The M1 matrix protein controls the filamentous phenotype of influenza A virus.
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Transmission of a 2009 H1N1 pandemic influenza virus occurs before fever is detected, in the ferret modelCryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal endCompounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part I: Influenza life-cycle and currently available drugsThe Rab11 pathway is required for influenza A virus budding and filament formationThe M segment of the 2009 pandemic influenza virus confers increased neuraminidase activity, filamentous morphology, and efficient contact transmissibility to A/Puerto Rico/8/1934-based reassortant virusesMutations in haemagglutinin that affect receptor binding and pH stability increase replication of a PR8 influenza virus with H5 HA in the upper respiratory tract of ferrets and may contribute to transmissibilityResidue 41 of the Eurasian avian-like swine influenza a virus matrix protein modulates virion filament length and efficiency of contact transmissionThe short stalk length of highly pathogenic avian influenza H5N1 virus neuraminidase limits transmission of pandemic H1N1 virus in ferretsSpecific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitroSpherical influenza viruses have a fitness advantage in embryonated eggs, while filament-producing strains are selected in vivoInfection of human airway epithelium by human and avian strains of influenza a virus.Critical assessment of influenza VLP production in Sf9 and HEK293 expression systems.Pandemic H1N1 2009 influenza virus with the H275Y oseltamivir resistance neuraminidase mutation shows a small compromise in enzyme activity and viral fitness.A single amino acid in the HA of pH1N1 2009 influenza virus affects cell tropism in human airway epithelium, but not transmission in ferrets.An influenza reassortant with polymerase of pH1N1 and NS gene of H3N2 influenza A virus is attenuated in vivo.Structural organization of a filamentous influenza A virus.Avian Influenza virus glycoproteins restrict virus replication and spread through human airway epithelium at temperatures of the proximal airways.Influenza virus m2 ion channel protein is necessary for filamentous virion formation.The morphology and composition of influenza A virus particles are not affected by low levels of M1 and M2 proteins in infected cells.Comparative analysis of enzymatically produced novel linear DNA constructs with plasmids for use as DNA vaccines.Biological activities of 'noninfectious' influenza A virus particlesA crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.Conserved and host-specific features of influenza virion architecture.Respiratory syncytial virus assembles into structured filamentous virion particles independently of host cytoskeleton and related proteinsFilament-producing mutants of influenza A/Puerto Rico/8/1934 (H1N1) virus have higher neuraminidase activities than the spherical wild-type.Influenza virus assembly and budding.Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus productionStructural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and MorphologyA Comparison of Red Fluorescent Proteins to Model DNA Vaccine Expression by Whole Animal In Vivo Imaging.A Single Amino Acid in the M1 Protein Responsible for the Different Pathogenic Potentials of H5N1 Highly Pathogenic Avian Influenza Virus Strains.NS1 proteins of avian influenza A viruses can act as antagonists of the human alpha/beta interferon response.A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.Ultracentrifugation deforms unfixed influenza A virions.Filamentous influenza virus enters cells via macropinocytosis.The cytoplasmic tail domain of influenza B virus hemagglutinin is important for its incorporation into virions but is not essential for virus replication in cell culture in the presence of compensatory mutations.Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus.Species difference in ANP32A underlies influenza A virus polymerase host restrictionInvestigation of influenza virus polymerase activity in pig cells.
P2860
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P2860
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
@en
type
label
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
@en
prefLabel
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
@en
P1433
P1476
The M1 matrix protein controls the filamentous phenotype of influenza A virus.
@en
P2093
Barclay WS
Elleman CJ
P304
P356
10.1016/J.VIROL.2003.12.009
P407
P577
2004-03-01T00:00:00Z