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. 1992 Mar;66(3):1814–1816. doi: 10.1128/jvi.66.3.1814-1816.1992

Use of suppressor analysis to identify DNA polymerase mutations in herpes simplex virus which affect deoxynucleoside triphosphate substrate specificity.

Y S Wang 1, S Woodward 1, J D Hall 1
PMCID: PMC240950  PMID: 1310785

Abstract

Herpes simplex virus DNA polymerase mutations which map in the N-terminal part of the protein and appear to alter deoxynucleoside triphosphate (dNTP) substrate specificity are described. These mutations suppress a drug hypersensitivity associated with the downstream mutation, Aphr10. We suggest that the mutant residues form part of the dNTP-binding site, a site previously thought to be confined to the C terminus.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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