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

Intragenic complementation of herpes simplex virus ICP8 DNA-binding protein mutants.

Journal of virology - 1 Feb 1993

Gao M, Knipe D M

Abstract excerpt

The major DNA-binding protein, or infected-cell protein 8 (ICP8), of herpes simplex virus is required for viral DNA synthesis and normal regulation of viral gene expression. Previous genetic analysis has indicated that the carboxyl-terminal 28 residues are the only portion of ICP8 capable of acting independently as a nuclear localization signal. In this study, we constructed a mutant virus (n11SV) in which the...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Line
Share to DNA-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Genetic Complementation Test

Share to Molecular Sequence Data

Share to Mutation

Share to Phenotype

Share to Plasmids

Source

Open in PubMed Open full text

Identifiers

PMID: 8380469
DOI: 10.1128/JVI.67.2.876-885.1993
PMCID: PMC237441

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Intragenic complementation of herpes simplex virus ICP8 DNA-binding protein mutants.PMID 8380469Read ↗

Amino acid substitution mutations in the herpes simplex virus ICP27 protein define an essential gene regulation function.Semantic proximity Read ↗

Intracellular localization of the herpes simplex virus type 1 major transcriptional regulatory protein, ICP4, is affected by ICP27.Semantic proximity Read ↗

Overexpression of the herpes simplex virus type 1 immediate-early regulatory protein, ICP27, is responsible for the aberrant localization of ICP0 and mutant forms of ICP4 in ICP4 mutant virus-infected cells.Semantic proximity Read ↗

Mapping of functional regions in the amino-terminal portion of the herpes simplex virus ICP27 regulatory protein: importance of the leucine-rich nuclear export signal and RGG Box RNA-binding domain.Semantic proximity Read ↗

Simian virus 40 Vp1 DNA-binding domain is functionally separable from the overlapping nuclear localization signal and is required for effective virion formation and full viability.Semantic proximity Read ↗

Genetic evidence for two distinct transactivation functions of the herpes simplex virus alpha protein ICP27.Semantic proximity Read ↗

Eleven loci encoding trans-acting factors are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA replicationSemantic proximity Read ↗

Altered properties of the herpes simplex virus ICP8 DNA-binding protein in cells infected with ICP27 mutant viruses.Semantic proximity Read ↗

Open reading frames UL44, IRS1/TRS1, and UL36-38 are required for transient complementation of human cytomegalovirus oriLyt-dependent DNA synthesisSemantic proximity Read ↗

Potential role for herpes simplex virus ICP8 DNA replication protein in stimulation of late gene expression.Semantic proximity Read ↗

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

The conserved carboxyl-terminal half of herpes simplex virus type 1 regulatory protein ICP27 is dispensable for viral growth in the presence of compensatory mutations.Semantic proximity Read ↗

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