Antibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytes
about
Identification and characterization of a novel Plasmodium falciparum adhesin involved in erythrocyte invasionPfRH2b specific monoclonal antibodies inhibit merozoite invasionPlasmodium falciparum merozoite invasion is inhibited by antibodies that target the PfRh2a and b binding domainsComplement receptor 1 is a sialic acid-independent erythrocyte receptor of Plasmodium falciparumPlasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human ErythrocytesUsing mutagenesis and structural biology to map the binding site for the Plasmodium falciparum merozoite protein PfRh4 on the human immune adherence receptor.A thrombospondin structural repeat containing rhoptry protein from Plasmodium falciparum mediates erythrocyte invasionPlasmodium falciparum merozoite surface protein 3: oligomerization, self-assembly, and heme complex formationPlasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasionAn EGF-like protein forms a complex with PfRh5 and is required for invasion of human erythrocytes by Plasmodium falciparumComplement receptor 1 is the host erythrocyte receptor for Plasmodium falciparum PfRh4 invasion ligand.Insights into the Immunological Properties of Intrinsically Disordered Malaria Proteins Using Proteome Scale Predictions.Plasmodium falciparum uses a key functional site in complement receptor type-1 for invasion of human erythrocytes.Triggers of key calcium signals during erythrocyte invasion by Plasmodium falciparumPlasmodium falciparum reticulocyte binding-like homologue protein 2 (PfRH2) is a key adhesive molecule involved in erythrocyte invasion.Complement receptor 1 and malaria.Lack of evidence from studies of soluble protein fragments that Knops blood group polymorphisms in complement receptor-type 1 are driven by malaria.The blood-stage malaria antigen PfRH5 is susceptible to vaccine-inducible cross-strain neutralizing antibody.The Plasmodium falciparum erythrocyte invasion ligand Pfrh4 as a target of functional and protective human antibodies against malaria.Reticulocyte and erythrocyte binding-like proteins function cooperatively in invasion of human erythrocytes by malaria parasitesEvidence for erythrocyte-binding antigen 175 as a component of a ligand-blocking blood-stage malaria vaccine.Network-based gene prediction for Plasmodium falciparum malaria towards genetics-based drug discovery.Characterization of Inhibitors and Monoclonal Antibodies That Modulate the Interaction between Plasmodium falciparum Adhesin PfRh4 with Its Erythrocyte Receptor Complement Receptor 1.Enhancing blockade of Plasmodium falciparum erythrocyte invasion: assessing combinations of antibodies against PfRH5 and other merozoite antigens.Structurally conserved erythrocyte-binding domain in Plasmodium provides a versatile scaffold for alternate receptor engagement.Comparison of allele frequencies of Plasmodium falciparum merozoite antigens in malaria infections sampled in different years in a Kenyan populationIdentification of a reticulocyte-specific binding domain of Plasmodium vivax reticulocyte-binding protein 1 that is homologous to the PfRh4 erythrocyte-binding domain.Identification and prioritization of merozoite antigens as targets of protective human immunity to Plasmodium falciparum malaria for vaccine and biomarker development.Erythrocyte-binding antigens of Plasmodium falciparum are targets of human inhibitory antibodies and function to evade naturally acquired immunity.Identifying novel Plasmodium falciparum erythrocyte invasion receptors using systematic extracellular protein interaction screensReticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparumcAMP-dependent protein kinase from Plasmodium falciparum: an update.Cytoskeletal and membrane remodelling during malaria parasite invasion of the human erythrocyte.Structural characterization of the erythrocyte binding domain of the reticulocyte binding protein homologue family of Plasmodium yoelii.Differences in erythrocyte receptor specificity of different parts of the Plasmodium falciparum reticulocyte binding protein homologue 2a.Identification and immunological characterization of the ligand domain of Plasmodium vivax reticulocyte binding protein 1a.Optimization of incubation conditions of Plasmodium falciparum antibody multiplex assays to measure IgG, IgG1-4, IgM and IgE using standard and customized reference pools for sero-epidemiological and vaccine studies.
P2860
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P2860
Antibodies to reticulocyte binding protein-like homologue 4 inhibit invasion of Plasmodium falciparum into human erythrocytes
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@ast
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@en
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@nl
type
label
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@ast
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@en
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@nl
prefLabel
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@ast
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@en
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@nl
P2860
P50
P921
P3181
P356
P1476
Antibodies to reticulocyte bin ...... iparum into human erythrocytes
@en
P2093
Linda Reiling
P2860
P304
P3181
P356
10.1128/IAI.00048-09
P407
P577
2009-06-01T00:00:00Z