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Article

The C-terminal third of UL42, a HSV-1 DNA replication protein, is dispensable for viral growth.

Virology - 1 Jun 1993

Gao M, DiTusa S F, Cordingley M G

Abstract excerpt

UL42 is the herpes simplex virus type 1 DNA polymerase (Pol) accessory protein and is required for viral DNA replication and growth. Previous results from this laboratory demonstrated that the N-terminal two thirds of the protein contains all of the biochemical activities of the protein which can be measured in vitro. These activities include dsDNA-binding, association with DNA polymerase, and stimulation of...

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Source

Identifiers

PMID: 8389077
DOI: 10.1006/viro.1993.1304

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Click a neighbor to travelStep 1 · 12 closest

The C-terminal third of UL42, a HSV-1 DNA replication protein, is dispensable for viral growth.PMID 8389077Read ↗

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A novel functional domain of an alpha-like DNA polymerase. The binding site on the herpes simplex virus polymerase for the viral UL42 protein.Semantic proximity Read ↗

Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.Semantic proximity Read ↗

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Phenylalanine residues at the carboxyl terminus of the herpes simplex virus 1 UL20 membrane protein regulate cytoplasmic virion envelopment and infectious virus production.Semantic proximity Read ↗

The UL15 protein of herpes simplex virus type 1 is necessary for the localization of the UL28 and UL33 proteins to viral DNA replication centresSemantic proximity Read ↗

The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region.Semantic proximity Read ↗

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