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

Mutations Near the N Terminus of Vaccinia Virus G9 Protein Overcome Restrictions on Cell Entry and Syncytium Formation Imposed by the A56/K2 Fusion Regulatory Complex.

Journal of virology - 4 May 2020

Cotter Catherine A, Moss Bernard

Abstract excerpt

The entry/fusion complex (EFC) consists of 11 conserved proteins embedded in the membrane envelope of mature poxvirus particles. Poxviruses also encode proteins that localize in cell membranes and negatively regulate superinfection and syncytium formation. The vaccinia virus (VACV) A56/K2 fusion regulatory complex associates with the G9/A16 EFC subcomplex, but functional support for the importance of this...

Read the complete abstract on PubMed

Topics

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

Share to Giant Cells
Share to Host-Pathogen Interactions

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

Share to Membrane Fusion

Share to Protein Interaction Domains and Motifs

Share to Vaccinia virus

Share to Viral Proteins

Share to Viral Regulatory and Accessory Proteins

Share to Virus Internalization

Source

Open in PubMed Open full text

Identifiers

PMID: 32132239
DOI: 10.1128/JVI.00077-20
PMCID: PMC7199393

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

Mutations Near the N Terminus of Vaccinia Virus G9 Protein Overcome Restrictions on Cell Entry and Syncytium Formation Imposed by the A56/K2 Fusion Regulatory Complex.PMID 32132239Read ↗

Structural dissection of vaccinia G9 identifies residues essential for membrane fusion and complex assembly.Semantic proximity Read ↗

Experimental Evolution To Isolate Vaccinia Virus Adaptive G9 Mutants That Overcome Membrane Fusion Inhibition via the Vaccinia Virus A56/K2 Protein Complex.Semantic proximity Read ↗

Vaccinia virus A56/K2 fusion regulatory protein interacts with the A16 and G9 subunits of the entry fusion complex.Semantic proximity Read ↗

Vaccinia Virus A6 Is a Two-Domain Protein Requiring a Cognate N-Terminal Domain for Full Viral Membrane Assembly Activity.Semantic proximity Read ↗

Structure-Function Analysis of Two Interacting Vaccinia Proteins That Are Critical for Viral Morphogenesis: L2 and A30.5.Semantic proximity Read ↗

The vaccinia virus A56 protein: a multifunctional transmembrane glycoprotein that anchors two secreted viral proteinsSemantic proximity Read ↗

Identification of β2 microglobulin, the product of B2M gene, as a Host Factor for Vaccinia Virus Infection by Genome-Wide CRISPR genetic screensSemantic proximity Read ↗

A genome-wide haploid genetic screen for essential factors in vaccinia virus infection identifies TMED10 as regulator of macropinocytosisSemantic proximity Read ↗

A Conserved Tripeptide Sequence at the C Terminus of the Poxvirus DNA Processivity Factor D4 Is Essential for Protein Integrity and Function.Semantic proximity Read ↗

Structural Insights into the Impact of the M142I Mutation in Monkeypox Virus G9 Protein on Subcomplex Formation Revealed by AlphaFold 3 Modeling.Semantic proximity Read ↗

Vaccinia virus induces cell fusion at acid pH and this activity is mediated by the N-terminus of the 14-kDa virus envelope protein.Semantic proximity Read ↗

Enigmatic origin of the poxvirus membrane from the endoplasmic reticulum shown by 3D imaging of vaccinia virus assembly mutants.Semantic proximity Read ↗

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