Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A mutation in the DNA polymerase accessory factor of herpes simplex virus 1 restores viral DNA replication in the presence of raltegravir.

Journal of virology - 1 Oct 2014

Zhou Bin, Yang Kui, Wills Elizabeth, Tang Liang, Baines Joel D

Abstract excerpt

UNLABELLED: Previous reports showed that raltegravir, a recently approved antiviral compound that targets HIV integrase, can inhibit the nuclease function of human cytomegalovirus (HCMV terminase) in vitro. In this study, subtoxic levels of raltegravir were shown to inhibit the replication of fou...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cytomegalovirus
Share to Exodeoxyribonucleases
Share to Gene Expression Regulation, Viral

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Herpesvirus 1, Human

Share to Herpesvirus 2, Human

Share to Muromegalovirus

Share to Pyrrolidinones

Share to Raltegravir Potassium

Source

Open in PubMed Open full text

Identifiers

PMID: 25008933
DOI: 10.1128/JVI.01540-14
PMCID: PMC4178803

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25008933-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A mutation in the DNA polymerase accessory factor of herpes simplex virus 1 restores viral DNA replication in the presence of raltegravir.PMID 25008933Read ↗

Large Subunit of the Human Herpes Simplex Virus Terminase as a Promising Target in Design of Anti-Herpesvirus AgentsSemantic proximity Read ↗

Structure and inhibition of herpesvirus DNA packaging terminase nuclease domain.Semantic proximity Read ↗

The DNA helicase–primase complex as a target for herpes viral infectionSemantic proximity Read ↗

The Exonuclease Activity of Herpes Simplex Virus 1 UL12 Is Required for Production of Viral DNA That Can Be Packaged To Produce Infectious Virus.Semantic proximity Read ↗

A Mutation in the Herpes Simplex Virus Type 1 (HSV-1) UL29 Gene is Associated with Anti-Herpesvirus Drugs' Susceptibility.Semantic proximity Read ↗

HSV-1 Delta ribonucleotide reductase as a Model to Investigate Molnupiravir-Induced MutagenesisSemantic proximity Read ↗

Deciphering letermovir's mode of action and resistance mutation effects.Semantic proximity Read ↗

Accelerated Evolution of Maribavir Resistance in a Cytomegalovirus Exonuclease Domain II MutantSemantic proximity Read ↗

Genotypic characterization of herpes simplex virus DNA polymerase UL42 processivity factor.Semantic proximity Read ↗

Resistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and management.Semantic proximity Read ↗

Host DNA repair factors empower a mechanism of antiviral nucleoside analog resistanceSemantic proximity Read ↗

The human cytomegalovirus terminase complex as an antiviral target: a close-up viewSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.