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Disruption of a GATA motif in the Duffy gene promoter abolishes erythroid gene expression in Duffy–negative individuals
The mRNA for the Duffy blood group antigen, the erythrocyte receptor for the Plasmodium vivax malaria parasite, has recently been cloned and shown to encode a widely expressed chemokine receptor.Expand
The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast
The Rhesus blood-group antigens are defined by a complex association of membrane polypeptides that includes the non-glycosylated Rh proteins (RhD and RhCE) and the RHag glycoprotein, which isExpand
RhBG and RhCG, the putative ammonia transporters, are expressed in the same cells in the distal nephron.
Two nonerythroid homologs of the blood group Rh proteins, RhCG and RhBG, which share homologies with specific ammonia transporters in primitive organisms and plants, could represent members of a newExpand
A dominant mutation in the gene encoding the erythroid transcription factor KLF1 causes a congenital dyserythropoietic anemia.
The congenital dyserythropoietic anemias (CDAs) are inherited red blood cell disorders whose hallmarks are ineffective erythropoiesis, hemolysis, and morphological abnormalities of erythroblasts inExpand
Expression of RhCG, a new putative NH(3)/NH(4)(+) transporter, along the rat nephron.
Two non-erythroid members of the erythrocyte Rhesus (Rh) protein family, RhBG and RhCG, have been recently cloned in the kidney. These proteins share homologies with specific NH(3)/NH(4)(+)Expand
Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47.
Rh(null) red cells are characteristically stomato-spherocytic. This and other evidence suggest that the Rh complex represents a major attachment site between the membrane lipid bilayer and theExpand
Molecular cloning and primary structure of the human blood group RhD polypeptide.
The RH (rhesus) blood group locus from RhD-positive donors is composed of two homologous structural genes, one of which encodes the Cc and Ee polypeptides, whereas the other, which is missing in theExpand
Comparison of the carbohydrate-binding specificities of seven N-acetyl-D-galactosamine-recognizing lectins.
Seven plant lectins, Dolichos biflorus agglutinin (DBA), Griffonia simplicifolia agglutinin (GSA, isolectin A4), Helix pomatia agglutinin (HPA), soybean (Glycine max) agglutinin (SBA), Salvia sclareaExpand
Genetic basis of the RhD-positive and RhD-negative blood group polymorphism as determined by Southern analysis
Several lines of evidence have previously indicated that the RhD, c, and E blood group antigens are most likely carried by three distinct but homologous red blood cell membrane proteins. To determineExpand
RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane
We have determined CO2 permeabilities, PCO2, of red cells of normal human blood and of blood deficient in various blood group proteins by a previously described mass spectrometric technique. WhileExpand