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Article

Evaluation of colocalization interactions between the IE110, IE175, and IE63 transactivator proteins of herpes simplex virus within subcellular punctate structures.

Journal of virology - 1 Jan 1995

Mullen M A, Gerstberger S, Ciufo D M, Mosca J D, Hayward G S

Abstract excerpt

A number of previous studies have implied that three herpes simplex virus-encoded nuclear transactivator proteins, IE175 (ICP4), IE110 (ICP0), and IE63 (ICP27), may cooperate in transcriptional and posttranscriptional stimulation of viral gene expression. Using double-label immunofluorescence assays (IFA) in transient expression assays, we have examined the intracellular localization of these three proteins in...

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Source

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Identifiers

PMID: 7983744
DOI: 10.1128/JVI.69.1.476-491.1995
PMCID: PMC188596

Genes

PML

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.

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Evaluation of colocalization interactions between the IE110, IE175, and IE63 transactivator proteins of herpes simplex virus within subcellular punctate structures.PMID 7983744Read ↗

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Structural and Functional Heterogeneity of Nuclear BodiesSemantic proximity Read ↗

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Translocation and colocalization of ICP4 and ICP0 in cells infected with herpes simplex virus 1 mutants lacking glycoprotein E, glycoprotein I, or the virion host shutoff product of the UL41 gene.Semantic proximity Read ↗

Viral Immediate-Early Proteins Abrogate the Modification by SUMO-1 of PML and Sp100 Proteins, Correlating with Nuclear Body DisruptionSemantic proximity Read ↗

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