. 357, eaan2762.
8. Thompson, M.K.; Ehlinger, A.C.; Chazin, W.J. “Analysis of Functional Dynamics of Modular Multi-Domain Proteins by SAXS and NMR.” Invited for Methods in Enzymology. 2017. 529, 49-76.
9. O’Brien, E.; Holt, M.E.; Thompson, M.K.; Salay, L.E.; Ehlinger, A.C.; Chazin, W.J.; Barton, J.K. “The [4Fe4S] Cluster Functions as a Redox Switch in Human DNA Primase Using DNA Charge Transport.” Science. 2017. 355, 318.
- Featured in American Chemical Society’s Chemical and Engineering news
- Featured in the Royal Society of Chemistry’s Chemistry World
10. Thompson, M.K.; Keithly, M.E.; Sulikowski, G.A.; Armstrong, R.N. “Diversity in the Fosfomycin Resistance Proteins.” Persp. in Sci. 2015. 4, 17-23.
11. Thompson, M.K.; Keithly, M.E.; Goodman, M.C.; Hammer, N.D.; Cook, P.D.; Jagessar, K.L.; Harp, J.; Skaar, E.P.; Armstrong, R.N. “Structure and function of the genomically-encoded fosfomycin resistance enzyme, FosB, from Staphylococcus aureus.” Biochem. 2014. 53(4), 755–765.
- Highlighted at the 58th Biophysical Society annual meeting
- Featured on American Association for the Advancement of Science (AAAS) breaking news
- Featured in the Vanderbilt University Medical Center newspaper, the VUMC Reporter
12. Thompson, M.K.; Keithly, M.E.; Harp, J.; Cook, P.D.; Jagessar, K.L.; Sulikowski, G.A.; Armstrong, R.N. “Structural and chemical aspects of resistance to the antibiotic, fosfomycin, conferred by FosB from Bacillus cereus.” Biochem. 2013. 52(41), 7350–7362.
13. Plummer, A.; Thompson, M.K.; Franzen, S. “Role of polarity of the distal pocket in the control of inhibitor binding in dehaloperoxidase-hemoglobin.” Biochem. 2013. 52(13), 2218-2227.
14. Schkolnik G., Utesch T., Zhao J., Jiang S., Thompson M.K., Mroginski M.A., Hildebrandt P., Franzen S. “Catalytic efficiency of
dehaloperoxidase A is controlled by electrostatics–application of the vibrational Stark effect to understand enzyme kinetics.”
Biochem. Biophys. Res. Commun. 2013. 430(3), 1011-1015.
- Recommended by F1000.
15. Zhao, J.; de Serrano, V.; Dumarieh, R.; Thompson, M.K.; Ghiladi, R.A.; Franzen, S. “The role of the distal histidine in H2O2 activation and heme protection in both peroxidase and globin functions.” J. Phys. Chem. B. 2012. 116, 12065-12077.
16. Franzen, S.; Thompson, M.K.; Ghiladi, R.A. “The Dehaloperoxidase Paradox.” Biochem. Biophys. Acta. 2012. 1824, 578-588.
17. D’Antonio, E.L.; D’Antonio, J.; de Serrano, V.; Gracz, H.; Thompson, M.K.; Ghiladi, R.A.; Franzen, S.; Bowden, E.F.; “Mutation of methionine-86 in dehaloperoxidase: Effects of the Asp-His-Fe triad in a 3/3 globin.” Biochem. 2011. 50(44), 9664-9680.
18. Thompson, M.K.; Franzen, S.; Davis, M.F.; Oliver, R.C.; Krueger, J.K. “Dehaloperoxidase-hemoglobin from Amphitrite ornata is primarily a monomer in solution.” J. Phys. Chem. B. 2011, 115(14), 4266-4272.
19. Nicoletti, F.P.; Thompson, M.K.; Franzen, S.; Smulevich, G. “Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.” J. Biol. Inorg. Chem. 2011, 16(4), 611-619.
20. Szatkowski, L.; Thompson, M.K.; Kiminski, R.; Franzen, S.; Dybala-Defratyka, A. “Oxidative dechlorination of halogenated phenols catalyzed by two distinct enzymes: Horseradish peroxidase and dehaloperoxidase.” Arch. Biochem. Biophys. 2011, 505, 22-32.
21. Thompson, M.K.; Franzen, S.; Ghiladi, R.A.; Reeder, B.J.; Svistunenko, D.A. “Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine.” J. Am. Chem. Soc. 2010, 132(49) 17501-17510.
22. Ma, H.; Thompson, M.K.; Gaff, J.; Franzen, F. “Kinetic analysis of a naturally occurring bioremediation enzyme: Dehaloperoxidase-hemoglobin from Amphitrite ornata.” J. Phys. Chem. B. 2010, 114(43), 13823-13829.
23. Thompson M.K.; Davis, M.F.; de Serrano, V.; Nicoletti, F.P.; Howes, B.D.; Smulevich, G.; Franzen, S. “Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.” Biophys. J. 2010, 99(5), 1586-1595.
24. D’Antonio, J.; D’Antonio, E.L.; Thompson, M.K.; Bowden, E.F.; Franzen, S.; Smirnova, T.; Ghiladi, R.A. “Spectroscopic and mechanistic investigations of dehaloperoxidase B from Amphitrite ornata.” Biochem. 2010, 49, 6600-6616.
25. Nicoletti, F.P.; Thompson, M.K.; Howes, B.D.; Franzen, S.; Smulevich, G. “New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata. Biochem. 2010, 49, 1903-1912.
2. Travis, S., Green, K.D., Gilbert, N.C., Tsodikov, O.V., Garneau-Tsodikova, S., and Thompson, M.K. "Inhibition of Fosfomycin Resistance Protein FosB from Gram-Positive Pathogens by Phosphonoformate." Biochemistry. 2023.
3. Wiltsie, V.; Travis, S.; Shay, M. R.; Simmons, Z.; Frantom, P.; Thompson, M. K. "Structural and functional characterization of fosfomycin resistance conferred by FosB from Enterococcus faecium." Protein Science. 2022.
4. Travis, S.; Shay, M.R.; Manabe, S.; Gilbert, N.C.; Frantom, P.A.; Thompson, M.K. "Characterization of the Genomically Encoded Fosfomycin Resistance Enzyme From Mycobacterium abscessus." MedChemComm. 2019.
5. Johnson, C.N.; Potet, F.; Thompson, M.K.; Kroncke, B.M.; Glazer, A.M.; Voehler, M.W.; Knollmann, B.C.; George, A.L; Chazin, W.J. “A Novel Mechanism of Calmodulin Modulation of the Human Cardiac Sodium Channel.” Cell Structure. 2018.
6. Droege, K.D.; Keithly, M.E.; Sanders, C.R.; Armstrong, R.N.; Thompson, M.K. “Structural Dynamics of 15-Lipoxygenase-2 via Hydrogen-Deuterium Exchange.” Biochem. 2017. 56(38), 5065–5074.
- Recommended by F1000
7. O’Brien, E.; Holt, M.E.; Thompson, M.K.; Salay, L.E.; Ehlinger, A.C.; Chazin, W.J.; Barton, J.K. Response to comments on “The [4Fe4S] Cluster Functions as a Redox Switch in Human DNA Primase Using DNA Charge Transport.” Science. 2017. 357, eaan2762.
8. Thompson, M.K.; Ehlinger, A.C.; Chazin, W.J. “Analysis of Functional Dynamics of Modular Multi-Domain Proteins by SAXS and NMR.” Invited for Methods in Enzymology. 2017. 529, 49-76.
9. O’Brien, E.; Holt, M.E.; Thompson, M.K.; Salay, L.E.; Ehlinger, A.C.; Chazin, W.J.; Barton, J.K. “The [4Fe4S] Cluster Functions as a Redox Switch in Human DNA Primase Using DNA Charge Transport.” Science. 2017. 355, 318.
- Featured in American Chemical Society’s Chemical and Engineering news
- Featured in the Royal Society of Chemistry’s Chemistry World
10. Thompson, M.K.; Keithly, M.E.; Sulikowski, G.A.; Armstrong, R.N. “Diversity in the Fosfomycin Resistance Proteins.” Persp. in Sci. 2015. 4, 17-23.
11. Thompson, M.K.; Keithly, M.E.; Goodman, M.C.; Hammer, N.D.; Cook, P.D.; Jagessar, K.L.; Harp, J.; Skaar, E.P.; Armstrong, R.N. “Structure and function of the genomically-encoded fosfomycin resistance enzyme, FosB, from Staphylococcus aureus.” Biochem. 2014. 53(4), 755–765.
- Highlighted at the 58th Biophysical Society annual meeting
- Featured on American Association for the Advancement of Science (AAAS) breaking news
- Featured in the Vanderbilt University Medical Center newspaper, the VUMC Reporter
12. Thompson, M.K.; Keithly, M.E.; Harp, J.; Cook, P.D.; Jagessar, K.L.; Sulikowski, G.A.; Armstrong, R.N. “Structural and chemical aspects of resistance to the antibiotic, fosfomycin, conferred by FosB from Bacillus cereus.” Biochem. 2013. 52(41), 7350–7362.
13. Plummer, A.; Thompson, M.K.; Franzen, S. “Role of polarity of the distal pocket in the control of inhibitor binding in dehaloperoxidase-hemoglobin.” Biochem. 2013. 52(13), 2218-2227.
14. Schkolnik G., Utesch T., Zhao J., Jiang S., Thompson M.K., Mroginski M.A., Hildebrandt P., Franzen S. “Catalytic efficiency of
dehaloperoxidase A is controlled by electrostatics–application of the vibrational Stark effect to understand enzyme kinetics.”
Biochem. Biophys. Res. Commun. 2013. 430(3), 1011-1015.
- Recommended by F1000.
15. Zhao, J.; de Serrano, V.; Dumarieh, R.; Thompson, M.K.; Ghiladi, R.A.; Franzen, S. “The role of the distal histidine in H2O2 activation and heme protection in both peroxidase and globin functions.” J. Phys. Chem. B. 2012. 116, 12065-12077.
16. Franzen, S.; Thompson, M.K.; Ghiladi, R.A. “The Dehaloperoxidase Paradox.” Biochem. Biophys. Acta. 2012. 1824, 578-588.
17. D’Antonio, E.L.; D’Antonio, J.; de Serrano, V.; Gracz, H.; Thompson, M.K.; Ghiladi, R.A.; Franzen, S.; Bowden, E.F.; “Mutation of methionine-86 in dehaloperoxidase: Effects of the Asp-His-Fe triad in a 3/3 globin.” Biochem. 2011. 50(44), 9664-9680.
18. Thompson, M.K.; Franzen, S.; Davis, M.F.; Oliver, R.C.; Krueger, J.K. “Dehaloperoxidase-hemoglobin from Amphitrite ornata is primarily a monomer in solution.” J. Phys. Chem. B. 2011, 115(14), 4266-4272.
19. Nicoletti, F.P.; Thompson, M.K.; Franzen, S.; Smulevich, G. “Degradation of sulfide by dehaloperoxidase-hemoglobin from Amphitrite ornata.” J. Biol. Inorg. Chem. 2011, 16(4), 611-619.
20. Szatkowski, L.; Thompson, M.K.; Kiminski, R.; Franzen, S.; Dybala-Defratyka, A. “Oxidative dechlorination of halogenated phenols catalyzed by two distinct enzymes: Horseradish peroxidase and dehaloperoxidase.” Arch. Biochem. Biophys. 2011, 505, 22-32.
21. Thompson, M.K.; Franzen, S.; Ghiladi, R.A.; Reeder, B.J.; Svistunenko, D.A. “Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine.” J. Am. Chem. Soc. 2010, 132(49) 17501-17510.
22. Ma, H.; Thompson, M.K.; Gaff, J.; Franzen, F. “Kinetic analysis of a naturally occurring bioremediation enzyme: Dehaloperoxidase-hemoglobin from Amphitrite ornata.” J. Phys. Chem. B. 2010, 114(43), 13823-13829.
23. Thompson M.K.; Davis, M.F.; de Serrano, V.; Nicoletti, F.P.; Howes, B.D.; Smulevich, G.; Franzen, S. “Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.” Biophys. J. 2010, 99(5), 1586-1595.
24. D’Antonio, J.; D’Antonio, E.L.; Thompson, M.K.; Bowden, E.F.; Franzen, S.; Smirnova, T.; Ghiladi, R.A. “Spectroscopic and mechanistic investigations of dehaloperoxidase B from Amphitrite ornata.” Biochem. 2010, 49, 6600-6616.
25. Nicoletti, F.P.; Thompson, M.K.; Howes, B.D.; Franzen, S.; Smulevich, G. “New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata. Biochem. 2010, 49, 1903-1912.
