Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding

scientific article published on 17 September 2008

Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JVI.02654-07
P932PMC publication ID2573269
P698PubMed publication ID18799571

P50authorKatharine BossartQ42720230
Lin-Fa WangQ61982175
P2093author name stringDimiter S Dimitrov
Zhongyu Zhu
Christopher C Broder
Dimple Khetawat
Andrew C Hickey
Jared R Patch
Kimberly A Bishop
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N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entryQ40287207
Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virusQ40423310
Amino acid substitutions in a conserved region in the stalk of the Newcastle disease virus HN glycoprotein spike impair its neuraminidase activity in the globular domainQ40965267
Functional chimeric HN glycoproteins derived from Newcastle disease virus and human parainfluenza virus-3.Q41136835
Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spikeQ41338008
Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural modelQ42184295
The attachment protein of Hendra virus has high structural similarity but limited primary sequence homology compared with viruses in the genus ParamyxovirusQ42687244
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Location of, immunogenicity of and relationships between neutralization epitopes on the attachment protein (G) of Hendra virusQ45423695
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Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virusQ25257200
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Hendra virus infection in a veterinarian.Q34583061
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Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectorsQ35758686
Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusionQ35868157
Detection of an interaction between the HN and F proteins in Newcastle disease virus-infected cellsQ35890850
Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion proteinQ36098830
Paramyxovirus membrane fusion: lessons from the F and HN atomic structuresQ36346778
Interacting Domains of the HN and F Proteins of Newcastle Disease VirusQ36474158
Fusogenic mechanisms of enveloped-virus glycoproteins analyzed by a novel recombinant vaccinia virus-based assay quantitating cell fusion-dependent reporter gene activation.Q36634800
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Paramyxoviruses: different receptors - different mechanisms of fusionQ37019201
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 proteinQ37596488
Biological significance of the second receptor binding site of Newcastle disease virus hemagglutinin-neuraminidase proteinQ37596521
An oligosaccharide at the C-terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusionQ38345409
P433issue22
P407language of work or nameEnglishQ1860
P921main subjectHendra virusQ1604979
P304page(s)11398-11409
P577publication date2008-09-17
P1433published inJournal of VirologyQ1251128
P1476titleResidues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor binding
P478volume82

Reverse relations

cites work (P2860)
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