Structural bases for substrate recognition and activity in Meaban virus nucleoside-2′-O-methyltransferase
about
Identification of a novel antiviral inhibitor of the flavivirus guanylyltransferase enzymeStructure and functionality in flavivirus NS-proteins: perspectives for drug designStructural and Functional Analyses of a Conserved Hydrophobic Pocket of Flavivirus MethyltransferaseStructural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferaseWest Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning MechanismGenetic Interactions among the West Nile Virus Methyltransferase, the RNA-Dependent RNA Polymerase, and the 5' Stem-Loop of Genomic RNASeparate molecules of West Nile virus methyltransferase can independently catalyze the N7 and 2′-O methylations of viral RNA capPhosphorylation of yellow fever virus NS5 alters methyltransferase activityAnalysis of Flavivirus NS5 Methyltransferase Cap BindingCrystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interfaceStructural analysis of human 2′-O-ribose methyltransferases involved in mRNA cap structure formationRNA methyltransferases involved in 5' cap biosynthesisPerturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongationThe crystal structure of Zika virus NS5 reveals conserved drug targetsFlavivirus RNA cap methyltransferase: structure, function, and inhibition.Evaluation of Adamantane Derivatives as Inhibitors of Dengue Virus mRNA Cap Methyltransferase by Docking and Molecular Dynamics Simulations.Flavivirus methyltransferase: a novel antiviral targetRefolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase.Mutagenesis of the dengue virus type 2 NS5 methyltransferase domain.Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales.
P2860
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P2860
Structural bases for substrate recognition and activity in Meaban virus nucleoside-2′-O-methyltransferase
description
2007 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունիսին հրատարակված գիտական հոդված
@hy
article scientifique (publié 2007-06)
@fr
articolo scientifico (pubblicato il 2007-06)
@it
artigo científico (publicado na 2007-06)
@pt
artículu científicu espublizáu en 2007
@ast
im Juni 2007 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: June 2007)
@en
vedecký článok (publikovaný 2007-06)
@sk
videnskabelig artikel (udgivet 2007-06)
@da
name
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@ast
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@en
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@nl
type
label
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@ast
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@en
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@nl
prefLabel
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@ast
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@en
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@nl
P2860
P50
P356
P1433
P1476
Structural bases for substrate ...... leoside-2′-O-methyltransferase
@en
P2093
Frederic Peyrane
P2860
P304
P356
10.1110/PS.072758107
P50
P577
2007-06-01T00:00:00Z