John C. Randell, Ph.D.

Affiliations: 
2003 Harvard University, Cambridge, MA, United States 
Area:
Molecular Biology, Biochemistry, Microbiology Biology
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Donald M. Coen grad student 2003 Harvard
 (Processivity of the herpes simplex virus DNA polymerase: Role of high -affinity DNA binding by the processivity subunit.)
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Publications

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Jiang C, Hwang YT, Wang G, et al. (2007) Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis. Journal of Virology. 81: 12077-9
Jiang C, Hwang YT, Randell JC, et al. (2007) Mutations that decrease DNA binding of the processivity factor of the herpes simplex virus DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease the fidelity of DNA replication. Journal of Virology. 81: 3495-502
Randell JC, Komazin G, Jiang C, et al. (2005) Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis. Journal of Virology. 79: 12025-34
Randell JC, Coen DM. (2004) The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. Journal of Molecular Biology. 335: 409-13
Randell JC, Coen DM. (2001) Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor. Molecular Cell. 8: 911-20
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