about
P688
Structure of malaria invasion protein RH5 with erythrocyte basigin and blocking antibodiesBasigin is a receptor essential for erythrocyte invasion by Plasmodium falciparumMultiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasionAnalyses of interactions between heparin and the apical surface proteins of Plasmodium falciparumP113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5An EGF-like protein forms a complex with PfRh5 and is required for invasion of human erythrocytes by Plasmodium falciparumEssential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium falciparum Invasion of ErythrocytesStructural basis for inhibition of erythrocyte invasion by antibodies to Plasmodium falciparum protein CyRPAPfRH5: a novel reticulocyte-binding family homolog of plasmodium falciparum that binds to the erythrocyte, and an investigation of its receptorRH5-Basigin interaction plays a major role in the host tropism of Plasmodium falciparum.Association of antibodies to Plasmodium falciparum reticulocyte binding protein homolog 5 with protection from clinical malaria.A PfRH5-based vaccine is efficacious against heterologous strain blood-stage Plasmodium falciparum infection in aotus monkeys.Crystal structure of PfRh5, an essential P. falciparum ligand for invasion of human erythrocytes.A full-length recombinant Plasmodium falciparum PfRH5 protein induces inhibitory antibodies that are effective across common PfRH5 genetic variants.Neutralization of Plasmodium falciparum merozoites by antibodies against PfRH5.Human Cyclophilin B forms part of a multi-protein complex during erythrocyte invasion by Plasmodium falciparum.Reticulocyte-binding protein homologue 5 - an essential adhesin involved in invasion of human erythrocytes by Plasmodium falciparum.A single amino acid change in the Plasmodium falciparum RH5 (PfRH5) human RBC binding sequence modifies its structure and determines species-specific binding activity.P. falciparum RH5-Basigin interaction induces changes in the cytoskeleton of the host RBC.Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex
P921
Q24289322-30BA2BBB-4ED9-4A41-937C-140D4BEB6A2AQ24297064-B0B92BFC-59AC-43FD-AA0F-4E9B5653DB9BQ27230042-33EDDFEB-98BF-4A43-8F93-3D10571643AFQ27972735-63793F5A-751B-420A-99B6-A89FEE9E0E00Q30042821-66BB8346-5B62-47D9-A0EB-368BF303C0B7Q30043132-F82CEC80-8502-42DA-890A-24F940D6A79EQ30049125-15009D0A-3AB1-4DF7-9961-1E6422FFE2FDQ30049152-4855787C-577C-4D13-86C4-0841D91DA233Q30049204-B9FE70CC-80E3-4891-8796-F6011B99D6A6Q30356310-E1410141-ED63-4549-A9EC-FDEC5C8216BFQ33820897-D4921A49-422F-41C8-BFFD-62C41FC3694BQ34978590-605B99D4-C3AD-4909-92F1-100804117AF8Q35167000-BED77524-A0FD-4859-9DD4-C26C1022A232Q36511421-2C18EA9C-4C20-4EDC-B063-991F57373809Q37412559-D6341240-799D-4A45-94E6-DD4F1ED1D2EEQ47125734-97E526EB-228F-455F-8BB8-B74A869F4048Q47887452-985E7236-79D7-483E-BDEB-3D6520613EEAQ47995418-1948637D-6C78-47E0-8D77-F70E1DD49988Q48274383-BB3AE4C0-A438-4121-91BD-E2559A44592BQ61703703-4315B829-37F5-41F2-B24C-8A77AE03B29D
P921
description
protein
@id
proteïne in Plasmodium falciparum 3D7
@nl
protèin
@ace
name
reticulocyte binding protein homologue 5
@en
reticulocyte binding protein homologue 5
@nl
type
label
reticulocyte binding protein homologue 5
@en
reticulocyte binding protein homologue 5
@nl
altLabel
MAL4P1.224
@en
PFD1145c
@en
prefLabel
reticulocyte binding protein homologue 5
@en
reticulocyte binding protein homologue 5
@nl
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P3382
PF3D7_0424100.1