Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Automatic assignment of GO terms using logical inference, based on on inter-ontology links

PfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptor.

Reticulocyte-binding protein homologue 5 - an essential adhesin involved in invasion of human erythrocytes by Plasmodium falciparum.

An EGF-like protein forms a complex with PfRh5 and is required for invasion of human erythrocytes by Plasmodium falciparum.

Basigin is a receptor essential for erythrocyte invasion by Plasmodium falciparum.

Analyses of interactions between heparin and the apical surface proteins of Plasmodium falciparum.

RH5-Basigin interaction plays a major role in the host tropism of Plasmodium falciparum.

Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes.

Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion.

Essential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium falciparum Invasion of Erythrocytes.

One-step design of a stable variant of the malaria invasion protein RH5 for use as a vaccine immunogen.

P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5.

Structure of the malaria vaccine candidate antigen CyRPA and its complex with a parasite invasion inhibitory antibody.

Structural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPA.

P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton of the host RBC.

Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex.

Human Antibodies that Slow Erythrocyte Invasion Potentiate Malaria-Neutralizing Antibodies.