Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
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Self-assembling protein nanoparticles in the design of vaccinesMultiBac turns sweetVirus-like particle (VLP)-based vaccines for pandemic influenza: performance of a VLP vaccine during the 2009 influenza pandemicH5N1 vaccines in humansThe influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packagingReverse Genetics Approaches for the Development of Influenza VaccinesMalaria vaccine based on self-assembling protein nanoparticlesThe Rab11 pathway is required for influenza A virus budding and filament formationVirus-like particle vaccine containing hemagglutinin confers protection against 2009 H1N1 pandemic influenzaCharacterization of the 1918 "Spanish" influenza virus matrix gene segmentVirus-like particle vaccine induces protective immunity against homologous and heterologous strains of influenza virus.Immunogenicity of H1N1 influenza virus-like particles produced in Nicotiana benthamiana.Critical assessment of influenza VLP production in Sf9 and HEK293 expression systems.Influenza vaccines based on virus-like particlesEvolution of the M gene of the influenza A virus in different host species: large-scale sequence analysis.Recombinant Hemagglutinin and Virus-Like Particle Vaccines for H7N9 Influenza VirusSwine-origin pandemic H1N1 influenza virus-like particles produced in insect cells induce hemagglutination inhibiting antibodies in BALB/c mice.Progress in developing virus-like particle influenza vaccines.Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: a comparison of two insect cell lines as production platforms for influenza vaccinesDevelopment and strategies of cell-culture technology for influenza vaccine.Vaccination inducing broad and improved cross protection against multiple subtypes of influenza A virus.H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies that preferentially bind to the oligomeric form of influenza virus hemagglutinin in humans.Mutations in the membrane-proximal region of the influenza A virus M2 protein cytoplasmic tail have modest effects on virus replication.Three-dimensional analysis of ribonucleoprotein complexes in influenza A virusCholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Multigene expression of protein complexes by iterative modification of genomic Bacmid DNAProduction and immunogenicity of chimeric virus-like particles containing the spike glycoprotein of infectious bronchitis virus.Novel antiviral activity of neuraminidase inhibitors against an avian influenza a virus.Delivery of woodchuck hepatitis virus-like particle presented influenza M2e by recombinant attenuated Salmonella displaying a delayed lysis phenotype.Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domainRequirements for budding of paramyxovirus simian virus 5 virus-like particles.Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5.Construction and characterization of insect cell-derived influenza VLP: cell binding, fusion, and EGFP incorporation.YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42Residual baculovirus in insect cell-derived influenza virus-like particle preparations enhances immunogenicity.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 influenza A virus matrix protein M1 and its self-assemblies at low pH.Influenza virus-like particles as an antigen-carrier platform for the ESAT-6 epitope of Mycobacterium tuberculosisThe highly conserved arginine residues at positions 76 through 78 of influenza A virus matrix protein M1 play an important role in viral replication by affecting the intracellular localization of M1
P2860
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P2860
Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
Formation of wild-type and chi ...... only four structural proteins
@en
Formation of wild-type and chi ...... only four structural proteins.
@nl
type
label
Formation of wild-type and chi ...... only four structural proteins
@en
Formation of wild-type and chi ...... only four structural proteins.
@nl
prefLabel
Formation of wild-type and chi ...... only four structural proteins
@en
Formation of wild-type and chi ...... only four structural proteins.
@nl
P2860
P1433
P1476
Formation of wild-type and chi ...... only four structural proteins
@en
P2093
P2860
P304
P356
10.1128/JVI.75.13.6154-6165.2001
P407
P577
2001-07-01T00:00:00Z