Cooperative binding of multimeric phosphoprotein (P) of vesicular stomatitis virus to polymerase (L) and template: pathways of assembly.
about
Antagonistic Pleiotropy Involving Promoter Sequences in a VirusStructure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, PCrystal Structure of the Nipah Virus Phosphoprotein Tetramerization DomainUnderstanding and altering cell tropism of vesicular stomatitis virusNewly identified phosphorylation site in the vesicular stomatitis virus P protein is required for viral RNA synthesisModel-based design of growth-attenuated virusesA role for the Sendai virus P protein trimer in RNA synthesis.Optimal replication activity of vesicular stomatitis virus RNA polymerase requires phosphorylation of a residue(s) at carboxy-terminal domain II of its accessory subunit, phosphoprotein P.Role of the hypervariable hinge region of phosphoprotein P of vesicular stomatitis virus in viral RNA synthesis and assembly of infectious virus particles.Phosphorylation of vesicular stomatitis virus phosphoprotein P is indispensable for virus growth.Modification of Asn374 of nsP1 suppresses a Sindbis virus nsP4 minus-strand polymerase mutantStructural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoproteinCrystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virusIdentification of a novel tripartite complex involved in replication of vesicular stomatitis virus genome RNA.Constitutive phosphorylation of the vesicular stomatitis virus P protein modulates polymerase complex formation but is not essential for transcription or replication.Phosphorylation within the amino-terminal acidic domain I of the phosphoprotein of vesicular stomatitis virus is required for transcription but not for replicationA vesiculovirus showing a steepened transcription gradient and dominant trans-repression of virus transcription.Oligomerization of Mumps Virus Phosphoprotein.N-terminal phosphorylation of phosphoprotein of vesicular stomatitis virus is required for preventing nucleoprotein from binding to cellular RNAs and for functional template formation.Mapping and functional role of the self-association domain of vesicular stomatitis virus phosphoprotein.Dissection of individual functions of the Sendai virus phosphoprotein in transcription.Identification of a minimal size requirement for termination of vesicular stomatitis virus mRNA: implications for the mechanism of transcription.Restriction of measles virus RNA synthesis by a mouse host cell line: trans-complementation by polymerase components or a human cellular factor(s)Tracking fluorescence-labeled rabies virus: enhanced green fluorescent protein-tagged phosphoprotein P supports virus gene expression and formation of infectious particles.The interaction between the Nipah virus nucleocapsid protein and phosphoprotein regulates virus replication
P2860
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P2860
Cooperative binding of multimeric phosphoprotein (P) of vesicular stomatitis virus to polymerase (L) and template: pathways of assembly.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Cooperative binding of multime ...... emplate: pathways of assembly.
@en
Cooperative binding of multimeric phosphoprotein
@nl
type
label
Cooperative binding of multime ...... emplate: pathways of assembly.
@en
Cooperative binding of multimeric phosphoprotein
@nl
prefLabel
Cooperative binding of multime ...... emplate: pathways of assembly.
@en
Cooperative binding of multimeric phosphoprotein
@nl
P2860
P1433
P1476
Cooperative binding of multime ...... template: pathways of assembly
@en
P2860
P304
P407
P577
1995-12-01T00:00:00Z