Role of N-linked glycosylation of the Hendra virus fusion protein
about
Modes of paramyxovirus fusion: a Henipavirus perspectiveCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyRole of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.The human metapneumovirus small hydrophobic protein has properties consistent with those of a viroporin and can modulate viral fusogenic activity.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesSite occupancy and glycan compositional analysis of two soluble recombinant forms of the attachment glycoprotein of Hendra virus.Beyond anchoring: the expanding role of the hendra virus fusion protein transmembrane domain in protein folding, stability, and function.Multiple Novel Functions of Henipavirus O-glycans: The First O-glycan Functions Identified in the Paramyxovirus FamilyA conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation.N-linked glycosylation attenuates H3N2 influenza viruses.N-Glycans on the Nipah virus attachment glycoprotein modulate fusion and viral entry as they protect against antibody neutralizationStructure and stabilization of the Hendra virus F glycoprotein in its prefusion formTrimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.Hendra virus fusion protein transmembrane domain contributes to pre-fusion protein stability.Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH.C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.N-glycans on Nipah virus fusion protein protect against neutralization but reduce membrane fusion and viral entry.Biochemical, conformational, and immunogenic analysis of soluble trimeric forms of henipavirus fusion glycoproteins.Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling.Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion proteinCanine distemper viruses expressing a hemagglutinin without N-glycans lose virulence but retain immunosuppression.
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P2860
Role of N-linked glycosylation of the Hendra virus fusion protein
description
2005 nî lūn-bûn
@nan
2005年の論文
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2005年論文
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2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
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2005年論文
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2005年论文
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2005年论文
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2005年论文
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name
Role of N-linked glycosylation of the Hendra virus fusion protein
@en
Role of N-linked glycosylation of the Hendra virus fusion protein
@nl
type
label
Role of N-linked glycosylation of the Hendra virus fusion protein
@en
Role of N-linked glycosylation of the Hendra virus fusion protein
@nl
prefLabel
Role of N-linked glycosylation of the Hendra virus fusion protein
@en
Role of N-linked glycosylation of the Hendra virus fusion protein
@nl
P2093
P2860
P921
P1433
P1476
Role of N-linked glycosylation of the Hendra virus fusion protein
@en
P2093
Cara Theresia Pager
James Richard Carter
Rebecca Ellis Dutch
Stephen Derrick Fowler
P2860
P304
P356
10.1128/JVI.79.12.7922-7925.2005
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P577
2005-06-01T00:00:00Z