Proteolytic processing of human cytomegalovirus glycoprotein B (gpUL55) is mediatedby the human endoprotease furin

This publication has 11 references indexed in Scilit:

• Glycoprotein B of Human Cytomegalovirus Promotes Virion Penetration into Cells, Transmission of Infection from Cell to Cell, and Fusion of Infected Cells
  Virology, 1993
• A Mutation of Furin Causes the Lack of Precursor-Processing Activity in Human Colon Carcinoma LoVo Cells
  Biochemical and Biophysical Research Communications, 1993
• Stable constitutive expression of glycoprotein B (gpUL55) of human cytomegalovirus in permissive astrocytoma cells
  Journal of General Virology, 1993
• Identification and Functional Expression of a New Member of the Mammalian Kex2-Like Processing Endoprotease Family: Its Striking Structural Similarity to PACE41
  The Journal of Biochemistry, 1993
• Identification of a Second Human Subtilisin-Like Protease Gene in thefes/fpsRegion of Chromosome 15
  DNA and Cell Biology, 1991
• Mammalian subtilisins: The long-sought dibasic processing endoproteases
  Cell, 1991
• Human fur gene encodes a yeast KEX2-like endoprotease that cleaves pro-beta-NGF in vivo.
  The Journal of cell biology, 1990
• Inhibition of endoproteolytic cleavage of cytomegalovirus (HCMV) glycoprotein B by palmitoyl-peptidyl-chloromethyl ketone
  Virology, 1990
• Human cytomegalovirus strain towne glycoprotein B is processed by proteolytic cleavage
  Virology, 1988
• The Molecular Biology of Influenza Virus Pathogenicity
  Published by Elsevier ,1988