Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication. - Wikidata - awgldk - TriplyDB

Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication.

Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication.

http://www.wikidata.org/entity/Q41965791

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Ubiquitination and deubiquitination of NP protein regulates influenza A virus RNA replication Structure of Crimean-Congo Hemorrhagic Fever Virus Nucleoprotein: Superhelical Homo-Oligomers and the Role of Caspase-3 Cleavage Biochemical and Structural Evidence in Support of a Coherent Model for the Formation of the Double-Helical Influenza A Virus Ribonucleoprotein Biochemical characterization of enzyme fidelity of influenza A virus RNA polymerase complex Conserved features of the PB2 627 domain impact influenza virus polymerase function and replication Emerging antiviral targets for influenza A virus.Structures of influenza A proteins and insights into antiviral drug targets.Genetic variations of nucleoprotein gene of influenza A viruses isolated from swine in Thailand.Identification of influenza A nucleoprotein body domain residues essential for viral RNA expression expose antiviral target.Evolutionary characterization of the pandemic H1N1/2009 influenza virus in humans based on non-structural genes.Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrier Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis.RNA virus replication complexes A big role for small RNAs in influenza virus replication Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms Molecular dynamics studies of the nucleoprotein of influenza A virus: role of the protein flexibility in RNA binding Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complex Screening methods for influenza antiviral drug discovery.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.Chimeric NP non coding regions between type A and C influenza viruses reveal their role in translation regulation Internal initiation of influenza virus replication of viral RNA and complementary RNA in vitro NP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein.Prediction of RNA binding residues: an extensive analysis based on structure and function to select the best predictor.Modeling the intracellular dynamics of influenza virus replication to understand the control of viral RNA synthesis.Pre-mRNA Processing Factor Prp18 Is a Stimulatory Factor of Influenza Virus RNA Synthesis and Possesses Nucleoprotein Chaperone Activity.A Nucleolar Protein, Ribosomal RNA Processing 1 Homolog B (RRP1B), Enhances the Recruitment of Cellular mRNA in Influenza Virus Transcription.The Functions of BMP3 in Rabbit Articular Cartilage Repair.A small-RNA enhancer of viral polymerase activity.pp32 and APRIL are host cell-derived regulators of influenza virus RNA synthesis from cRNA.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.Non-encapsidation activities of the capsid proteins of positive-strand RNA viruses.Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza.Resveratrol, sirtuins, and viruses.Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Protein Interacts with Nsp9 and Cellular DHX9 To Regulate Viral RNA Synthesis Activation of the interferon induction cascade by influenza a viruses requires viral RNA synthesis and nuclear export.

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P2860

Interaction of the influenza a virus nucleocapsid protein with the viral RNA polymerase potentiates unprimed viral RNA replication.

http://www.wikidata.org/entity/Q41965791

description

2008 nî lūn-bûn

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Interaction of the influenza a ...... nprimed viral RNA replication.

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Interaction of the influenza a ...... nprimed viral RNA replication.

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Interaction of the influenza a ...... nprimed viral RNA replication.

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P1433

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Journal of Virology

P1476

Interaction of the influenza a ...... unprimed viral RNA replication

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P2093

Laura L Newcomb

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Rei-Lin Kuo

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Robert M Krug

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Yizhi Jane Tao

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Yunyun Jiang

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P2860

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA

The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits

Model suggesting that replication of influenza virus is regulated by stabilization of replicative intermediates

Different de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.

The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex

A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.

Polyadenylation sites for influenza virus mRNA.

Influenza virion transcriptase: synthesis in vitro of large, polyadenylic acid-containing complementary RNA

RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites.

Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent

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29-36

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10.1128/JVI.02293-07

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1

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83

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18945782

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2612335

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