A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs.
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Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complexTime course and cellular localization of SARS-CoV nucleoprotein and RNA in lungs from fatal cases of SARS.Common and unique features of viral RNA-dependent polymerasesCrystal structure of the RNA-dependent RNA polymerase from influenza C virus.Influenza a virus assembly intermediates fuse in the cytoplasmThe structural basis for cap binding by influenza virus polymerase subunit PB2Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymerase3D structure of the influenza virus polymerase complex: localization of subunit domains.Mutational analysis of the influenza virus cRNA promoter and identification of nucleotides critical for replication.Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediatesDifferent de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.Fragile X mental retardation protein stimulates ribonucleoprotein assembly of influenza A virusUpolu virus and Aransas Bay virus, two presumptive bunyaviruses, are novel members of the family OrthomyxoviridaeBiochemical characterization of enzyme fidelity of influenza A virus RNA polymerase complexIdentification of a PA-binding peptide with inhibitory activity against influenza A and B virus replicationThe N-terminal fragment of a PB2 subunit from the influenza A virus (A/Hong Kong/156/1997 H5N1) effectively inhibits RNP activity and viral replicationImparting temperature sensitivity and attenuation in ferrets to A/Puerto Rico/8/34 influenza virus by transferring the genetic signature for temperature sensitivity from cold-adapted A/Ann Arbor/6/60.New insights into the nonconserved noncoding region of the subtype-determinant hemagglutinin and neuraminidase segments of influenza A viruses.Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Postreassortment amino acid substitutions in influenza A viruses.Polymerase activity of hybrid ribonucleoprotein complexes generated from reassortment between 2009 pandemic H1N1 and seasonal H3N2 influenza A viruses.The RNA polymerase PB2 subunit of influenza A/HongKong/156/1997 (H5N1) restricts the replication of reassortant ribonucleoprotein complexes [corrected]Mutations in polymerase genes enhanced the virulence of 2009 pandemic H1N1 influenza virus in miceReplication and transcription activities of ribonucleoprotein complexes reconstituted from avian H5N1, H1N1pdm09 and H3N2 influenza A virusesThe N-terminal region of the PA subunit of the RNA polymerase of influenza A/HongKong/156/97 (H5N1) influences promoter binding.Artificial hybrids of influenza A virus RNA polymerase reveal PA subunit modulates its thermal sensitivity.Genotype diversity of H9N2 viruses isolated from wild birds and chickens in Hunan Province, China.Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon.Single-molecule FRET reveals a corkscrew RNA structure for the polymerase-bound influenza virus promoter.The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.Influenza A virus polymerase: structural insights into replication and host adaptation mechanismsMutational analyses of the influenza A virus polymerase subunit PA reveal distinct functions related and unrelated to RNA polymerase activity.Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complexInteractions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I.Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.Screen anti-influenza lead compounds that target the PA(C) subunit of H5N1 viral RNA polymerase.Identification of human H1N2 and human-swine reassortant H1N2 and H1N1 influenza A viruses among pigs in Ontario, Canada (2003 to 2005).Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation
P2860
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P2860
A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs.
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
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@en
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@nl
type
label
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@en
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@nl
prefLabel
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@en
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@nl
P2093
P2860
P1433
P1476
A single amino acid mutation i ...... lytic cleavage of capped RNAs.
@en
P2093
George G Brownlee
Jane Sharps
Louise J Mingay
Mandy Crow
Pierre Fechter
P2860
P304
P356
10.1128/JVI.76.18.8989-9001.2002
P407
P50
P577
2002-09-01T00:00:00Z