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

Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage phi6.

Journal of virology - 1 Dec 1998

Paatero A O, Mindich L, Bamford D H

Abstract excerpt

Bacteriophage phi6 is a complex enveloped double-stranded RNA virus with a segmented genome and replication strategy quite similar to that of the Reoviridae. An in vitro packaging and replication system using purified components is available. The positive-polarity genomic segments are translocated into a preformed polymerase complex (procapsid) particle. This particle is composed of four proteins: the...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Binding Sites
Share to DNA, Viral

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

Share to Genes, Viral

Share to Microscopy, Electron

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 9811745
DOI: 10.1128/JVI.72.12.10058-10065.1998
PMCID: PMC110533

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

Mutational analysis of the role of nucleoside triphosphatase P4 in the assembly of the RNA polymerase complex of bacteriophage phi6.PMID 9811745Read ↗

Isolation and analysis of mutants of double-stranded-RNA bacteriophage phi6 with altered packaging specificity.Semantic proximity Read ↗

A structural model of the genome packaging process in a membrane-containing double stranded DNA virus.Semantic proximity Read ↗

Chemical modification patterns of active and inactive as well as procapsid-bound and unbound DNA-packaging RNAof bacterial virus Phi29.Semantic proximity Read ↗

The in vivo function of phage phi29 nucleoid-associated protein p6 requires formation of dimers.Semantic proximity Read ↗

Efficient DNA packaging of bacteriophage PRD1 requires the unique vertex protein P6.Semantic proximity Read ↗

Complete inhibition of virion assembly in vivo with mutant procapsid RNA essential for phage phi 29 DNA packaging.Semantic proximity Read ↗

The portal protein plays essential roles at different steps of the SPP1 DNA packaging process.Semantic proximity Read ↗

Boundary of pRNA functional domains and minimum pRNA sequence requirement for specific connector binding and DNA packaging of phage phi29.Semantic proximity Read ↗

Disenfranchised DNA: biochemical analysis of mutant øX174 DNA-binding proteins may further elucidate the evolutionary significance of the unessential packaging protein A.Semantic proximity Read ↗

Analysis of specific binding involved in genomic packaging of the double-stranded-RNA bacteriophage phi6.Semantic proximity Read ↗

Rotavirus core shell subdomains involved in polymerase encapsidation into virus-like particles.Semantic proximity Read ↗

Identification of an Intramolecular Switch That Controls the Interaction of Helicase nsp10 with Membrane-Associated nsp12 of Porcine Reproductive and Respiratory Syndrome Virus.Semantic proximity Read ↗

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