Education

Ph.D. in Chemistry, University of Utah Salt Lake City, UT, 2003

Current position

Research and Development Engineer, Stanford University, Stanford, USA (11/2010-present)

Publications

1. O'Gorman, W. E., Huang, H., Wei, Y. L., Davis, K. L., Leipold, M. D., Bendall, S. C., Kidd, B. A., Dekker, C. L., Maecker, H. T., Chien, Y. H. and Davis, M. M. (2014). The Split Virus Influenza Vaccine rapidly activates immune cells through Fcgamma receptors. Vaccine 32(45): 5989-5997.
   
2. Horowitz, A., Strauss-Albee, D. M., Leipold, M., Kubo, J., Nemat-Gorgani, N., Dogan, O. C., Dekker, C. L., Mackey, S., Maecker, H. and Swan, G. E. (2013). Genetic and environmental determinants of human NK cell diversity revealed by mass cytometry. Sci Transl Med 5(208): 208ra145-208ra145.
   
3. Leipold, M. D. and Maecker, H. T. (2012). Mass cytometry: protocol for daily tuning and running cell samples on a CyTOF mass cytometer. J Vis Exp(69): e4398.
   
4. Leipold, M. D., Ornatsky, O., Baranov, V., Whitfield, C. and Nitz, M. (2011). Development of mass cytometry methods for bacterial discrimination. Anal Biochem 419(1): 1-8.
   
5. Leipold, M. D., Herrera, I., Ornatsky, O., Baranov, V. and Nitz, M. (2009). ICP-MS-based multiplex profiling of glycoproteins using lectins conjugated to lanthanide-chelating polymers. J Proteome Res 8(2): 443-449.
   
6. Leipold, M. D., Vinogradov, E. and Whitfield, C. (2007). Glycosyltransferases involved in biosynthesis of the outer core region of Escherichia coli lipopolysaccharides exhibit broader substrate specificities than is predicted from lipopolysaccharide structures. J Biol Chem 282(37): 26786-26792.
   
7. Leipold, M. D., Kaniuk, N. A. and Whitfield, C. (2007). The C-terminal Domain of the Escherichia coli WaaJ glycosyltransferase is important for catalytic activity and membrane association. J Biol Chem 282(2): 1257-1264.
   
8. Leipold, M. D., Workman, H., Muller, J. G., Burrows, C. J. and David, S. S. (2003). Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2. Biochemistry 42(38): 11373-11381.
   
9. Burrows, C. J., Muller, J. G., Kornyushyna, O., Luo, W., Duarte, V., Leipold, M. D. and David, S. S. (2002). Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals. Environ Health Perspect 110 Suppl 5: 713-717.
   
10. Leipold, M. D., Muller, J. G., Burrows, C. J. and David, S. S. (2000). Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG. Biochemistry 39(48): 14984-14992.