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

A P22 scaffold protein mutation increases the robustness of head assembly in the presence of excess portal protein.

Journal of virology - 1 Oct 2002

Moore Sean D, Prevelige Peter E

Abstract excerpt

Bacteriophage with linear, double-stranded DNA genomes package DNA into preassembled protein shells called procapsids. Located at one vertex in the procapsid is a portal complex composed of a ring of 12 subunits of portal protein. The portal complex serves as a docking site for the DNA packaging enzymes, a conduit for the passage of DNA, and a binding site for the phage tail. An excess of the P22 portal protein...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophage P22
Share to Capsid
Share to Glutamic Acid

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

Share to Glycine

Share to Protein Precursors

Share to Viral Structural Proteins

Share to Virion

Share to Virus Assembly

Source

Open in PubMed Open full text

Identifiers

PMID: 12239300
DOI: 10.1128/jvi.76.20.10245-10255.2002
PMCID: PMC136566

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

A P22 scaffold protein mutation increases the robustness of head assembly in the presence of excess portal protein.PMID 12239300Read ↗

Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation.Semantic proximity Read ↗

Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly.Semantic proximity Read ↗

Bacteriophage p22 portal vertex formation in vivo.Semantic proximity Read ↗

Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA.Semantic proximity Read ↗

Peering down the barrel of a bacteriophage portal: the genome packaging and release valve in p22.Semantic proximity Read ↗

Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.Semantic proximity Read ↗

Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype.Semantic proximity Read ↗

Identification of additional coat-scaffolding interactions in a bacteriophage P22 mutant defective in maturation.Semantic proximity Read ↗

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

Effects of an early conformational switch defect during ϕX174 morphogenesis are belatedly manifested late in the assembly pathway.Semantic proximity Read ↗

Fine structure genetic and physical map of the gene 3 to 10 region of the bacteriophage P22 chromosome.Semantic proximity Read ↗

Intragenic suppression of a capsid assembly-defective P22 tailspike mutation.Semantic proximity Read ↗

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