Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits - Wikidata - awgldk - TriplyDB

Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits

Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits

http://www.wikidata.org/entity/Q35635186

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Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome Human butyrate-induced transcript 1 interacts with hepatitis C virus NS5A and regulates viral replication Cochaperone Activity of Human Butyrate-Induced Transcript 1 Facilitates Hepatitis C Virus Replication through an Hsp90-Dependent Pathway Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 Subunit The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part I: Influenza life-cycle and currently available drugs Inhibition of heat-shock protein 90 reduces Ebola virus replication Heat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivo Heat-shock protein 90 promotes nuclear transport of herpes simplex virus 1 capsid protein by interacting with acetylated tubulin Heat shock protein 90 positively regulates Chikungunya virus replication by stabilizing viral non-structural protein nsP2 during infection Hsp90 protein interacts with phosphorothioate oligonucleotides containing hydrophobic 2'-modifications and enhances antisense activity Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase.Interplay between influenza A virus and host factors: targets for antiviral intervention.Full factorial analysis of mammalian and avian influenza polymerase subunits suggests a role of an efficient polymerase for virus adaptation Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.The innate immunity of guinea pigs against highly pathogenic avian influenza virus infection Influenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activation Interferon-inducible protein Mx1 inhibits influenza virus by interfering with functional viral ribonucleoprotein complex assembly The host-dependent interaction of alpha-importins with influenza PB2 polymerase subunit is required for virus RNA replication.A key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes.Artificial hybrids of influenza A virus RNA polymerase reveal PA subunit modulates its thermal sensitivity.Hsp90 directly modulates the spatial distribution of AF9/MLLT3 and affects target gene expression.Influenza virus infection induces the nuclear relocalization of the Hsp90 co-chaperone p23 and inhibits the glucocorticoid receptor response.Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.Protein analysis of purified respiratory syncytial virus particles reveals an important role for heat shock protein 90 in virus particle assembly.Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I.Hsp90 interacts specifically with viral RNA and differentially regulates replication initiation of Bamboo mosaic virus and associated satellite RNA HMGB1 protein binds to influenza virus nucleoprotein and promotes viral replication Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation NP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.A cell-based screening system for influenza A viral RNA transcription/replication inhibitors DnaJA1/Hsp40 is co-opted by influenza A virus to enhance its viral RNA polymerase activity Interaction of the influenza A virus polymerase PB2 C-terminal region with importin alpha isoforms provides insights into host adaptation and polymerase assembly.The NS1 protein of influenza A virus interacts with heat shock protein Hsp90 in human alveolar basal epithelial cells: implication for virus-induced apoptosis.Active participation of cellular chaperone Hsp90 in regulating the function of rotavirus nonstructural protein 3 (NSP3).Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin.Comprehensive proteomic analysis of influenza virus polymerase complex reveals a novel association with mitochondrial proteins and RNA polymerase accessory factors Cell death regulation during influenza A virus infection by matrix (M1) protein: a model of viral control over the cellular survival pathway

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P2860

Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunits

http://www.wikidata.org/entity/Q35635186

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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P1433

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P1433

Journal of Virology

P1476

Involvement of Hsp90 in assemb ...... virus RNA polymerase subunits

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P2093

Atsushi Kawaguchi

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Fumitaka Momose

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Kyosuke Nagata

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Tadasuke Naito

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P2860

PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activators

Role of ran binding protein 5 in nuclear import and assembly of the influenza virus RNA polymerase complex

High-efficiency transformation of mammalian cells by plasmid DNA

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

The active sites of the influenza cap-dependent endonuclease are on different polymerase subunits

The NPI-1/NPI-3 (karyopherin alpha) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal.

Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein

NPI-1, the human homolog of SRP-1, interacts with influenza virus nucleoprotein

Two signals mediate nuclear localization of influenza virus (A/WSN/33) polymerase basic protein 2

Structure and mechanism of the Hsp90 molecular chaperone machinery

P304

1339-1349

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scholarly article

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10.1128/JVI.01917-06

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3

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81

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2006-11-22T00:00:00Z

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6675854

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17121807

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P921

travel-associated infection

P932

1797515

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