Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.
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Modes of paramyxovirus fusion: a Henipavirus perspectiveBimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringUnity in diversity: shared mechanism of entry among paramyxovirusesStructure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalkStructure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomainInteraction between the Hemagglutinin-Neuraminidase and Fusion Glycoproteins of Human Parainfluenza Virus Type III Regulates Viral Growth In VivoStructural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.Cell-type specific requirements for thiol/disulfide exchange during HIV-1 entry and infectionTriggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsMechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entryFusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.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.Envelope protein dynamics in paramyxovirus entry.Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.Fixation of oligosaccharides to a surface may increase the susceptibility to human parainfluenza virus 1, 2, or 3 hemagglutinin-neuraminidase.'a'-Position-mutated and G4-mutated hemagglutinin-neuraminidase proteins of Newcastle disease virus impair fusion and hemagglutinin-neuraminidase-fusion interaction by different mechanisms.Glycoprotein interactions in paramyxovirus fusion.Measles virus hemagglutinin: structural insights into cell entry and measles vaccine.The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.Probing the spatial organization of measles virus fusion complexesDiscerning intersecting fusion-activation pathways in the Nipah virus using machine learning.Measles virus fusion shifts into gear.Viral Entry Properties Required for Fitness in Humans Are Lost through Rapid Genomic Change during Viral Isolation.The Role of Carbohydrates in Viral Infections
P2860
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P2860
Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Engineered intermonomeric disu ...... mechanism of fusion promotion.
@en
type
label
Engineered intermonomeric disu ...... mechanism of fusion promotion.
@en
prefLabel
Engineered intermonomeric disu ...... mechanism of fusion promotion.
@en
P2093
P2860
P356
P1433
P1476
Engineered intermonomeric disu ...... mechanism of fusion promotion.
@en
P2093
Anne M Mirza
Paul J Mahon
Ronald M Iorio
Thomas A Musich
P2860
P304
10386-10396
P356
10.1128/JVI.00581-08
P407
P577
2008-08-27T00:00:00Z