Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Raymonde Rosa"'
Autor:
Ernest Beutler, Richard J. Labotka, Michel Cohen-Solal, Raymonde Rosa, Raoul Wolf, Catherine Yim, Arthur S. Schneider, Beryl Westwood, Stefan Eber, Ahti Lammi
Publikováno v:
Blood Cells, Molecules, and Diseases. 22:115-125
In order to investigate the basis of the repeated occurrence of the 1591C mutation (TPI 1591C, 105 Glu-Asp) in multiple unrelated families throughout the world, we studied five microsatellite and short tandem repeat markers that lie within a 1.77 meg
Autor:
Constantin T. Craescu, M.C. Garel, Marie-Claude Calvin, Jean Rosa, Raymonde Rosa, Nicole Arous
Publikováno v:
Proceedings of the National Academy of Sciences. 91:3593-3597
To date no definite and undisputed treatment has been found for sickle cell anemia, which is characterized by polymerization of a deoxygenated hemoglobin mutant (HbS) giving rise to deformed erythrocytes and vasoocclusive complications. Since the ery
Autor:
Jean Rosa, Raymonde Rosa, Frédéric Galactéros, Virginie Joulin, Michel Cohen-Solal, Valérie Lemarchandel, Colette Valentin
Publikováno v:
Scopus-Elsevier
Erythrocyte bisphosphoglycerate mutase (BPGM) deficiency is a rare disease associated with a decrease in 2,3-diphosphoglycerate concentration. A complete BPGM deficiency was described in 1978 by Rosa et al (J Clin Invest 62:907, 1978) and was shown t
Publikováno v:
Biochimie, Vol. 74, No 6 (1992) pp. 519-526
Using the crystallographic structure of yeast monophosphoglycerate mutase (MPGM) as a framework we constructed a three-dimensional model of the homologous human erythrocyte bisphosphoglycerate mutase (BPGM). The modeling procedure consisted of substi
Autor:
Raymonde Rosa, Yves Blouquit, M.C. Garel, Michel Cohen-Solal, Philippe Leboulch, Judit Castella-Escola, Colette Valentin, Fernando Climent-Romeo, David M. Ojcius, Virginie Joulin
Publikováno v:
Gene. 91:225-232
The human muscle-specific phosphoglycerate mutase encoding gene (PGAM-M) has been cloned from a genomic cosmid library and sequenced. The sequence corresponding to the coding region was evaluated and revised by sequencing of the protein itself, fully
Autor:
Yves Blouquit, M.C. Garel, Michel Cohen-Solal, Marie-Claude Calvin, Marie-Odette Prehu, Raymonde Rosa, Jean-Philippe Rosa
Publikováno v:
Biochimie. 72:337-343
Bisphosphoglycerate mutase (EC 5.4.2.4.) is an erythrocyte-specific enzyme whose main function is to synthesize 2,3-diphosphoglycerate (glycerate-2,3-P2) an effector of the delivery of O2 in the tissues. In addition to its main synthase activity the
Autor:
Raymonde Rosa, Nicole Arous, Valérie Lemarchandel, Marie-Claude Calvin, M.C. Garel, Constantin T. Craescu, Jean Rosa, Marie-Odette Prehu
Publikováno v:
European journal of biochemistry. 213(1)
Human bisphosphoglycerate mutase (GriP2 mutase) is a trifunctional enzyme which synthesizes and degrades GriP2 in red cells. Among the amino acid residues involved in its active site there are two conserved histidine residues, His10 which is phosphor
Publikováno v:
Journal of molecular biology. 218(2)
Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c
Publikováno v:
Biochemical and Biophysical Research Communications. 368:837
Publikováno v:
Human Genetics. 38:209-215
A new case of a defect in red cell pyrimidine 5'-nucleotide (P5N) activity was found in a large family from Guadeloupe in the West Indies. The propositus presented a characteristic hemolytic anemia with red cell basophilic stippling, an increased GSH