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

Structure-function analysis of the Sendai virus F and HN cytoplasmic domain: different role for the two proteins in the production of virus particle.

Virology - 10 May 2000

Fouillot-Coriou N, Roux L

Abstract excerpt

The role of the cytoplasmic domain (cytd) of the Sendai virus HN and F glycoproteins in the process of virus assembly and budding are evaluated. Recombinant Sendai virus (rSeV) mutants are generated carrying modifications in the cytd of each of the glycoprotein separately. The modifications include increasing truncations and/or amino acid sequence substitutions. Following steady-state (35)[S]methionine/cysteine...

Read the complete abstract on PubMed

Topics

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

Share to Glycoproteins
Share to HeLa Cells
Share to HN Protein

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

Share to Respirovirus

Share to Sequence Alignment

Share to Structure-Activity Relationship

Share to Viral Fusion Proteins

Share to Virion

Source

Identifiers

PMID: 10793005
DOI: 10.1006/viro.2000.0291

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

Structure-function analysis of the Sendai virus F and HN cytoplasmic domain: different role for the two proteins in the production of virus particle.PMID 10793005Read ↗

Mutation of the TYTLE motif in the cytoplasmic tail of the sendai virus fusion protein deeply affects viral assembly and particle production.Semantic proximity Read ↗

The respiratory syncytial virus fusion protein targets to the perimeter of inclusion bodies and facilitates filament formation by a cytoplasmic tail-dependent mechanism.Semantic proximity Read ↗

Importance of the cysteine-rich carboxyl-terminal half of V protein for Sendai virus pathogenesisSemantic proximity Read ↗

Nontransmissible virus-like particle formation by F-deficient sendai virus is temperature sensitive and reduced by mutations in M and HN proteins.Semantic proximity Read ↗

Assembly-defective point mutants of the human immunodeficiency virus type 1 Gag precursor phenotypically expressed in recombinant baculovirus-infected cells.Semantic proximity Read ↗

Alteration of Sendai virus morphogenesis and nucleocapsid incorporation due to mutation of cysteine residues of the matrix protein.Semantic proximity Read ↗

Important Role for the Transmembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Protein during EntrySemantic proximity Read ↗

Role of the Transmembrane Domains of prM and E Proteins in the Formation of Yellow Fever Virus EnvelopeSemantic proximity Read ↗

Characterization of Sendai virus M protein mutants that can partially interfere with virus particle production.Semantic proximity Read ↗

Site-directed mutations in Sindbis virus E2 glycoprotein's cytoplasmic domain and the 6K protein lead to similar defects in virus assembly and budding.Semantic proximity Read ↗

Sendai virus M protein binds independently to either the F or the HN glycoprotein in vivoSemantic proximity Read ↗

Mutations in the Cytoplasmic Domain of the Newcastle Disease Virus Fusion Protein Confer Hyperfusogenic Phenotypes Modulating Viral Replication and PathogenicitySemantic proximity Read ↗

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