Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2) - Wikidata - awgldk - TriplyDB

Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

http://www.wikidata.org/entity/Q27642013

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Emerging roles for the influenza A virus nuclear export protein (NEP)The interaction between the PARP10 protein and the NS1 protein of H5N1 AIV and its effect on virus replication Genomic signatures of human versus avian influenza A viruses The Feat of Packaging Eight Unique Genome Segments Nucleocytoplasmic shuttling of influenza A virus proteins Recent progress in structure-based anti-influenza drug design The Skap-hom Dimerization and PH Domains Comprise a 3′-Phosphoinositide-Gated Molecular Switch Plant Actin-binding Protein SCAB1 Is Dimeric Actin Cross-linker with Atypical Pleckstrin Homology Domain 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 Specific residues in the 2009 H1N1 swine-origin influenza matrix protein influence virion morphology and efficiency of viral spread in vitro A Novel Antiviral Target Structure Involved in the RNA Binding, Dimerization, and Nuclear Export Functions of the Influenza A Virus Nucleoprotein Extreme evolutionary conservation of functionally important regions in H1N1 influenza proteome.Characteristics of nucleocytoplasmic transport of H1N1 influenza A virus nuclear export protein.Persistent host markers in pandemic and H5N1 influenza viruses Survival analysis of infected mice reveals pathogenic variations in the genome of avian H1N1 viruses Complete-proteome mapping of human influenza A adaptive mutations: implications for human transmissibility of zoonotic strains.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.Surveillance in Eastern India (2007-2009) revealed reassortment event involving NS and PB1-F2 gene segments among co-circulating influenza A subtypes.Evolutionary characterization of the pandemic H1N1/2009 influenza virus in humans based on non-structural genes.Structural organization of a filamentous influenza A virus.Prediction of protein-protein interaction sites using an ensemble method.Attenuating mutations of the matrix gene of influenza A/WSN/33 virus.The nuclear export protein of H5N1 influenza A viruses recruits Matrix 1 (M1) protein to the viral ribonucleoprotein to mediate nuclear export.A crucial role of N-terminal domain of influenza A virus M1 protein in interaction with swine importin α1 protein.Influenza virus ribonucleoprotein complexes gain preferential access to cellular export machinery through chromatin targeting.Comparative analysis of seven viral nuclear export signals (NESs) reveals the crucial role of nuclear export mediated by the third NES consensus sequence of nucleoprotein (NP) in influenza A virus replication.Nucleolin interacts with influenza A nucleoprotein and contributes to viral ribonucleoprotein complexes nuclear trafficking and efficient influenza viral replication.Influenza A: understanding the viral life cycle Multifunctional adaptive NS1 mutations are selected upon human influenza virus evolution in the mouse.Appearance of L90I and N205S Mutations in Effector Domain of NS1 Gene of pdm (09) H1N1 Virus from India during 2009-2013.Structure-based design of NS2 mutants for attenuated influenza A virus vaccines YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 Interaction of NS2 with AIMP2 facilitates the switch from ubiquitination to SUMOylation of M1 in influenza A virus-infected cells.A comprehensive map of the influenza A virus replication cycle Cell penetrable human scFv specific to middle domain of matrix protein-1 protects mice from lethal influenza.Human immunodeficiency virus rev-binding protein is essential for influenza a virus replication and promotes genome trafficking in late-stage infection.Cellular networks involved in the influenza virus life cycle.Crystal structures of influenza A virus matrix protein M1: variations on a theme A nuclear export signal in the matrix protein of Influenza A virus is required for efficient virus replication.Identification of combinatorial host-specific signatures with a potential to affect host adaptation in influenza A H1N1 and H3N2 subtypes.

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Crystal structure of the M1 protein-binding domain of the influenza A virus nuclear export protein (NEP/NS2)

http://www.wikidata.org/entity/Q27642013

description

2003 nî lūn-bûn

@nan

2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

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The EMBO Journal

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Crystal structure of the M1 pr ...... clear export protein (NEP/NS2)

@en

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Carlo Petosa

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Florence Baudin

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Isabelle Petit

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Rob W H Ruigrok

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P2860

Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor

Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1

Influenza B and C virus NEP (NS2) proteins possess nuclear export activities.

CRM1-mediated recycling of snurportin 1 to the cytoplasm

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin alpha

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

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin alpha

CRM1 is an export receptor for leucine-rich nuclear export signals

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4646-4655

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271357

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10.1093/EMBOJ/CDG449

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18

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22

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Wim P Burmeister

Christoph W Müller

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2003-09-01T00:00:00Z

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5265003

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12970177

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protein structure

crystal structure

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212717

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