Experimental determination of the membrane topology of the Plasmodium protease Plasmepsin V.

Fundamental Roles of the Golgi-Associated Toxoplasma Aspartyl Protease, ASP5, at the Host-Parasite Interface. PLoS Pathog (2015) 0.86

Export of malaria proteins requires co-translational processing of the PEXEL motif independent of phosphatidylinositol-3-phosphate binding. Nat Commun (2016) 0.80

A genetic approach to analyzing membrane protein topology. Science (1986) 9.01

Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science (2004) 7.01

A host-targeting signal in virulence proteins reveals a secretome in malarial infection. Science (2004) 6.16

Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes. Cell (2008) 3.80

Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein. Nat Biotechnol (2004) 3.68

Transformation of malaria parasites by the spontaneous uptake and expression of DNA from human erythrocytes. Nucleic Acids Res (2001) 3.06

High-efficiency transformation of Plasmodium falciparum by the lepidopteran transposable element piggyBac. Proc Natl Acad Sci U S A (2005) 2.48

Nalpha -terminal acetylation of eukaryotic proteins. J Biol Chem (2000) 2.39

Uncovering common principles in protein export of malaria parasites. Cell Host Microbe (2012) 2.16

Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte. Nature (2010) 1.97

An aspartyl protease directs malaria effector proteins to the host cell. Nature (2010) 1.92

In vivo and in vitro protein solubility assays using split GFP. Nat Methods (2006) 1.92

PTEX is an essential nexus for protein export in malaria parasites. Nature (2014) 1.85

PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes. Nature (2014) 1.82

N-terminal processing of proteins exported by malaria parasites. Mol Biochem Parasitol (2008) 1.81

A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells. J Cell Biol (2006) 1.73

Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes. Blood (2005) 1.56

Trafficking of STEVOR to the Maurer's clefts in Plasmodium falciparum-infected erythrocytes. EMBO J (2005) 1.50

Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum. Mol Biochem Parasitol (2005) 1.48

N-terminal acetylation inhibits protein targeting to the endoplasmic reticulum. PLoS Biol (2011) 1.48

Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface. Blood (2006) 1.44

Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell. Cell (2012) 1.26

Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export. PLoS Pathog (2013) 1.24

Trafficking determinants for PfEMP3 export and assembly under the Plasmodium falciparum-infected red blood cell membrane. Mol Microbiol (2005) 1.21

Protein acetylation in archaea, bacteria, and eukaryotes. Archaea (2010) 1.15

Brefeldin A inhibits transport of the glycophorin-binding protein from Plasmodium falciparum into the host erythrocyte. Biochem J (1994) 1.10

Sequence requirements for the export of the Plasmodium falciparum Maurer's clefts protein REX2. Mol Microbiol (2008) 1.08

The host targeting motif in exported Plasmodium proteins is cleaved in the parasite endoplasmic reticulum. Mol Biochem Parasitol (2010) 1.08

The Maurer's cleft protein MAHRP1 is essential for trafficking of PfEMP1 to the surface of Plasmodium falciparum-infected erythrocytes. Mol Microbiol (2008) 1.07

Export of PfSBP1 to the Plasmodium falciparum Maurer's clefts. Traffic (2008) 0.98

The C-terminal portion of the cleaved HT motif is necessary and sufficient to mediate export of proteins from the malaria parasite into its host cell. Mol Microbiol (2013) 0.90

Synthesis and secretion of proteins by released malarial parasites. Mol Biochem Parasitol (1992) 0.89

Application of split-green fluorescent protein for topology mapping membrane proteins in Escherichia coli. Protein Sci (2012) 0.81

Return to sender: use of Plasmodium ER retrieval sequences to study protein transport in the infected erythrocyte and predict putative ER protein families. Parasitol Res (2009) 0.79

Diversion at the ER: How Plasmodium falciparum exports proteins into host erythrocytes. F1000Res (2012) 0.79

Use of self-assembling GFP to determine protein topology and compartmentalisation in the Plasmodium falciparum-infected erythrocyte. Mol Biochem Parasitol (2012) 0.77