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

Trimethylation of Histone H3 Lysine 4 by Set1 in the Lytic Infection of Human Herpes Simplex Virus 1

26 May 2006

Abstract excerpt

Human herpes simplex virus 1 (HSV-1) is a double-stranded DNA virus that causes facial, ocular, and encephalitic disease in humans. Previous work showed that the genome of HSV-1 is associated with acetylated and methylated histones during lytic infection. However, the physiological role of histone modifications in lytic infection of HSV-1 is unclear. We examined the role of protein methylation in lytic infection...

Read the complete abstract on PubMed

Topics

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

Share to Herpesvirus Infections and Treatments
Share to HIV Research and Treatment
Share to Viral-associated cancers and disorders

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 16731913
DOI: 10.1128/jvi.00169-06

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Trimethylation of Histone H3 Lysine 4 by Set1 in the Lytic Infection of Human Herpes Simplex Virus 1PMID 16731913Read ↗

Epigenetically repressing human cytomegalovirus lytic infection and reactivation from latency in THP-1 model by targeting H3K9 and H3K27 histone demethylasesSemantic proximity Read ↗

A Novel Selective LSD1/KDM1A Inhibitor Epigenetically Blocks Herpes Simplex Virus Lytic Replication and Reactivation from LatencySemantic proximity Read ↗

Inhibition of the histone demethylase LSD1 blocks alpha-herpesvirus lytic replication and reactivation from latency.Semantic proximity Read ↗

Targeting the JMJD2 Histone Demethylases to Epigenetically Control Herpesvirus Infection and Reactivation from LatencySemantic proximity Read ↗

Targeting m6A modification inhibits herpes virus 1 infectionSemantic proximity Read ↗

Deletion of Herpes Simplex Virus 1 MicroRNAs miR-H1 and miR-H6 Impairs ReactivationSemantic proximity Read ↗

DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV‐1 infectionSemantic proximity Read ↗

Host Methyltransferases and Demethylases: Potential New Epigenetic Targets for HIV Cure Strategies and BeyondSemantic proximity Read ↗

Mutational inactivation of herpes simplex virus 1 microRNAs identifies viral mRNA targets and reveals phenotypic effects in culture.Semantic proximity Read ↗

Herpesviral ICP0 Protein Promotes Two Waves of Heterochromatin Removal on an Early Viral Promoter during Lytic InfectionSemantic proximity Read ↗

Inhibition of LSD1 reduces herpesvirus infection, shedding, and recurrence by promoting epigenetic suppression of viral genomes.Semantic proximity Read ↗

Single-genome analysis reveals heterogeneous association of the Herpes Simplex Virus genome with H3K27me2 and the reader PHF20L1 following infection of human fibroblastsSemantic proximity Read ↗

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