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Research Interests
DNA Repair, Molecular Mechanisms of Cancer, Nucleic Acid Chemistry and Enzymology, Iron-Sulfur Proteins
We use chemical approaches to investigate the fascinating area of DNA repair. Damage to DNA can result in deleterious outcomes, such as cancer and aging; fortunately, most DNA damage is repaired by DNA repair enzymes! Our laboratory focuses on the repair of damaged DNA bases which is mediated by the process of base excision repair.


Research Overview
1. Recognition of Damaged DNA by MutY and the Role of MUTYH Variants in Colorectal Cancer

2. Role of [4Fe-4S] Clusters in Base Excision Repair Enzymes

3. Beyond OG


Funding
The David Lab is presently funded by:
We gratefully acknowledge past funding from:


Selected Publications
  • "Base-excision repair of oxidative DNA damage," David, S. S., O'Shea, V.L., Kundu, S., Nature, 2007, 447(7147),941-50.

  • "Unusual Structural Features of Hydantoin Lesions Translate into Efficient Recognition by Escherichia coli Fpg." Biochemistry, 2007, 21;46(33),9355-65.

  • "An Electron Trap for DNA-bound Repair Enzymes: A Strategy for DNA-mediated Signaling," Yavin, E., Stemp, E.D.A., O'Shea, V.L., David, S. S., Barton, J.K., Proc. Natl. Acad. Sci, USA, 2006, 103, 3610-3614.

  • "Insight into the Role of Tyrosine 82 and Glycine 253 in the Escherichia coli Adenine Glycosylase MutY, " Livingston, A.L., Kundu, S., Pozzi, M.H., Anderson, D.W., David, S. S., Biochemistry, 2005, 44, 14179-14190.

  • "A Role for Iron-Sulfur Clusters in DNA Repair," Lukianova, O.A., David, S. S., Curr. Op. Chem. Biol., 2005, 9, 145-151

  • "Protein-DNA Charge Transport: Redox Activation of a DNA Repair Protein by Guanine Radical, " Yavin, E., Boal, A. K., Stemp, E. D.A., Boon, E.M., Livingston, A.L., O'Shea, V.L., David, S.S., Barton, J.K., Proc. Natl. Acad. Sci. USA, 2005, 102, 3552-3557

  • "Insight into the functional consequences of hMYH variants associated with colorectal cancer: Distinct differences in the adenine glycosylase activity and the response to AP endonucleases of Y150C and G365D murine MYH," Pope, M.A., Chmiel, N.H., David, S.S., DNA Repair, 2005, 4, 315-325. 38.

  • "A Residue in MutY Important for Catalysis Identified by Photocross-Linking and Mass Spectrometry, " Chepanoske, C. L., Lukianova, O. A., Lombard, M., Golinelli-Cohen, M.-P., David, S. S., Biochemistry, 2004, 43, 651-662

  • "Probing the Requirements for Recognition and Catalysis in Fpg and MutY With Nonpolar Adenine Isosteres, " Francis, A. W., Helquist, S. A., Kool, E. T., David, S. S., J. Am. Chem. Soc, 2003, 125, 16235-16242.

  • "Recognition and Removal of Oxidized Guanines in Duplex DNA by the Base Excision Repair Enzymes hOGG1, yOGG1 and yOGG2, " Leipold, M. D., Workman, H., Muller, J.G., Burrows, C. J., David, S. S., Biochemistry, 2003, 42, 11373-1138129

  • "Escherichia coli MutY and Fpg Utilize a Processive Mechanism for Target Location," Francis, A. W. and David, S. S., Biochemistry, 2003, 42, 801-810.

  • "Inherited variants of hMYH associated with colorectal cancer exhibit a compromised ability to recognize and repair A:OG (7,8-dihydro-8-oxo-2'-deoxyguanosine) mismatches in DNA," Chmiel, N.H.; Livingston, A.L.; David, S.S., Journal of Molecular Biology, 2003, 327, 431-443.