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

Structure and Assembly of a T =1 Virus-Like Particle in BK Polyomavirus

12 Apr 2005

Abstract excerpt

In polyomaviruses the pentameric capsomers are interlinked by the long C-terminal arm of the structural protein VP1. The T=7 icosahedral structure of these viruses is possible due to an intriguing adaptability of this linker arm to the different local environments in the capsid. To explore the assembly process, we have compared the structure of two virus-like particles (VLPs) formed, as we found, in a...

Read the complete abstract on PubMed

Topics

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

Share to Bacteriophages and microbial interactions
Share to Parvovirus B19 Infection Studies
Share to Polyomavirus and related diseases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15827148
DOI: 10.1128/jvi.79.9.5337-5345.2005

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure and Assembly of a T =1 Virus-Like Particle in BK PolyomavirusPMID 15827148Read ↗

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

New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron MicroscopySemantic proximity Read ↗

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

Cryo-EM structure of the bacteriophage T4 isometric head at 3.3-Å resolution and its relevance to the assembly of icosahedral viruses.Semantic proximity Read ↗

Three-dimensional structure of vaccinia virus-produced human papillomavirus type 1 capsidsSemantic proximity Read ↗

Seeing the Herpesvirus Capsid at 8.5 ÅSemantic proximity Read ↗

Structural and functional similarities between the capsid proteins of bacteriophages T4 and HK97 point to a common ancestry.Semantic proximity Read ↗

Identification of a conserved virion-stabilizing network inside the interprotomer pocket of enterovirusesSemantic proximity Read ↗

Visualization of a missing link in retrovirus capsid assembly.Semantic proximity Read ↗

CryoEM and mutagenesis reveal that the smallest capsid protein cements and stabilizes Kaposi's sarcoma-associated herpesvirus capsidSemantic proximity Read ↗

The 2.6-Angstrom Structure of Infectious Bursal Disease Virus-Derived T=1 Particles Reveals New Stabilizing Elements of the Virus CapsidSemantic proximity Read ↗

Critical Residues Involved in the Coassembly of L1 and L2 Capsid Proteins of Human Papillomavirus 16.Semantic proximity Read ↗

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