ArticleCellular microbiology2009
Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum.
Article in Cellular microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 64 citations in OpenAlex.
- Rhomboid Proteases in Plasmodium spp. : Biology, Functional Roles, and Therapeutic Potential.Acta parasitologica · 2026Review
- Article
- Transcriptome analysis reveals molecular targets of erythrocyte invasion phenotype diversity in naturalFrontiers in parasitology · 2024Article
- Sequential roles for red blood cell binding proteins enable phased commitment to invasion for malaria parasites.Nature communications · 2023Article
- Population dynamics and drug resistance mutations in Plasmodium falciparum on the Bijagós Archipelago, Guinea-Bissau.Scientific reports · 2023Article
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- Molecular Characterization and Immunological Evaluation of TruncatedFrontiers in immunology · 2021Article
- Dual Plasmepsin-Targeting Antimalarial Agents Disrupt Multiple Stages of the Malaria Parasite Life Cycle.Cell host & microbe · 2020Article
- Transcriptomic Responses to Thermal Stress and Varied Phosphorus Conditions inMicroorganisms · 2019Article
- Genomic and transcriptomic comparisons of closely related malaria parasites differing in virulence and sequestration pattern.Wellcome open research · 2018Article
- The Genome of Haemoproteus tartakovskyi and Its Relationship to Human Malaria Parasites.Genome biology and evolution · 2016Article
- Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.PLoS pathogens · 2015Article
- Characterization of Inhibitors and Monoclonal Antibodies That Modulate the Interaction between Plasmodium falciparum Adhesin PfRh4 with Its Erythrocyte Receptor Complement Receptor 1.The Journal of biological chemistry · 2015Article
- Inhibition of Plasmepsin V activity demonstrates its essential role in protein export, PfEMP1 display, and survival of malaria parasites.PLoS biology · 2014Article
- Using mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.The Journal of biological chemistry · 2014Article
- Article
- Analyses of interactions between heparin and the apical surface proteins of Plasmodium falciparum.Scientific reports · 2013Article
- Triggers of key calcium signals during erythrocyte invasion by Plasmodium falciparum.Nature communications · 2013Article
- Red blood cell polymorphism and susceptibility to Plasmodium vivax.Advances in parasitology · 2013Review
- Two functional reticulocyte binding-like (RBL) invasion ligands of zoonotic Plasmodium knowlesi exhibit differential adhesion to monkey and human erythrocytes.Malaria journal · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Apicomplexan parasite responsible for the most virulent form of malaria, Plasmodium falciparum, invades human erythrocytes through multiple ligand-receptor interactions. The P. falciparum reticulocyte-binding protein homologue (PfRh or PfRBL) family have been implicated in the invasion process but their exact role is unknown. PfRh1 and PfRh4, members of this protein family, bind to red blood cells and function in merozoite invasion during which they undergo a series of proteolytic cleavage events before and during entry into the host cell. The ectodomain of PfRh1 and PfRh4 are processed to produce fragments consistent with cleavage in the transmembrane domain and released into the supernatant, at about the time of invasion, in a manner consistent with rhomboid protease cleavage. Processing of both PfRh1 and PfRh4, and by extrapolation all membrane-bound members of this protein family, is important for function and release of these proteins on the merozoite surface and they along with EBA-175 are important components of the tight junction, the transient structure that links the erythrocyte via receptor-ligand interactions to the actin-myosin motor in the invading merozoite.
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What OpenQuestion holds
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.