Isolation of a biologically active soluble form of the hemagglutinin-neuraminidase protein of Sendai virus.
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Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivoSecond sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionParainfluenza virusesDimeric Architecture of the Hendra Virus Attachment Glycoprotein: Evidence for a Conserved Mode of AssemblyStructure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion PromotionGlycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulenceN-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site.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.Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion.Fusion deficiency induced by mutations at the dimer interface in the Newcastle disease virus hemagglutinin-neuraminidase is due to a temperature-dependent defect in receptor bindingMolecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirus.Receptor-binding specificity of the human parainfluenza virus type 1 hemagglutinin-neuraminidase glycoprotein.Isolation of the measles virus hemagglutinin protein in a soluble form by protease digestionDifferences in the role of the cytoplasmic domain of human parainfluenza virus fusion proteins.Sequence and structure alignment of Paramyxoviridae attachment proteins and discovery of enzymatic activity for a morbillivirus hemagglutinin.Two single amino acid substitutions in the intervening region of Newcastle disease virus HN protein attenuate viral replication and pathogenicity.Crystals of hemagglutinin-neuraminidase of parainfluenza virus contain triple-stranded helices.Intracellular maturation and transport of the SV5 type II glycoprotein hemagglutinin-neuraminidase: specific and transient association with GRP78-BiP in the endoplasmic reticulum and extensive internalization from the cell surface.Intracellular processing and transport of NH2-terminally truncated forms of a hemagglutinin-neuraminidase type II glycoprotein.Analysis of the primary T-cell response to Sendai virus infection in C57BL/6 mice: CD4+ T-cell recognition is directed predominantly to the hemagglutinin-neuraminidase glycoproteinCrystallization of biologically active hemagglutinin-neuraminidase glycoprotein dimers proteolytically cleaved from human parainfluenza virus type 1.Homooligomerization of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza virus type 3 occurs before the acquisition of correct intramolecular disulfide bonds and mature immunoreactivity.A dual drug regimen synergistically blocks human parainfluenza virus infection.Defective assembly and intracellular transport of mutant paramyxovirus hemagglutinin-neuraminidase proteins containing altered cytoplasmic domains.O glycosylation of glycoprotein G of human respiratory syncytial virus is specified within the divergent ectodomainLoss of the N-linked glycan at residue 173 of human parainfluenza virus type 1 hemagglutinin-neuraminidase exposes a second receptor-binding site.Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.A 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.A Y526Q mutation in the Newcastle disease virus HN protein reduces its functional activities and attenuates virus replication and pathogenicity.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.Quantitative comparison of human parainfluenza virus hemagglutinin-neuraminidase receptor binding and receptor cleavageFunctional interaction between paramyxovirus fusion and attachment proteins.Importance of the cytoplasmic tails of the measles virus glycoproteins for fusogenic activity and the generation of recombinant measles viruses.Probing the spatial organization of measles virus fusion complexesDomain architecture and oligomerization properties of the paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein.
P2860
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P2860
Isolation of a biologically active soluble form of the hemagglutinin-neuraminidase protein of Sendai virus.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Isolation of a biologically ac ...... idase protein of Sendai virus.
@en
type
label
Isolation of a biologically ac ...... idase protein of Sendai virus.
@en
prefLabel
Isolation of a biologically ac ...... idase protein of Sendai virus.
@en
P2093
P2860
P1433
P1476
Isolation of a biologically ac ...... idase protein of Sendai virus.
@en
P2093
S D Thompson
P2860
P304
P407
P577
1988-12-01T00:00:00Z