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Crystal structure of the matrix protein VP40 from Ebola virusCrystal structure of vesicular stomatitis virus matrix protein.The packaging signal of influenza viral RNA molecules.Mammalian expression of virus-like particles for advanced mimicry of authentic influenza virusAlteration of protein levels during influenza virus H1N1 infection in host cells: a proteomic survey of host and virus reveals differential dynamicsA promoter mutation in the haemagglutinin segment of influenza A virus generates an effective candidate live attenuated vaccineInvolvement 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.Protective immunity against influenza in HLA-A2 transgenic mice by modified vaccinia virus Ankara vectored vaccines containing internal influenza proteins.Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Architecture of a nascent viral fusion pore.Structural organization of a filamentous influenza A virus.How cells tune viral mechanics--insights from biophysical measurements of influenza virus.Biochemical characterization of rous sarcoma virus MA protein interaction with membranes.The morphology and composition of influenza A virus particles are not affected by low levels of M1 and M2 proteins in infected cells.Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium.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 domainThe 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.YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42Stepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration.The cytoplasmic tail of the influenza A virus M2 protein plays a role in viral assembly.A comprehensive map of the influenza A virus replication cycleStructural analysis of influenza A virus matrix protein M1 and its self-assemblies at low pH.Crystal structures of influenza A virus matrix protein M1: variations on a themeEffect of Osmotic Pressure on the Stability of Whole Inactivated Influenza Vaccine for Coating on Microneedles.Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particlesA nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.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.pH-Dependent Formation and Disintegration of the Influenza A Virus Protein Scaffold To Provide Tension for Membrane FusionIn vitro and in vivo replication of influenza A H1N1 WSN33 viruses with different M1 proteins.Protein-lipid interactions critical to replication of the influenza A virus.Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly.The Matrix protein M1 from influenza C virus induces tubular membrane invaginations in an in vitro cell membrane model.Association of influenza virus proteins with membrane rafts.Palmitoylation contributes to membrane curvature in Influenza A virus assembly and hemagglutinin-mediated membrane fusion.Phosphatidylserine Lateral Organization Influences the Interaction of Influenza Virus Matrix Protein 1 with Lipid Membranes.Lateral Organization of Influenza Virus Proteins in the Budozone Region of the Plasma Membrane.Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
Membrane interaction of influenza virus M1 protein.
@en
type
label
Membrane interaction of influenza virus M1 protein.
@en
prefLabel
Membrane interaction of influenza virus M1 protein.
@en
P2093
P356
P1433
P1476
Membrane interaction of influenza virus M1 protein.
@en
P2093
P304
P356
10.1006/VIRO.1999.0134
P407
P577
2000-02-01T00:00:00Z