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

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.

Archives of virology - 1 Sept 2006

Gedvilaite A, Aleksaite E, Staniulis J, Ulrich R, Sasnauskas K

Abstract excerpt

The hamster polyomavirus major capsid protein VP1 was modified in its carboxy-terminal region by consecutive truncations and single amino acid exchanges. The ability of yeast-expressed VP1 variants to form virus-like particles (VLPs) strongly depended on the size and position of the truncation. VP1 variants lacking 21, 69, and 79 amino acid (aa) residues in their carboxy-terminal region efficiently formed VLPs...

Read the complete abstract on PubMed

Topics

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

Share to Capsid Proteins
Share to Codon, Nonsense

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

Share to Electrophoresis, Polyacrylamide Gel

Share to Microscopy, Electron, Transmission

Share to Polyomavirus

Share to Recombinant Proteins

Share to Sequence Deletion

Share to Virus Assembly

Source

Identifiers

PMID: 16575481
DOI: 10.1007/s00705-006-0745-8

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

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.PMID 16575481Read ↗

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

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

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

Optimized production strategy of the major capsid protein HPV 16L1 non-assembly variant in E. coliSemantic proximity Read ↗

Poliovirus capsid proteins derived from P1 precursors with glutamine-valine cleavage sites have defects in assembly and RNA encapsidation.Semantic proximity Read ↗

N-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitroSemantic proximity Read ↗

Production of recombinant VP1-derived virus-like particles from novel human polyomaviruses in yeastSemantic proximity Read ↗

Expression and antigenic characterization of the major capsid proteins of human polyomaviruses BK and JC in Saccharomyces cerevisiaeSemantic proximity Read ↗

Comparative Molecular Biology Approaches for the Production of Poliovirus Virus-Like Particles Using Pichia pastorisSemantic proximity Read ↗

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

Purification of Virus-like Particles of Recombinant Human Papillomavirus Type 11 Major Capsid Protein L1 from Saccharomyces cerevisiaeSemantic proximity Read ↗

Functional requirements of the yellow fever virus capsid protein.Semantic proximity Read ↗

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