Neutralization map of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus: domains recognized by monoclonal antibodies that prevent receptor recognition
about
Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionCharacterization of Newcastle disease virus isolates by reverse transcription PCR coupled to direct nucleotide sequencing and development of sequence database for pathotype prediction and molecular epidemiological analysisMonoclonal antibodies against the adeno-associated virus type 2 (AAV-2) capsid: epitope mapping and identification of capsid domains involved in AAV-2-cell interaction and neutralization of AAV-2 infectionNewcastle disease virus in Madagascar: identification of an original genotype possibly deriving from a died out ancestor of genotype IV.Structural and functional relationship between the receptor recognition and neuraminidase activities of the Newcastle disease virus hemagglutinin-neuraminidase protein: receptor recognition is dependent on neuraminidase activity.Monoclonal antibody routinely used to identify avirulent strains of Newcastle disease virus binds to an epitope at the carboxy terminus of the hemagglutinin-neuraminidase protein and recognizes individual mesogenic and velogenic strains.Genotypic and pathotypic characterization of Newcastle disease viruses from India.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.High pathogenicity and low genetic evolution of avian paramyxovirus type I (Newcastle disease virus) isolated from live bird markets in Uganda.Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsFusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor bindingA host-restricted viral vector for antigen-specific immunization against Lyme disease pathogen.Package of NDV-pseudotyped HIV-Luc virus and its application in the neutralization assay for NDV infection.Role of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusionDisulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virusSequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin.Characterization of emerging Newcastle disease virus isolates in China.Construction of a camelid VHH yeast two-hybrid library and the selection of VHH against haemagglutinin-neuraminidase protein of the Newcastle disease virus.Characterization of virulent Newcastle disease viruses from vaccinated chicken flocks in Eastern China.Individual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F protein.Complete genome sequence of a newly emerging newcastle disease virusCharacterization of a recombinant Newcastle disease virus vaccine strain.Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.High genetic diversity of Newcastle disease virus in poultry in West and Central Africa: cocirculation of genotype XIV and newly defined genotypes XVII and XVIIIA mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation.Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein.Loss of N-linked glycosylation from the hemagglutinin-neuraminidase protein alters virulence of Newcastle disease virus.Mutated form of the Newcastle disease virus hemagglutinin-neuraminidase interacts with the homologous fusion protein despite deficiencies in both receptor recognition and fusion promotion.Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hemagglutinin-neuraminidase glycoprotein: effects on antigenic structure and function.Fusion mutants of Newcastle disease virus selected with monoclonal antibodies to the hemagglutinin-neuraminidase.Molecular Characterization of Thermostable Newcastle disease virus Isolated from Pigeon.Molecular characterization of hemagglutinin-neuraminidase fragment gene of Newcastle disease virus isolated from periodically-vaccinated farms.
P2860
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P2860
Neutralization map of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus: domains recognized by monoclonal antibodies that prevent receptor recognition
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Neutralization map of the hema ...... t prevent receptor recognition
@en
type
label
Neutralization map of the hema ...... t prevent receptor recognition
@en
prefLabel
Neutralization map of the hema ...... t prevent receptor recognition
@en
P2093
P2860
P1433
P1476
Neutralization map of the hema ...... t prevent receptor recognition
@en
P2093
J P Sheehan
R J Syddall
R L Glickman
P2860
P304
P407
P577
1991-09-01T00:00:00Z