Picture of Dr. Stanley Moore

Dr. Stanley Moore BSc, PhD Faculty, Biochemistry

About Dr. Stanley Moore

Ph.D., University of Alberta, 1994, Structural Biology
B.Sc. Honours, Dalhousie University, 1986, Chemistry


Biography

Dr. Moore was born and raised in Halifax, Nova Scotia. He attended Queen Elizabeth High School and studied Chemistry at Dalhousie University, earning his BSc with Honors in 1986. From 1986 to 1987, he worked on the identification of marine natural products at the National Research Council's Atlantic Research Laboratory under the supervision of Dr. Jeffrey L. C. Wright. Dr Moore completed PhD studies in Biochemistry at the University of Alberta in 1994, where he studied protein crystallography under the supervision of Michael N. G. James. In 1994, Dr Moore took up a Post Doctoral Fellowship with Edward N. Baker at Massey University in New Zealand, where he worked on determining the structures of various proteins including lactoferrin, transferrin and aldehyde dehydrogenase. Dr Moore joined the faculty of Massey University in 1998 as a Lecturer and remained there for four years. Since 2002, Dr Moore has been an Associate Professor in the Dept. of Biochemistry at the University of Saskatchewan. His current research interests include the flagellum secretion system in Helicobacter pylori, and chromatin modifying systems in higher eukaryotes.

** Dr. Moore doesn't endorse smoking - however, he does infrequently partake in the occasional black licorice cigar!

Selected Publications

  • Clancy, C. D., Forde, B. M., Moore, S. A. and O’Toole, P. W. (2012). Draft genome sequences of Helicobacter pylori strains 17874 and P79. J. Bact. 194, 2402 doi:10.1128/JB.00230-12.
  • Schiemann, A. H., Li, F., Weake, V. M., Belikoff, E. J., Klemmer, K. C., Moore, S. A. and Scott, M. J. (2010). Sex-biased transcription enhancement by a 5' tethered Gal4-MOF histone acetyltransferase fusion protein inDrosophila. BMC Mol. Biol. 11, 80.
  • Moore, S. A., Ferhatoglu, Y., Jia, Y. Al-Jiab, R. and Scott, M. J. (2010). Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono or dimethyl lysine20 on histone H4. J. Biol. Chem. 285, 40879-40890.
  • Caly, D. L., O'Toole, P. W. and Moore, S. A. (2010). The 2.2 Å resolution structure of the HP0958 protein fromHelicobacter pylori reveals a kinked antiparallel coiled coil hairpin domain and a highly conserved Zn-ribbon domain. J. Mol. Biol. 403, 405-419.
  • Moore, S. A., and Jia, Y. (2010). Structure of the cytoplasmic domain of the flagellar secretion apparatus component FlhA from Helicobacter pylori. J. Biol. Chem. 285, 21060-21069.
  • Douillard, F. P., Ryan, K. A., Lane, M. C., Caly, D. C., Moore, S. A., Penn, C. W., Hinds, J. and O'Toole, P. W. (2010). The HP0256 gene product is involved in motility and cell envelope architecture of Helicobacter pylori. BMC Microbiol. 10, 106.