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Archive | 1986

Serological and Biochemical Investigations on the N.E. Variety of the Dantu Red Cell Phenotype

Wolfgang Dahr; John J. Moulds; Phyllis Unger; Dominique Blanchard; Jean Pierre Cartron

Studies during the last decade have established that the MNSs blood group locus corresponds to two, presumably adjacent, genes whiff encode the amino-acid sequences of two (MN and Ss) sialoglycoproteins (SGPs) or glycophorins (A and B) in human red cell (RBC) membranes (reviews: 1–4). The structural difference between the M and N antigens is determined by amino-acid polymorphisms at the 1st (Ser/Leu) and 5th (Gly/Glu) positions of the MN SGP, the complete sequence of which was elucidated (5–8). The sequence of the N-terminal 26 residues (res.) of the Ss SGP is identical with that of the N-specific MN SGP (8,9). This explains the occurrence of an additional N antigen, denoted as ‘N’, on the Ss SGP. A Met/Thr polymorphism at the 29th position of the Ss SGP represents the structural difference between the S and s antigens (8). Recently (10), the sequence of the intramembraneous domain (res. 36–72) of the Ss SGP was determined and found to be rather similar to the corresponding region (res. 65–101) of the MN SGP (Fig. 1).


Archive | 1988

Biochemical Characterization of Class VII and VIII Cells within the Miltenberger System

Wolfgang Dahr; Konrad Beyreuther; E. Dybkjaer; J. Moulds; V. Vengelen-Tyler

The various antigens of the MNSs blood group system are located on two homologous, sialic acid-rich glycoproteins (SGPs) in human red blood cell (RBC) membranes: glycophorin A (GP A; MN SGP; α) and GP B (Ss SGP or δ) (for reviews see Dahr 1986; Lisowska 1987; Moulds & Dahr 1987). The ‘MNSs locus’, located on chromosome 4, appears to comprise two adjacent genes that encode the amino-acid sequences of these two molecules.


Biological Chemistry | 1980

Structure of the Ss Blood Group Antigens, II. A Methionine/Threonine Polymorphism within the N-terminal Sequence of the Ss Glycoprotein

Wolfgang Dahr; Konrad Beyreuther; Heinz Steinbach; Wilhelm Gielen; Jürgen Krüger


FEBS Journal | 1982

N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C) from human erythrocyte membranes.

Wolfgang Dahr; Konrad Beyreuther; Maria Kordowicz; Jürgen Krüuger


Biological chemistry Hoppe-Seyler | 1985

Altered membrane sialoglycoproteins in human erythrocytes lacking the Gerbich blood group antigens.

Wolfgang Dahr; John J. Moulds; Gertrud Baumeister; Marilyn Moulds; Siegrid Kiedrowski; Michael Hummel


Biological Chemistry | 1980

Structure of the Ss blood group antigens. I. Isolation of Ss-active glycopeptides and differentiation of the antigens by modification of methionine.

Wolfgang Dahr; Wilhelm Gielen; Konrad Beyreuther; Jürgen Krüger


FEBS Journal | 1987

Gerbich blood group deficiency of the Ge:-1,-2,-3 and Ge :-1,-2,3 types Immunochemical study and genomic analysis with cDNA probes

Caroline Le Van Kim; Yves Colin; Dominique Blanchard; Wolfgang Dahr; Jaqueline London; Jean-Pierre Cartron


Biological chemistry Hoppe-Seyler | 1986

High frequency antigens of human erythrocyte membrane sialoglycoproteins, III. Studies on the EnaFR, Wrb and Wra antigens.

Wolfgang Dahr; Susan L. Wilkinson; Peter D. Issitt; Konrad Beyreuther; Michael Hummel; Phyllis Morel


FEBS Journal | 1989

Structural homology between glycophorins C and D of human erythrocytes

Bouchra El-Maliki; Dominique Blanchard; Wolfgang Dahr; Konrad Beyreuther; Jean-Pierre Cartron


FEBS Journal | 1987

Hybrid glycophorins from human erythrocyte membranes Isolation and complete structural analysis of the novel sialoglycoprotein from St(a + ) red cells

Dominique Blanchard; Wolfgang Dahr; Konrad Beyreuther; John J. Moulds; Jean-Pierre Cartron

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Bernard Fournet

Centre national de la recherche scientifique

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Maria Kordowicz

Polish Academy of Sciences

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E. Dybkjaer

University of Copenhagen

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