Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy. - Wikidata - wikimedia - TriplyDB

Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.

Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.

http://www.wikidata.org/entity/Q30382441

about

Apical transport of influenza A virus ribonucleoprotein requires Rab11-positive recycling endosome Perspective of Use of Antiviral Peptides against Influenza Virus Respiratory virus modulation of host nucleocytoplasmic transport; target for therapeutic intervention?ARHGEF17 is an essential spindle assembly checkpoint factor that targets Mps1 to kinetochores Time-Resolved Visualisation of Nearly-Native Influenza A Virus Progeny Ribonucleoproteins and Their Individual Components in Live Infected Cells mRNA capping: biological functions and applications Dual-color fluorescence lifetime correlation spectroscopy to quantify protein-protein interactions in live cell.Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms Mutational analyses of the influenza A virus polymerase subunit PA reveal distinct functions related and unrelated to RNA polymerase activity.Human-like PB2 627K influenza virus polymerase activity is regulated by importin-α1 and -α7.Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complex Interactions between the influenza A virus RNA polymerase components and retinoic acid-inducible gene I.Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocation Importin α3/Qip1 is involved in multiplication of mutant influenza virus with alanine mutation at amino acid 9 independently of nuclear transport function Influenza A viruses with different amino acid residues at PB2-627 display distinct replication properties in vitro and in vivo: revealing the sequence plasticity of PB2-627 position Interaction of the influenza A virus polymerase PB2 C-terminal region with importin alpha isoforms provides insights into host adaptation and polymerase assembly.Intracellular expression of camelid single-domain antibodies specific for influenza virus nucleoprotein uncovers distinct features of its nuclear localization.Antibodies to the core proteins of Nairobi sheep disease virus/Ganjam virus reveal details of the distribution of the proteins in infected cells and tissues Temperature-Sensitive Mutants in the Influenza A Virus RNA Polymerase: Alterations in the PA Linker Reduce Nuclear Targeting of the PB1-PA Dimer and Result in Viral Attenuation Factors affecting the quantification of biomolecular interactions by fluorescence cross-correlation spectroscopy.Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.Codon Deletions in the Influenza A Virus PA Gene Generate Temperature-Sensitive Viruses.Transport of the influenza virus genome from nucleus to nucleus The influenza virus RNA synthesis machine: advances in its structure and function.Recent applications of fluorescence correlation spectroscopy in live systems.Role of the PB2 627 Domain in Influenza A Virus Polymerase Function The RNA-dependent RNA polymerase of the influenza A virus.Molecular interactions and trafficking of influenza A virus polymerase proteins analyzed by specific monoclonal antibodies.Replication-competent influenza A virus that encodes a split-green fluorescent protein-tagged PB2 polymerase subunit allows live-cell imaging of the virus life cycle.Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1.Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5.Correcting for spectral cross-talk in dual-color fluorescence cross-correlation spectroscopy Regulation of influenza RNA polymerase activity and the switch between replication and transcription by the concentrations of the vRNA 5' end, the cap source, and the polymerase.A peptide derived from the C-terminus of PB1 inhibits influenza virus replication by interfering with viral polymerase assembly.Dual-color fluorescence cross-correlation spectroscopy on a planar optofluidic chip.Quantifying Membrane Protein Oligomerization with Fluorescence Cross-Correlation Spectroscopy.Influenza A Virus Cell Entry, Replication, Virion Assembly and Movement

P2860

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P2860

Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.

http://www.wikidata.org/entity/Q30382441

description

2009 nî lūn-bûn

@nan

2009 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Nuclear import and assembly of ...... ross-correlation spectroscopy.

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Nuclear import and assembly of ...... ross-correlation spectroscopy.

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type

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Nuclear import and assembly of ...... ross-correlation spectroscopy.

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Nuclear import and assembly of ...... ross-correlation spectroscopy.

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Nuclear import and assembly of ...... ross-correlation spectroscopy.

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Nuclear import and assembly of ...... ross-correlation spectroscopy.

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P1433

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P1433

Journal of Virology

P1476

Nuclear import and assembly of ...... ross-correlation spectroscopy.

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P2093

Lars Ferbitz

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Nathalie Daigle

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Sergiy V Avilov

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Sébastien Huet

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P2860

Evolution and ecology of influenza A viruses

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

Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunit

Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymerase

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein

Nuclear traffic of influenza virus proteins and ribonucleoprotein complexes.

Nuclear location of all three influenza polymerase proteins and a nuclear signal in polymerase PB2

Identification of two separate domains in the influenza virus PB1 protein involved in the interaction with the PB2 and PA subunits: a model for the viral RNA polymerase structure.

Spatial regulation of Fus3 MAP kinase activity through a reaction-diffusion mechanism in yeast pheromone signalling.

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

P304

1254-1264

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scholarly article

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10.1128/JVI.01533-09

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3

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P478

84

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Stephen Anthony Cusack

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2009-11-11T00:00:00Z

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38083433

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P698

19906916

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P921

travel-associated infection

P932

2812328

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