Michael D. Wyatt, Ph.D.

Associate Professor of Biomedicinal Chemistry

Laboratory: CLS 515A | Lab Phone: 803-777-5792

(803)777-0856 | CLS 515C

Dr. Wyatt's Email

Dr. Michael Wyatt

Research Interest

DNA Repair

Cancer Chemotherapy

Molecular Pharmacology



Bachelor of Science, Chemistry
Furman University, 1991 

Master of Science, Chemistry
Furman University, 1992 

Doctor of Philosophy, Molecular Pharmacology
University College London, 1996

Postdoctoral Associate, Genetic Toxicology,
Harvard School of Public Health, 1999

Awards & Honors

  • Chemistry Fellowship, Furman University, 1991-1992.
  • Post Graduate Fellowship, University College London, 1992-1996.
  • 1st Prize, Postgraduate Student Poster Exhibition, University College London, 1993.
  • Upjohn Travel Award for Meritorious Abstracts, 86th Annual American Association for Cancer Research Meeting, 1995.
  • Outstanding Poster, 86th Annual American Association for Cancer Research Meeting, 1995.
  • National Institutes of Health Institutional Training Grant fellowship March 1996-February 1997.
  • NIH/NCI NRSA Individual Fellowship Award March 1997-March 1999.
  • F32 CA73135, “Role of human 3-MeA DNA glycosylase in alkylation repair.”  
  • NIH/NIEHS, “Transition to Independent Positions” Award.  K22 ES00333:  “Substrate Recognition Mechanism of DNA Repair Enzymes.”         9/01/99-08/31/02
  • USC College of Pharmacy Researcher of the year, 2001. 
  • South Carolina College of Pharmacy “Extra Mile” Award, 2015.
  • Reviewer for the NIH Cancer Etiology Study Section (2016/01 CE), October 8-9, 2015.
  • Reviewer, Special Emphasis Panel/Scientific Review Group ZRG1 BST-U (55) “High Throughput Screening Assays for Probe Discovery.” January 20, 2016.


  • Premnath, P., Craig, S., Liu, S., Perkins, T., Anderson, E., Grigoroudis, A., Kontopidis, G., Wyatt M.D., Pittman, D., McInnes, C. (2015). Iterative conversion of cyclin binding groove peptides into drug-like CDK inhibitors with anti-tumor activity.  Journal of Medicinal Chemistry, 58, 433-442. PMID 25454794.
  • Craig, S., Wyatt M.D., McInnes, C. (2014). Current Assessment of Polo-Like Kinases as anti-tumor drug targets. Expert Opinion in Drug Discovery. 9, 773-789. PMID 24819909
  • Das, D., Preeti, R., Mohapatra, P., Satapathy S.R., Siddharth S., Tamir, T., Jain, V., Bharatam, P.V., Wyatt M.D., Kundu C.N. (2014). 5-Fluorouracil mediated anti-cancer activity in colon cancer cells is through the induction of Adenomatous Polyposis Coli: Implication of the long-patch base excision repair pathway. DNA Repair, 21, 15-25. PMID 25460919
  • Nagaria, P., Svilar, D., Brown, A.R., Wang, X., Sobol, R.W., Wyatt, M.D. (2013). SMUG1 but not UNG DNA Glycosylase contributes to the cellular response to recovery from 5-fluorouracil induced replication stress. Mutation Research, 733-734, 26-32. PMID: 23253900.
  • Yang, Z., Waldman, A.S., Wyatt, M.D.  (2012). Expression and regulation of RAD51 mediate cellular responses to chemotherapeutics.  Biochemical Pharmacology, 83, 741-746. DOI: 10.1016/j.bcp.2011.12.022. PMC3278513
  • McInnes, C., Estes, K., Baxter, M., Yang, Z., Farag, D.B., Johnson, P., Lazo, J., Wang, J., Wyatt M.D. (2012). Targeting sub-cellular localization through the Polo-Box Domain: non-ATP competitive inhibitors recapitulate a PLK1 phenotype. Molecular Cancer Therapeutics, 11, 1672-1682. PMC3711794. An image from this article was featured on the cover of the August issue and mentioned in the “Highlights of this Issue.”
  • Rajesh, P., Litvinchuk, A., Pittman, D.L., Wyatt, M.D. (2011). The homologous recombination protein RAD51D mediates the processing of 6-thioguanine lesions downstream of mismatch repair.  Molecular Cancer Research, 9, 206-214.  The article and one of its images were featured in the February “Highlights of this issue.” PMC3041871.
  • Rajesh, P., Rajesh, C., Wyatt, M.D., Pittman D.L. (2010).  RAD51D protects against MLH1 dependent cytotoxic responses to O6-methylguanine.  DNA Repair, 9, 458-467.  PMC2858319.
  • Wyatt, M.D., and Wilson, D.M. III.  (2009).  Participation of DNA repair in the response to 5-fluorouracil.  Cell. Mol. Life Sci., 66, 788-99. Review.  PMC2649968.

More Publications

  • Alkilany, A.M., Nagaria, P., Hexel, C.R., Shaw, T.J., Murphy, C.J., Wyatt, M.D. (2009).  Cellular uptake and cytotoxicity of gold nanorods: Molecular origin of cytotoxicity and surface effects.  Small, 5, 701-708. PMID: 19226599.
  • Jones, L.E., Ying, L., Hofseth, A.B., Jelezcova, E., Sobol, R.W.,Ambs, S., Harris, C.C., Espey, M.G., Hofseth, L.J., Wyatt, M.D.  (2009).  Differential effects of reactive nitrogen species on DNA base excision repair initiated by the alkyladenine DNA glycosylase.  Carcinogenesis, 30, 2123-2129. PMC2792317. 
  • Luo, Y., Walla, M., Wyatt, M.D. (2008).  Uracil incorporation into genomic DNA does not predict toxicity caused by chemotherapeutic inhibition of thymidylate synthase.  DNA Repair, 7, 162-169.  PMC2258137.
  • Yang, Z., Waldman, A.S., Wyatt, M.D. (2008).  DNA damage signaling and homologous recombination responses induced by thymidylate deprivation.  Biochemical Pharmacology, 76, 987-996.  PMC2574569.
  • Wyatt, M.D. and Pittman, D.L.  (2006) Methylating agents and DNA repair responses: methylated bases and sources of strand breaks.  Chemical  Research in Toxicology, 19, 1580-1594.  The review article was featured on the cover of the December issue.  PMC2542901.  


  • Li L., Connor, E.E., Berger, S.H., Wyatt, M.D. (2005). Determination of apoptosis, uracil incorporation, DNA strand breaks, and sister chromatid exchanges under conditions of thymidylate deprivation in a model of BER deficiency.  Biochemical Pharmacology. 70, 1458-1468.  PMID: 16191427.
  • Connor, E.E., Mwamuka, J., Gole, A., Murphy, C.J., Wyatt, M.D.  (2005).  Gold nanoparticles are taken up by human cells but do not cause acute cytotoxicity.  Small , 1, 325-327.  PMID: 17193451.
  • Li L., Berger, S.H., Wyatt, M.D. (2004). Involvement of base excision repair in response to therapy targeted at thymidylate synthase.  Molecular Cancer Therapeutics, 6, 747-753.  
  • Connor, E.E. and Wyatt, M.D. (2002).  Active site clashes prevent the human 3-methyladenine DNA glycsosylase from improperly removing bases.  Chemistry & Biology, 9, 1033-1041. PMID: 12323378
  • Wyatt, M.D. and Samson, L.D. (2000).  The influence of DNA structure on hypoxanthine and 1, N6 ethenoadenine release by murine 3-methyladenine DNA glycosylase.  Carcinogenesis, 21, 901-908.  PMID: 10783310.
  • Lau, A., Wyatt, M.D.,  Glassner, B., Samson, L.D., Ellenberger, T. (2000).  Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG. Proc. Natl. Acad. Sci. USA, 97, 13573-13578.