Constitutive phosphorylation of the vesicular stomatitis virus P protein modulates polymerase complex formation but is not essential for transcription or replication.
about
Newly identified phosphorylation site in the vesicular stomatitis virus P protein is required for viral RNA synthesisMapping the interacting domains between the rabies virus polymerase and phosphoprotein.A 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.Structural studies on the authentic mumps virus nucleocapsid showing uncoiling by the phosphoproteinBoth viral transcription and replication are reduced when the rabies virus nucleoprotein is not phosphorylatedCell-type-specific growth restriction of vesicular stomatitis virus polR mutants is linked to defective viral polymerase function.Overproduction of double-stranded RNA in vesicular stomatitis virus-infected cells activates a constitutive cell-type-specific antiviral responsePhosphorylation of the hepatitis delta virus antigensPhosphorylation within the amino-terminal acidic domain I of the phosphoprotein of vesicular stomatitis virus is required for transcription but not for replicationCritical phosphoprotein elements that regulate polymerase architecture and function in vesicular stomatitis virusAkt plays a critical role in replication of nonsegmented negative-stranded RNA virusesN-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.Restriction of measles virus RNA synthesis by a mouse host cell line: trans-complementation by polymerase components or a human cellular factor(s)Insertion of enhanced green fluorescent protein in a hinge region of vesicular stomatitis virus L polymerase protein creates a temperature-sensitive virus that displays no virion-associated polymerase activity in vitro.Functional characterization of the major and minor phosphorylation sites of the P protein of Borna disease virus.
P2860
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P2860
Constitutive phosphorylation of the vesicular stomatitis virus P protein modulates polymerase complex formation but is not essential for transcription or replication.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Constitutive phosphorylation o ...... transcription or replication.
@ast
Constitutive phosphorylation o ...... transcription or replication.
@en
type
label
Constitutive phosphorylation o ...... transcription or replication.
@ast
Constitutive phosphorylation o ...... transcription or replication.
@en
prefLabel
Constitutive phosphorylation o ...... transcription or replication.
@ast
Constitutive phosphorylation o ...... transcription or replication.
@en
P2093
P2860
P1433
P1476
Constitutive phosphorylation o ...... r transcription or replication
@en
P2093
D M Canter
D Spadafora
J Perrault
R L Jackson
P2860
P304
P407
P577
1996-07-01T00:00:00Z