ArticleInfection and immunity2011
Global identification of multiple substrates for Plasmodium falciparum SUB1, an essential malarial processing protease.
Article in Infection and immunity, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
59 citing papers in PubMed, 95 citations in OpenAlex.
- Peptidic Phosphonates as Irreversible Covalent Inhibitors ofACS medicinal chemistry letters · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Peptidic Boronic AcidJournal of medicinal chemistry · 2024Article
- Protein length distribution is remarkably uniform across the tree of life.Genome biology · 2023Article
- A malaria parasite phospholipase facilitates efficient asexual blood stage egress.PLoS pathogens · 2023Article
- Article
- Immunogenicity Analysis of the RecombinantPathogens (Basel, Switzerland) · 2022Article
- Prefoldin subunit 6 of Plasmodium falciparum binds merozoite surface protein-1.FEBS open bio · 2022Article
- Cell biological analysis reveals an essential role for Pfcerli2 in erythrocyte invasion by malaria parasites.Communications biology · 2022Article
- Autocatalytic activation of a malarial egress protease is druggable and requires a protein cofactor.The EMBO journal · 2021Article
- Peptidic boronic acids are potent cell-permeable inhibitors of the malaria parasite egress serine protease SUB1.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure of the Plasmodium falciparum PfSERA5 pseudo-zymogen.Protein science : a publication of the Protein Society · 2020Article
- The parasitophorous vacuole of the blood-stage malaria parasite.Nature reviews. Microbiology · 2020Review
- Dual Plasmepsin-Targeting Antimalarial Agents Disrupt Multiple Stages of the Malaria Parasite Life Cycle.Cell host & microbe · 2020Article
- PfCERLI1 is a conserved rhoptry associated protein essential for Plasmodium falciparum merozoite invasion of erythrocytes.Nature communications · 2020Article
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- Targeting malaria parasite invasion of red blood cells as an antimalarial strategy.FEMS microbiology reviews · 2019Review
- Cyclic AMP signalling controls key components of malaria parasite host cell invasion machinery.PLoS biology · 2019Article
- PfMSA180 is a novel Plasmodium falciparum vaccine antigen that interacts with human erythrocyte integrin associated protein (CD47).Scientific reports · 2019Article
- Structural Insights Into KeyFrontiers in microbiology · 2019Review
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
The protozoan pathogen responsible for the most severe form of human malaria, Plasmodium falciparum, replicates asexually in erythrocytes within a membrane-bound parasitophorous vacuole (PV). Following each round of intracellular growth, the PV membrane (PVM) and host cell membrane rupture to release infectious merozoites in a protease-dependent process called egress. Previous work has shown that, just prior to egress, an essential, subtilisin-like parasite protease called PfSUB1 is discharged into the PV lumen, where it directly cleaves a number of important merozoite surface and PV proteins. These include the essential merozoite surface protein complex MSP1/6/7 and members of a family of papain-like putative proteases called SERA (serine-rich antigen) that are implicated in egress. To determine whether PfSUB1 has additional, previously unrecognized substrates, we have performed a bioinformatic and proteomic analysis of the entire late asexual blood stage proteome of the parasite. Our results demonstrate that PfSUB1 is responsible for the proteolytic processing of a range of merozoite, PV, and PVM proteins, including the rhoptry protein RAP1 (rhoptry-associated protein 1) and the merozoite surface protein MSRP2 (MSP7-related protein-2). Our findings imply multiple roles for PfSUB1 in the parasite life cycle, further supporting the case for considering the protease as a potential new antimalarial drug target.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.