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

Sequence comparison between the phosphoprotein mRNAs of human and bovine respiratory syncytial viruses identifies a divergent domain in the predicted protein.

The Journal of general virology - 1 Sept 1992

Mallipeddi S K, Samal S K

Abstract excerpt

The nucleotide and deduced amino acid sequences of the phosphoprotein (P) mRNA of bovine respiratory syncytial virus (BRSV) strain A51908 have been determined. The P mRNA is 860 nucleotides long with a single large open reading frame and the encoded polypeptide is 241 amino acids long. Comparison with the corresponding sequences of human respiratory syncytial virus (HRSV) subgroups A and B revealed 72 to 74%...

Topics

Amino Acid Sequence
Animals
Antigens, Viral
Base Sequence
Cattle
Genetic Variation
HN Protein
Humans
Molecular Sequence Data
Phosphoproteins
RNA, Messenger

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Respiratory Syncytial Viruses

Sequence Homology, Nucleic Acid

Viral Envelope Proteins

Viral Proteins

Source

Identifiers

PMID: 1402819
DOI: 10.1099/0022-1317-73-9-2441

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1402819-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Sequence comparison between the phosphoprotein mRNAs of human and bovine respiratory syncytial viruses identifies a divergent domain in the predicted protein.PMID 1402819Read ↗

New Insights into Structural Disorder in Human Respiratory Syncytial Virus Phosphoprotein and Implications for Binding of Protein PartnersSemantic proximity Read ↗

Sequence analysis of the phosphoprotein gene of peste des petits ruminants (PPR) virus: editing of the gene transcriptSemantic proximity Read ↗

The bulk of the phosphorylation of human respiratory syncytial virus phosphoprotein is not essential but modulates viral RNA transcription and replicationSemantic proximity Read ↗

Mapping the domains on the phosphoprotein of bovine respiratory syncytial virus required for N–P and P–L interactions using a minigenome systemSemantic proximity Read ↗

Characterization of BoHV-4 ORF45Semantic proximity Read ↗

Interactions between the Nucleoprotein and the Phosphoprotein of Pneumoviruses: Structural Insight for Rational Design of AntiviralsSemantic proximity Read ↗

Structural phosphoprotein M2-1 of the human respiratory syncytial virus is an RNA binding protein.Semantic proximity Read ↗

A short leucine-rich sequence in the Borna disease virus p10 protein mediates association with the viral phospho- and nucleoproteinsSemantic proximity Read ↗

A small highly basic protein is encoded in overlapping frame within the P gene of vesicular stomatitis virusSemantic proximity Read ↗

Complete nucleotide sequence of the phosphoprotein of the Yamagata-1 strain of a defective subacute sclerosing panencephalitis (SSPE) virus.Semantic proximity Read ↗

Serine 105 and 120 are important phosphorylation sites for porcine reproductive and respiratory syndrome virus N protein function.Semantic proximity Read ↗

Tetrameric coiled coil domain of Sendai virus phosphoprotein.Semantic proximity Read ↗

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