Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymerase - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q27655568

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Enzymology of RNA cap synthesis Recent progress in structure-based anti-influenza drug design Evidence for a Novel Mechanism of Influenza Virus-Induced Type I Interferon Expression by a Defective RNA-Encoded Protein mRNA capping: biological functions and applications Structural and Biochemical Basis for Development of Influenza Virus Inhibitors Targeting the PA Endonuclease Structural and Functional Characterization of K339T Substitution Identified in the PB2 Subunit Cap-binding Pocket of Influenza A Virus The N-Terminal Domain of PA from Bat-Derived Influenza-Like Virus H17N10 Has Endonuclease Activity Conformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virus Structural analysis of H1N1 and H7N9 influenza A virus PA in the absence of PB1 The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design New small-molecule drug design strategies for fighting resistant influenza A Compounds with anti-influenza activity: present and future of strategies for the optimal treatment and management of influenza. Part II: Future compounds against influenza virus Tracking the Evolution of Polymerase Genes of Influenza A Viruses during Interspecies Transmission between Avian and Swine Hosts Identification of a PA-binding peptide with inhibitory activity against influenza A and B virus replication The N-terminal fragment of a PB2 subunit from the influenza A virus (A/Hong Kong/156/1997 H5N1) effectively inhibits RNP activity and viral replication Identification of high-affinity PB1-derived peptides with enhanced affinity to the PA protein of influenza A virus polymerase Progress of small molecular inhibitors in the development of anti-influenza virus agents.Conserved features of the PB2 627 domain impact influenza virus polymerase function and replication Survival analysis of infected mice reveals pathogenic variations in the genome of avian H1N1 viruses Phylogenetic Analysis and Functional Characterization of the Influenza A H5N1 PB2 Gene.Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.Structures of influenza A proteins and insights into antiviral drug targets.Rapid acquisition of polymorphic virulence markers during adaptation of highly pathogenic avian influenza H5N8 virus in the mouse Polymerase activity of hybrid ribonucleoprotein complexes generated from reassortment between 2009 pandemic H1N1 and seasonal H3N2 influenza A viruses.Interferon-inducible protein Mx1 inhibits influenza virus by interfering with functional viral ribonucleoprotein complex assembly Virulence determinants of pandemic A(H1N1)2009 influenza virus in a mouse model.Characterization in vitro and in vivo of a pandemic H1N1 influenza virus from a fatal case.Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrier Influenza virus RNA polymerase: insights into the mechanisms of viral RNA synthesis.Innate immune evasion strategies of influenza viruses Hantavirus nucleocapsid protein has distinct m7G cap- and RNA-binding sites.CoESPRIT: a library-based construct screening method for identification and expression of soluble protein complexes Influenza A virus-generated small RNAs regulate the switch from transcription to replication.Association of the influenza virus RNA polymerase subunit PB2 with the host chaperonin CCT.The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon.Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms A novel functional site in the PB2 subunit of influenza A virus essential for acetyl-CoA interaction, RNA polymerase activity, and viral replication.Structural and functional characterization of an influenza virus RNA polymerase-genomic RNA complex Detecting remote sequence homology in disordered proteins: discovery of conserved motifs in the N-termini of Mononegavirales phosphoproteins Amino acid substitutions in PB1 of avian influenza viruses influence pathogenicity and transmissibility in chickens.

P2860

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P2860

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

http://www.wikidata.org/entity/Q27655568

description

2009 nî lūn-bûn

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2009 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունիսին 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

@zh-hant

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

Structural insight into the es ...... influenza virus RNA polymerase

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Structural insight into the es ...... influenza virus RNA polymerase

@en

Structural insight into the es ...... influenza virus RNA polymerase

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type

label

Structural insight into the es ...... influenza virus RNA polymerase

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Structural insight into the es ...... influenza virus RNA polymerase

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Structural insight into the es ...... influenza virus RNA polymerase

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Structural insight into the es ...... influenza virus RNA polymerase

@ast

Structural insight into the es ...... influenza virus RNA polymerase

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Structural insight into the es ...... influenza virus RNA polymerase

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The EMBO Journal

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Structural insight into the es ...... influenza virus RNA polymerase

@en

P2093

Atsushi Kawaguchi

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

Eiji Obayashi

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

Jeremy R H Tame

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Kanako Sugiyama

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

Kyosuke Nagata

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

Sam-Yong Park

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Yukari Suzuki

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

P2860

Structural basis for the transition from initiation to elongation transcription in T7 RNA polymerase

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

The structural basis for cap binding by influenza virus polymerase subunit PB2

Crystal structure of the polymerase PA(C)-PB1(N) complex from an avian influenza H5N1 virus

The structural basis for an essential subunit interaction in influenza virus RNA polymerase

Host Determinant Residue Lysine 627 Lies on the Surface of a Discrete, Folded Domain of Influenza Virus Polymerase PB2 Subunit

Crystal structure of an avian influenza polymerase PA(N) reveals an endonuclease active site

The cap-snatching endonuclease of influenza virus polymerase resides in the PA subunit

Inference of macromolecular assemblies from crystalline state

SOLVE and RESOLVE: automated structure solution and density modification

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1803-11

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scholarly article

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2206487

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10.1038/EMBOJ.2009.138

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12

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28

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2009-06-17T00:00:00Z

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24445704

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19461581

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2699363

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