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

Identification of viral membrane proteins required for cell fusion and viral dissemination that are modified during vaccinia virus persistence.

Virology - 1 Jan 1994

Ortiz M A, Paez E

Abstract excerpt

Wild-type vaccinia virus WR strain forms non-fusogenic (F-) large plaques and is hemagglutinin positive (HA+) under normal conditions of virus infection. We have analyzed a collection of spontaneous, highly attenuated mutants of vaccinia virus isolated from persistently infected Friend erythroleukemia cells (E. Paez, S. Dallo, and M. Esteban, J. Virol. 61, 2642-2647, 1987) for the ability to express HA during...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Molecular Sequence Data

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

Share to Mutation

Share to Recombination, Genetic

Share to Restriction Mapping

Share to Sequence Deletion

Share to Tumor Cells, Cultured

Source

Identifiers

PMID: 8259650
DOI: 10.1006/viro.1994.1018

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

Identification of viral membrane proteins required for cell fusion and viral dissemination that are modified during vaccinia virus persistence.PMID 8259650Read ↗

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.Semantic proximity Read ↗

Mutations in the vaccinia virus A33R and B5R envelope proteins that enhance release of extracellular virions and eliminate formation of actin-containing microvilli without preventing tyrosine phosphorylation of the A36R protein.Semantic proximity Read ↗

Cooperation between different RNA virus genomes produces a new phenotype.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 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 ↗

Functional Analysis of Recombinant Respiratory Syncytial Virus Deletion Mutants Lacking the Small Hydrophobic and/or Attachment Glycoprotein GeneSemantic proximity Read ↗

Rapid selection in modified BHK-21 cells of a foot-and-mouth disease virus variant showing alterations in cell tropism.Semantic proximity Read ↗

The nature of naturally occurring mutations in the hemagglutinin gene of vaccinia virus and the sequence of immediately adjacent genes.Semantic proximity Read ↗

Vaccinia virus glycoprotein A34R is required for infectivity of extracellular enveloped virus.Semantic proximity Read ↗

Introduction of the six major genomic deletions of modified vaccinia virus Ankara (MVA) into the parental vaccinia virus is not sufficient to reproduce an MVA-like phenotype in cell culture and in mice.Semantic proximity Read ↗

Phenotypic mixing with recombinant haemagglutinin of high cleavability mediates multi-cycle replication of human influenza virus in cell culture.Semantic proximity Read ↗

Genes A27L and F13L as Genetic Markers for the Isolation of Recombinant Vaccinia Virus.Semantic proximity Read ↗

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