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.
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PA subunit from influenza virus polymerase complex interacts with a cellular protein with homology to a family of transcriptional activatorsStructural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymeraseFunctional analysis of PA binding by influenza a virus PB1: effects on polymerase activity and viral infectivity3D structure of the influenza virus polymerase complex: localization of subunit domains.Upolu virus and Aransas Bay virus, two presumptive bunyaviruses, are novel members of the family OrthomyxoviridaeSingle gene reassortants identify a critical role for PB1, HA, and NA in the high virulence of the 1918 pandemic influenza virusProgress in identifying virulence determinants of the 1918 H1N1 and the Southeast Asian H5N1 influenza A viruses.Full factorial analysis of mammalian and avian influenza polymerase subunits suggests a role of an efficient polymerase for virus adaptationNuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.Conservation and diversity of influenza A H1N1 HLA-restricted T cell epitope candidates for epitope-based vaccines.Postreassortment amino acid substitutions in influenza A viruses.Biological characterization of highly pathogenic avian influenza H5N1 viruses that infected humans in Egypt in 2014-2015.Polymerase activity of hybrid ribonucleoprotein complexes generated from reassortment between 2009 pandemic H1N1 and seasonal H3N2 influenza A viruses.Small molecule inhibitors of influenza A and B viruses that act by disrupting subunit interactions of the viral polymerase.Genetic trans-complementation establishes a new model for influenza virus RNA transcription and replication.Influenza A virus polymerase: structural insights into replication and host adaptation mechanismsMutational analyses of the influenza A virus polymerase subunit PA reveal distinct functions related and unrelated to RNA polymerase activity.Amino acid substitutions in PB1 of avian influenza viruses influence pathogenicity and transmissibility in chickens.Emerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.HMGB1 protein binds to influenza virus nucleoprotein and promotes viral replicationMolecular signature of high yield (growth) influenza a virus reassortants prepared as candidate vaccine seeds.Tracking the Evolution in Phylogeny, Structure and Function of H5N1 Influenza Virus PA Gene.TRIM32 Senses and Restricts Influenza A Virus by Ubiquitination of PB1 PolymeraseA new generation of modified live-attenuated avian influenza viruses using a two-strategy combination as potential vaccine candidates.Glycine at Position 622 in PB1 Contributes to the Virulence of H5N1 Avian Influenza Virus in Mice.Three amino acid changes in PB1-F2 of highly pathogenic H5N1 avian influenza virus affect pathogenicity in mallard ducks.Compatibility among polymerase subunit proteins is a restricting factor in reassortment between equine H7N7 and human H3N2 influenza viruses.A complicated message: Identification of a novel PB1-related protein translated from influenza A virus segment 2 mRNA.A quantitative strategy to detect changes in accessibility of protein regions to chemical modification on heterodimerization.The influenza virus RNA synthesis machine: advances in its structure and function.Antiviral strategies against influenza virus: towards new therapeutic approaches.Polycistronic Expression of the Influenza A Virus RNA-Dependent RNA Polymerase by Using the Thosea asigna Virus 2A-Like Self-Processing Sequence.Molecular interactions and trafficking of influenza A virus polymerase proteins analyzed by specific monoclonal antibodies.Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences.Characterization of influenza virus PB1 protein binding to viral RNA: two separate regions of the protein contribute to the interaction domain.The replication activity of influenza virus polymerase is linked to the capacity of the PA subunit to induce proteolysis.Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification.Influenza A virus polymerase inhibits type I interferon induction by binding to interferon beta promoter stimulator 1.A single amino acid mutation in the PA subunit of the influenza virus RNA polymerase inhibits endonucleolytic cleavage of capped RNAs.Mutations in the N-terminal region of influenza virus PB2 protein affect virus RNA replication but not transcription.
P2860
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P2860
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.
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Identification of two separate ...... iral RNA polymerase structure.
@ast
Identification of two separate ...... iral RNA polymerase structure.
@en
Identification of two separate ...... iral RNA polymerase structure.
@nl
type
label
Identification of two separate ...... iral RNA polymerase structure.
@ast
Identification of two separate ...... iral RNA polymerase structure.
@en
Identification of two separate ...... iral RNA polymerase structure.
@nl
altLabel
Identification of two separate ...... viral RNA polymerase structure
@en
prefLabel
Identification of two separate ...... iral RNA polymerase structure.
@ast
Identification of two separate ...... iral RNA polymerase structure.
@en
Identification of two separate ...... iral RNA polymerase structure.
@nl
P2860
P356
P1476
Identification of two separate ...... viral RNA polymerase structure
@en
P2093
P2860
P304
P356
10.1093/NAR/24.22.4456
P407
P50
P577
1996-11-01T00:00:00Z