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The Rh blood group system: a review.
The purpose of this review is to provide an overview of several aspects of the Rh blood group system, including the confusing terminology, progress in molecular understanding, and how this developing knowledge can be used in the clinical setting.
Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175
The interest in BAEBL's reduced binding to Gerbich erythrocytes derives from the high frequency of theGerbich phenotype in some regions of Papua New Guinea where P. falciparum is hyperendemic.
Isolation and functional characterization of human erythroblasts at distinct stages: implications for understanding of normal and disordered erythropoiesis in vivo.
By examining the dynamic changes of expression of membrane proteins during in vitro human terminal erythroid differentiation, band 3 and α4 integrin are identified as optimal surface markers for isolating 5 morphologically distinct populations at successive developmental stages and should facilitate a comprehensive cellular and molecular characterization of each specific developmental stage of human erythroblasts.
Glycophorin C is the receptor for the Plasmodium falciparum erythrocyte binding ligand PfEBP-2 (baebl).
It is reported in this paper that glycophorin C (GPC) is the receptor for PfEBP-2 (baebl, EBA-140), the newly identified erythrocyte binding ligand of Plasmodium falciparum, and the binding domain on GPC is potentially restricted to amino acid residues 14 through 22 within exon 2.
Erythrocyte detergent-resistant membrane proteins: their characterization and selective uptake during malarial infection.
Ten internalized DRM proteins show varied lipid and peptidic anchors indicating that, contrary to the prevailing model of apicomplexan vacuole formation, DRM association, rather than lipid anchors, provides the preferred criteria for protein recruitment to the malarial vacuoles.
The molecular genetics of the human I locus and molecular background explain the partial association of the adult i phenotype with congenital cataracts.
It is demonstrated that the human I locus expresses 3 IGnT forms, designated IGnTA, IGnTB, and IGnTC, which have different exon 1, but identical exons 2 and 3, coding regions, which offer a new perspective on the formation and expression of the I antigen in different cells and provide insight into the questions derived from investigation of the adult i phenotype.
Localization of the protein 4.1-binding site on human erythrocyte glycophorins C and D.
It is shown that purified protein 4.1 binds much less strongly to alkali-stripped membranes from erythrocytes of individuals with total glycophorin C and D deficiency (Leach phenotype) than to alkaline- Stripped normal membranes.