John C. Randell, Ph.D. - Publications
Affiliations: | 2003 | Harvard University, Cambridge, MA, United States |
Area:
Molecular Biology, Biochemistry, Microbiology BiologyYear | Citation | Score | |||
---|---|---|---|---|---|
2007 | Jiang C, Hwang YT, Wang G, Randell JC, Coen DM, Hwang CB. 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. PMID 17715219 DOI: 10.1128/Jvi.01133-07 | 0.732 | |||
2007 | Jiang C, Hwang YT, Randell JC, Coen DM, Hwang CB. 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. PMID 17229696 DOI: 10.1128/Jvi.02359-06 | 0.71 | |||
2005 | Randell JC, Komazin G, Jiang C, Hwang CB, Coen DM. 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. PMID 16140778 DOI: 10.1128/Jvi.79.18.12025-12034.2005 | 0.74 | |||
2004 | Randell JC, Coen DM. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. Journal of Molecular Biology. 335: 409-13. PMID 14672651 DOI: 10.1016/J.Jmb.2003.10.064 | 0.728 | |||
2001 | Randell JC, Coen DM. Linear diffusion on DNA despite high-affinity binding by a DNA polymerase processivity factor. Molecular Cell. 8: 911-20. PMID 11684025 DOI: 10.1016/S1097-2765(01)00355-0 | 0.686 | |||
Show low-probability matches. |