about
Vaccine-induced antibodies linked to bovine neonatal pancytopenia (BNP) recognize cattle major histocompatibility complex class I (MHC I)Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesisCore protein of pestiviruses is processed at the C terminus by signal peptide peptidase.Function of bovine CD46 as a cellular receptor for bovine viral diarrhea virus is determined by complement control protein 1Role of the Low-Density Lipoprotein Receptor in Entry of Bovine Viral Diarrhea VirusProcessing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7Recombinational history and molecular evolution of western equine encephalomyelitis complex alphavirusesProcessing of the envelope glycoproteins of pestivirusesProcessing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virusHigh-level secretion of recombinant monomeric murine and human single-chain Fv antibodies from Drosophila S2 cellsCrystal structure of the pestivirus envelope glycoprotein E(rns) and mechanistic analysis of its ribonuclease activityMorphology and Molecular Composition of Purified Bovine Viral Diarrhea Virus EnvelopeSingle amino acid substitution (G42E) in the receptor binding domain of mouse mammary tumour virus envelope protein facilitates infection of non-murine cells in a transferrin receptor 1-independent mannerCongenital infection with atypical porcine pestivirus (APPV) is associated with disease and viral persistence.Construction and Rescue of a Molecular Clone of Deformed Wing Virus (DWV)Molecular cloning and nucleotide sequence of the genome of hog cholera virusX-ray structure of the pestivirus NS3 helicase and its conformation in solution.Characterisation of vaccine-induced, broadly cross-reactive IFN-γ secreting T cell responses that correlate with rapid protection against classical swine fever virus.The core protein of classical Swine Fever virus is dispensable for virus propagation in vitroBiosynthesis of classical swine fever virus nonstructural proteins.Proteins encoded in the 5' region of the pestivirus genome--considerations concerning taxonomy.Characterization of two Austrian porcine reproductive and respiratory syndrome virus (PRRSV) field isolates reveals relationship to East Asian strains.CD46 is a cellular receptor for bovine viral diarrhea virus.Sindbis virus RNA polymerase is degraded by the N-end rule pathway.Using ubiquitin to follow the metabolic fate of a protein.Functional characterization of bovine viral diarrhea virus nonstructural protein 5A by reverse genetic analysis and live cell imaging.Autocatalytic cleavage within classical swine fever virus NS3 leads to a functional separation of protease and helicase.Aura alphavirus subgenomic RNA is packaged into virions of two sizes.The viral RNase E(rns) prevents IFN type-I triggering by pestiviral single- and double-stranded RNAs.RNase-dependent inhibition of extracellular, but not intracellular, dsRNA-induced interferon synthesis by Erns of pestiviruses.Novel Pestivirus Species in Pigs, Austria, 2015.The core protein of a pestivirus protects the incoming virus against IFN-induced effectors.Nonreplicative RNA Recombination of an Animal Plus-Strand RNA Virus in the Absence of Efficient Translation of Viral Proteins.Characterization of essential domains and plasticity of the classical Swine Fever virus Core protein.Characterization of helper virus-independent cytopathogenic classical swine fever virus generated by an in vivo RNA recombination system.Classical swine fever virus glycoprotein E rns is an endoribonuclease with an unusual base specificity.Regulation of Semliki Forest virus RNA replication: a model for the control of alphavirus pathogenesis in invertebrate hosts.Molecular characterization of hog cholera virus.Genomic localization of hog cholera virus glycoproteins.
P50
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hulumtues
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հետազոտող
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P1053
D-4143-2017
P106
P1153
6701685008
P21
P31
P3829
P496
0000-0002-2951-7471