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Article

The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virus

23 Mar 2004

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 15063123
DOI: 10.1016/j.virol.2004.01.025

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The C-terminal domain of the pVP2 precursor is essential for the interaction between VP2 and VP3, the capsid polypeptides of infectious bursal disease virusPMID 15063123Read ↗

The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2.Semantic proximity Read ↗

Structure of the aminoterminal domain of the birnaviral multifunctional VP3 protein and its unexplored critical roleSemantic proximity Read ↗

Infectious Bursal Disease Virus Capsid Protein VP3 Interacts both with VP1, the RNA-Dependent RNA Polymerase, and with Viral Double-Stranded RNASemantic proximity Read ↗

Electrostatic interactions between capsid and scaffolding proteins mediate the structural polymorphism of a double-stranded RNA virus.Semantic proximity Read ↗

The Maturation Process of pVP2 Requires Assembly of Infectious Bursal Disease Virus CapsidsSemantic proximity Read ↗

Crystal structure of infectious bursal disease virus VP2 subviral particle at 2.6 Å resolution: Implications in virion assembly and immunogenicitySemantic proximity Read ↗

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Roles of the PVM M2-1, M2-2 and P gene ORF 2 (P-2) proteins in viral replicationSemantic proximity Read ↗

C Terminus of Infectious Bursal Disease Virus Major Capsid Protein VP2 Is Involved in Definition of the T Number for Capsid AssemblySemantic proximity Read ↗

Identification of crucial residues of conformational epitopes on VP2 protein of infectious bursal disease virus by phage display.Semantic proximity Read ↗

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