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

Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication.

Journal of virology - 1 Dec 2010

Nakayama Sanae, Murata Takayuki, Yasui Yoshihiro, Murayama Kazutaka, Isomura Hiroki, Kanda Teru, Tsurumi Tatsuya

Abstract excerpt

The Epstein-Barr virus BMRF1 DNA polymerase processivity factor, which is essential for viral genome replication, exists mainly as a C-shaped head-to-head homodimer but partly forms a ring-shaped tetramer through tail-to-tail association. Based on its molecular structure, several BMRF1 mutant vir...

Read the complete abstract on PubMed

Topics

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

Share to Antigens, Viral
Share to Cell Nucleus
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Antibody Technique

Share to Herpesvirus 4, Human

Share to Kidney

Share to Protein Multimerization

Share to Virus Replication

Source

Open in PubMed Open full text

Identifiers

PMID: 20926567
DOI: 10.1128/JVI.01394-10
PMCID: PMC3004297

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20926567-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication.PMID 20926567Read ↗

Crystal structure of epstein-barr virus DNA polymerase processivity factor BMRF1.Semantic proximity Read ↗

Architecture of Replication Compartments Formed during Epstein-Barr Virus Lytic ReplicationSemantic proximity Read ↗

Bromovirus RNA Replication Compartment Formation Requires Concerted Action of 1a's Self-Interacting RNA Capping and Helicase DomainsSemantic proximity Read ↗

Mutations of amino acids in the DNA-recognition domain of Epstein-Barr virus ZEBRA protein alter its sub-nuclear localization and affect formation of replication compartments.Semantic proximity Read ↗

'PIPs' in DNA polymerase: PCNA interaction affairs.Semantic proximity Read ↗

Kaposi's sarcoma-associated herpesvirus processivity factor-8 dimerizes in cytoplasm before being translocated to nucleus.Semantic proximity Read ↗

Hepatitis B virus polymerase restricts LINE-1 retrotranspositionSemantic proximity Read ↗

Activation of TRAF5 and TRAF6 signal cascades negatively regulates the latent replication origin of Epstein-Barr virus through p38 mitogen-activated protein kinase.Semantic proximity Read ↗

Characterization of the DNA-binding site repertoire for the Epstein - Barr virus transcription factor RSemantic proximity Read ↗

Stabilization of the EBNA1 protein on the Epstein-Barr virus latent origin of DNA replication by a DNA looping mechanism.Semantic proximity Read ↗

Ectromelia virus RING finger protein is localized in virus factories and is required for virus replication in macrophagesSemantic proximity Read ↗

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