A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.
about
Pandemic Threat Posed by Avian Influenza A VirusesStructure of the guanylyltransferase domain of human mRNA capping enzymeSpecific HDV RNA-templated transcription by pol II in vitroDefinition of the minimal viral components required for the initiation of unprimed RNA synthesis by influenza virus RNA polymeraseEnzymology of RNA cap synthesisHuman and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycleFunction and regulation of retinoic acid-inducible gene-IIdentification of potential conserved RNA secondary structure throughout influenza A coding regionsThe Feat of Packaging Eight Unique Genome SegmentsShutoff of Host Gene Expression in Influenza A Virus and Herpesviruses: Similar Mechanisms and Common ThemesDevelopment of next-generation respiratory virus vaccines through targeted modifications to viral immunomodulatory genesmRNA capping: biological functions and applicationsThe putative polymerase sequence of infectious salmon anemia virus suggests a new genus within the Orthomyxoviridae.An endonuclease switching mechanism in the virion RNA and cRNA promoters of Thogoto orthomyxovirusA second, non-canonical RNA-dependent RNA polymerase in SARS CoronavirusNucleoprotein viral RNA and mRNA of Thogoto virus: a novel "cap-stealing" mechanism in tick-borne orthomyxoviruses?The 5' ends of Thogoto virus (Orthomyxoviridae) mRNAs are homogeneous in both length and sequenceIn vitro polymerase activity of Thogoto virus: evidence for a unique cap-snatching mechanism in a tick-borne orthomyxovirusThe structural basis for cap binding by influenza virus polymerase subunit PB2Structural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymeraseBunyaviridae RNA Polymerases (L-Protein) Have an N-Terminal, Influenza-Like Endonuclease Domain, Essential for Viral Cap-Dependent TranscriptionThe N-Terminal Domain of the Arenavirus L Protein Is an RNA Endonuclease Essential in mRNA TranscriptionCap binding and immune evasion revealed by Lassa nucleoprotein structureCrystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 ComplexStructural and Biochemical Basis for Development of Influenza Virus Inhibitors Targeting the PA EndonucleaseStructural Analysis of Specific Metal Chelating Inhibitor Binding to the Endonuclease Domain of Influenza pH1N1 (2009) PolymeraseStructural and Functional Characterization of K339T Substitution Identified in the PB2 Subunit Cap-binding Pocket of Influenza A VirusCrystallographic Fragment Screening and Structure-Based Optimization Yields a New Class of Influenza Endonuclease InhibitorsConformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virusCrystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virusComparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domainsHigh-Resolution Structure of the N-Terminal Endonuclease Domain of the Lassa Virus L Polymerase in Complex with Magnesium Ions3-Hydroxyquinolin-2(1 H )-ones As Inhibitors of Influenza A EndonucleaseThe active sites of the influenza cap-dependent endonuclease are on different polymerase subunitsThe three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complexRecombinant influenza virus polymerase: requirement of both 5' and 3' viral ends for endonuclease activity.The influenza virus panhandle is involved in the initiation of transcription.The RNA polymerase of influenza virus, bound to the 5' end of virion RNA, acts in cis to polyadenylate mRNA.RNA-dependent activation of primer RNA production by influenza virus polymerase: different regions of the same protein subunit constitute the two required RNA-binding sites.The Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug Design
P2860
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P2860
A unique cap(m7GpppXm)-dependent influenza virion endonuclease cleaves capped RNAs to generate the primers that initiate viral RNA transcription.
description
1981 nî lūn-bûn
@nan
1981 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի մարտին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
name
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@ast
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@en
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@nl
type
label
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@ast
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@en
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@nl
altLabel
A unique cap(m7GpppXm)-depende ...... itiate viral RNA transcription
@en
prefLabel
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@ast
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@en
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@nl
P2093
P3181
P1433
P1476
A unique cap(m7GpppXm)-depende ...... tiate viral RNA transcription.
@en
P2093
P304
P3181
P356
10.1016/0092-8674(81)90449-9
P407
P577
1981-03-01T00:00:00Z