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Henipavirus mediated membrane fusion, virus entry and targeted therapeuticsCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyA dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin bindingHendra and Nipah viruses: different and dangerous.Endothelial galectin-1 binds to specific glycans on nipah virus fusion protein and inhibits maturation, mobility, and function to block syncytia formation.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recyclingRespiratory syncytial virus glycoproteins uptake occurs through clathrin-mediated endocytosis in a human epithelial cell lineCharacterization of a third generation lentiviral vector pseudotyped with Nipah virus envelope proteins for endothelial cell transduction.Mutations in the Transmembrane Domain and Cytoplasmic Tail of Hendra Virus Fusion Protein Disrupt Virus-Like-Particle Assembly.Preventing Cleavage of the Respiratory Syncytial Virus Attachment Protein in Vero Cells Rescues the Infectivity of Progeny Virus for Primary Human Airway Cultures.Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment.C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.Contribution of endocytic motifs in the cytoplasmic tail of herpes simplex virus type 1 glycoprotein B to virus replication and cell-cell fusion.Surface density of the Hendra G protein modulates Hendra F protein-promoted membrane fusion: role for Hendra G protein trafficking and degradation.Antibody-Induced Internalization of the Human Respiratory Syncytial Virus Fusion Protein.Cytoplasmic Motifs in the Nipah Virus Fusion Protein Modulate Virus Particle Assembly and Egress.Nipah virus infection and glycoprotein targeting in endothelial cells.RSV glycoprotein and genomic RNA dynamics reveal filament assembly prior to the plasma membraneEphrin-B2 expression critically influences Nipah virus infection independent of its cytoplasmic tail.Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein.Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion proteinTyrosine residues in the cytoplasmic domains affect sorting and fusion activity of the Nipah virus glycoproteins in polarized epithelial cells.The nipah virus fusion protein is cleaved within the endosomal compartment.
P2860
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P2860
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Endocytosis of the Nipah virus glycoproteins
@en
type
label
Endocytosis of the Nipah virus glycoproteins
@en
prefLabel
Endocytosis of the Nipah virus glycoproteins
@en
P2093
P2860
P1433
P1476
Endocytosis of the Nipah virus glycoproteins
@en
P2093
Andrea Maisner
Carola Vogt
Markus Eickmann
Sandra Diederich
P2860
P304
P356
10.1128/JVI.79.6.3865-3872.2005
P407
P577
2005-03-01T00:00:00Z