A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
- 7 February 2006
- Vol. 346 (2) , 251-257
- https://doi.org/10.1016/j.virol.2006.01.007
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Cathepsin L Is Involved in Proteolytic Processing of the Hendra Virus Fusion ProteinJournal of Virology, 2005
- Endocytosis Plays a Critical Role in Proteolytic Processing of the Hendra Virus Fusion ProteinJournal of Virology, 2005
- EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirusNature, 2005
- Endosomal Proteolysis of the Ebola Virus Glycoprotein Is Necessary for InfectionScience, 2005
- Endocytosis of the Nipah Virus GlycoproteinsJournal of Virology, 2005
- Ubiquitous Activation of the Nipah Virus Fusion Protein Does Not Require a Basic Amino Acid at the Cleavage SiteJournal of Virology, 2004
- Subcellular Localization and Calcium and pH Requirements for Proteolytic Processing of the Hendra Virus Fusion ProteinJournal of Virology, 2004
- Membrane Fusion Tropism and Heterotypic Functional Activities of theNipah VirusandHendra VirusEnvelope GlycoproteinsJournal of Virology, 2002
- Nipah Virus: A Recently Emergent Deadly ParamyxovirusScience, 2000
- Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketonesBiochimie, 1994