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

Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9.

Virology - 20 Dec 2009

Fradet-Turcotte Amélie, Brault Karine, Titolo Steve, Howley Peter M, Archambault Jacques

Abstract excerpt

The E1 helicase from BPV and HPV16 interacts with Ubc9 to facilitate viral genome replication. We report that HPV11 E1 also interacts with Ubc9 in vitro and in the yeast two-hybrid system. Residues in E1 involved in oligomerization (353-435) were sufficient for binding to Ubc9 in vitro, but the o...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Organisms, Genetically Modified
Share to Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Transport

Share to Small Ubiquitin-Related Modifier Proteins

Share to Ubiquitin-Conjugating Enzyme UBC9

Share to Ubiquitin-Conjugating Enzymes

Share to Viral Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19836047
DOI: 10.1016/j.virol.2009.09.020
PMCID: PMC4654619

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19836047-2026-09-02.2. 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 · 8 closest

Characterization of papillomavirus E1 helicase mutants defective for interaction with the SUMO-conjugating enzyme Ubc9.PMID 19836047Read ↗

Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteins.Semantic proximity Read ↗

Nuclear Accumulation of the Papillomavirus E1 Helicase Blocks S-Phase Progression and Triggers an ATM-Dependent DNA Damage ResponseSemantic proximity Read ↗

Mutations in the human papillomavirus type 16 E2 protein identify multiple regions of the protein involved in binding to E1.Semantic proximity Read ↗

Characterization of amino acid residues within the N-terminal region of Ubc9 that play a role in Ubc9 nuclear localization.Semantic proximity Read ↗

Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein.Semantic proximity Read ↗

Mapping of HPV-11 E1 binding site and determination of other important cis elements for replication of the origin.Semantic proximity Read ↗

Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.Semantic proximity Read ↗

Identification of a substrate recognition site on Ubc9.Semantic proximity Read ↗

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