Identification of Crucial Hydrogen-Bonding Residues for the Interaction of Herpes Simplex Virus DNA Polymerase Subunits via Peptide Display, Mutational, and Calorimetric Approaches

The catalytic subunit, Pol, of herpes simplex virus DNA polymerase interacts via its extreme C terminus with the processivity subunit, UL42. This interaction is critical for viral replication and thus a potential target for antiviral drug action. To investigate the Pol-binding region on UL42, we eng...

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Bibliografische gegevens

Gepubliceerd in:	J Virol
Hoofdauteurs:	Bridges, Kristie Grove, Chow, Connie S., Coen, Donald M.
Formaat:	Artigo
Taal:	Inglês
Gepubliceerd in:	American Society for Microbiology (ASM) 2001
Onderwerpen:	Replication
Online toegang:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC114902/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11333878/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/JVI.75.11.4990-4998.2001
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