Dr. Paul Boehmer, PhD head shot

Contact Info

AZ Biomedical Collaborative 1
Room Number
Interim Associate Dean for Research and Professor
College of Medicine Phx Basic Medical Sciences


  • Postdoctoral Fellowship: Stanford University, CA, 1990 – 1994. 
  • PhD: University of Newcastle upon Tyne, UK, 1990.


  • Balzarini J, Menni M, Das K, van Berckelaer L, Ford A, Maguire NM, Liekens S, Boehmer PE, Arnold E, Götte M and Maguire AR. Guanine α-carboxy nucleoside phosphonate (G-α-CNP) shows a different inhibitory kinetic profile against the DNA polymerases of human immunodeficiency virus (HIV) and herpes viruses. Biochem. Pharmacol. (2017) 136, 51-61.
  • Rupesh KR, Smith A, and Boehmer PE. Ligand induced stabilization of the melting temperature of the HSV-1 single-strand DNA binding protein using the thermal shift assay. Biochem. Biophys. Res. Commun. (2014) 454, 604-608.
  • Hsieh JC, Kuta R, Amour C and Boehmer PE Identification of two novel functional p53 response elements in the herpes simplex virus-1 genome. Virology. (2014) 460-461, 45-54.
  • Bogani F, Corredeira I, Fernandez V, Sattler U, Rutvisuttinunt W, Defais M, and Boehmer PE. Association between the Herpes Simplex Virus-1 DNA Polymerase and Uracil DNA Glycosylase. J. Biol. Chem. (2010) 285, 27664-27672.
  • Bogani F, Chua CN and Boehmer PE. Reconstitution of uracil DNA glycosylase-initiated base excision repair in herpes simplex virus-1. J. Biol. Chem. (2009) 284, 16784-16790.

For a complete listing of Dr. Boehmer's publications, search PubMed.

Research Interests

Genome integrity, herpes virology, infectious diseases

Research Summary

We are using HSV-1 as a model for genome transactions and to further understand this important human virus. We are examining the role of novel 5’ dRP lyase and 3’ DNA phosphatase activities of the viral DNA polymerase. We hypothesize that these activities prevent mutagenesis, to ensure virus viability during lytic replication and for reactivation from latency. We are also studying a role for p53 in controlling viral gene expression to regulate the balance between lytic replication and latency.