Monomeric Nucleoprotein of Influenza A Virus - Test2 - elhamkhani - TriplyDB

Monomeric Nucleoprotein of Influenza A Virus

Monomeric Nucleoprotein of Influenza A Virus

http://www.wikidata.org/entity/Q27677207

about

Structure-based discovery of the novel antiviral properties of naproxen against the nucleoprotein of influenza A virus.Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic Strategies Nucleocytoplasmic shuttling of influenza A virus proteins Time-Resolved Visualisation of Nearly-Native Influenza A Virus Progeny Ribonucleoproteins and Their Individual Components in Live Infected Cells Structural basis for encapsidation of genomic RNA by La Crosse Orthobunyavirus nucleoprotein The crystal structure and RNA-binding of an orthomyxovirus nucleoprotein A Novel Antiviral Target Structure Involved in the RNA Binding, Dimerization, and Nuclear Export Functions of the Influenza A Virus Nucleoprotein Interactome analysis of the influenza A virus transcription/replication machinery identifies protein phosphatase 6 as a cellular factor required for efficient virus replication.Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis.CNOT4-Mediated Ubiquitination of Influenza A Virus Nucleoprotein Promotes Viral RNA Replication.Common mechanism for RNA encapsidation by negative-strand RNA viruses.Insight into the Ebola virus nucleocapsid assembly mechanism: crystal structure of Ebola virus nucleoprotein core domain at 1.8 Å resolution Phosphorylation at the homotypic interface regulates nucleoprotein oligomerization and assembly of the influenza virus replication machinery Phosphorylation controls the nuclear-cytoplasmic shuttling of influenza A virus nucleoprotein Structure-based design of novel naproxen derivatives targeting monomeric nucleoprotein of Influenza A virus.Binding of RNA by the Nucleoproteins of Influenza Viruses A and B.A Nucleolar Protein, Ribosomal RNA Processing 1 Homolog B (RRP1B), Enhances the Recruitment of Cellular mRNA in Influenza Virus Transcription.Deep mutational scanning identifies sites in influenza nucleoprotein that affect viral inhibition by MxA Ubiquitination up-regulates influenza virus polymerase function.Influenza virus nucleoprotein: structure, RNA binding, oligomerization and antiviral drug target.Antiviral strategies against influenza virus: towards new therapeutic approaches.Learning from structure-based drug design and new antivirals targeting the ribonucleoprotein complex for the treatment of influenza.Rapid and Direct VHH and Target Identification by Staphylococcal Surface Display Libraries Influenza A Virus Nucleoprotein: A Highly Conserved Multi-Functional Viral Protein as a Hot Antiviral Drug Target.Synergy of two low-affinity NLSs determines the high avidity of influenza A virus nucleoprotein NP for human importin α isoforms.Influenza virus recruits host protein kinase C to control assembly and activity of its replication machinery.Mechanism of preferential packaging of negative sense genomic RNA by viral nucleoproteins in Crimean-Congo hemorrhagic Fever virus.Structural characterization of recombinant IAV polymerase reveals a stable complex between viral PA-PB1 heterodimer and host RanBP5.Structural studies of influenza virus RNPs by electron microscopy indicate molecular contortions within NP supra-structures.Influenza A virus nucleoprotein targets subnuclear structures.Threonine 80 phosphorylation of non-structural protein 1 regulates the replication of influenza A virus by reducing the binding affinity with RIG-I.Potyvirus virion structure shows conserved protein fold and RNA binding site in ssRNA viruses.Regulation of influenza A virus nucleoprotein oligomerization by phosphorylation Mutations Conferring Increased Sensitivity to Tripartite Motif 22 Restriction Accumulated Progressively in the Nucleoprotein of Seasonal Influenza A (H1N1) Viruses between 1918 and 2009.In silico Structural characterization of podocin and assessment of nephrotic syndrome-associated podocin mutants.

P2860

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P2860

Monomeric Nucleoprotein of Influenza A Virus

http://www.wikidata.org/entity/Q27677207

description

2013 nî lūn-bûn

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2013 թուականի Մարտին հրատարակուած գիտական յօդուած

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2013 թվականի մարտին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

@zh-hk

2013年論文

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2013年論文

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2013年论文

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name

Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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type

label

Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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prefLabel

Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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Monomeric Nucleoprotein of Influenza A Virus

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JOURNAL.PPAT.1003275

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Monomeric nucleoprotein of influenza A virus

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P2093

Anny Slama-Schwok

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

Bernard Delmas

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

Carmelo Di Primo

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

Florence Baudin

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

Rob W H Ruigrok

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

Sylvie Chenavas

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

Xinping Li

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

P2860

The hexamer structure of Rift Valley fever virus nucleoprotein suggests a mechanism for its assembly into ribonucleoprotein complexes

The structure of a biologically active influenza virus ribonucleoprotein complex

The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA

Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine design

Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation

Cap binding and immune evasion revealed by Lassa nucleoprotein structure

Structure of the Lassa virus nucleoprotein reveals a dsRNA-specific 3' to 5' exonuclease activity essential for immune suppression

Inhibition of influenza virus replication via small molecules that induce the formation of higher-order nucleoprotein oligomers

Structure of the Vesicular Stomatitis Virus N0-P Complex

Phleboviruses encapsidate their genomes by sequestering RNA bases

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e1003275

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scholarly article

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2206509

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10.1371/JOURNAL.PPAT.1003275

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3

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9

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Leandro F Estrozi

Thibaut Crépin

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2013-03-28T00:00:00Z

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236106136

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23555270

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3610751

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