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UnknownProteolytic activation of the essential parasitophorous vacuole cysteine protease SERA6 accompanies malaria parasite egress from its host erythrocyte.
Not available
S-EPMC3488066 | biostudies-literature
ProteomicsAutocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor
Malaria parasite egress from host erythrocytes (RBCs) is regulated by discharge of a parasite serine protease called SUB1 into the parasitophorous vacuole (PV). There, SUB1 activates a PV-resident cysteine protease called SERA6, enabling host RBC rupture through SERA6-mediated degradation of the RBC...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2021-03-16 | PXD024084 | Pride
Lc-msms Malaria Protease Sub1 Sera6 
UnknownAutocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor.
Not available
S-EPMC8167364 | biostudies-literature
UnknownA protease cascade regulates release of the human malaria parasite Plasmodium falciparum from host red blood cells.
Not available
S-EPMC6089347 | biostudies-literature
UnknownAutocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor
Not available
S-SCDT-EMBOJ-2020-107226 | biostudies-other
UnknownEvidence for a common role for the serine-type Plasmodium falciparum serine repeat antigen proteases: implications for vaccine and drug design.
Not available
S-EPMC2168336 | biostudies-literature
UnknownCharacteristic features of the SERA multigene family in the malaria parasite.
Not available
S-EPMC7132891 | biostudies-literature
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