The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function.
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Influenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1.Antiviral response in pandemic influenza virusesPB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranesGenomic signatures of human versus avian influenza A virusesIdentification of potential conserved RNA secondary structure throughout influenza A coding regionsLarge-scale sequencing of human influenza reveals the dynamic nature of viral genome evolutionViral control of mitochondrial apoptosisThe proapoptotic influenza A virus protein PB1-F2 forms a nonselective ion channelCellular RNA binding proteins NS1-BP and hnRNP K regulate influenza A virus RNA splicingStructure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferaseInsights into the interaction between influenza virus and pneumococcusInfluenza A virus PB1-F2 protein contributes to viral pathogenesis in miceThe PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages.ORF005L from infectious spleen and kidney necrosis virus is located in the inner mitochondrial membrane and induces apoptosis.Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumoniaSurvival analysis of infected mice reveals pathogenic variations in the genome of avian H1N1 virusesProgress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses.Twenty amino acids at the C-terminus of PA-X are associated with increased influenza A virus replication and pathogenicity.Human Dendritic Cell Response Signatures Distinguish 1918, Pandemic, and Seasonal H1N1 Influenza Viruses.The effects of influenza A virus PB1-F2 protein on polymerase activity are strain specific and do not impact pathogenesisA Serine12Stop mutation in PB1-F2 of the 2009 pandemic (H1N1) influenza A: a possible reason for its enhanced transmission and pathogenicity to humans.Perspectives on influenza evolution and the role of research.PB1-F2 proteins from H5N1 and 20 century pandemic influenza viruses cause immunopathology.Molecular characterization and comparative analysis of pandemic H1N1/2009 strains with co-circulating seasonal H1N1/2009 strains from eastern India.Effect of 1918 PB1-F2 expression on influenza A virus infection kinetics.Virulence and genetic compatibility of polymerase reassortant viruses derived from the pandemic (H1N1) 2009 influenza virus and circulating influenza A viruses.Influenza A viruses: new research developments.Differential contribution of PB1-F2 to the virulence of highly pathogenic H5N1 influenza A virus in mammalian and avian species.The influenza A virus protein PB1-F2: killing two birds with one stone?Surveillance in Eastern India (2007-2009) revealed reassortment event involving NS and PB1-F2 gene segments among co-circulating influenza A subtypes.Influenza virus protein PB1-F2 inhibits the induction of type I interferon by binding to MAVS and decreasing mitochondrial membrane potentialComprehensive global amino acid sequence analysis of PB1F2 protein of influenza A H5N1 viruses and the influenza A virus subtypes responsible for the 20th-century pandemics.Kinetics of coinfection with influenza A virus and Streptococcus pneumoniae.Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes.Amino Acid Residues 68-71 Contribute to Influenza A Virus PB1-F2 Protein Stability and FunctionsInnate immune evasion strategies of influenza virusesNLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein.PB1-F2 influenza A virus protein adopts a beta-sheet conformation and forms amyloid fibers in membrane environments.PB1-F2 attenuates virulence of highly pathogenic avian H5N1 influenza virus in chickens.RLR-mediated antiviral innate immunity requires oxidative phosphorylation activity.
P2860
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P2860
The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@ast
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@en
type
label
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@ast
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@en
prefLabel
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@ast
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@en
P2093
P2860
P1433
P1476
The influenza A virus PB1-F2 p ...... srupts mitochondrial function.
@en
P2093
Daniela Malide
Felicita Hornung
Jack R Bennink
James S Gibbs
P2860
P304
P356
10.1128/JVI.77.13.7214-7224.2003
P407
P577
2003-07-01T00:00:00Z