The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target.
about
Mutations within the conserved NS1 nuclear export signal lead to inhibition of influenza A virus replicationThe H5N1 influenza virus NS genes selected after 1998 enhance virus replication in mammalian cellsRecent progress in structure-based anti-influenza drug designStructural basis for suppression of a host antiviral response by influenza A virusX-ray structure of NS1 from a highly pathogenic H5N1 influenza virusStructure of NS1A effector domain from the influenza A/Udorn/72 virusX-ray structures of NS1 effector domain mutantsNuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes.The end of the message: multiple protein-RNA interactions define the mRNA polyadenylation siteFunctions of the influenza A virus NS1 protein in antiviral defenseCompounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part II: Future compounds against influenza virusThe interactomes of influenza virus NS1 and NS2 proteins identify new host factors and provide insights for ADAR1 playing a supportive role in virus replicationDimer interface of the effector domain of non-structural protein 1 from influenza A virus: an interface with multiple functionsHeterologous SH3-p85beta inhibits influenza A virus replication.Progress of small molecular inhibitors in the development of anti-influenza virus agents.Multiple anti-interferon actions of the influenza A virus NS1 proteinAccumulation of human-adapting mutations during circulation of A(H1N1)pdm09 influenza virus in humans in the United Kingdom.Oligonucleotides derived from the packaging signal at the 5' end of the viral PB2 segment specifically inhibit influenza virus in vitro.Emerging antiviral targets for influenza A virus.Structures of influenza A proteins and insights into antiviral drug targets.Inefficient control of host gene expression by the 2009 pandemic H1N1 influenza A virus NS1 proteinDifferential effects of NS1 proteins of human pandemic H1N1/2009, avian highly pathogenic H5N1, and low pathogenic H5N2 influenza A viruses on cellular pre-mRNA polyadenylation and mRNA translation.The influenza virus NS1 protein as a therapeutic target.Cysteine and histidine shuffling: mixing and matching cysteine and histidine residues in zinc finger proteins to afford different folds and function.Roles of the phosphorylation of specific serines and threonines in the NS1 protein of human influenza A viruses.Influenza virus A/Beijing/501/2009(H1N1) NS1 interacts with β-tubulin and induces disruption of the microtubule network and apoptosis on A549 cells.Novel inhibitor of influenza non-structural protein 1 blocks multi-cycle replication in an RNase L-dependent manner.Distinctive interactions of the Arabidopsis homolog of the 30 kD subunit of the cleavage and polyadenylation specificity factor (AtCPSF30) with other polyadenylation factor subunitsPrediction of protein-protein interaction sites using an ensemble method.The NS segment of an H5N1 highly pathogenic avian influenza virus (HPAIV) is sufficient to alter replication efficiency, cell tropism, and host range of an H7N1 HPAIVInnate immune evasion strategies of influenza viruses(19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus.The poly(A)-dependent transcriptional pause is mediated by CPSF acting on the body of the polymerase.Activation of c-jun N-terminal kinase upon influenza A virus (IAV) infection is independent of pathogen-related receptors but dependent on amino acid sequence variations of IAV NS1.Nuclear localized Influenza nucleoprotein N-terminal deletion mutant is deficient in functional vRNP formation.Influenza A H3N2 subtype virus NS1 protein targets into the nucleus and binds primarily via its C-terminal NLS2/NoLS to nucleolin and fibrillarinCPSF30 and Wdr33 directly bind to AAUAAA in mammalian mRNA 3' processingSpecies-specific inhibition of RIG-I ubiquitination and IFN induction by the influenza A virus NS1 proteinThe primary function of RNA binding by the influenza A virus NS1 protein in infected cells: Inhibiting the 2'-5' oligo (A) synthetase/RNase L pathway.A high diversity of Eurasian lineage low pathogenicity avian influenza A viruses circulate among wild birds sampled in Egypt.
P2860
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P2860
The CPSF30 binding site on the NS1A protein of influenza A virus is a potential antiviral target.
description
2006 nî lūn-bûn
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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2006 թվականի ապրիլին հրատարակված գիտական հոդված
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年學術文章
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name
The CPSF30 binding site on the ...... a potential antiviral target.
@ast
The CPSF30 binding site on the ...... a potential antiviral target.
@en
type
label
The CPSF30 binding site on the ...... a potential antiviral target.
@ast
The CPSF30 binding site on the ...... a potential antiviral target.
@en
prefLabel
The CPSF30 binding site on the ...... a potential antiviral target.
@ast
The CPSF30 binding site on the ...... a potential antiviral target.
@en
P2093
P2860
P1433
P1476
The CPSF30 binding site on the ...... a potential antiviral target.
@en
P2093
Diana L Noah
Karen Y Twu
Rei-Lin Kuo
Robert M Krug
P2860
P304
P356
10.1128/JVI.80.8.3957-3965.2006
P577
2006-04-01T00:00:00Z