Lorena S. Beese

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	Brandeis University Yale University
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.^[1] 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.^[2]

Research Interests

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

Selected Works

• Orans, J. McSweeney; Iyer, R.R.; Hast, M.A.; Hellinga, H.W.; Modrich, P.; Beese, L.S. (2011). "Structure of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family". Cell. 145 (2): 212–223. doi:10.1016/j.cell.2011.03.005. PMC 3093132. PMID 21496642.
• Wu, E.Y.; 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. 286: 19758–67. doi:10.1074/jbc.M110.191130. PMC 3103354. 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. doi:10.1016/j.chembiol.2009.01.014. PMC 2671474. PMID 19246009.
• 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. doi:10.1074/jbc.M805330200. PMC 2581548. PMID 18713740.
• Warren, JJ; Pohlhaus, TJ; Changela, A; Iyer, RR; Modrich, PL; Beese, LS (2007). "Structure of the human MutSalpha DNA lesion recognition complex". Mol Cell. 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. USA. 103 (52): 19701–6. doi:10.1073/pnas.0609580103.
• Terry, K.L.; Casey, P.J.; Beese, L.S. (2006). "Conversion of protein farnesyltransferase to a geranylgeranyltransferase". Biochemistry. 45 (32): 9746–55. doi:10.1021/bi060295e.
• 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. doi:10.1194/jlr.r600002-jlr200.
• 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.; Beese, L.S. (2004). "Structures of mismatch replication errors observed in a DNA polymerase". Cell. 116: 803–816. doi:10.1016/s0092-8674(04)00252-1.
• Hsu, G.W.; Ober, M.; Carell, T.; Beese, L.S. (2004). "Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase". Nature. 431 (7005): 217–21. doi:10.1038/nature02908.
• Johnson, S.J.; Taylor, J.S.; Beese, L.S. (2003). "Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations". Proc. Natl. Acad. Sci. USA. 100 (7): 3895–3900. doi:10.1073/pnas.0630532100.
• Taylor, J.S.; Reid, T.S.; Terry, K.L.; Casey, P.J.; Beese, L.S. (2003). "Structure of mammalian protein geranylgeranyltransferase type-1". EMBO J. 22 (22): 5963–5974. doi:10.1093/emboj/cdg571. PMC 275430. PMID 14609943.
• Long, SB; Casey, P.; Beese, LS (2002). "The reaction path of protein farnesyltransferase at atomic resolution". Nature. 419 (6907): 645–50. doi:10.1038/nature00986. PMID 12374986.
• 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. 98 (23): 12948–53. doi:10.1073/pnas.241407898. PMC 60805. PMID 11687658.
• Kiefer, J. R.; Mao, C.; Braman, J. C.; Beese, L. S. (1998). "Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal [see comments]". Nature. 6664: 304–7.

References

1. "Lorena Beese, Member Directory". National Academy of Sciences. Retrieved 30 March 2016.
2. "Lorena S. Beese (Primary)". Biochemistry Lab, Duke University School of Medicine. Retrieved 30 March 2016.