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Article

Sequences related to SUMO interaction motifs in herpes simplex virus 1 protein ICP0 act cooperatively to stimulate virus infection.

Journal of virology - 1 Mar 2014

Everett Roger D, Boutell Chris, Pheasant Kathleen, Cuchet-Lourenço Delphine, Orr Anne

Abstract excerpt

UNLABELLED: Herpes simplex virus type 1 immediate-early protein ICP0 is an E3 ubiquitin ligase of the RING finger class that degrades several cellular proteins during infection. This activity is essential for its functions in stimulating efficient lytic infection and productive reactivation from latency. ICP0 targets a number of proteins that are modified by the small ubiquitin-like SUMO family of proteins, and...

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Share to Herpesvirus 1, Human
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Promyelocytic Leukemia Protein

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Source

Open in PubMed Open full text

Identifiers

PMID: 24352468
DOI: 10.1128/JVI.03417-13
PMCID: PMC3958091

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.

Related research

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Research trail→

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Sequences related to SUMO interaction motifs in herpes simplex virus 1 protein ICP0 act cooperatively to stimulate virus infection.PMID 24352468Read ↗

Effect of SUMO-SIM Interaction on the ICP0-Mediated Degradation of PML Isoform II and Its Associated Proteins in Herpes Simplex Virus 1 Infection.Semantic proximity Read ↗

Alphaherpesvirus Proteins Related to Herpes Simplex Virus Type 1 ICP0 Affect Cellular Structures and ProteinsSemantic proximity Read ↗

Identification of TRIM27 as a Novel Degradation Target of Herpes Simplex Virus 1 ICP0Semantic proximity Read ↗

Novel Role for Protein Inhibitor of Activated STAT 4 (PIAS4) in the Restriction of Herpes Simplex Virus 1 by the Cellular Intrinsic Antiviral Immune Response.Semantic proximity Read ↗

Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro.Semantic proximity Read ↗

A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7.Semantic proximity Read ↗

ICP0 induces the accumulation of colocalizing conjugated ubiquitin.Semantic proximity Read ↗

The Viral SUMO–Targeted Ubiquitin Ligase ICP0 is Phosphorylated and Activated by Host Kinase Chk2Semantic proximity Read ↗

The Herpes Simplex Virus ICP0 RING Finger Domain Inhibits IRF3- and IRF7-Mediated Activation of Interferon-Stimulated GenesSemantic proximity Read ↗

Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23Semantic proximity Read ↗

Interactome and Ubiquitinome Analyses Identify Functional Targets of Herpes Simplex Virus 1 Infected Cell Protein 0Semantic proximity Read ↗

Herpes simplex virus 1 alpha regulatory protein ICP0 functionally interacts with cellular transcription factor BMAL1Semantic proximity Read ↗

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