Found: 19
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Activation loop phosphorylation and cGMP saturation of PKG regulate egress of malaria parasites.
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- PLoS Pathogens, 2024, v. 20, n. 6, p. 1, doi. 10.1371/journal.ppat.1012360
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- Article
A choline-releasing glycerophosphodiesterase essential for phosphatidylcholine biosynthesis and blood stage development in the malaria parasite.
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- eLife, 2023, p. 1, doi. 10.7554/eLife.82207
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- Article
Autocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor.
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- EMBO Journal, 2021, v. 40, n. 11, p. 1, doi. 10.15252/embj.2020107226
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- Article
Characterization of P. falciparum dipeptidyl aminopeptidase 3 specificity identifies differences in amino acid preferences between peptide‐based substrates and covalent inhibitors.
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- FEBS Journal, 2019, v. 286, n. 20, p. 3998, doi. 10.1111/febs.14953
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- Article
Cyclic AMP signalling controls key components of malaria parasite host cell invasion machinery.
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- PLoS Biology, 2019, v. 17, n. 5, p. 1, doi. 10.1371/journal.pbio.3000264
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- Article
Essentiality of Plasmodium falciparum plasmepsin V.
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- PLoS ONE, 2018, v. 13, n. 12, p. 1, doi. 10.1371/journal.pone.0207621
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- Article
Targeted Deletion of a Plasmodium Site-2 Protease Impairs Life Cycle Progression in the Mammalian Host.
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- PLoS ONE, 2017, v. 12, n. 1, p. 1, doi. 10.1371/journal.pone.0170260
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- Article
P lasmodium falciparum SERA5 plays a non-enzymatic role in the malarial asexual blood-stage lifecycle.
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- Molecular Microbiology, 2015, v. 96, n. 2, p. 368, doi. 10.1111/mmi.12941
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- Article
The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.
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- Nature Communications, 2014, v. 5, n. 5, p. 3726, doi. 10.1038/ncomms4726
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- Article
Corrigendum: The malaria parasite egress protease SUB1 is a calcium-dependent redox switch subtilisin.
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- Nature Communications, 2014, v. 5, n. 5, p. 4031, doi. 10.1038/ncomms5031
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- Article
Molecular Determinants for Subcellular Trafficking of the Malarial Sheddase PfSUB2.
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- Traffic, 2013, v. 14, n. 10, p. 1053, doi. 10.1111/tra.12092
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- Article
Malaria Parasite cGMP-dependent Protein Kinase Regulates Blood Stage Merozoite Secretory Organelle Discharge and Egress
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- PLoS Pathogens, 2013, v. 9, n. 5, p. 1, doi. 10.1371/journal.ppat.1003344
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- Article
Juxtamembrane Shedding of Plasmodium falciparum AMA1 Is Sequence Independent and Essential, and Helps Evade Invasion-Inhibitory Antibodies.
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- PLoS Pathogens, 2011, v. 7, n. 12, p. 1, doi. 10.1371/journal.ppat.1002448
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- Article
A multifunctional serine protease primes the malaria parasite for red blood cell invasion.
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- EMBO Journal, 2009, v. 28, n. 6, p. 725, doi. 10.1038/emboj.2009.22
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- Article
An Inhibitory Antibody Blocks Interactions between Components of the Malarial Invasion Machinery.
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- PLoS Pathogens, 2009, v. 5, n. 1, p. 1, doi. 10.1371/journal.ppat.1000273
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- Article
Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite.
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- Journal of Cell Biology, 2006, v. 174, n. 7, p. 1023, doi. 10.1083/jcb.200604136
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- Article
Molecular Identification of a Malaria Merozoite Surface Sheddase.
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- PLoS Pathogens, 2005, v. 1, n. 3, p. 241, doi. 10.1371/journal.ppat.0010029
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- Article
Distinct mechanisms govern proteolytic shedding of a key invasion protein in apicomplexan pathogens.
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- Molecular Microbiology, 2005, v. 57, n. 5, p. 1342, doi. 10.1111/j.1365-2958.2005.04772.x
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- Article
Subtilisin-like proteases of the malaria parasite.
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- Molecular Microbiology, 2004, v. 53, n. 1, p. 55, doi. 10.1111/j.1365-2958.2004.04144.x
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- Article