The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding. - Wikidata - awgldk - TriplyDB

The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.

The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.

http://www.wikidata.org/entity/Q36933890

about

Influenza A virus coding regions exhibit host-specific global ordered RNA structure Influenza virus M2 protein mediates ESCRT-independent membrane scission Relevance of Viroporin Ion Channel Activity on Viral Replication and Pathogenesis Recent progress in structure-based anti-influenza drug design Viral membrane scission Identification of a novel splice variant form of the influenza A virus M2 ion channel with an antigenically distinct ectodomain Solution structure and functional analysis of the influenza B proton channel Influenza M2 proton channels Specific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitro Broad-Range Antiviral Activity of Hydrogen Sulfide Against Highly Pathogenic RNA Viruses Influenza virus M2 protein ion channel activity helps to maintain pandemic 2009 H1N1 virus hemagglutinin fusion competence during transport to the cell surface.Critical assessment of influenza VLP production in Sf9 and HEK293 expression systems.Universal M2 ectodomain-based influenza A vaccines: preclinical and clinical developments.Evolution of the M gene of the influenza A virus in different host species: large-scale sequence analysis.Influenza A virus ribonucleoproteins modulate host recycling by competing with Rab11 effectors.Caveolin-1 influences human influenza A virus (H1N1) multiplication in cell culture.Role of the B Allele of Influenza A Virus Segment 8 in Setting Mammalian Host Range and Pathogenicity.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.Mutations in the membrane-proximal region of the influenza A virus M2 protein cytoplasmic tail have modest effects on virus replication.Novel vaccines against influenza viruses.Influenza A virus uses intercellular connections to spread to neighboring cells Conformational analysis of the full-length M2 protein of the influenza A virus using solid-state NMR.Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain A coevolution analysis for identifying protein-protein interactions by Fourier transform Influenza virus m2 ion channel protein is necessary for filamentous virion formation.A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Tyrosines in the influenza A virus M2 protein cytoplasmic tail are critical for production of infectious virus particles 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.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Effect of envelope proteins on the mechanical properties of influenza virus Role of the CM2 protein in the influenza C virus replication cycle At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.Influenza virus budding does not require a functional AAA+ ATPase, VPS4 Colocalization of different influenza viral RNA segments in the cytoplasm before viral budding as shown by single-molecule sensitivity FISH analysis.Photoinduced electron transfer and fluorophore motion as a probe of the conformational dynamics of membrane proteins: application to the influenza a M2 proton channel Influenza virus assembly and budding.RAB11A is essential for transport of the influenza virus genome to the plasma membrane.Influence of solubilizing environments on membrane protein structures A pH-dependent conformational ensemble mediates proton transport through the influenza A/M2 protein Quantitative analysis of the lipidomes of the influenza virus envelope and MDCK cell apical membrane

P2860

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P2860

The influenza virus M2 protein cytoplasmic tail interacts with the M1 protein and influences virus assembly at the site of virus budding.

http://www.wikidata.org/entity/Q36933890

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

The influenza virus M2 protein ...... at the site of virus budding.

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type

label

The influenza virus M2 protein ...... at the site of virus budding.

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The influenza virus M2 protein ...... at the site of virus budding.

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P1433

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Journal of Virology

P1476

The influenza virus M2 protein ...... at the site of virus budding.

@en

P2093

Benjamin J Chen

http://www.w3.org/2001/XMLSchema#string

David Jackson

http://www.w3.org/2001/XMLSchema#string

George P Leser

http://www.w3.org/2001/XMLSchema#string

Robert A Lamb

http://www.w3.org/2001/XMLSchema#string

P2860

Efficient selection for high-expression transfectants with a novel eukaryotic vector

Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.

The influenza A virus M2 cytoplasmic tail is required for infectious virus production and efficient genome packaging

Mechanism for proton conduction of the M(2) ion channel of influenza A virus

Sequences of mRNAs derived from genome RNA segment 7 of influenza virus: colinear and interrupted mRNAs code for overlapping proteins

Generation of influenza A viruses entirely from cloned cDNAs

Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells.

The M2 ectodomain is important for its incorporation into influenza A virions.

Influenza virus assembly and lipid raft microdomains: a role for the cytoplasmic tails of the spike glycoproteins.

Effect of cytoplasmic tail truncations on the activity of the M(2) ion channel of influenza A virus.

P304

10059-10070

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scholarly article

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10.1128/JVI.01184-08

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20

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82

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2008-08-13T00:00:00Z

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23169326

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18701586

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2566248

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