The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.
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The ambiguous base-pairing and high substrate efficiency of T-705 (Favipiravir) Ribofuranosyl 5'-triphosphate towards influenza A virus polymeraseThe influenza A segment 7 mRNA 3' splice site pseudoknot/hairpin familyClonogenic assay of type a influenza viruses reveals noninfectious cell-killing (apoptosis-inducing) particlesRecent Advances in Developing Small Molecules Targeting Nucleic AcidA novel small-molecule binds to the influenza A virus RNA promoter and inhibits viral replicationMutational analysis of the influenza virus cRNA promoter and identification of nucleotides critical for replication.Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.Influenza virus activation of the interferon systemIdentification of a PA-binding peptide with inhibitory activity against influenza A and B virus replicationInteractome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Polymerase activity of hybrid ribonucleoprotein complexes generated from reassortment between 2009 pandemic H1N1 and seasonal H3N2 influenza A viruses.The N-terminal region of the PA subunit of the RNA polymerase of influenza A/HongKong/156/97 (H5N1) influences promoter binding.Influenza A virus-generated small RNAs regulate the switch from transcription to replication.Single-molecule FRET reveals a corkscrew RNA structure for the polymerase-bound influenza virus promoter.Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complexCellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocationDnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activityDisruption of the viral polymerase complex assembly as a novel approach to attenuate influenza A virus.The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit.Temperature sensitive influenza A virus genome replication results from low thermal stability of polymerase-cRNA complexes.Bunyamwera bunyavirus RNA synthesis requires cooperation of 3'- and 5'-terminal sequences.A small-RNA enhancer of viral polymerase activity.Mutations at alternative 5' splice sites of M1 mRNA negatively affect influenza A virus viability and growth rate.Isolation and characterization of the positive-sense replicative intermediate of a negative-strand RNA virus.Identification of conserved RNA secondary structures at influenza B and C splice sites reveals similarities and differences between influenza A, B, and C.Influenza virus RNA structure: unique and common features.Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding.Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza.Activation of the interferon induction cascade by influenza a viruses requires viral RNA synthesis and nuclear export.The RNA-dependent RNA polymerase of the influenza A virus.A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs.A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase promotes the generation of defective interfering RNAs.Activation of influenza virus RNA polymerase by the 5' and 3' terminal duplex of genomic RNA.The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex.Mutational analyses of packaging signals in influenza virus PA, PB1, and PB2 genomic RNA segments.Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer.Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5.In vitro assembly of PB2 with a PB1-PA dimer supports a new model of assembly of influenza A virus polymerase subunits into a functional trimeric complex.Association of the influenza A virus RNA-dependent RNA polymerase with cellular RNA polymerase II.Comparation of the effects of different 5'-untranslated regions (UTRs) on gene expression in HEK293 cells.
P2860
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P2860
The RNA polymerase of influenza a virus is stabilized by interaction with its viral RNA promoter.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@en
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@nl
type
label
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@en
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@nl
prefLabel
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@en
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@nl
P2860
P1433
P1476
The RNA polymerase of influenz ...... n with its viral RNA promoter.
@en
P2093
George G Brownlee
Jane L Sharps
P2860
P304
P356
10.1128/JVI.76.14.7103-7113.2002
P407
P577
2002-07-01T00:00:00Z