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Michael Currens

Paula Krosky, Ph.D.

National Cancer Institute-Frederick SAIC-Frederick
Address: Building 440
Frederick, MD 21702-1201

Phone: 301-846-7246
Fax: 301-846-6775
Email: pkrosky@mail.ncifcrf.gov

Current Interests

We are currently providing biochemical and molecular biology support for several STB program projects. These efforts can be divided into two categories. 1) The design, evaluation, and implementation of high-throughput screening assays including recombinant expression and purification of selected target proteins, biochemical characterization of these proteins, and adaptation of assays to an appropriate, small scale, robotic format. 2) The characterization of intracellular effects of molecularly targeted drugs including substantiation of the cell-based mechanism of action and validation of pharmacodynamic markers which will be used to monitor the molecular response in animal and clinical samples.

Credentials

Dr. Paula Krosky received a B.A. in biology and chemistry from Mary Baldwin College in 1992 and a Ph.D in medicinal chemistry from the University of Michigan in 1997. She spent almost four years as a post-doctoral fellow in the laboratory of Donald Coen at the Harvard Medical School before joining the Developmental Therapeutics Program at NCI-Frederick in the fall of 2001.

Recent Publications:

Krosky PM, Baek MC, Jahng WJ, Barrera I, Harvey RJ, Biron KK, Coen DM, Sethna PB. The human cytomegalovirus UL44 protein is a substrate for the UL97 protein kinase. J Virol. 2003 Jul;77(14):7720-7.

Krosky PM, Baek MC, Coen DM. The human cytomegalovirus UL97 protein kinase, an antiviral drug target, is required at the stage of nuclear egress. J Virol. 2003 Jan;77(2):905-14.

Baek MC, Krosky PM, Coen DM. Relationship between autophosphorylation and phosphorylation of exogenous substrates by the human cytomegalovirus UL97 protein kinase. J Virol. 2002 Dec;76(23):11943-52.

Baek MC, Krosky PM, He Z, Coen DM. Specific Phosphorylation of Exogenous Protein and Peptide Substrates by the Human Cytomegalovirus UL97 Protein Kinase. IMPORTANCE OF THE P+5 POSITION. J Biol Chem. 2002 Aug 16;277(33):29593-9.

Krosky PM, Borysko KZ, Nassiri MR, Devivar RV, Ptak RG, Davis MG, Biron KK, Townsend LB, Drach JC. Phosphorylation of beta-D-ribosylbenzimidazoles is not required for activity against human cytomegalovirus. Antimicrob Agents Chemother. 2002 Feb;46(2):478-86.

Krosky PM, Ptak RG, Underwood MR, Biron KK, Townsend LB, Drach JC. Differences in DNA packaging genes and sensitivity to benzimidazole ribonucleosides between human cytomegalovirus strains AD169 and Towne. Antivir Chem Chemother. 2000 Sep;11(5):349-52.

Prichard MN, Gao N, Jairath S, Mulamba G, Krosky P, Coen DM, Parker BO, Pari GS. A recombinant human cytomegalovirus with a large deletion in UL97 has a severe replication deficiency. J Virol. 1999 Jul;73(7):5663-70.

Krosky PM, Underwood MR, Turk SR, Feng KW, Jain RK, Ptak RG, Westerman AC, Biron KK, Townsend LB, Drach JC. Resistance of human cytomegalovirus to benzimidazole ribonucleosides maps to two open reading frames: UL89 and UL56. J Virol. 1998 Jun;72(6):4721-8.


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