Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
about
Biological functions and biogenesis of secreted bacterial outer membrane vesiclesThe genomic and epidemiological dynamics of human influenza A virusVirus entry, assembly, budding, and membrane raftsAdvancements in the development of subunit influenza vaccinesCryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal endInfluenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.The packaging signal of influenza viral RNA molecules.The 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 virusesThe neuraminidase and matrix genes of the 2009 pandemic influenza H1N1 virus cooperate functionally to facilitate efficient replication and transmissibility in pigsSpecific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitroMammalian expression of virus-like particles for advanced mimicry of authentic influenza virusPerfringolysin O association with ordered lipid domains: implications for transmembrane protein raft affinity.Characterization of the 1918 "Spanish" influenza virus matrix gene segmentPersistent host markers in pandemic and H5N1 influenza virusesInfluenza A and B virus intertypic reassortment through compatible viral packaging signals.Incorporation of membrane-anchored flagellin into influenza virus-like particles enhances the breadth of immune responses.Optimizing viral protein yield of influenza virus strain A/Vietnam/1203/2004 by modification of the neuraminidase gene.Influenza vaccines based on virus-like particlesBroad Spectrum Anti-Influenza Agents by Inhibiting Self-Association of Matrix Protein 1.Involvement of an Arginine Triplet in M1 Matrix Protein Interaction with Membranes and in M1 Recruitment into Virus-Like Particles of the Influenza A(H1N1)pdm09 Virus.CD4+ T-cell expansion predicts neutralizing antibody responses to monovalent, inactivated 2009 pandemic influenza A(H1N1) virus subtype H1N1 vaccine.Architecture of a nascent viral fusion pore.Visualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.An enzymatic virus-like particle assay for sensitive detection of virus entryEvidence that Gag facilitates HIV-1 envelope association both in GPI-enriched plasma membrane and detergent resistant membranes and facilitates envelope incorporation onto virions in primary CD4+ T cells.Genetic content of Influenza H3N2 vaccine seedsPseudotypes of vesicular stomatitis virus with CD4 formed by clustering of membrane microdomains during buddingThe morphology and composition of influenza A virus particles are not affected by low levels of M1 and M2 proteins in infected cells.Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release.Plasma membrane rafts play a critical role in HIV-1 assembly and release.Integrity of membrane lipid rafts is necessary for the ordered assembly and release of infectious Newcastle disease virus particlesVirus particle release from glycosphingolipid-enriched microdomains is essential for dendritic cell-mediated capture and transfer of HIV-1 and henipavirus.The cholesterol recognition/interaction amino acid consensus motif of the influenza A virus M2 protein is not required for virus replication but contributes to virulence.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.Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domainStructure-based design of NS2 mutants for attenuated influenza A virus vaccinesThe compensatory G88R change is essential in restoring the normal functions of influenza A/WSN/33 virus matrix protein 1 with a disrupted nuclear localization signal.Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts.At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.Gag regulates association of human immunodeficiency virus type 1 envelope with detergent-resistant membranes.
P2860
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P2860
Influenza virus assembly: effect of influenza virus glycoproteins on the membrane association of M1 protein
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Influenza virus assembly: effe ...... rane association of M1 protein
@ast
Influenza virus assembly: effe ...... rane association of M1 protein
@en
type
label
Influenza virus assembly: effe ...... rane association of M1 protein
@ast
Influenza virus assembly: effe ...... rane association of M1 protein
@en
prefLabel
Influenza virus assembly: effe ...... rane association of M1 protein
@ast
Influenza virus assembly: effe ...... rane association of M1 protein
@en
P2093
P2860
P1433
P1476
Influenza virus assembly: effe ...... rane association of M1 protein
@en
P2093
P2860
P304
P356
10.1128/JVI.74.18.8709-8719.2000
P407
P577
2000-09-01T00:00:00Z