Primary structure of the West Nile flavivirus genome region coding for all nonstructural proteins.Castle E., Leidner U., Nowak T., Wengler G., Wengler G.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC RNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 149:10-26 (1986)Cited in1
An infectious clone of the West Nile flavivirus.Yamshchikov V.F., Wengler G., Perelygin A.A., Brinton M.A., Compans R.W.View abstractCited forSEQUENCE REVISION TO 1908; 2018-2036; 2242 AND 2859-2860CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 281:294-304 (2001)Cited in1
Sequence analysis of the viral core protein and the membrane-associated proteins V1 and NV2 of the flavivirus West Nile virus and of the genome sequence for these proteins.Castle E., Nowak T., Leidner U., Wengler G., Wengler G.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-291CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 145:227-236 (1985)Cited in1
Sequence analysis of the membrane protein V3 of the flavivirus West Nile virus and of its gene.Wengler G., Castle E., Leidner U., Nowak T., Wengler G.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 255-854CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 147:264-274 (1985)Cited in1
Studies on the glycosylation of flavivirus E proteins and the role of carbohydrate in antigenic structure.Winkler G., Heinz F.X., Kunz C.View abstractCited forABSENCE OF GLYCOSYLATION (ENVELOPE PROTEIN E)CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 159:237-243 (1987)Cited in6
Analysis of disulfides present in the membrane proteins of the West Nile flavivirus.Nowak T., Wengler G.View abstractCited forDISULFIDE BONDS (ENVELOPE PROTEIN E)CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCVirology 156:127-137 (1987)Cited in1
Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway.Chu J.J., Ng M.L.View abstractCited forFUNCTION (ENVELOPE PROTEIN E)CategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 78:10543-10555 (2004)Cited in1
Nuclear localization of flavivirus RNA synthesis in infected cells.Uchil P.D., Kumar A.V., Satchidanandam V.View abstractCited forSUBCELLULAR LOCATION (RNA-DIRECTED RNA POLYMERASE NS5)StrainE101CategoriesSubcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 80:5451-5464 (2006)Cited in4
Structure and function of flavivirus NS5 methyltransferase.Zhou Y., Ray D., Zhao Y., Dong H., Ren S., Li Z., Guo Y., Bernard K.A., Shi P.-Y., Li H.View abstractCited forFUNCTION (RNA-DIRECTED RNA POLYMERASE NS5), MUTAGENESIS OF LYS-2586; ASP-2671; LYS-2707 AND GLU-2743CategoriesFunction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Virol. 81:3891-3903 (2007)Cited in3
Cleavage preference distinguishes the two-component NS2B-NS3 serine proteinases of Dengue and West Nile viruses.Shiryaev S.A., Kozlov I.A., Ratnikov B.I., Smith J.W., Lebl M., Strongin A.Y.View abstractCited forPROTEOLYTIC PROCESSING (GENOME POLYPROTEIN)CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. J. 401:743-752 (2007)Cited in2
Human Sec3 protein is a novel transcriptional and translational repressor of flavivirus.Bhuvanakantham R., Li J., Tan T.T., Ng M.L.View abstractCited forINTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), SUBCELLULAR LOCATION (CAPSID PROTEIN C)CategoriesInteraction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell. Microbiol. 12:453-472 (2010)Cited in4Mapped to2
West Nile virus and dengue virus capsid protein negates the antiviral activity of human Sec3 protein through the proteasome pathway.Bhuvanakantham R., Ng M.L.View abstractCited forINTERACTION WITH HUMAN EXOC1 (CAPSID PROTEIN C), FUNCTION (CAPSID PROTEIN C), MUTAGENESIS OF VAL-14CategoriesFunction, Interaction, Phenotypes & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell. Microbiol. 15:1688-1706 (2013)Cited in3Mapped to4
Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms of Dengue and Zika Virus Pathogenesis.Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L., Johnson J.R., Von Dollen J., Ramage H.R.[...], Krogan N.J.View abstractCited forINTERACTION WITH HUMAN PAF1 COMPLEX (RNA-DIRECTED RNA POLYMERASE NS5)CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCCell 175:1931-1945 (2018)Cited in13
Role of PDZ-binding motif from West Nile virus NS5 protein on viral replication.Giraud E., Del Val C.O., Caillet-Saguy C., Zehrouni N., Khou C., Caillet J., Jacob Y., Pardigon N., Wolff N.View abstractCited forDOMAIN (RNA-DIRECTED RNA POLYMERASE NS5)CategoriesFamily & DomainsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCSci. Rep. 11:3266-3266 (2021)Cited in1
Structural basis for the activation of flaviviral NS3 proteases from dengue and West Nile virus.Erbel P., Schiering N., D'Arcy A., Renatus M., Kroemer M., Lim S.P., Yin Z., Keller T.H., Vasudevan S.G., Hommel U.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1420-1688CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Struct. Mol. Biol. 13:372-373 (2006)Cited in11
Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold.Aleshin A.E., Shiryaev S.A., Strongin A.Y., Liddington R.C.View abstractCited forX-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1419-1679CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProtein Sci. 16:795-806 (2007)Cited in1Mapped to1
Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody.Cherrier M.V., Kaufmann B., Nybakken G.E., Lok S.M., Warren J.T., Chen B.R., Nelson C.A., Kostyuchenko V.A., Holdaway H.A.[...], Fremont D.H.View abstractCited forX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 291-688CategoriesStructureSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 28:3269-3276 (2009)Cited in32Mapped to1