Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
about
A malaria invasion receptor, the 175-kilodalton erythrocyte binding antigen of Plasmodium falciparum recognizes the terminal Neu5Ac(alpha 2-3)Gal- sequences of glycophorin AFalciparum malaria parasites invade erythrocytes that lack glycophorin A and B (MkMk). Strain differences indicate receptor heterogeneity and two pathways for invasionIdentification of two new hemagglutinins of Escherichia coli, N-acetyl-D-glucosamine-specific fimbriae and a blood group M-specific agglutinin, by cloning the corresponding genes in Escherichia coli K-12Identification and expression in Escherichia coli of merozoite stage-specific genes of the human malarial parasite Plasmodium falciparum.Antibodies in malarial sera to parasite antigens in the membrane of erythrocytes infected with early asexual stages of Plasmodium falciparum.Surface proteins of Plasmodium falciparum merozoites binding to the erythrocyte receptor, glycophorin.Antimalarial immunity in Saimiri monkeys. Immunization with surface components of asexual blood stages.Polymorphism of a high molecular weight schizont antigen of the human malaria parasite Plasmodium falciparum.Possible pitfalls in the identification of glycophorin-binding proteins of Plasmodium falciparumExpression of Plasmodium falciparum surface antigens in Escherichia coli.Role of the carbohydrate domains of glycophorins as erythrocyte receptors for invasion by Plasmodium falciparum merozoitesDifferentiation of human erythroid cells is associated with increased O-glycosylation of the major sialoglycoprotein, glycophorin A.Human antibodies to a Mr 155,000 Plasmodium falciparum antigen efficiently inhibit merozoite invasion.Specific binding of neoglycoproteins to Toxoplasma gondii tachyzoites.Host cell response to coccidian infection: an introspective survey.Primary structure of the 175K Plasmodium falciparum erythrocyte binding antigen and identification of a peptide which elicits antibodies that inhibit malaria merozoite invasion.Erythrophagocytosis of desialylated red blood cells is responsible for anaemia during Trypanosoma vivax infection.Carbohydrate-binding specificities of anti-erythrocyte lectins (haemagglutinins) in Anopheles gambiae gut extracts and haemolymph.
P2860
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P2860
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
description
1983 nî lūn-bûn
@nan
1983年の論文
@ja
1983年学术文章
@wuu
1983年学术文章
@zh
1983年学术文章
@zh-cn
1983年学术文章
@zh-hans
1983年学术文章
@zh-my
1983年学术文章
@zh-sg
1983年學術文章
@yue
1983年學術文章
@zh-hant
name
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@en
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@nl
type
label
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@en
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@nl
prefLabel
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@en
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@nl
P2093
P356
P1433
P1476
Lectin-like polypeptides of P. falciparum bind to red cell sialoglycoproteins.
@en
P2093
P2888
P304
P356
10.1038/301704A0
P407
P577
1983-02-01T00:00:00Z
P6179
1000176171