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

Interaction of human cytomegalovirus pUL84 with casein kinase 2 is required for oriLyt-dependent DNA replication.

Journal of virology - 1 Mar 2009

Gao Yang, Pari Gregory S

Abstract excerpt

Human cytomegalovirus pUL84 is a phosphorylated protein that is required for lytic DNA replication and participates in regulation of virus gene expression. We previously used a proteomics assay to show that human cytomegalovirus pUL84 interacts with casein kinase 2 (CK2). We now have demonstrated that pUL84 is a substrate for CK2 in vitro, and we have determined that two putative CK2 phosphorylation sites within...

Read the complete abstract on PubMed

Topics

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

Share to Casein Kinase II
Share to Cytomegalovirus
Share to DNA Replication

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

Share to Gene Expression Regulation, Viral

Share to Open Reading Frames

Share to Phosphorylation

Share to Viral Proteins

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 19091862
DOI: 10.1128/JVI.02339-08
PMCID: PMC2643710

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 · 12 closest

Interaction of human cytomegalovirus pUL84 with casein kinase 2 is required for oriLyt-dependent DNA replication.PMID 19091862Read ↗

Role of the Specific Interaction of UL112-113 p84 with UL44 DNA Polymerase Processivity Factor in Promoting DNA Replication of Human CytomegalovirusSemantic proximity Read ↗

Human cytomegalovirus UL84 oligomerization and heterodimerization domains act as transdominant inhibitors of oriLyt-dependent DNA replication: evidence that IE2-UL84 and UL84-UL84 interactions are required for lytic DNA replication.Semantic proximity Read ↗

A mutation deleting sequences encoding the amino terminus of human cytomegalovirus UL84 impairs interaction with UL44 and capsid localization.Semantic proximity Read ↗

Characteristics of Immediate-Early 2 (IE2) and UL84 Proteins in UL84-Independent Strains of Human Cytomegalovirus (HCMV).Semantic proximity Read ↗

Human Cytomegalovirus pUL79 Is an Elongation Factor of RNA Polymerase II for Viral Gene TranscriptionSemantic proximity Read ↗

The protein kinase pUL97 of human cytomegalovirus interacts with and phosphorylates the DNA polymerase processivity factor pUL44.Semantic proximity Read ↗

Identification and Functional Characterization of Phosphorylation Sites of the Human Papillomavirus 31 E8^E2 Protein.Semantic proximity Read ↗

Phosphorylation by CK2 increases the SUMO-dependent activity of Cytomegalovirus transactivator IE2Semantic proximity Read ↗

A protein kinase CK2 site flanking the nuclear targeting signal enhances nuclear transport of human cytomegalovirus ppUL44.Semantic proximity Read ↗

Functional and structural insights into HCMV terminase accessory proteins pUL77 and pUL93.Semantic proximity Read ↗

Amino acids of conserved kinase motifs of cytomegalovirus protein UL97 are essential for autophosphorylation.Semantic proximity Read ↗

The Flexible Loop of the Human Cytomegalovirus DNA Polymerase Processivity Factor ppUL44 Is Required for Efficient DNA Binding and Replication in CellsSemantic proximity Read ↗

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