Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
about
Identification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus MethyltransferaseCrystal structure of RlmM, the 2'O-ribose methyltransferase for C2498 of Escherichia coli 23S rRNACrystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interfaceNovel Broad Spectrum Inhibitors Targeting the Flavivirus MethyltransferasePerturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongationInfectious DNAs derived from insect-specific flavivirus genomes enable identification of pre- and post-entry host restrictions in vertebrate cellsPredicted structure and domain organization of rotavirus capping enzyme and innate immune antagonist VP3Substitution 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.S-adenosyl-homocysteine is a weakly bound inhibitor for a flaviviral methyltransferaseAptamer Displacement Screen for Flaviviral RNA Methyltransferase Inhibitors.Dengue 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.Experimental therapies for yellow feverSelective inhibition of the West Nile virus methyltransferase by nucleoside analogs.Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.Flavivirus RNA synthesis in vitroRefolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase.Structure and function of Zika virus NS5 protein: perspectives for drug design.The structure of the binary methyltransferase-SAH complex from Zika virus reveals a novel conformation for the mechanism of mRNA capping.
P2860
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P2860
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@ast
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@en
type
label
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@ast
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@en
prefLabel
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@ast
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@en
P2093
P2860
P1433
P1476
Flavivirus RNA cap methyltransferase: structure, function, and inhibition.
@en
P2093
P2860
P2888
P304
P356
10.1007/S11515-010-0660-Y
P577
2010-08-01T00:00:00Z