Lorena S. Beese

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Lorena S. Beese
Born Lorena Sue Beese
Residence Durham, North Carolina
Fields Cancer Research, DNA replication, DNA mismatch repair
Institutions Duke University School of Medicine
Alma mater
Spouse Homme Hellinga

Lorena Beese is a James B. Duke Professor of Biochemistry at Duke University. She received her PhD in Biophysics from Brandeis University and did her postdoctoral work with Dr. Thomas A. Steitz at Yale University. In 2009 Dr. Beese was elected to the National Academy of Sciences. Her research interests include structural biochemistry of DNA replication and human DNA mismatch repair and its connection to carcinogenesis. She is also interested in protein prenylation enzymes as targets for structure-based discovery of anticancer therapeutics and re-purposing of such therapeutics to treat pathogenic fungi and malaria.

Research Interests[edit]

  • Signal transduction
  • Structure based drug design
  • DNA replication
  • DNA mismatch repair
  • Observing enzymes in action

Selected Works[edit]

  • Orans, J. McSweeney, E.A., Iyer, R.R., Hast, M.A., Hellinga, H.W., Modrich, P., and Beese, L.S. (2011) Structure of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family. Cell 145(2):212-223 (PMCID:3093132).
  • Wu, E.Y. and Beese, L.S. (2011) The structure of a high fidelity DNA polymerase bound to a mismatched nucleotide reveals an ajar intermediate conformation in the nucleotide selection mechanism. J Biol Chem March 19, 2011. Epub ahead of print (PMID 21454515).
  • Hast, M.A., Fletcher, S., Cummings, C.G., Pusateri, E.E., Blaskovich, M.A., Rivas, K., Gelb, M.H., Van Voorhis, C.V., Sebti, S.M., Hamilton, A.D. & Beese, L.S. (2009) Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. Chemistry & Biology 16:181-192 (PMCID: 2671474).
  • Hast, M.A. & Beese, L.S. (2008) Structure of protein geranylgeranyltransferase-I from the human pathogen Candida albicans complexed with a lipid substrate. J Biol Chem 283 (46):31933-40 (PMCID: 2581548).
  • Warren JJ, Pohlhaus TJ, Changela A, Iyer RR, Modrich PL, Beese LS. (2007)”Structure of the human MutSalpha DNA lesion recognition complex.” Mol Cell. 2007 May 25;26(4):579-92.
  • Warren, J.J., Forsberg, L.J., & Beese, L.S. (2006) The structural basis for the mutagenicity of O6-methyl-guanine lesions. Proc Natl Acad Sci. Dec 26;103(52):19701-6.
  • Terry, K.L., Casey, P.J. & Beese, L.S. (2006) Conversion of protein farnesyltransferase to a geranylgeranyltransferase. Biochemistry 45(32):9746-55.
  • Lane, K.T. & Beese, L.S. (2006) Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. Journal of Lipid Research 47(4):681-699.
  • Beese, L., & Harvard University. (2005). Structure and mechanism of protein prenyltransferases: Analysis of a cancer therapeutic target.
  • Beese, L., & Harvard University. (2005). Structures and mechanisms of a DNA polymerase: Nature's copier and spellchecker in action.
  • Johnson, S.J. and Beese, L.S. (2004) Structures of mismatch replication errors observed in a DNA polymerase. Cell, Vol. 116, March 19, 803-816.
  • Hsu, G.W., Ober, M., Carell, T. and Beese, L.S. (2004) Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature Sep 9;431(7005):217-21. Epub 2004 Aug 22.
  • S.J. Johnson, J.S. Taylor, and L.S. Beese (2003). Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proc Natl Acad Sci Apr 1;100(7):3895-3900.
  • J.S. Taylor, T.S. Reid, K.L. Terry, P.J. Casey, and L.S. Beese (2003). Structure of mammalian protein geranylgeranyltransferase type-1. EMBO J 22(22):5963-5974.
  • Long, SB, Casey, P., Beese, LS (2002) The reaction path of protein farnesyltransferase at atomic resolution. Nature Oct 10; 419(6907):645-50.
  • Long SB, Hancock PJ, Kral AM, Hellinga HW, Beese LS. (2001) The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. Proc Natl Acad Sci U S A Nov 6;98(23):12948-53.
  • J. R. Kiefer, C. Mao, J. C. Braman and L. S. Beese (1998) “Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal [see comments].” Nature 6664:304-7.