Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.
about
Structure-based discovery of the novel antiviral properties of naproxen against the nucleoprotein of influenza A virus.Connecting the study of wild influenza with the potential for pandemic diseaseTime-Resolved Visualisation of Nearly-Native Influenza A Virus Progeny Ribonucleoproteins and Their Individual Components in Live Infected CellsStructural and Functional Characterization of K339T Substitution Identified in the PB2 Subunit Cap-binding Pocket of Influenza A VirusAvian influenza virus h3 hemagglutinin may enable high fitness of novel human virus reassortantsConserved features of the PB2 627 domain impact influenza virus polymerase function and replicationMutations to PB2 and NP proteins of an avian influenza virus combine to confer efficient growth in primary human respiratory cells.The ecology and adaptive evolution of influenza A interspecies transmissionAdaptation of avian influenza A virus polymerase in mammals to overcome the host species barrierEmerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Influenza virus adaptation PB2-627K modulates nucleocapsid inhibition by the pathogen sensor RIG-I.A novel small-molecule inhibitor of influenza A virus acts by suppressing PA endonuclease activity of the viral polymerase.Bridging the past and the future of virology: surface plasmon resonance as a powerful tool to investigate virus/host interactions.Influenza virus nucleoprotein: structure, RNA binding, oligomerization and antiviral drug target.Cross-protection of influenza A virus infection by a DNA aptamer targeting the PA endonuclease domain.Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza.Role of the PB2 627 Domain in Influenza A Virus Polymerase FunctionUnstable polymerase-nucleoprotein interaction is not responsible for avian influenza virus polymerase restriction in human cells.Host restriction of influenza virus polymerase activity by PB2 627E is diminished on short viral templates in a nucleoprotein-independent manner.Amino acid substitutions affecting aspartic acid 605 and valine 606 decrease the interaction strength between the influenza virus RNA polymerase PB2 '627' domain and the viral nucleoprotein.
P2860
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P2860
Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Influenza polymerase activity ...... host-specific residue K/E627.
@ast
Influenza polymerase activity ...... host-specific residue K/E627.
@en
Influenza polymerase activity ...... host-specific residue K/E627.
@nl
type
label
Influenza polymerase activity ...... host-specific residue K/E627.
@ast
Influenza polymerase activity ...... host-specific residue K/E627.
@en
Influenza polymerase activity ...... host-specific residue K/E627.
@nl
prefLabel
Influenza polymerase activity ...... host-specific residue K/E627.
@ast
Influenza polymerase activity ...... host-specific residue K/E627.
@en
Influenza polymerase activity ...... host-specific residue K/E627.
@nl
P2093
P2860
P50
P1433
P1476
Influenza polymerase activity ...... host-specific residue K/E627.
@en
P2093
Andy Ka-Leung Ng
Mandy Ka-Han Lam
Pang-Chui Shaw
Shannon Wing-Ngor Au
Sze-Ting Choi
Wai-Hon Chan
P2860
P304
P356
10.1371/JOURNAL.PONE.0036415
P407
P577
2012-05-03T00:00:00Z