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

Cell-cycle-dependent EBNA1-DNA crosslinking promotes replication termination at oriP and viral episome maintenance.

Cell - 4 Feb 2021

Dheekollu Jayaraju, Wiedmer Andreas, Ayyanathan Kasirajan, Deakyne Julianna S, Messick Troy E, Lieberman Paul M

Abstract excerpt

Epstein-Barr virus (EBV) is an oncogenic human herpesvirus that persists as a multicopy episome in proliferating host cells. Episome maintenance is strictly dependent on EBNA1, a sequence-specific DNA-binding protein with no known enzymatic activities. Here, we show that EBNA1 forms a cell cycle-dependent DNA crosslink with the EBV origin of plasmid replication oriP. EBNA1 tyrosine 518 (Y518) is essential for...

Read the complete abstract on PubMed

Topics

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

Share to B-Lymphocytes
Share to Cross-Linking Reagents

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

Share to DNA Adducts

Share to DNA Replication

Share to Endonucleases

Share to Epstein-Barr Virus Nuclear Antigens

Share to Replication Origin

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 33482082
DOI: 10.1016/j.cell.2020.12.022
PMCID: PMC8186250

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

Cell-cycle-dependent EBNA1-DNA crosslinking promotes replication termination at oriP and viral episome maintenance.PMID 33482082Read ↗

Structural Basis for Cooperative Binding of EBNA1 to the Epstein-Barr Virus Dyad Symmetry Minimal Origin of ReplicationSemantic proximity Read ↗

Maintenance of Epstein–Barr virus (EBV) <i>oriP</i> -based episomes requires EBV-encoded nuclear antigen-1 chromosome-binding domains, which can be replaced by high-mobility group-I or histone H1Semantic proximity Read ↗

The Linking Regions of EBNA1 Are Essential for Its Support of Replication and TranscriptionSemantic proximity Read ↗

Identification of EBNA1 amino acid sequences required for the interaction of the functional elements of the Epstein-Barr virus latent origin of DNA replicationSemantic proximity Read ↗

The Amino Terminus of Epstein-Barr Virus (EBV) Nuclear Antigen 1 Contains AT Hooks That Facilitate the Replication and Partitioning of Latent EBV Genomes by Tethering Them to Cellular ChromosomesSemantic proximity Read ↗

Initiation of DNA replication within oriP is dispensable for stable replication of the latent Epstein-Barr virus chromosome after infection of established cell lines.Semantic proximity Read ↗

Telomere Repeat Binding Factors TRF1, TRF2, and hRAP1 Modulate Replication of Epstein-Barr Virus OriPSemantic proximity Read ↗

Regulation of EBNA1 protein stability and DNA replication activity by PLOD1 lysine hydroxylaseSemantic 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 ↗

EBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance.Semantic proximity Read ↗

The Epstein-Barr Virus Episome Maneuvers between Nuclear Chromatin Compartments during ReactivationSemantic proximity Read ↗

HCF1 and OCT2 Cooperate with EBNA1 To Enhance OriP-Dependent Transcription and Episome Maintenance of Latent Epstein-Barr VirusSemantic proximity Read ↗

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