The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
about
Definition of the minimal viral components required for the initiation of unprimed RNA synthesis by influenza virus RNA polymeraseEnzymology of RNA cap synthesisCommon and unique features of viral RNA-dependent polymerasesStructure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunitNucleoside Monophosphate Complex Structures of the Endonuclease Domain from the Influenza Virus Polymerase PA Subunit Reveal the Substrate Binding Site inside the Catalytic CenterThe structural basis for cap binding by influenza virus polymerase subunit PB2Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 SubunitStructural and Biochemical Basis for Development of Influenza Virus Inhibitors Targeting the PA EndonucleaseConformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virus3D structure of the influenza virus polymerase complex: localization of subunit domains.The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug DesignMesoionic heterocyclic compounds as candidate messenger RNA cap analogue inhibitors of the influenza virus RNA polymerase cap-binding activityUpolu virus and Aransas Bay virus, two presumptive bunyaviruses, are novel members of the family OrthomyxoviridaeIdentification of a PA-binding peptide with inhibitory activity against influenza A and B virus replicationHeat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivoPandemic and seasonal influenza: therapeutic challengesMutations associated with severity of the pandemic influenza A(H1N1)pdm09 in humans: a systematic review and meta-analysis of epidemiological evidence.Progress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses.PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells.Identification of influenza A nucleoprotein body domain residues essential for viral RNA expression expose antiviral target.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.Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.Influenza A: understanding the viral life cycleDifferential localization and function of PB1-F2 derived from different strains of influenza A virusInfluenza A virus polymerase: structural insights into replication and host adaptation mechanismsMinimum molecular architectures for transcription and replication of the influenza virus.Nuclear localized Influenza nucleoprotein N-terminal deletion mutant is deficient in functional vRNP formation.Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocationNP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.A unique strategy for mRNA cap methylation used by vesicular stomatitis 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.Tracking the Evolution in Phylogeny, Structure and Function of H5N1 Influenza Virus PA Gene.Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunitsFunctional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityInfluenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade.PA from an H5N1 highly pathogenic avian influenza virus activates viral transcription and replication and induces apoptosis and interferon expression at an early stage of infection
P2860
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P2860
The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits
description
2001 nî lūn-bûn
@nan
2001 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The active sites of the influe ...... different polymerase subunits
@ast
The active sites of the influe ...... different polymerase subunits
@en
The active sites of the influe ...... different polymerase subunits.
@nl
type
label
The active sites of the influe ...... different polymerase subunits
@ast
The active sites of the influe ...... different polymerase subunits
@en
The active sites of the influe ...... different polymerase subunits.
@nl
altLabel
The active sites of the influe ...... different polymerase subunits
@en
prefLabel
The active sites of the influe ...... different polymerase subunits
@ast
The active sites of the influe ...... different polymerase subunits
@en
The active sites of the influe ...... different polymerase subunits.
@nl
P2093
P2860
P3181
P356
P1433
P1476
The active sites of the influe ...... different polymerase subunits
@en
P2093
P2860
P304
P3181
P356
10.1093/EMBOJ/20.8.2078
P407
P577
2001-04-17T00:00:00Z