Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity.
about
Trisaccharide containing α2,3-linked sialic acid is a receptor for mumps virusInfection of lymphoblastoid cell lines by Kaposi's sarcoma-associated herpesvirus: critical role of cell-associated virus.Progress in understanding and controlling respiratory syncytial virus: still crazy after all these yearsTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Paramyxovirus fusion and entry: multiple paths to a common endEngineering, Structure and Immunogenicity of the Human Metapneumovirus F Protein in the Postfusion Conformation.Nipah virus envelope-pseudotyped lentiviruses efficiently target ephrinB2-positive stem cell populations in vitro and bypass the liver sink when administered in vivoThe respiratory syncytial virus fusion protein and neutrophils mediate the airway mucin response to pathogenic respiratory syncytial virus infection.Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sitesStructural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development.Viral entry mechanisms: the increasing diversity of paramyxovirus entry.Residues of the human metapneumovirus fusion (F) protein critical for its strain-related fusion phenotype: implications for the virus replication cycle.Side chain packing below the fusion peptide strongly modulates triggering of the Hendra virus F proteinDetection of respiratory syncytial virus fusion protein variants between 2009 and 2012 in China.Recombinant Sendai viruses expressing fusion proteins with two furin cleavage sites mimic the syncytial and receptor-independent infection properties of respiratory syncytial virus.
P2860
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P2860
Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity.
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
Insertion of the two cleavage ...... tachment protein for activity.
@en
type
label
Insertion of the two cleavage ...... tachment protein for activity.
@en
prefLabel
Insertion of the two cleavage ...... tachment protein for activity.
@en
P2093
P2860
P356
P1433
P1476
Insertion of the two cleavage ...... tachment protein for activity.
@en
P2093
Blanca García-Barreno
Joanna Rawling
José A Melero
P2860
P304
P356
10.1128/JVI.00078-08
P407
P577
2008-04-02T00:00:00Z