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. (Q42624074)

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scientific article published on April 2004

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English	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.	scientific article published on April 2004

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scholarly article

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26 December 2019

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 (English)

1 reference

Europe PubMed Central

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26 December 2019

Infectious bursal disease virus

object named as

infectious bursal disease virus

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José R Castón

5

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26 December 2019

2

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26 December 2019

Antonio Maraver

4

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26 December 2019

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Ana Oña

1

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26 December 2019

Fernando Abaitua

3

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26 December 2019

Jose F Rodríguez

6

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26 December 2019

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1 April 2004

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26 December 2019

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3 November 2017

322

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26 December 2019

1

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26 December 2019

135-142

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26 December 2019

Assembly of the T = 4 Nudaurelia capensis omega virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Large conformational changes in the maturation of a simple RNA virus, nudaurelia capensis omega virus (NomegaV).

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assembly

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

The maturation process of pVP2 requires assembly of infectious bursal disease virus capsids

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

The capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Expression of ORF A1 of infectious bursal disease virus results in the formation of virus-like particles

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

HIV-1 gag proteins: diverse functions in the virus life cycle

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Birnavirus RNA polymerase is related to polymerases of positive strand RNA viruses

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Biochemistry and immunology of infectious bursal disease virus

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Characterization of the RNA-binding activity of VP3, a major structural protein of Infectious bursal disease virus.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

The Oligomerization Domain of VP3, the Scaffolding Protein of Infectious Bursal Disease Virus, Plays a Critical Role in Capsid Assembly

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Different architectures in the assembly of infectious bursal disease virus capsid proteins expressed in insect cells

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

The two segments of the infectious bursal disease virus genome are circularized by a 90,000-Da protein

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Co-translational folding of an alphavirus capsid protein in the cytosol of living cells

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Analysis of the capsid processing strategy of Thosea asigna virus using baculovirus expression of virus-like particles

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Interactions in vivo between the proteins of infectious bursal disease virus: capsid protein VP3 interacts with the RNA-dependent RNA polymerase, VP1.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

Homotypic interactions of the infectious bursal disease virus proteins VP3, pVP2, VP4, and VP5: mapping of the interacting domains

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

A second form of infectious bursal disease virus-associated tubule contains VP4.

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

based on heuristic

inferred from DOI database lookup

VP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particles

1 reference

https://api.crossref.org/works/10.1016%2FJ.VIROL.2004.01.025

7 January 2021

based on heuristic

inferred from DOI database lookup

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