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
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Different domains of the RNA polymerase of infectious bursal disease virus contribute to virulenceActivation mechanism of a noncanonical RNA-dependent RNA polymeraseAutoproteolytic Activity Derived from the Infectious Bursal Disease Virus Capsid ProteinElectrostatic interactions between capsid and scaffolding proteins mediate the structural polymorphism of a double-stranded RNA virusThe endosomal pathway and the Golgi complex are involved in the infectious bursal disease virus life cycle.A protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability.The C-terminal amyloidogenic peptide contributes to self-assembly of Avibirnavirus viral proteaseThe maturation process of pVP2 requires assembly of infectious bursal disease virus capsidsThe capsid of infectious bursal disease virus contains several small peptides arising from the maturation process of pVP2Structural basis for the development of avian virus capsids that display influenza virus proteins and induce protective immunity.Host proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.Rescue of infectious birnavirus from recombinant ribonucleoprotein complexesEspirito Santo virus: a new birnavirus that replicates in insect cells.C terminus of infectious bursal disease virus major capsid protein VP2 is involved in definition of the T number for capsid assemblyMolecular determinants of virulence, cell tropism, and pathogenic phenotype of infectious bursal disease virus.Intracellular interference of infectious bursal disease virus.Exchange of the C-terminal part of VP3 from very virulent infectious bursal disease virus results in an attenuated virus with a unique antigenic structure.Infectious bursal disease virus capsid protein VP3 interacts both with VP1, the RNA-dependent RNA polymerase, and with viral double-stranded RNA.Identification and molecular characterization of the RNA polymerase-binding motif of infectious bursal disease virus inner capsid protein VP3.The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.VP2 of Infectious Bursal Disease Virus Induces Apoptosis via Triggering Oral Cancer Overexpressed 1 (ORAOV1) Protein Degradation.Structural peptides of a nonenveloped virus are involved in assembly and membrane translocationThe last C-terminal residue of VP3, glutamic acid 257, controls capsid assembly of infectious bursal disease virusGenome assembly and particle maturation of the birnavirus infectious pancreatic necrosis virus.Infectious Bursal Disease Virus VP3 Upregulates VP1-Mediated RNA-Dependent RNA ReplicationThe 2.6-Angstrom structure of infectious bursal disease virus-derived T=1 particles reveals new stabilizing elements of the virus capsidMosquito and Drosophila entomobirnaviruses suppress dsRNA- and siRNA-induced RNAiViral suppressors of RNAi employ a rapid screening mode to discriminate viral RNA from cellular small RNA.VP1 and VP3 are required and sufficient for translation initiation of uncapped IBDV genomic dsRNA.Infectious Bursal Disease Virus hijacks endosomal membranes as the scaffolding structure for viral replication.The RNA-binding protein of a double-stranded RNA virus acts like a scaffold protein
P2860
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P2860
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
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
VP1, the putative RNA-dependen ...... tion into virus-like particles
@ast
VP1, the putative RNA-dependen ...... tion into virus-like particles
@en
type
label
VP1, the putative RNA-dependen ...... tion into virus-like particles
@ast
VP1, the putative RNA-dependen ...... tion into virus-like particles
@en
prefLabel
VP1, the putative RNA-dependen ...... tion into virus-like particles
@ast
VP1, the putative RNA-dependen ...... tion into virus-like particles
@en
P2093
P2860
P1433
P1476
VP1, the putative RNA-dependen ...... tion into virus-like particles
@en
P2093
A Fernández-Arias
E Lombardo
J F Rodriguez
J L Carrascosa
J R Castón
P2860
P304
P577
1999-08-01T00:00:00Z