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Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes.
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A Systematic Targeted Genetic Screen Identifies Proteins Involved in Cytoadherence of the Malaria Parasite P. falciparum.
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The mature N-termini of effector proteins confer specificity of export.
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Distribution of malaria parasite-derived phosphatidylcholine in the infected erythrocyte.
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Formation of ER-lumenal intermediates during export of Plasmodium proteins containing transmembrane-like hydrophobic sequences.
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The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.
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A member of the tryptophan-rich protein family is required for efficient sequestration of Plasmodium berghei schizonts.
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Secretory processes in Plasmodium.
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Fluorescence photobleaching analysis for the study of cellular dynamics.
Eur Biophys J. 2002 Mar;31(1):36-51. doi: 10.1007/s00249-001-0202-2.
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Pfsbp1, a Maurer's cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton.
Mol Biochem Parasitol. 2000 Nov;111(1):107-21. doi: 10.1016/s0166-6851(00)00301-7.
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Secretory protein trafficking and organelle dynamics in living cells.
Annu Rev Cell Dev Biol. 2000;16:557-89. doi: 10.1146/annurev.cellbio.16.1.557.
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Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway.
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