Pages that link to "Q27485168"

The following pages link to Structural bases for substrate recognition and activity in Meaban virus nucleoside-2′-O-methyltransferase (Q27485168):

Displaying 25 items.

• Identification of a novel antiviral inhibitor of the flavivirus guanylyltransferase enzyme (Q22583530) (← links)
• Structure and functionality in flavivirus NS-proteins: perspectives for drug design (Q23011530) (← links)
• Structural and Functional Analyses of a Conserved Hydrophobic Pocket of Flavivirus Methyltransferase (Q24289239) (← links)
• Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase (Q27482178) (← links)
• West Nile Virus Methyltransferase Catalyzes Two Methylations of the Viral RNA Cap through a Substrate-Repositioning Mechanism (Q27485750) (← links)
• Genetic Interactions among the West Nile Virus Methyltransferase, the RNA-Dependent RNA Polymerase, and the 5' Stem-Loop of Genomic RNA (Q27486408) (← links)
• Separate molecules of West Nile virus methyltransferase can independently catalyze the N7 and 2′-O methylations of viral RNA cap (Q27486587) (← links)
• Phosphorylation of yellow fever virus NS5 alters methyltransferase activity (Q27487335) (← links)
• Analysis of Flavivirus NS5 Methyltransferase Cap Binding (Q27488373) (← links)
• Crystal Structure of the full-length Japanese encephalitis virus NS5 reveals a conserved methyltransferase-polymerase interface (Q27679697) (← links)
• Structural analysis of human 2′-O-ribose methyltransferases involved in mRNA cap structure formation (Q27681232) (← links)
• Crystal structure of dengue virus methyltransferase without S-adenosyl-L-methionine (Q27695629) (← links)
• RNA methyltransferases involved in 5' cap biosynthesis (Q28080819) (← links)
• Perturbation in the conserved methyltransferase-polymerase interface of flavivirus NS5 differentially affects polymerase initiation and elongation (Q28651848) (← links)
• The crystal structure of Zika virus NS5 reveals conserved drug targets (Q29365336) (← links)
• Flavivirus RNA cap methyltransferase: structure, function, and inhibition (Q35212106) (← links)
• Evaluation of Adamantane Derivatives as Inhibitors of Dengue Virus mRNA Cap Methyltransferase by Docking and Molecular Dynamics Simulations (Q36092127) (← links)
• Flavivirus methyltransferase: a novel antiviral target (Q37197519) (← links)
• Chapter 2. New insights into flavivirus nonstructural protein 5. (Q37584190) (← links)
• Flavivirus RNA methylation (Q38184248) (← links)
• Biochemical characterization of the (nucleoside-2'O)-methyltransferase activity of dengue virus protein NS5 using purified capped RNA oligonucleotides (7Me)GpppAC(n) and GpppAC(n). (Q38350216) (← links)
• Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase (Q40185164) (← links)
• Flaviviral methyltransferase/RNA interaction: structural basis for enzyme inhibition (Q40387581) (← links)
• Mutagenesis of the dengue virus type 2 NS5 methyltransferase domain (Q40419510) (← links)
• Identification and Characterization of a Ribose 2'-O-Methyltransferase Encoded by the Ronivirus Branch of Nidovirales (Q40677885) (← links)