The nipah virus fusion protein is cleaved within the endosomal compartment.
about
Modes of paramyxovirus fusion: a Henipavirus perspectiveUnity in diversity: shared mechanism of entry among paramyxovirusesHuman Metapneumovirus Is Capable of Entering Cells by Fusion with Endosomal MembranesCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyInduction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a TriggerRole of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.Hendra and Nipah viruses: different and dangerous.Entry and fusion of emerging paramyxoviruses.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.Herpes virus fusion and entry: a story with many characters.Complementing defective viruses that express separate paramyxovirus glycoproteins provide a new vaccine vector approach.Analysis of cathepsin and furin proteolytic enzymes involved in viral fusion protein activation in cells of the bat reservoir host.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Quantitative analysis of Nipah virus proteins released as virus-like particles reveals central role for the matrix protein.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesComplete genome sequence of avian paramyxovirus type 7 (strain Tennessee) and comparison with other paramyxoviruses.Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recyclingA conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation.The Hemagglutinin of Bat-Associated Influenza Viruses Is Activated by TMPRSS2 for pH-Dependent Entry into Bat but Not Human Cells.Cell Walls and the Convergent Evolution of the Viral Envelope.Developments towards effective treatments for Nipah and Hendra virus infection.A conserved region between the heptad repeats of paramyxovirus fusion proteins is critical for proper F protein folding.Differential role for low pH and cathepsin-mediated cleavage of the viral spike protein during entry of serotype II feline coronaviruses.Characterization of a third generation lentiviral vector pseudotyped with Nipah virus envelope proteins for endothelial cell transduction.Chloroquine administration does not prevent Nipah virus infection and disease in ferrets.Viral entry mechanisms: the increasing diversity of paramyxovirus entry.Aromatic amino acids in the juxtamembrane domain of severe acute respiratory syndrome coronavirus spike glycoprotein are important for receptor-dependent virus entry and cell-cell fusion.Henipavirus pathogenesis and antiviral approaches.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.Surface glycoproteins of an African henipavirus induce syncytium formation in a cell line derived from an African fruit bat, Hypsignathus monstrosus.Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment.A cathepsin-cleavage site between the adenovirus capsid protein IX and a tumor-targeting ligand improves targeted transduction.C-terminal tyrosine residues modulate the fusion activity of the Hendra virus fusion protein.A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascadeGlycoprotein interactions in paramyxovirus fusion.Surface density of the Hendra G protein modulates Hendra F protein-promoted membrane fusion: role for Hendra G protein trafficking and degradation.Mutation of YMYL in the Nipah virus matrix protein abrogates budding and alters subcellular localization.Nipah virus infection and glycoprotein targeting in endothelial cells.
P2860
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P2860
The nipah virus fusion protein is cleaved within the endosomal compartment.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh-hant
name
The nipah virus fusion protein is cleaved within the endosomal compartment.
@en
The nipah virus fusion protein is cleaved within the endosomal compartment.
@nl
type
label
The nipah virus fusion protein is cleaved within the endosomal compartment.
@en
The nipah virus fusion protein is cleaved within the endosomal compartment.
@nl
altLabel
The nipah virus fusion protein is cleaved within the endosomal compartment
@en
prefLabel
The nipah virus fusion protein is cleaved within the endosomal compartment.
@en
The nipah virus fusion protein is cleaved within the endosomal compartment.
@nl
P2860
P50
P356
P1476
The nipah virus fusion protein is cleaved within the endosomal compartment.
@en
P2093
Andrea Maisner
Sandra Diederich
P2860
P304
29899-29903
P356
10.1074/JBC.M504598200
P407
P577
2005-06-16T00:00:00Z