Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer.
about
Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosomeThe polymerase of negative-stranded RNA virusesThe structure of a biologically active influenza virus ribonucleoprotein complexThe structural basis for cap binding by influenza virus polymerase subunit PB2Structural Basis of the Influenza A Virus RNA Polymerase PB2 RNA-binding Domain Containing the Pathogenicity-determinant Lysine 627 ResidueOrganization of the influenza virus replication machineryIdentification 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.The nucleoprotein of newly emerged H7N9 influenza A virus harbors a unique motif conferring resistance to antiviral human MxA.An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase.Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.Structures of influenza A proteins and insights into antiviral drug targets.Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase.The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication.The N-terminal region of the PA subunit of the RNA polymerase of influenza A/HongKong/156/97 (H5N1) influences promoter binding.Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication.The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complexArchitecture and regulation of negative-strand viral enzymatic machineryIntegrating computational modeling and functional assays to decipher the structure-function relationship of influenza virus PB1 protein.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.A small-RNA enhancer of viral polymerase activity.Different incubation temperatures affect viral polymerase activity and yields of low-pathogenic avian influenza viruses in embryonated chicken eggs.Three amino acid changes in PB1-F2 of highly pathogenic H5N1 avian influenza virus affect pathogenicity in mallard ducks.Crystallization and X-ray diffraction analysis of the RNA primer/promoter-binding domain of influenza A virus RNA-dependent RNA polymerase PB2.Configuration of viral ribonucleoprotein complexes within the influenza A virion.A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.Structure of influenza virus ribonucleoprotein complexes and their packaging into virions.The influenza virus RNA synthesis machine: advances in its structure and function.Structure and assembly of the influenza A virus ribonucleoprotein complex.New-generation screening assays for the detection of anti-influenza compounds targeting viral and host functions.The RNA-dependent RNA polymerase of the influenza A virus.Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.Limited compatibility of polymerase subunit interactions in influenza A and B viruses.Nuclear dynamics of influenza A virus ribonucleoproteins revealed by live-cell imaging studies.Evidence that the C-terminal PB2-binding region of the influenza A virus PB1 protein is a discrete alpha-helical domain.Screening for Novel Small-Molecule Inhibitors Targeting the Assembly of Influenza Virus Polymerase Complex by a Bimolecular Luminescence Complementation-Based Reporter SystemAdaptive mutations resulting in enhanced polymerase activity contribute to high virulence of influenza A virus in mice.Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein.Detection and characterization of influenza A virus PA-PB2 interaction through a bimolecular fluorescence complementation assay.
P2860
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P2860
Three-dimensional model for the isolated recombinant influenza virus polymerase heterotrimer.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Three-dimensional model for th ...... virus polymerase heterotrimer.
@en
type
label
Three-dimensional model for th ...... virus polymerase heterotrimer.
@en
prefLabel
Three-dimensional model for th ...... virus polymerase heterotrimer.
@en
P2093
P2860
P50
P356
P1476
Three-dimensional model for th ...... virus polymerase heterotrimer.
@en
P2093
Eva Torreira
Juan Ortín
Núria Jorba
Rob W H Ruigrok
Yolanda Fernández
P2860
P304
P356
10.1093/NAR/GKM336
P577
2007-05-21T00:00:00Z