Dr. Michael W. Thompson is an instructor of zoology and biology at Laramie County Community College.
He earned a B.S. in chemistry and zoology from the University of Louisville in Louisville, Kentucky, in 1993, a Ph.D. in biochemistry from the University of Kentucky in Lexington, Kentucky, in 2000, and completed a postdoctoral fellowship at Vanderbilt University in the Department of Pathology in Nashville, Tennessee.
His research interests include the molecular mechanisms of tissue remodeling during inflammation through studies of the activation of matrix metalloproteinase-2 (MMP-2) and lactoferrin, and the molecular mechanisms of the bifunctional enzyme leukotriene A4 hydrolase.
Michael has many scientific publications and has contributed to several freshman-level general biology textbooks.
In his spare time, Michael is an avid outdoor recreation enthusiast who enjoys cycling, running, triathlon, hiking, photography and creative writing.
1. Seipelt, R.L., Bailey, F.C., Schaible, A., and Thompson, M.W. (2010). Asn362 is essential for zinc binding and catalysis in the peptidase reaction of Saccharomyces cerevisiae leukotriene A4 hydrolase. Biochimica et Biophysica Acta Proteins and Proteomics 1804, 2070-2076.
2. Thompson, M.W., Beasley, K.A., Schmidt, M.D., and Seipelt, R.L. (2009). Arginyl aminopeptidase-like 1 (RNPEPL1) is an alternatively processed aminopeptidase with specificity for methionine, glutamine, and citrulline residues. Protein and Peptide Letters 16, 1256-1266.
3. Tharp, A.C., Laha, M., Panizzi, P., Thompson, M.W., Fuentes-Prior, P., and Bock, P.E. (2009) Plasminogen substrate recognition by the streptokinase-plasminogen catalytic complex is facilitated by Arg253, Lys256, and Lys257 in the streptokinase -domain and kringle 5 of the substrate. Journal of Biological Chemistry 284, 19511-19521.
4. Newsome, A.L., Johnson, J.P., Seipelt, R.L., and Thompson, M.W. (2007). Apolactoferrin inhibits the catalytic domain of matrix metalloproteinase-2 by zinc chelation. Biochemistry and Cell Biology 85, 563-572.
5. Thompson, M.W., Archer, E.D., Romer, C.E., and Seipelt, R.L. (2006). A conserved tyrosine residue is essential for transition state stabilization in Saccharomyces cerevisiae leukotriene A4 hydrolase. Peptides 27, 1701-1709.
6. Thompson, M.W. and Hersh, L.B. (2004). The puromycin-sensitive aminopeptidase: its role in neurological, reproductive, immunological, and proliferative disorders. In N.M. Hooper and U. Lendeckel (Eds.), Aminopeptidases in Biology and Disease (1-15). New York: Kluwer.
7. Thompson, M.W., Govindaswami, M., and Hersh, L.B. (2003). Mutation of active site residues of the puromycin-sensitive aminopeptidase: conversion of the enzyme into a catalytically inactive binding protein. Archives of Biochemistry and Biophysics 413, 236-242.
8. Thompson, M.W. and Hersh, L.B. (2003). Analysis of conserved residues of the human puromycin-sensitive aminopeptidase. Peptides 24, 1359-1365.
9. Ma, Z., Daquin, A., Yao, J., Rodgers, D., Thompson, M.W. and Hersh, L.B. (2003). Proteolytic cleavage of the puromycin sensitive aminopeptidase generates a substrate binding domain. Archives of Biochemistry and Biophysics 415, 80-86.
10. Stoltze, L., Schirle, M., Schwarz, G., Schroter, C., Thompson, M. W., Hersh, L. B., Kalbacher, H., Stevanovic, S., Rammensee, H. G., and Schild, H. (2000). Two new proteases in the MHC class I processing pathway. Nature Immunology 1, 413-418.
11. Thompson, M.W., Tobler, A.R., Fontana, A., and Hersh, L.B. (1999). Cloning and analysis of the gene for the human puromycin-sensitive aminopeptidase. Biochemistry and Biophysical Research Communications 258, 234-240.
12. Csuhai, E., Safavi, A., Thompson, M.W., and Hersh, L.B. (1998). Proteolytic inactivation of secreted neuropeptides. In V. Y. H. Hook (Ed.), Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing (173-189). Austin, TX: Landes.