The influenza A virus NS1 protein interacts with the nucleoprotein of viral ribonucleoprotein complexes.
about
Conserved features of the PB2 627 domain impact influenza virus polymerase function and replicationMultiple Natural Substitutions in Avian Influenza A Virus PB2 Facilitate Efficient Replication in Human CellsIdentification of influenza A nucleoprotein body domain residues essential for viral RNA expression expose antiviral target.The influenza virus NS1 protein as a therapeutic target.Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis.Influenza virus infection induces the nuclear relocalization of the Hsp90 co-chaperone p23 and inhibits the glucocorticoid receptor response.Multifunctional adaptive NS1 mutations are selected upon human influenza virus evolution in the mouse.Nuclear localized Influenza nucleoprotein N-terminal deletion mutant is deficient in functional vRNP formation.The NS1 protein of influenza A virus interacts with cellular processing bodies and stress granules through RNA-associated protein 55 (RAP55) during virus infectionThe RNA-binding domain of influenzavirus non-structural protein-1 cooperatively binds to virus-specific RNA sequences in a structure-dependent mannerIdentification of RNA helicase A as a cellular factor that interacts with influenza A virus NS1 protein and its role in the virus life cycleYB-1 functions as a porter to lead influenza virus ribonucleoprotein complexes to microtubules.Mapping the phosphoproteome of influenza A and B viruses by mass spectrometry.Influenza A virus nucleoprotein induces apoptosis in human airway epithelial cells: implications of a novel interaction between nucleoprotein and host protein Clusterin.Proteomics-based methods for discovery, quantification, and validation of protein-protein interactions.The homologous tripartite viral RNA polymerase of A/swine/Korea/CT1204/2009(H1N2) influenza virus synergistically drives efficient replication and promotes respiratory droplet transmission in ferretsAn NS-segment exonic splicing enhancer regulates influenza A virus replication in mammalian cells.Viral proteins that bind double-stranded RNA: countermeasures against host antiviral responses.Influenza A Virus NS1 Protein Promotes Efficient Nuclear Export of Unspliced Viral M1 mRNA.Cellular DDX21 RNA helicase inhibits influenza A virus replication but is counteracted by the viral NS1 proteinThreonine 80 phosphorylation of non-structural protein 1 regulates the replication of influenza A virus by reducing the binding affinity with RIG-I.Implications of segment mismatch for influenza A virus evolution.Major contribution of the RNA-binding domain of NS1 in the pathogenicity and replication potential of an avian H7N1 influenza virus in chickens.
P2860
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P2860
The influenza A virus NS1 protein interacts with the nucleoprotein of viral ribonucleoprotein complexes.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@en
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@nl
type
label
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@en
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@nl
prefLabel
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@en
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@nl
P2093
P2860
P50
P356
P1433
P1476
The influenza A virus NS1 prot ...... l ribonucleoprotein complexes.
@en
P2093
Geoffrey Chase
Katja Bier
Nicole C Robb
Pang-Chui Shaw
P2860
P304
P356
10.1128/JVI.02562-10
P407
P577
2011-03-16T00:00:00Z