Amanda McCullough, PhD
- Email:
- mcculloa@ohsu.edu
- Position:
- Assistant Professor, Molecular and Medical Genetics, OHSU School of Medicine
- Assistant Scientist, CROET
- Office:
- CROET2588
Read more about Dr. McCullough's research
Research Interests
The McCullough laboratory is interested in the regulation and roles of DNA repair in cellular responses to environmental stress and how defects in these systems correlate with human cancers, aging, and other disease states. Currently our research includes: 1) identification of the genes and pathways involved in cellular responses to formaldehyde-induced DNA-protein crosslinks; 2) biochemical and cellular characterization of human oxidative DNA damage-specific repair glycosylases MUTYH and NEIL1 associated with colon cancer and metabolic syndrome, respectively; and 3) biochemical mechanisms and therapeutic applications of ultraviolet (UV) light-induced DNA damage-specific glycosylases for potential therapeutic use in preventing UV-induced non-melanoma skin cancers and immunosuppression.
Biography
Dr. McCullough received her doctoral degree in Cellular and Molecular Biology from the University of Vermont. She completed postdoctoral training at Oregon Health & Science University and the University of Texas Medical Branch in Galveston Texas. She was an Assistant Professor in the Department of Human Biological Chemistry and Genetics at the University of Texas before joining CROET in August 2003.
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Links
Selected Publications
Bendert de Graaf, M.S., Clore, A.J., McCullough, A.K. Cellular Pathways for DNA Repair and Damage Tolerance of Formaldehyde-Induced DNA-Protein Crosslinks. DNA Repair, 2009 June 9 [Epub ahead of print].
Trapp, C., McCullough, AK, Epe, B. The basal levels of 8-oxoG and other oxidative modifications in intact mitochondrial DNA are low even in repair-deficient (Ogg1-/-/Csb-/-) mice. Mut. Research, 2007;625:155-63.
Roy, L., Wood, TG, Dizdaroglu, M., McCullough, AK, and Lloyd, RS. Polymorphic Variants of the Human Neil1: Structure-Function Analyses. J. Biol. Chem. 282: 15790-15798, 2007.
Walker, R.K., McCullough, A.K., Lloyd, R.S. Uncoupling of Nucleotide Flipping and DNA Bending by the T4 Pyrimidine Dimer DNA Glycosylase. Biochemistry 45 (47): 14192-14200, 2006.
Golan, G, Zharkov, DO, Grollman, AP, Dodson, ML, McCullough, AK, Lloyd, RS, Shoham, G. Structure of T4 pyrimidine dimer glycosylase in a reduced imine covalent complex with abasic site-containing DNA. J Molec Biol 362(2): 241-58, 2006.
Vartanian, V., Lowell, B., Minko, I.G., Wood, T.G., Ceci, J.D., George, S., Ballinger, S.W., Corless, C.L., McCullough, A.K., and Lloyd, R.S. The Metabolic Syndrome Resulting from a Knockout of the NEIL1 DNA Glycosylase. Proc Natl Acad Sci U S A. Feb;103:1864-1869, 2006.
Manuel, R. C., Hitomi, K., Arvai, A. S., House, P. G., Kurtz, A. J., Dodson, M. L., McCullough, A. K., John A. Tainer and R. Stephen Lloyd. Reaction Intermediates in the Catalytic Mechanism of Escherichia coli MutY DNA Glycosylase. J. Biol. Chem. 279 (45):46930-9, 2004.
Wooden, S. H., Bassett, H. M., Wood, T.G., and McCullough, A.K. Identification of critical residues required for the mutation avoidance function of human MutY (hMYH) and implications in colorectal cancer. Cancer Letters 205:89-95, 2004.
Jaruga, P., Jabil, R., McCullough, A.K., Rodriguez, H., Dizdaroglu, M., and Lloyd, R.S. Chlorella virus pyrimidine dimer glycosylase excises ultraviolet radiation- and hydroxyl radical-induced products 4,6-diamino-5-formamidopyrimidine and 2,6-diamino-4-hydroxy-5-formamidopyrimidine from DNA. Photochemistry and Photobiology 75(2):85-91, 2002.
Boldogh, I., Milligan, D., Lee, M.S., Bassett, H., Lloyd, R.S., McCullough, A. K. hMYH cell cycle-dependent expression, subcellular localization and association with replication foci: evidence suggesting replication-coupled repair of adenine:8-oxoguanine mispairs. Nucleic Acids Res. 29: 2802-2809; 2001.
McCullough, A. K., Sanchez, A., Dodson, M. L., Marapaka, P., Taylor, J.-S. and Lloyd, R. S. The Reaction Mechanism of DNA Glycosylase/AP Lyases at Abasic Sites Biochemistry 40: 561-568; 2001.
