Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding.
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Nucleoside 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 PB2Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymeraseStructural and Biochemical Basis for Development of Influenza Virus Inhibitors Targeting the PA EndonucleaseStructural and Functional Characterization of K339T Substitution Identified in the PB2 Subunit Cap-binding Pocket of Influenza A VirusCrystallographic Fragment Screening and Structure-Based Optimization Yields a New Class of Influenza Endonuclease InhibitorsComparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domainsHeat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivoMutational analysis of the binding pockets of the diketo acid inhibitor L-742,001 in the influenza virus PA endonucleaseThe N-terminal fragment of a PB2 subunit from the influenza A virus (A/Hong Kong/156/1997 H5N1) effectively inhibits RNP activity and viral replicationPersistent host markers in pandemic and H5N1 influenza virusesInfluenza A Virus Protein PA-X Contributes to Viral Growth and Suppression of the Host Antiviral and Immune ResponsesA Novel Endonuclease Inhibitor Exhibits Broad-Spectrum Anti-Influenza Virus Activity In VitroReassortment and mutation of the avian influenza virus polymerase PA subunit overcome species barriersPolymerase 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]Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrierReplication 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.Generation and Comprehensive Analysis of Host Cell Interactome of the PA Protein of the Highly Pathogenic H5N1 Avian Influenza Virus in Mammalian CellsArtificial hybrids of influenza A virus RNA polymerase reveal PA subunit modulates its thermal sensitivity.Genomic and protein structural maps of adaptive evolution of human influenza A virus to increased virulence in the mouse.Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.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.Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Screen anti-influenza lead compounds that target the PA(C) subunit of H5N1 viral RNA polymerase.Cyclin T1/CDK9 interacts with influenza A virus polymerase and facilitates its association with cellular RNA polymerase II.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 combination of HA and PA mutations enhances virulence in a mouse-adapted H6N6 influenza A 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.Functional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalitySelective Degradation of Host RNA Polymerase II Transcripts by Influenza A Virus PA-X Host Shutoff Protein.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 infectionAn overlapping protein-coding region in influenza A virus segment 3 modulates the host responseIdentification of novel influenza A virus proteins translated from PA mRNAThe PA-gene-mediated lethal dissemination and excessive innate immune response contribute to the high virulence of H5N1 avian influenza virus in miceIdentification of the N-terminal domain of the influenza virus PA responsible for the suppression of host protein synthesis.
P2860
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P2860
Amino acid residues in the N-terminal region of the PA subunit of influenza A virus RNA polymerase play a critical role in protein stability, endonuclease activity, cap binding, and virion RNA promoter binding.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@en
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@nl
type
label
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@en
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@nl
prefLabel
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@en
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@nl
P2093
P2860
P356
P1433
P1476
Amino acid residues in the N-t ...... d virion RNA promoter binding.
@en
P2093
Florian I Schmidt
George G Brownlee
Mandy Crow
P2860
P304
P356
10.1128/JVI.00600-06
P407
P577
2006-08-01T00:00:00Z