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

Site-directed mutation affecting polyomavirus capsid self-assembly in vitro.

Nature - 1 Jan 2000

Garcea R L, Salunke D M, Caspar D L

Abstract excerpt

Nonequivalent bonding of identical protein subunits occurs in the polyomavirus capsid were identical pentameric capsomeres occupy both hexavalent and pentavalent positions in the icosahedral surface lattice. The polyomavirus major capsid protein VP1, purified after expression of the recombinant gene in Escherichia coli, has been isolated as capsomeres that self-assemble into capsid-like structures in vitro. The...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Capsid

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

Share to Escherichia coli

Share to Macromolecular Substances

Share to Microscopy, Electron

Share to Mutation

Share to Protein Processing, Post-Translational

Source

Identifiers

PMID: 3041229
DOI: 10.1038/329086a0

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

Site-directed mutation affecting polyomavirus capsid self-assembly in vitro.PMID 3041229Read ↗

DNA-Induced Structural Changes in the Papillomavirus CapsidSemantic proximity Read ↗

Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.Semantic proximity Read ↗

Mutational analysis of human papillomavirus type 16 major capsid protein L1: the cysteines affecting the intermolecular bonding and structure of L1-capsids.Semantic proximity Read ↗

Mutational analysis of the carboxyl-terminal region of the SV40 major capsid protein VP1.Semantic proximity Read ↗

The Assembly-Activating Protein Promotes Stability and Interactions between AAV's Viral Proteins to Nucleate Capsid Assembly.Semantic proximity Read ↗

Structure-based engineering of papillomavirus major capsid l1: controlling particle assembly.Semantic proximity Read ↗

The cauliflower mosaic virus capsid protein: assembly and nucleic acid binding in vitro.Semantic proximity Read ↗

A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly.Semantic proximity Read ↗

Cysteine residues in the major capsid protein, Vp1, of the JC virus are important for protein stability and oligomer formation.Semantic proximity Read ↗

Size and position of truncations in the carboxy-terminal region of major capsid protein VP1 of hamster polyomavirus expressed in yeast determine its assembly capacity.Semantic proximity Read ↗

Mutant canine oral papillomavirus L1 capsid proteins which form virus-like particles but lack native conformational epitopes.Semantic proximity Read ↗

Regions of the herpes simplex virus scaffolding protein that are important for intermolecular self-interaction.Semantic proximity Read ↗

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