Stephen P. Methot
  • Institut de Recherches Cliniques de Montréal, Canada
研究方向
  • Immunology
个人信息

Education

B.S. in Molecular Biology and Biochemistry, Simon Fraser University, 2010

Current position

Doctoral student in Experimental Medicine, Department of Medicine, McGill University, Montreal, Canada

Publications

  1. Methot, S. P. and Di Noia, J. M. (2015). Pharmacological manipulation of AID. Oncotarget 6(29): 26550-26551.
  2. Methot, S. P., Litzler, L. C., Trajtenberg, F., Zahn, A., Robert, F., Pelletier, J., Buschiazzo, A., Magor, B. G. and Di Noia, J. M. (2015). Consecutive interactions with HSP90 and eEF1A underlie a functional maturation and storage pathway of AID in the cytoplasm. J Exp Med 212(4): 581-596.
  3. Zahn, A., Eranki, A. K., Patenaude, A. M., Methot, S. P., Fifield, H., Cortizas, E. M., Foster, P., Imai, K., Durandy, A., Larijani, M., Verdun, R. E. and Di Noia, J. M. (2014). Activation induced deaminase C-terminal domain links DNA breaks to end protection and repair during class switch recombination. Proc Natl Acad Sci U S A 111(11): E988-997.
  4. Hu, Y., Ericsson, I., Torseth, K., Methot, S. P., Sundheim, O., Liabakk, N. B., Slupphaug, G., Di Noia, J. M., Krokan, H. E. and Kavli, B. (2013). A combined nuclear and nucleolar localization motif in activation-induced cytidine deaminase (AID) controls immunoglobulin class switching. J Mol Biol 425(2): 424-443.
  5. Baker, J. H., Kyle, A. H., Bartels, K. L., Methot, S. P., Flanagan, E. J., Balbirnie, A., Cran, J. D. and Minchinton, A. I. (2013). Targeting the tumour vasculature: exploitation of low oxygenation and sensitivity to NOS inhibition by treatment with a hypoxic cytotoxin. PLoS One 8(10): e76832.
  6. Orthwein, A., Zahn, A., Methot, S. P., Godin, D., Conticello, S. G., Terada, K. and Di Noia, J. M. (2012). Optimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1. EMBO J 31(3): 679-691.
  7. Poon, L. C., Methot, S. P., Morabi-Pazooki, W., Pio, F., Bennet, A. J. and Sen, D. (2011). Guanine-rich RNAs and DNAs that bind heme robustly catalyze oxygen transfer reactions. J Am Chem Soc 133(6): 1877-1884.