The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.
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Activation mechanism of a noncanonical RNA-dependent RNA polymeraseAutoproteolytic Activity Derived from the Infectious Bursal Disease Virus Capsid ProteinStructure of a VP1-VP3 Complex Suggests How Birnaviruses Package the VP1 PolymeraseElectrostatic interactions between capsid and scaffolding proteins mediate the structural polymorphism of a double-stranded RNA virusA protein with simultaneous capsid scaffolding and dsRNA-binding activities enhances the birnavirus capsid mechanical stability.The VP3 factor from viruses of Birnaviridae family suppresses RNA silencing by binding both long and small RNA duplexesStructural basis for the development of avian virus capsids that display influenza virus proteins and induce protective immunity.The association of receptor of activated protein kinase C 1(RACK1) with infectious bursal disease virus viral protein VP5 and voltage-dependent anion channel 2 (VDAC2) inhibits apoptosis and enhances viral replication.Avibirnavirus VP4 Protein Is a Phosphoprotein and Partially Contributes to the Cleavage of Intermediate Precursor VP4-VP3 Polyprotein.Binding of the pathogen receptor HSP90AA1 to avibirnavirus VP2 induces autophagy by inactivating the AKT-MTOR pathway.VP3, a structural protein of infectious pancreatic necrosis virus, interacts with RNA-dependent RNA polymerase VP1 and with double-stranded RNAHost proteolytic activity is necessary for infectious bursal disease virus capsid protein assembly.The infectious bursal disease virus RNA-binding VP3 polypeptide inhibits PKR-mediated apoptosisVoltage-Dependent Anion Channel 1 Interacts with Ribonucleoprotein Complexes To Enhance Infectious Bursal Disease Virus Polymerase Activity.Infectious Bursal Disease Virus Subverts Autophagic Vacuoles To Promote Viral Maturation and Release.Espirito Santo virus: a new birnavirus that replicates in insect cells.Intracellular interference of infectious bursal disease virus.Nuclear factor NF45 interacts with viral proteins of infectious bursal disease virus and inhibits viral replicationStructural 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 capsidInfectious bursal disease virus capsid assembly and maturation by structural rearrangements of a transient molecular switch.Viral suppressors of RNAi employ a rapid screening mode to discriminate viral RNA from cellular small RNA.Infectious Bursal Disease Virus hijacks endosomal membranes as the scaffolding structure for viral replication.
P2860
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P2860
The oligomerization domain of VP3, the scaffolding protein of infectious bursal disease virus, plays a critical role in capsid assembly.
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2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
@zh-my
2003年学术文章
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name
The oligomerization domain of ...... tical role in capsid assembly.
@en
The oligomerization domain of ...... tical role in capsid assembly.
@nl
type
label
The oligomerization domain of ...... tical role in capsid assembly.
@en
The oligomerization domain of ...... tical role in capsid assembly.
@nl
prefLabel
The oligomerization domain of ...... tical role in capsid assembly.
@en
The oligomerization domain of ...... tical role in capsid assembly.
@nl
P2093
P2860
P1433
P1476
The oligomerization domain of ...... tical role in capsid assembly.
@en
P2093
Antonio Maraver
Dolores González
Fernando Abaitua
Florencio Pazos
Jose A Ruiz-Díaz
Jose F Rodriguez
Jose R Castón
Roberto Clemente
P2860
P304
P356
10.1128/JVI.77.11.6438-6449.2003
P407
P577
2003-06-01T00:00:00Z