Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
about
Influenza B and C virus NEP (NS2) proteins possess nuclear export activities.HIV-1 Vpr interacts with the nuclear transport pathway to promote macrophage infectionCrystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)Nuclear import and export of influenza virus nucleoprotein.The Influenza A Virus Genotype Determines the Antiviral Function of NF-κBInterferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids.Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrierUsing single-particle tracking to study nuclear trafficking of viral genes.Role of the influenza virus M1 protein in nuclear export of viral ribonucleoproteins.The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteinsViruses, microorganisms and scientists meet the nuclear pore. Leysin, VD, Switzerland, February 26-March 1, 1998.The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export.Individual influenza A virus mRNAs show differential dependence on cellular NXF1/TAP for their nuclear export.Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1A comprehensive map of the influenza A virus replication cycleChicken and duck myotubes are highly susceptible and permissive to influenza virus infection.Crystal structures of influenza A virus matrix protein M1: variations on a themeHeat shock protein 70 is related to thermal inhibition of nuclear export of the influenza virus ribonucleoprotein complex.Contributions of two nuclear localization signals of influenza A virus nucleoprotein to viral replication.Phosphorylation controls the nuclear-cytoplasmic shuttling of influenza A virus nucleoproteinFunctional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityThe 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 M1A Single Amino Acid in the M1 Protein Responsible for the Different Pathogenic Potentials of H5N1 Highly Pathogenic Avian Influenza Virus Strains.Nuclear import of influenza A viral ribonucleoprotein complexes is mediated by two nuclear localization sequences on viral nucleoprotein.Effect of M1 protein and low pH on nuclear transport of influenza virus ribonucleoproteinsAssociation of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.Identification and characterization of three novel nuclear export signals in the influenza A virus nucleoprotein.Cytoplasmic domain of influenza B virus BM2 protein plays critical roles in production of infectious virus.Human Heat shock protein 40 (Hsp40/DnaJB1) promotes influenza A virus replication by assisting nuclear import of viral ribonucleoproteins.Host Protein Moloney Leukemia Virus 10 (MOV10) Acts as a Restriction Factor of Influenza A Virus by Inhibiting the Nuclear Import of the Viral Nucleoprotein.Analysis of influenza B Virus NS1 protein trafficking reveals a novel interaction with nuclear speckle domainsDefective RNA replication and late gene expression in temperature-sensitive influenza viruses expressing deleted forms of the NS1 proteinMutational analysis of conserved amino acids in the influenza A virus nucleoprotein.Transport of the influenza virus genome from nucleus to nucleusTwo African swine fever virus proteins derived from a common precursor exhibit different nucleocytoplasmic transport activities.Generation of influenza A virus NS2 (NEP) mutants with an altered nuclear export signal sequence.Influenza B virus BM2 protein is a crucial component for incorporation of viral ribonucleoprotein complex into virions during virus assembly.Influenza virus entry and infection require host cell N-linked glycoprotein.Influenza a viruses with mutations in the m1 helix six domain display a wide variety of morphological phenotypes.
P2860
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P2860
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@ast
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@en
type
label
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@ast
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@en
prefLabel
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@ast
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@en
P2093
P2860
P1433
P1476
Nuclear trafficking of influenza virus ribonuleoproteins in heterokaryons
@en
P2093
P2860
P304
P407
P577
1996-05-01T00:00:00Z