Receptor-like specificity of a Plasmodium knowlesi malarial protein that binds to Duffy antigen ligands on erythrocytes
about
The cellular and molecular basis for malaria parasite invasion of the human red blood cellPlasmodium vivax DBP binding to Aotus nancymaae erythrocytes is Duffy antigen dependentA malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(alpha 2-3)Gal- sequences of glycophorin AA novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytesDimerization of Plasmodium vivax DBP is induced upon receptor binding and drives recognition of DARCMalaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responsesPlasmodium vivax invasion of human erythrocytes inhibited by antibodies directed against the Duffy binding proteinErythrocyte Binding Activity Displayed by a Selective Group of Plasmodium vivax Tryptophan Rich Antigens Is Inhibited by Patients' AntibodiesAncient human sialic acid variant restricts an emerging zoonotic malaria parasiteCharacterization of a membrane-associated rhoptry protein of Plasmodium falciparumA Plasmodium falciparum homologue of Plasmodium vivax reticulocyte binding protein (PvRBP1) defines a trypsin-resistant erythrocyte invasion pathwayA family of erythrocyte binding proteins of malaria parasites.Changes in parasite virulence induced by the disruption of a single member of the 235 kDa rhoptry protein multigene family of Plasmodium yoelii.Plasmodium falciparum field isolates commonly use erythrocyte invasion pathways that are independent of sialic acid residues of glycophorin AFy(a)/Fy(b) antigen polymorphism in human erythrocyte Duffy antigen affects susceptibility to Plasmodium vivax malariaEvidence for a switching mechanism in the invasion of erythrocytes by Plasmodium falciparum.Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasionNatural variation within the principal adhesion domain of the Plasmodium vivax duffy binding proteinDefining the erythrocyte binding domains of Plasmodium vivax tryptophan rich antigen 33.5.Finding the sweet spots of inhibition: understanding the targets of a functional antibody against Plasmodium vivax Duffy binding proteinTargeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion.Design and immunogenicity of a novel synthetic antigen based on the ligand domain of the Plasmodium vivax duffy binding protein.Species-specific features of DARC, the primate receptor for Plasmodium vivax and Plasmodium knowlesi.Plasmodium simium, a Plasmodium vivax-related malaria parasite: genetic variability of Duffy binding protein II and the Duffy antigen/receptor for chemokines.Recognition of Human Erythrocyte Receptors by the Tryptophan-Rich Antigens of Monkey Malaria Parasite Plasmodium knowlesi.Conserved and variant epitopes of Plasmodium vivax Duffy binding protein as targets of inhibitory monoclonal antibodies.Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175Proteases in host cell invasion by the malaria parasite.A new release on life: emerging concepts in proteolysis and parasite invasion.A Stem Cell Strategy Identifies Glycophorin C as a Major Erythrocyte Receptor for the Rodent Malaria Parasite Plasmodium berghei.Characterization of Inhibitors and Monoclonal Antibodies That Modulate the Interaction between Plasmodium falciparum Adhesin PfRh4 with Its Erythrocyte Receptor Complement Receptor 1.The domain on the Duffy blood group antigen for binding Plasmodium vivax and P. knowlesi malarial parasites to erythrocytes.Adaptation of the genetically tractable malaria pathogen Plasmodium knowlesi to continuous culture in human erythrocytes.Mapping regions containing binding residues within functional domains of Plasmodium vivax and Plasmodium knowlesi erythrocyte-binding proteins.Invasion of host cells by malaria parasites: a tale of two protein families.Role of Plasmodium vivax Duffy-binding protein 1 in invasion of Duffy-null Africans.Red blood cell polymorphism and susceptibility to Plasmodium vivax.Gene encoding erythrocyte binding ligand linked to blood stage multiplication rate phenotype in Plasmodium yoelii yoelii.Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparumConserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition.
P2860
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P2860
Receptor-like specificity of a Plasmodium knowlesi malarial protein that binds to Duffy antigen ligands on erythrocytes
description
1988 nî lūn-bûn
@nan
1988 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@ast
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@en
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@nl
type
label
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@ast
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@en
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@nl
prefLabel
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@ast
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@en
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@nl
P2093
P2860
P921
P3181
P356
P1476
Receptor-like specificity of a ...... ntigen ligands on erythrocytes
@en
P2093
D E Hudson
J D Haynes
J P Dalton
L H Miller
M H McGinniss
T J Hadley
P2860
P304
P3181
P356
10.1084/JEM.167.6.1873
P407
P577
1988-06-01T00:00:00Z