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

Deletion Analysis Defines a Carboxyl-Proximal Region of Sendai Virus P Protein That Binds to the Polymerase L Protein

1 Jul 1994

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophages and microbial interactions
Share to Viral Infections and Vectors
Share to Virology and Viral Diseases

Source

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

Identifiers

PMID: 8009828
DOI: 10.1006/viro.1994.1331

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

Deletion Analysis Defines a Carboxyl-Proximal Region of Sendai Virus P Protein That Binds to the Polymerase L ProteinPMID 8009828Read ↗

Reexamination of the Sendai Virus P Protein Domains Required for RNA Synthesis: A Possible Supplemental Role for the P ProteinSemantic proximity Read ↗

An Amino-Proximal Domain of the L Protein Binds to the P Protein in the Measles Virus RNA Polymerase ComplexSemantic proximity Read ↗

Mutations in conserved domain I of the Sendai virus L polymerase protein uncouple transcription and replication.Semantic proximity Read ↗

An Acidic Activation-like Domain of the Sendai Virus P Protein Is Required for RNA Synthesis and EncapsidationSemantic proximity Read ↗

The L-L oligomerization domain resides at the very N-terminus of the sendai virus L RNA polymerase protein.Semantic proximity Read ↗

Different substitutions at conserved amino acids in domains II and III in the Sendai L RNA polymerase protein inactivate viral RNA synthesis.Semantic proximity Read ↗

A Highly Conserved Region of the Sendai Virus Nucleocapsid Protein Contributes to the NP–NP Binding DomainSemantic proximity Read ↗

Mutations in conserved domain II of the large (L) subunit of the Sendai virus RNA polymerase abolish RNA synthesis.Semantic proximity Read ↗

Functional Characterisation of the Genomic and Antigenomic Promoters of Sendai VirusSemantic proximity Read ↗

Mutations in conserved domains IV and VI of the large (L) subunit of the sendai virus RNA polymerase give a spectrum of defective RNA synthesis phenotypes.Semantic proximity Read ↗

An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replicationSemantic proximity Read ↗

Complexes of Sendai virus NP-P and P-L proteins are required for defective interfering particle genome replication in vitroSemantic proximity Read ↗

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