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ProteomicsFunction of the Rh5 complex in invasion of human erythrocytes
The most severe form of malaria is caused by Plasmodium falciparum. These parasites invade human erythrocytes and an essential step in this process involves the ligand PfRh5, which forms a complex with CyRPA and PfRipr (RCR complex) and binds basigin on the host cell. We identified a heteromeric dis...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2022-12-14 | PXD036746 | Pride
Pfripr Basigin Ptramp Human erythrocytes Invasion complex Pfrh5 Malaria Css P. falciparum 
ProteomicsFunctional characterisation of components in two Plasmodium falciparum Cullin-RING-Ligase complexes
Ubiquitination is the key eukaryotic post-translational modification that governs protein degradation, localisation, and activity which is mediated by a concerted enzyme cascade. The largest superfamily of these enzymes include the Cullin-RING-Ligase (CRL) complexes. Plasmodium falciparum, the causa...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2026-01-09 | PXD072749 | Pride
ProteomicsGID/CTLH E3 ligase complex control cell fate programs for sexual development of Plasmodium falciparum
Transmission of the malaria parasite Plasmodium falciparum requires the formation of specialised sexual cells called gametocytes. A hallmark of P. falciparum gametocyte development is its long duration, during which the parasite undergoes dramatic cellular remodelling including morphological, physio...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2026-01-25 | PXD048861 | Pride
ProteomicsPlasmepsin X activates function of the PCRCR complex in P. falciparum by processing PfRh5 for binding to basigin and invasion of human erythrocytes
Plasmodium falciparum causes the most severe form of malaria in humans. The protozoan parasite develops within erythrocytes to mature schizonts, that contain more than 16 merozoites, which egress and invade fresh erythrocytes. The aspartic protease plasmepsin X (PMX), processes proteins and protease...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2023-04-05 | PXD039646 | Pride
Malaria Plasmepsin x Ip-ms Pcrcr 
ProteomicsIntact-cell thermal PISA-MS target-engagement profiling of M5717 in Plasmodium falciparum
Here we demonstrate eEF1-alpha and eEF2 stabilisation by M5717 in the intact-cell P. falciparum-infected red blood cells, using thermal Proteome Integral Solubility Alteration (Thermal PISA) assay coupled with Data Independent Acquisition Mass Spectrometry (DIA-MS).
ORGANISM(S): Plasmodium (plasmodium) 
2026-02-17 | PXD059612 | JPOST Repository
TranscriptomicsP. falciparum Heterochromatin Protein 1 Marks Genomic Loci Linked to Phenotypic Variation of Exported Virulence Factors
Epigenetic processes are the main conductors of phenotypic variation in eukaryotes. The malaria parasite Plasmodium falciparum employs antigenic variation of the major surface antigen PfEMP1, encoded by 60 var genes, to evade acquired immune responses. PfEMP1 also mediates sequestration of infected ...
ORGANISM(S): Plasmodium falciparum 
2010-05-06 | E-GEOD-17029 | biostudies-arrayexpress
ProteomicsIdentification of PMV as the target of WEHI-601
Live cell DIA Thermal PISA profiling of WEHI-601 target engagement.
ORGANISM(S): Plasmodium (plasmodium) 
2026-02-14 | PXD069420 | JPOST Repository
UnknownLactam Truncation Yields a Dihydroquinazolinone Scaffold with Potent Antimalarial Activity that Targets PfATP4.
Not available
S-EPMC11648822 | biostudies-literature
UnknownMolecular profiling reveals features of clinical immunity and immunosuppression in asymptomatic P. falciparum malaria
Not available
S-SCDT-MSB-2021-10824 | biostudies-other
ProteomicsWEHI991 drug target identification by DIA Solvent PISA
Here we demonstrate PfSTART1 engagement by WEHI991 in the P. falciparum proteome using organic solvent-based Proteome Integral Solubility Alteration (Solvent PISA) assay coupled with Data Independent Acquisition Mass Spectrometry (DIA-MS).
ORGANISM(S): Plasmodium (plasmodium) 
2024-05-01 | PXD048262 | JPOST Repository
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