Donald Coen, PhD
Professor of Biological Chemistry and Molecular Pharmacology, Harvard Medical School
Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.
Authors: Authors: Jiang C, Komazin-Meredith G, Tian W, Coen DM, Hwang CB.
J Virol
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J Virol
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Expression of extremely low levels of thymidine kinase from an acyclovir-resistant herpes simplex virus mutant supports reactivation from latently infected mouse trigeminal ganglia.
Authors: Authors: Besecker MI, Furness CL, Coen DM, Griffiths A.
J Virol
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J Virol
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Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein UL44 are crucial for interaction with the UL54 catalytic subunit.
The polymerase chain reaction.
Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase.
Authors: Authors: Bridges KG, Hua Q, Brigham-Burke MR, Martin JD, Hensley P, Dahl CE, Digard P, Weiss MA, Coen DM.
J Biol Chem
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J Biol Chem
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Effects of mutations in the Exo III motif of the herpes simplex virus DNA polymerase gene on enzyme activities, viral replication, and replication fidelity.
Mutational analysis of DNA polymerase substrate recognition and subunit interactions using herpes simplex virus as prototype.
The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
Restricted expression of herpes simplex virus lytic genes during establishment of latent infection by thymidine kinase-negative mutant viruses.
Effect of an amber mutation in the herpes simplex virus thymidine kinase gene on polypeptide synthesis and stability.
Authors: Authors: Irmiere AF, Manos MM, Jacobson JG, Gibbs JS, Coen DM.
Virology
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Virology
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