Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes. - Wikidata - wikimedia - TriplyDB

Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.

Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.

http://www.wikidata.org/entity/Q37743549

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Dual function of CD81 in influenza virus uncoating and budding Identification of Hsc70 as an influenza virus matrix protein (M1) binding factor involved in the virus life cycle Biological functions and biogenesis of secreted bacterial outer membrane vesicles Cryotomography of budding influenza A virus reveals filaments with diverse morphologies that mostly do not bear a genome at their distal end Emerging Infections of CNS: Avian Influenza A Virus, Rift Valley Fever Virus and Human Parechovirus 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 viruses Residue 41 of the Eurasian avian-like swine influenza a virus matrix protein modulates virion filament length and efficiency of contact transmission Specific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitro Spherical influenza viruses have a fitness advantage in embryonated eggs, while filament-producing strains are selected in vivo Broad Spectrum Anti-Influenza Agents by Inhibiting Self-Association of Matrix Protein 1.Structural organization of a filamentous influenza A virus.Influenza virus m2 ion channel protein is necessary for filamentous virion formation.Functional constraints of influenza A virus epitopes limit escape from cytotoxic T lymphocytes A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Novel antiviral activity of neuraminidase inhibitors against an avian influenza a virus.Influenza A: understanding the viral life cycle Effect of envelope proteins on the mechanical properties of influenza virus Structure-based design of NS2 mutants for attenuated influenza A virus vaccines Distribution of surface glycoproteins on influenza A virus determined by electron cryotomography.The 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.Filament-producing mutants of influenza A/Puerto Rico/8/1934 (H1N1) virus have higher neuraminidase activities than the spherical wild-type.YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 Influenza virus assembly and budding.Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.Distinct domains of the influenza a virus M2 protein cytoplasmic tail mediate binding to the M1 protein and facilitate infectious virus production Structural Analysis of the Roles of Influenza A Virus Membrane-Associated Proteins in Assembly and Morphology The 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 Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP.A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.Ultracentrifugation deforms unfixed influenza A virions.Overlapping roles of the Rous sarcoma virus Gag p10 domain in nuclear export and virion core morphology.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.Identification of Conserved Peptides Comprising Multiple T Cell Epitopes of Matrix 1 Protein in H1N1 Influenza Virus Two polar residues within C-terminal domain of M1 are critical for the formation of influenza A Virions.The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.Mutations at alternative 5' splice sites of M1 mRNA negatively affect influenza A virus viability and growth rate.In vitro and in vivo replication of influenza A H1N1 WSN33 viruses with different M1 proteins.The amphipathic helix of influenza A virus M2 protein is required for filamentous bud formation and scission of filamentous and spherical particles Influenza virus morphogenesis and budding.Specific nucleoprotein residues affect influenza virus morphology.

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Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.

http://www.wikidata.org/entity/Q37743549

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bilimsel makale

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scientific article published on January 2005

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vedecký článok

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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JVI.79.2.1262-1270.2005

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Journal of Virology

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Influenza a viruses with mutat ...... y of morphological phenotypes.

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David A Steinhauer

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John J Skehel

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Laura M Burleigh

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Lesley J Calder

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P2860

Effect of mutations affecting the p6 gag protein on human immunodeficiency virus particle release

Transport of incoming influenza virus nucleocapsids into the nucleus

Combined results from solution studies on intact influenza virus M1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer

Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1

In vitro dissection of the membrane and RNP binding activities of influenza virus M1 protein.

Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses.

Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent

Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine

Escaping from the cell: assembly and budding of negative-strand RNA viruses

Generation of influenza A viruses entirely from cloned cDNAs

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1262-1270

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scholarly article

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10.1128/JVI.79.2.1262-1270.2005

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2

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2005-01-01T00:00:00Z

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538569

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