Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus
about
Classical swine fever virus NS5A protein changed inflammatory cytokine secretion in porcine alveolar macrophages by inhibiting the NF-κB signaling pathwayCharacterization of an autonomous subgenomic pestivirus RNA repliconN-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesisBovine viral diarrhea virus strain Oregon: a novel mechanism for processing of NS2-3 based on point mutationsInsertion of a sequence encoding light chain 3 of microtubule-associated proteins 1A and 1B in a pestivirus genome: connection with virus cytopathogenicity and induction of lethal disease in cattle.Classical swine fever virus leader proteinase Npro is not required for viral replication in cell cultureComplete genomic sequence of border disease virus, a pestivirus from sheep.Identification and characterization of an RNA-dependent RNA polymerase activity within the nonstructural protein 5B region of bovine viral diarrhea virusCorrelation between point mutations in NS2 and the viability and cytopathogenicity of Bovine viral diarrhea virus strain Oregon analyzed with an infectious cDNA cloneThe RNA helicase and nucleotide triphosphatase activities of the bovine viral diarrhea virus NS3 protein are essential for viral replication.Generation and characterization of a hepatitis C virus NS3 protease-dependent bovine viral diarrhea virusE2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies.Mutational analysis of bovine viral diarrhea virus RNA-dependent RNA polymerase.A Cellular J-Domain Protein Modulates Polyprotein Processing and Cytopathogenicity of a PestivirusA recombinant classical swine fever virus stably expresses a marker geneThe carboxy-terminal sequence of the pestivirus glycoprotein E(rns) represents an unusual type of membrane anchor.Core protein of pestiviruses is processed at the C terminus by signal peptide peptidase.Recovery of Virulent and RNase-Negative Attenuated Type 2 Bovine Viral Diarrhea Viruses from Infectious cDNA ClonesThe NS5A Protein of Bovine Viral Diarrhea Virus Contains an Essential Zinc-Binding Site Similar to That of the Hepatitis C Virus NS5A ProteinClassical Swine Fever Virus Interferes with Cellular Antiviral Defense: Evidence for a Novel Function of NproCytopathogenicity of classical swine fever virus caused by defective interfering particlesRNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodiesProcessing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7Bovine viral diarrhea virus: characterization of a cytopathogenic defective interfering particle with two internal deletionsInternal entry of ribosomes is directed by the 5' noncoding region of classical swine fever virus and is dependent on the presence of an RNA pseudoknot upstream of the initiation codonBovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replicationSerine protease of pestiviruses: determination of cleavage sitesBovine Viral Diarrhea Virus Core Is an Intrinsically Disordered Protein That Binds RNARNA chaperoning and intrinsic disorder in the core proteins of FlaviviridaeCell-Derived Sequences in the N-Terminal Region of the Polyprotein of a Cytopathogenic PestivirusPathogenesis of mucosal disease: a cytopathogenic pestivirus generated by an internal deletionBiosynthesis and biochemical properties of the hepatitis C virus core proteinClassical Swine Fever Virus Can Remain Virulent after Specific Elimination of the Interferon Regulatory Factor 3-Degrading Function of NproThe Structure of Classical Swine Fever Virus Npro: A Novel Cysteine Autoprotease and Zinc-Binding Protein Involved in Subversion of Type I Interferon InductionClassical Swine Fever-An Updated ReviewA novel PCR-based method for high throughput prokaryotic expression of antimicrobial peptide genes.The core protein of classical Swine Fever virus is dispensable for virus propagation in vitroAnalysis of a pair of END+ and END- viruses derived from the same bovine viral diarrhea virus stock reveals the amino acid determinants in Npro responsible for inhibition of type I interferon production.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.
P2860
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P2860
Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus
description
1993 nî lūn-bûn
@nan
1993 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Processing of pestivirus polyp ...... of classical swine fever virus
@ast
Processing of pestivirus polyp ...... of classical swine fever virus
@en
Processing of pestivirus polyp ...... of classical swine fever virus
@nl
type
label
Processing of pestivirus polyp ...... of classical swine fever virus
@ast
Processing of pestivirus polyp ...... of classical swine fever virus
@en
Processing of pestivirus polyp ...... of classical swine fever virus
@nl
prefLabel
Processing of pestivirus polyp ...... of classical swine fever virus
@ast
Processing of pestivirus polyp ...... of classical swine fever virus
@en
Processing of pestivirus polyp ...... of classical swine fever virus
@nl
P2093
P2860
P3181
P1433
P1476
Processing of pestivirus polyp ...... of classical swine fever virus
@en
P2093
P2860
P304
P3181
P577
1993-12-01T00:00:00Z