The BPV-1 E5 oncoprotein expressed in Schizosaccharomyces pombe exhibits normal biochemical properties and binds to the endogenous 16-kDa component of the vacuolar proton-ATPase

This publication has 17 references indexed in Scilit:

• Bovine papillomavirus E5 oncoprotein binds to the 16K component of vacuolar H+-ATPases
  Nature, 1991
• Structure and pharmacology of the proton-ATPases
  Trends in Pharmacological Sciences, 1991
• Human chorionic gonadotropin α and human cytomegalovirus promoters are extremely active in the fission yeast Schizosaccharomyces pombe
  FEBS Letters, 1990
• The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors
  Cell, 1989
• The progenitor of ATP synthases was closely related to the current vacuolar H⁺‐ATPase
  FEBS Letters, 1989
• The E5 Transforming Gene of Bovine Papillomavirus Encodes a Small, Hydrophobic Polypeptide
  Science, 1986
• Genetic analysis of the 3′ early region transformation and replication functions of bovine papillomavirus type 1
  Virology, 1986
• A very strong enhancer is located upstream of an immediate early gene of human cytomegalovirus
  Cell, 1985
• In vitro tumorigenic transformation by a defined sub-genomic fragment of bovine papilloma virus DNA
  Nature, 1980
• A quantitative in vitro focus assay for bovine papilloma virus
  Virology, 1980