A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-beta and the viral helicase, NS3.
about
Molecular targets for flavivirus drug discoveryThe role of viral persistence in flavivirus biologyStructure and functionality in flavivirus NS-proteins: perspectives for drug designA physical interaction network of dengue virus and human proteinsStructural proteomics of dengue virusFlaviviral Replication Complex: Coordination between RNA Synthesis and 5'-RNA CappingCommon and unique features of viral RNA-dependent polymerasesA crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replicationStructure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing.Dengue virus nonstructural protein NS5 induces interleukin-8 transcription and secretion.Derivation and characterization of a dengue type 1 host range-restricted mutant virus that is attenuated and highly immunogenic in monkeys.Complementation analysis of the flavivirus Kunjin NS3 and NS5 proteins defines the minimal regions essential for formation of a replication complex and shows a requirement of NS3 in cis for virus assembly.Paired charge-to-alanine mutagenesis of dengue virus type 4 NS5 generates mutants with temperature-sensitive, host range, and mouse attenuation phenotypes.Structure-Based Mutational Analysis of the NS3 Helicase from Dengue VirusCrystal Structure of the Dengue Virus RNA-Dependent RNA Polymerase Catalytic Domain at 1.85-Angstrom ResolutionCrystal Structure of the NS3 Protease-Helicase from Dengue VirusA complex RNA motif defined by three discontinuous 5-nucleotide-long strands is essential for Flavivirus RNA replicationGenomic Epidemiology of a Dengue Virus Epidemic in Urban SingaporeCRM1-mediated Nuclear Export of Dengue Virus RNA Polymerase NS5 Modulates Interleukin-8 Induction and Virus ProductionCrystal Structure of a Novel Conformational State of the Flavivirus NS3 Protein: Implications for Polyprotein Processing and Viral ReplicationFocus on flaviviruses: current and future drug targetsCrystal Structure of the Dengue Virus Methyltransferase Bound to a 5′-Capped Octameric RNACrystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interfaceFlavivirus NS3 and NS5 proteins interaction network: a high-throughput yeast two-hybrid screenIdentification of new protein interactions between dengue fever virus and its hosts, human and mosquitoThe interface between methyltransferase and polymerase of NS5 is essential for flavivirus replicationPerturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongationA brief review on dengue molecular virology, diagnosis, treatment and prevalence in PakistanThe crystal structure of Zika virus NS5 reveals conserved drug targetsThe IMPORTance of the Nucleus during Flavivirus Replication.Potential Antivirals: Natural Products Targeting Replication Enzymes of Dengue and Chikungunya Viruses.Nsp9 and Nsp10 contribute to the fatal virulence of highly pathogenic porcine reproductive and respiratory syndrome virus emerging in China.Substitution of NS5 N-terminal domain of dengue virus type 2 RNA with type 4 domain caused impaired replication and emergence of adaptive mutants with enhanced fitness.Functional analysis of two cavities in flavivirus NS5 polymeraseThe C-terminal 50 amino acid residues of dengue NS3 protein are important for NS3-NS5 interaction and viral replicationProfiling of viral proteins expressed from the genomic RNA of Japanese encephalitis virus using a panel of 15 region-specific polyclonal rabbit antisera: implications for viral gene expression.A Combined Genetic-Proteomic Approach Identifies Residues within Dengue Virus NS4B Critical for Interaction with NS3 and Viral ReplicationPoint mutations in the West Nile virus (Flaviviridae; Flavivirus) RNA-dependent RNA polymerase alter viral fitness in a host-dependent manner in vitro and in vivoDengue Virus Nonstructural Protein 5 (NS5) Assembles into a Dimer with a Unique Methyltransferase and Polymerase InterfaceDengue virus nonstructural protein 5 adopts multiple conformations in solution.
P2860
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P2860
A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-beta and the viral helicase, NS3.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
A small region of the dengue v ...... a and the viral helicase, NS3.
@en
type
label
A small region of the dengue v ...... a and the viral helicase, NS3.
@en
prefLabel
A small region of the dengue v ...... a and the viral helicase, NS3.
@en
P2093
P1476
A small region of the dengue v ...... a and the viral helicase, NS3.
@en
P2093
Johansson M
Vasudevan SG
P304
P356
10.1099/0022-1317-82-4-735
P407
P577
2001-04-01T00:00:00Z