PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes
about
A single mutation in the PB1-F2 of H5N1 (HK/97) and 1918 influenza A viruses contributes to increased virulenceInfluenza virus PB1-F2 protein induces cell death through mitochondrial ANT3 and VDAC1.Identification of potential conserved RNA secondary structure throughout influenza A coding regionsLarge-scale sequencing of human influenza reveals the dynamic nature of viral genome evolutionThe proapoptotic influenza A virus protein PB1-F2 forms a nonselective ion channelSwitch from protective to adverse inflammation during influenza: viral determinants and hemostasis are caught as culprits.Influenza A virus PB1-F2 protein contributes to viral pathogenesis in miceThe PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages.Expression of the 1918 influenza A virus PB1-F2 enhances the pathogenesis of viral and secondary bacterial pneumoniaProgress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses.The contribution of PA-X to the virulence of pandemic 2009 H1N1 and highly pathogenic H5N1 avian influenza viruses.Twenty amino acids at the C-terminus of PA-X are associated with increased influenza A virus replication and pathogenicity.The effects of influenza A virus PB1-F2 protein on polymerase activity are strain specific and do not impact pathogenesisPB1-F2 expression by the 2009 pandemic H1N1 influenza virus has minimal impact on virulence in animal modelsPro-apoptotic Bax molecules densely populate the edges of membrane pores.PB1-F2 proteins from H5N1 and 20 century pandemic influenza viruses cause immunopathology.Differential contribution of PB1-F2 to the virulence of highly pathogenic H5N1 influenza A virus in mammalian and avian species.H5N1-SeroDetect EIA and rapid test: a novel differential diagnostic assay for serodiagnosis of H5N1 infections and surveillance.Influenza virus A/Beijing/501/2009(H1N1) NS1 interacts with β-tubulin and induces disruption of the microtubule network and apoptosis on A549 cells.Molecular signatures of virulence in the PB1-F2 proteins of H5N1 influenza viruses.Matrix protein 2 of influenza A virus blocks autophagosome fusion with lysosomes.Innate immune evasion strategies of influenza virusesNLRX1 prevents mitochondrial induced apoptosis and enhances macrophage antiviral immunity by interacting with influenza virus PB1-F2 protein.Highly pathogenic avian influenza A virus H5N1 NS1 protein induces caspase-dependent apoptosis in human alveolar basal epithelial cellsPB1-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.Transcriptomic analysis of host immune and cell death responses associated with the influenza A virus PB1-F2 protein.Kinetic characterization of PB1-F2-mediated immunopathology during highly pathogenic avian H5N1 influenza virus infectionSulfatide regulates caspase-3-independent apoptosis of influenza A virus through viral PB1-F2 protein.The influenza virus protein PB1-F2 interacts with IKKβ and modulates NF-κB signalling.The NS1 protein of influenza A virus interacts with heat shock protein Hsp90 in human alveolar basal epithelial cells: implication for virus-induced apoptosis.A comprehensive map of the influenza A virus replication cycleParadoxical lipid dependence of pores formed by the Escherichia coli alpha-hemolysin in planar phospholipid bilayer membranes.Immunopathogenic and antibacterial effects of H3N2 influenza A virus PB1-F2 map to amino acid residues 62, 75, 79, and 82.The Influenza Virus Protein PB1-F2 Increases Viral Pathogenesis through Neutrophil Recruitment and NK Cells Inhibition.Role of apoptosis and cytokines in influenza virus morbidity.A novel cytotoxic sequence contributes to influenza A viral protein PB1-F2 pathogenicity and predisposition to secondary bacterial infection.Pretreatment of mice with oligonucleotide prop5 protects them from influenza virus infections.The regulation of autophagy by influenza A virus.Swine influenza vaccines: current status and future perspectives.
P2860
Q21089626-BFD58EB5-BD17-49FD-A58E-8C1167A21174Q21090537-D0CB9F2E-D002-44C7-B2DA-D1E5753848BBQ24633659-75D0EAEA-84CF-491B-AA61-60BEF42C5BA0Q28275712-3D6C761A-7D04-42CB-A961-C480FBE29C26Q28474394-CE653D71-B54C-45F3-844B-ED395EA781EFQ30354127-19C4709A-9C7B-42EF-82D2-3D35FA07C737Q30355968-20A81438-EFFA-4F96-B4C1-986B1C7131ACQ30359236-6439D4E6-E1DE-44F5-A242-55067A7D585CQ30365855-1693CC59-75B9-4454-BE59-8C2ECF4C977DQ30369896-2A0F9245-AA41-48CA-BE93-9633104F5849Q30371441-7ACDCA7E-62E4-486E-9DEB-1BAB71AD292DQ30373730-E7C64671-B6D6-4DE6-B7DD-1C0203C040EAQ30381642-7532FECA-73B0-4231-91F0-0434632B5823Q30385984-85C420A8-AD25-416B-8224-884CBF8470D5Q30388868-325F2326-53E1-451E-B2F8-9764EEE4DEC9Q30391867-036FA32F-2F8B-486D-9DC8-017385A3F371Q30406151-FAC94B32-4F74-433A-A4C3-B6F2D5D8ED8CQ30407593-D0A0FC55-6183-4078-B120-112329598081Q30423381-8795F5F2-AE94-419A-B437-1C56B6ADFBC3Q30428356-CC9D64AD-ED7B-4241-A7B0-C4DFC5CE232DQ30491528-EB58A0E6-A7D4-4DD0-AA96-3B4215163925Q33646273-D629C413-5C28-4052-AFED-BF0EE94A5B68Q33665233-E3EAD529-BAE5-4D4D-AFAE-8C14647F57B4Q33787326-76C76C4B-516B-463B-884B-1D757840DC0EQ33800245-C936637F-F8D6-4077-B3C8-B53346C16D19Q33800303-A6FF22DB-42E8-4F60-AADB-242D1B3FBDA8Q34013619-25ED0580-2605-4097-9216-0FC3BDB65291Q34613342-490CC567-0256-443E-8B27-46018C251A1CQ34674604-CC9BDAA2-A00B-4CCE-9FB8-41B8119BA196Q34737708-48F27289-E68F-47C3-8D32-D3289FC308FBQ34993004-9AF6D49E-70A5-46CF-B817-965E3705BBCDQ35006697-E9C6DF0E-8FB0-48BC-9FD8-8AA9E91D7AB0Q35121277-53410F94-212C-48AA-BA76-8D2A2A2187D0Q35531645-55A8C3EC-50C7-45E1-A14F-5C06913C4583Q36178669-19A54CFE-93AB-40A0-9899-ADCB0307DDD2Q36231177-1F92356C-26C0-4268-8810-83183C636C37Q37547751-6D6710DD-07B1-43E9-A601-6DEF262DD97CQ37611821-89C6D054-525C-4752-B584-F6BAC4935E60Q37693635-5522604C-B2AE-4939-857C-C311BA881A6CQ37749889-83F2297A-CDD6-449A-B28A-BE7B1C8BC185
P2860
PB1-F2, an influenza A virus-encoded proapoptotic mitochondrial protein, creates variably sized pores in planar lipid membranes
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
name
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@ast
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@en
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@nl
type
label
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@ast
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@en
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@nl
prefLabel
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@ast
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@en
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@nl
P2093
P2860
P3181
P1433
P1476
PB1-F2, an influenza A virus-e ...... ores in planar lipid membranes
@en
P2093
A N Chanturiya
J W Yewdell
J Zimmerberg
P Henklein
U Schubert
P2860
P304
P3181
P356
10.1128/JVI.78.12.6304-6312.2004
P407
P577
2004-06-01T00:00:00Z