Overproduction of Pichia pastoris or Plasmodium falciparum protein disulfide isomerase affects expression, folding and O-linked glycosylation of a malaria vaccine candidate expressed in P. pastoris

This publication has 29 references indexed in Scilit:

• Antioxidant defense in Plasmodium falciparum – data mining of the transcriptome
  Malaria Journal, 2004
• Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
  Current Opinion in Biotechnology, 2002
• High-Level Production and Purification of P30P2MSP119, an Important Vaccine Antigen for Malaria, Expressed in the Methylotropic Yeast Pichia pastoris
  Protein Expression and Purification, 2001
• Glycobiology of Plasmodium falciparum
  Biochimie, 2001
• A Protein Disulfide Isomerase Gene Fusion Expression System That Increases the Extracellular Productivity of Bacillus brevis
  Applied and Environmental Microbiology, 2000
• Heterologous protein expression in the methylotrophic yeastPichia pastoris
  FEMS Microbiology Reviews, 2000
• Protein Glycosylation in the Malaria Parasite
  Parasitology Today, 1999
• Overview of N- and O-linked oligosaccharide structures found in various yeast species
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1999
• Rescue of Immunoglobulins from Insolubility Is Facilitated by PDI in the Baculovirus Expression System
  Protein Expression and Purification, 1996
• Recombinant Pfs25 protein of Plasmodium falciparum elicits malaria transmission-blocking immunity in experimental animals.
  The Journal of Experimental Medicine, 1991