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

Defective assembly of influenza A virus due to a mutation in the polymerase subunit PA.

Journal of virology - 1 Jan 2006

Regan John F, Liang Yuying, Parslow Tristram G

Abstract excerpt

The RNA-dependent RNA polymerase of influenza A virus is composed of three subunits that together synthesize all viral mRNAs and also replicate the viral genomic RNA segments (vRNAs) through intermediates known as cRNAs. Here we describe functional characterization of 16 site-directed mutants of one polymerase subunit, termed PA. In accord with earlier studies, these mutants exhibited diverse, mainly quantitative...

Read the complete abstract on PubMed

Topics

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

Share to Cell Line
Share to DNA-Directed RNA Polymerases
Share to Influenza A virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to RNA-Dependent RNA Polymerase

Share to RNA, Viral

Share to Viral Proteins

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 16352550
DOI: 10.1128/JVI.80.1.252-261.2006
PMCID: PMC1317532

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Defective assembly of influenza A virus due to a mutation in the polymerase subunit PA.PMID 16352550Read ↗

Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding.Semantic proximity Read ↗

Role of the PB2 627 Domain in Influenza A Virus Polymerase FunctionSemantic proximity Read ↗

Naturally occurring PAE206K point mutation in 2009 H1N1 pandemic influenza viruses impairs viral replication at high temperatures.Semantic proximity Read ↗

Disruption of the viral polymerase complex assembly as a novel approach to attenuate influenza A virus.Semantic proximity Read ↗

Threonine 157 of influenza virus PA polymerase subunit modulates RNA replication in infectious viruses.Semantic proximity Read ↗

Structure and assembly of the influenza A virus ribonucleoprotein complexSemantic proximity Read ↗

Mutational analysis of the influenza virus A/Victoria/3/75 PA protein: studies of interaction with PB1 protein and identification of a dominant negative mutant.Semantic proximity Read ↗

Mutational analysis identifies functional domains in the influenza A virus PB2 polymerase subunit.Semantic proximity Read ↗

Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation.Semantic proximity Read ↗

Mutations in the PA Protein of Avian H5N1 Influenza Viruses Affect Polymerase Activity and Mouse Virulence.Semantic proximity Read ↗

Functional Analysis of Conserved Motifs in Influenza Virus PB1 ProteinSemantic proximity Read ↗

Attenuated Strains of Influenza A Viruses Do Not Induce Degradation of RNA Polymerase IISemantic proximity Read ↗

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