Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus (Arteriviridae) are structural proteins of the virion.
about
The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent manner.The minor envelope glycoproteins GP2a and GP4 of porcine reproductive and respiratory syndrome virus interact with the receptor CD163.Porcine reproductive and respiratory syndrome virus comparison: divergent evolution on two continents.Antigenic and Biological Characterization of ORF2-6 Variants at Early Times Following PRRSV InfectionIdentification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: evidence for gene duplication during arterivirus evolution.Identification of a novel structural protein of arteriviruses.Interleukin-2 enhancer binding factor 2 interacts with the nsp9 or nsp2 of porcine reproductive and respiratory syndrome virus and exerts negatively regulatory effect on the viral replicationProtective humoral immune response induced by an inactivated porcine reproductive and respiratory syndrome virus expressing the hypo-glycosylated glycoprotein 5.Evolution of porcine reproductive and respiratory syndrome virus during sequential passages in pigs.Unique epitopes recognized by monoclonal antibodies against HP-PRRSV: deep understanding of antigenic structure and virus-antibody interaction.Precision engineering for PRRSV resistance in pigs: Macrophages from genome edited pigs lacking CD163 SRCR5 domain are fully resistant to both PRRSV genotypes while maintaining biological function.Broadening the heterologous cross-neutralizing antibody inducing ability of porcine reproductive and respiratory syndrome virus by breeding the GP4 or M genes.Nonstructural protein 2 of porcine reproductive and respiratory syndrome virus inhibits the antiviral function of interferon-stimulated gene 15.Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virusMonoclonal antibodies directed against conserved epitopes on the nucleocapsid protein and the major envelope glycoprotein of equine arteritis virus.Infectious transcripts from cloned genome-length cDNA of porcine reproductive and respiratory syndrome virus.A subset of porcine reproductive and respiratory syndrome virus GP3 glycoprotein is released into the culture medium of cells as a non-virion-associated and membrane-free (soluble) form.Kissing interaction between 3' noncoding and coding sequences is essential for porcine arterivirus RNA replication.Characterization of two new structural glycoproteins, GP(3) and GP(4), of equine arteritis virusHeterodimerization of the two major envelope proteins is essential for arterivirus infectivity.Formation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.Involvement of the matrix protein in attachment of porcine reproductive and respiratory syndrome virus to a heparinlike receptor on porcine alveolar macrophages.Posttranslational processing and identification of a neutralization domain of the GP4 protein encoded by ORF4 of Lelystad virus.Colocalization and interaction of the porcine arterivirus nucleocapsid protein with the small nucleolar RNA-associated protein fibrillarin.Porcine arterivirus infection of alveolar macrophages is mediated by sialic acid on the virus.Genetic diversity analysis of genotype 2 porcine reproductive and respiratory syndrome viruses emerging in recent years in ChinaA variable region in GP4 of European-type porcine reproductive and respiratory syndrome virus induces neutralizing antibodies against homologous but not heterologous virus strains.Genomic and antigenic variations of porcine reproductive and respiratory syndrome virus major envelope GP5 glycoprotein.Identification of a Novel Recombinant Type 2 Porcine Reproductive and Respiratory Syndrome Virus in China.Glycoprotein 3 of porcine reproductive and respiratory syndrome virus exhibits an unusual hairpin-like membrane topology.
P2860
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P2860
Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus (Arteriviridae) are structural proteins of the virion.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Proteins encoded by open readi ...... ctural proteins of the virion.
@en
Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus
@nl
type
label
Proteins encoded by open readi ...... ctural proteins of the virion.
@en
Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus
@nl
prefLabel
Proteins encoded by open readi ...... ctural proteins of the virion.
@en
Proteins encoded by open reading frames 3 and 4 of the genome of Lelystad virus
@nl
P2093
P2860
P1433
P1476
Proteins encoded by open readi ...... uctural proteins of the virion
@en
P2093
Meulenberg JJ
Moormann RJ
Petersen-den Besten A
van Essen-Zanbergen A
van Nieuwstadt AP
P2860
P304
P407
P577
1996-07-01T00:00:00Z