The signal sequence and C-terminal hydrophobic domain are required for localization of the sexual stage antigen Pgs28 to the surface of P. gallinaceum ookinetes

This publication has 12 references indexed in Scilit:

• Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
  The EMBO Journal, 2000
• 3′ UTR elements enhance expression of Pgs28, an ookinete protein of Plasmodium gallinaceum
  Molecular and Biochemical Parasitology, 2000
• Isolation and Functional Characterization of Two Distinct Sexual-Stage-Specific Promoters of the Human Malaria Parasite Plasmodium falciparum
  Molecular and Cellular Biology, 1999
• The biosynthesis and post-translational modification of Pbs21 an ookinete-surface protein of Plasmodium berghei
  Molecular and Biochemical Parasitology, 1999
• Glycosylphosphatidylinositol-dependent secretory transport in Trypanosoma brucei
  Biochemical Journal, 1998
• Identification of xanthurenic acid as the putative inducer of malaria development in the mosquito
  Nature, 1998
• Plasmodium gallinaceum:Fluorescent Staining of Zygotes and Ookinetes to Study Malaria Parasites in Mosquito
  Experimental Parasitology, 1998
• Protein Translocation Across the Membrane of the Endoplasmic Reticulum
  The Journal of Membrane Biology, 1997
• Transfection of the malaria parasite and expression of firefly luciferase.
  Proceedings of the National Academy of Sciences, 1993
• Pgs28 belongs to a family of epidermal growth factor-like antigens that are targets of malaria transmission-blocking antibodies.
  The Journal of Experimental Medicine, 1993