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

Dimerization of the Epstein-Barr virus ZEBRA protein in the yeast two-hybrid system. Comparison Of a ZEBRA variant with the B95-8 form.

Biochimie - 1 Feb 2000

Martel-Renoir D, Wesner M, Joab I

Abstract excerpt

Epstein-Barr virus (EBV) is a herpes virus associated with several human tumors. The EBV protein, ZEBRA, is a transactivator of the basic leucine zipper family (bZip). It binds to specific sequences on DNA and is able to interact with cellular proteins such as p53. The interaction of the ZEBRA protein with its cognate DNA sequences is stable as long as the dimerization domain is functional. Recent work from this...

Read the complete abstract on PubMed

Topics

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

Share to Dimerization
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fungal Proteins

Share to Herpesvirus 4, Human

Share to Leucine Zippers

Share to Trans-Activators

Share to Transcriptional Activation

Share to Viral Proteins

Source

Identifiers

PMID: 10727769
DOI: 10.1016/s0300-9084(00)00188-7

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dimerization of the Epstein-Barr virus ZEBRA protein in the yeast two-hybrid system. Comparison Of a ZEBRA variant with the B95-8 form.PMID 10727769Read ↗

The position of the ZEBRA activation domain does not influence its biological activity.Semantic proximity Read ↗

Amino acids in the basic domain of Epstein-Barr virus ZEBRA protein play distinct roles in DNA binding, activation of early lytic gene expression, and promotion of viral DNA replication.Semantic proximity Read ↗

bZIP proteins of human gammaherpesvirusesSemantic proximity Read ↗

Oncogenic Properties of the EBV ZEBRA ProteinSemantic proximity Read ↗

Phosphoacceptor site S173 in the regulatory domain of Epstein-Barr Virus ZEBRA protein is required for lytic DNA replication but not for activation of viral early genes.Semantic 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 ↗

Latency of Epstein-Barr virus is disrupted by gain-of-function mutant cellular AP-1 proteins that preferentially bind methylated DNA.Semantic proximity Read ↗

Phosphorylation of Epstein-Barr virus ZEBRA protein at its casein kinase 2 sites mediates its ability to repress activation of a viral lytic cycle late gene by Rta.Semantic proximity Read ↗

Replacing C189 in the bZIP domain of Zta with S, T, V, or A changes DNA binding specificity to four types of double-stranded DNA.Semantic proximity Read ↗

Leucine zipper domain is required for Kaposi sarcoma-associated herpesvirus (KSHV) K-bZIP protein to interact with histone deacetylase and is important for KSHV replication.Semantic proximity Read ↗

Mutant Cellular AP-1 Proteins Promote Expression of a Subset of Epstein-Barr Virus Late Genes in the Absence of Lytic Viral DNA Replication.Semantic proximity Read ↗

Characterization of the cell-penetrating properties of the Epstein-Barr virus ZEBRA trans-activator.Semantic proximity Read ↗

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