Faculty

Peter M. Burgers
Professor
Dept. of Biochemistry and
Molecular Biophysics

Office: 1911 South Building
Phone: 314-362-3872
Fax: 314-362-7183
Email: burgers@biochem.wustl.edu

Lab Website
Research Opportunities

Mailing Address:
WUSM - Biochemistry Dept.
660 S. Euclid Ave., MS8231
St. Louis, MO 63110

Rossi, M.L., Pike, J.E., Wang, W., Burgers, P.M., Campbell, J.L. and Bambara, R.A. Pif1 helicase directs eukaryotic Okazaki fragments toward the two-nuclease cleavage pathway for primer removal. J Biol Chem (E-pub ahead of print.) (2008).
Sommer, D., Stith, C.M., Burgers, P.M.J. and Lahue, R.S. Partial reconstitution of DNA large loop repair with purified proteins from Saccharomyces cerevisiae. Nuc Acid Res (E-pub ahead of print.) (2008).
Nick McElhinny, S.A., Gordenin, D.A., Stith, C.M., Burgers, P.M. and Kunkel, T.A. Division of labor at the eukaryotic replication fork. Mol Cell. 30:137-144 (2008).
Wardle, J., Burgers, P.M., Cann, I.K., Darley, K., Darley, K., Heslop, P., Johansson, E., Lin, L.J., McGlynn, P., Sanvoisin, J., Stith, C.M. and Connolly, B.A. Uracil recognition by replicative DNA polymerases is limited to the archaea, not occurring with bacteria and eukarya. Nucleic Acids Res 36:705-711 (2008).
Chilkova, O., Stenlund, P., Isoz, I., Stith, C,M., Grabowski, P., Lundstrom, E.B., Burgers, P.M. and Johansson, E. The eukaryotic leading and lagging strand DNA polymerases are loaded onto primer-ends via separate mechanisms but have comparable processivity in the presence of PCNA. Nucleic Acids Research 35:6588-6597 (2007).
McCulloch, S.D., Wood, A., Garg, P., Burgers, P.M. and Kunkel, T.A. Effects of accessory proteins on the bypass of a cis-syn thymine-thymine dimer by Saccharomyces cerevisiae DNA polymerase eta. Biochemistry 46:8888-8896 (2007).