Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biomedical Research Support Grants (S07)
Project #
2S07RR005381-26
Application #
3514740
Study Section
(NSS)
Project Start
1987-04-01
Project End
1988-03-31
Budget Start
1987-04-01
Budget End
1988-03-31
Support Year
26
Fiscal Year
1987
Total Cost
Indirect Cost
Name
Harvard University
Department
Type
Schools of Medicine
DUNS #
082359691
City
Boston
State
MA
Country
United States
Zip Code
02115
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Weisshart, K; Kuo, A A; Painter, G R et al. (1993) Conformational changes induced in herpes simplex virus DNA polymerase upon DNA binding. Proc Natl Acad Sci U S A 90:1028-32
Garber, D A; Beverley, S M; Coen, D M (1993) Demonstration of circularization of herpes simplex virus DNA following infection using pulsed field gel electrophoresis. Virology 197:459-62
Digard, P; Bebrin, W R; Weisshart, K et al. (1993) The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication. J Virol 67:398-406
Digard, P; Chow, C S; Pirrit, L et al. (1993) Functional analysis of the herpes simplex virus UL42 protein. J Virol 67:1159-68
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Gibbs, J S; Weisshart, K; Digard, P et al. (1991) Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site. Mol Cell Biol 11:4786-95
Digard, P; Coen, D M (1990) A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein. J Biol Chem 265:17393-6

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