Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM034930-10
Application #
2177661
Study Section
Virology Study Section (VR)
Project Start
1986-07-01
Project End
1999-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
10
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Ohio State University
Department
Microbiology/Immun/Virology
Type
Schools of Medicine
DUNS #
098987217
City
Columbus
State
OH
Country
United States
Zip Code
43210
Zhu, Yali; Stroud, Jason; Song, Liping et al. (2010) Kinetic approaches to understanding the mechanisms of fidelity of the herpes simplex virus type 1 DNA polymerase. J Nucleic Acids 2010:631595
Zhu, Yali; Song, Liping; Stroud, Jason et al. (2008) Mechanisms by which herpes simplex virus DNA polymerase limits translesion synthesis through abasic sites. DNA Repair (Amst) 7:95-107
Hanes, Jeremiah W; Zhu, Yali; Parris, Deborah S et al. (2007) Enzymatic therapeutic index of acyclovir. Viral versus human polymerase gamma specificity. J Biol Chem 282:25159-67
Song, Liping; Chaudhuri, Murari; Knopf, Charles W et al. (2004) Contribution of the 3'- to 5'-exonuclease activity of herpes simplex virus type 1 DNA polymerase to the fidelity of DNA synthesis. J Biol Chem 279:18535-43
Arana, Mercedes E; Song, Liping; Tanguy Le Gac, Nicolas et al. (2004) On the role of proofreading exonuclease in bypass of a 1,2 d(GpG) cisplatin adduct by the herpes simplex virus-1 DNA polymerase. DNA Repair (Amst) 3:659-69
Zhu, Yali; Trego, Kelly S; Song, Liping et al. (2003) 3' to 5' exonuclease activity of herpes simplex virus type 1 DNA polymerase modulates its strand displacement activity. J Virol 77:10147-53
Trego, Kelly S; Parris, Deborah S (2003) Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activity. J Virol 77:12646-59
Chaudhuri, Murari; Parris, Deborah S (2002) Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42. J Virol 76:10270-81
Thornton, K E; Chaudhuri, M; Monahan, S J et al. (2000) Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins: correlation with in vivo function. Virology 275:373-90
Henderson, J O; Ball-Goodrich, L J; Parris, D S (1998) Structure-function analysis of the herpes simplex virus type 1 UL12 gene: correlation of deoxyribonuclease activity in vitro with replication function. Virology 243:247-59

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