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Digard P

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Title Authors Year Journal
Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase. Digard P 2000 The Journal of biological chemistry
Mutational analysis of DNA polymerase substrate recognition and subunit interactions using herpes simplex virus as prototype. Digard P 1995 Methods in enzymology
Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. Digard P 1995 Proceedings of the National Academy of Sciences of the United States of America
Unusual regulation of expression of the herpes simplex virus DNA polymerase gene. Digard P 1993 J Virol
Functional analysis of the herpes simplex virus UL42 protein. Digard P 1993 Journal of virology
The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication. Digard P 1993 J Virol
Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site. Digard P 1991 Molecular and cellular biology
A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein. Digard P 1990 The Journal of biological chemistry

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