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

Inhibition of phosphorylation of cellular dUTP nucleotidohydrolase as a consequence of herpes simplex virus infection.

Journal of cellular biochemistry - 1 Aug 1990

Lirette R, Caradonna S

Abstract excerpt

During an infection with herpes simplex virus, activity of cellular dUTPase decreases as a function of time, post-infection, while virus-encoded dUTPase activity increases. Prelabeling of cells with 35S-methionine and immunoprecipitation analysis, using monoclonal antibodies, indicates that cellular dUTPase protein levels remain the same (with respect to levels in uninfected cells) throughout the infection...

Read the complete abstract on PubMed

Topics

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

Share to HeLa Cells
Share to Mutation
Share to Phosphorylation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Precipitin Tests

Share to Protein Processing, Post-Translational

Share to Restriction Mapping

Share to Serine

Share to Simplexvirus

Source

Identifiers

PMID: 2168898
DOI: 10.1002/jcb.240430406

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 8 closest

Inhibition of phosphorylation of cellular dUTP nucleotidohydrolase as a consequence of herpes simplex virus infection.PMID 2168898Read ↗

Phosphorylation of Herpes Simplex Virus 1 dUTPase Upregulated Viral dUTPase Activity To Compensate for Low Cellular dUTPase Activity for Efficient Viral ReplicationSemantic proximity Read ↗

Herpes simplex virus 1 inhibits phosphorylation of RNA polymerase II CTD serine-7Semantic proximity Read ↗

Phosphorylation of a herpes simplex virus 1 dUTPase by a viral protein kinase, Us3, dictates viral pathogenicity in the central nervous system but not at the periphery.Semantic proximity Read ↗

Association of a M(r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5- mutants of herpes simplex virus 1.Semantic proximity Read ↗

A mutant of herpes simplex virus type 1 in which the UL13 protein kinase gene is disrupted.Semantic proximity Read ↗

Phosphorylation of the herpes simplex virus tegument protein VP22 has no effect on incorporation of VP22 into the virus but is involved in optimal expression and virion packaging of ICP0.Semantic proximity Read ↗

Replication properties of dUTPase-deficient mutants of caprine and ovine lentiviruses.Semantic proximity Read ↗

Identification of a physiological phosphorylation site of the herpes simplex virus 1-encoded protein kinase Us3 which regulates its optimal catalytic activity in vitro and influences its function in infected cells.Semantic proximity Read ↗

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