Valerie L. O'Shea Murray, Ph.D., is a technical specialist in the firm's Biotechnology & Chemical Practice Group, where she assists in the preparation and prosecution of U.S. and foreign patent applications; aids in the formulation of invalidity, non-infringement, freedom-to-operate, clearance, and patentability opinions; and provides litigation support. Her technical areas of expertise include protein and nucleic acid biochemistry, enzymology, chemical biology, biophysics (including single molecule and microfluidic bio-assays), structural biology, and molecular and cellular biology.
Prior to joining the firm, Valerie was an NIH NRSA Postdoctoral Research Fellow at the University of California, Berkeley. Her postdoctoral research with Professor James Berger in the Department of Molecular and Cell Biology focused on elucidating mechanisms of ATPase motors and switches involved in DNA replication initiation. She then moved with the Berger lab to the Department of Biophysics and Biophysical Chemistry at Johns Hopkins University School of Medicine where she continued her research as a Senior Research Specialist. Her work has been attributed to resolving long-standing questions in the field, showing that bacterial replicative helicase loading proceeds via a ring-breaking mechanism, and revealed the roles of ATP binding and hydrolysis in regulating bacterial helicase loading.
Valerie’s graduate research under Professor Sheila David in the Department of Chemistry at the University of Utah involved mechanistic and structural investigations of a DNA repair glycosylase, MutY. Her studies demonstrated that MutY utilizes a mechanism similar to retaining glycosidases for repairing oxidative DNA damage.
Valerie was a recipient of an NIH NRSA postdoctoral fellowship, as well as two NIH pre-doctoral training fellowships in Multidisciplinary Cancer Research and Biological Chemistry, respectively. She presented her work at several conferences, including the American Chemical Society conference, the Environmental Mutagen Society meeting, the FASEB Nucleic Acid Enzymes conference, the Keystone conference on DNA Replication, and as a speaker at the FASEB Helicases and Nucleic Acid Based Machines conference. Valerie served as an editor of the Berkeley Science Review magazine, and lobbied Congress for NIH funding as a participant of ASBMB’s Hill Day.
Valerie received her Ph.D. and her B.S. degree in chemistry from University of Utah.
- O’Shea VL*, Woods RD*, Chu A, Cao A, Richards JL, Horvath MP, David SS. Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases. Nucleic Acids Research, 2016, 44, 801-810. (*contributed equally to the study as first authors)
- O’Shea VL and Berger JM, Loading strategies of ring-shaped nucleic acid translocases and helicases. Current Opinion in Structural Biology, 2014, 25C, 16–24.
- Strycharska MS, Arias-Polomo E, Lyubimov AY, Erzberger JP, O’Shea VL, Bustamante C, Berger JM. Nucleotide and partner-protein control of bacterial replicative helicase structure and function. Molecular Cell, 2013, 52, 844–854.
- O’Shea VL*, Arias-Polomo E*, Hood IV, Berger JM. The bacterial DnaC helicase loader is a DnaB ring breaker. Cell, 2013, 153, 438–448. (*contributed equally to the study as first authors)
- Michelson AZ, Rozenberg A, Tian Y, Sun X, Davis J, Francis AW, O'Shea VL, Halasyam M, Manlove AH, David SS, Lee JK. Gas-phase studies of substrates for the DNA mismatch repair enzyme MutY. J. Amer. Chem. Soc., 2012, 134, 19839–19850.
- O’Shea VL*, Livingston AL*, Kim T, Kool E, David SS. Unnatural substrates reveal the importance of 8-oxoguanine for in vivo repair by MutY. Nature Chemical Biology, 2008, 4, 51–58. (*contributed equally to the study as first authors)
- David SS, O’Shea VL, Kundu S. Base-excision repair of oxidative DNA damage. Nature, 2007, 447, 941–950.
- Yavin E, Stemp EDA, O’Shea VL, David SS, Barton JK. Electron-trap for DNA-bound repair enzymes: A strategy for DNA-mediated signaling. Proc. Natl. Acad. Sci. U.S.A., 2006, 103, 3610–3614.
- Boal AK, Yavin E, Lukianova OA, O’Shea VL, David SS, Barton JK. DNA-Bound Redox Activity of DNA Repair Glycosylases Containing [4Fe-4S] Clusters. Biochemistry, 2005, 44, 8397–8407.
- Yavin E, Boal AK, Stemp EDA, Boon EM, Livingston AL, O'Shea VL, David SS, Barton JK. Protein-DNA Charge Transport: Redox Activation of a DNA Repair Protein by Guanine Radical. Proc. Natl. Acad. Sci. U.S.A., 2005, 102, 3546–3551.