Georges Schapira
Affiliations: | Biochemistry | CNRS, Paris, Île-de-France, France |
Area:
Molecular BiologyGoogle:
"Georges Schapira"Mean distance: 42746.4 (cluster 56)
Cross-listing: Neurotree
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Publications
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Delaunay J, Maleknia N, Schapira G. (1971) Rabbit hemoglobin. The heterogeneity of the beta-chain. Biochimica Et Biophysica Acta. 229: 712-5 |
Blum N, Maleknia N, Schapira G. (1970) [Regulation of the synthesis of hemoglobin by its subunits]. Bulletin De La Sociã©Tã© De Chimie Biologique. 52: 1279-86 |
Schapira G, Kruh J, Labie D, et al. (1970) [Genetic control of hemoglobin biosynthesis and its abnormalities]. Annales De Mã©Decine Interne. 121: 619-23 |
Schapira G, Benrubi M, Maleknia N, et al. (1969) [Rabbit hemoglobin: a varient resulting from allelomorphism and not from an ambiguiity: Hb a 29 Val replaced by Leu]. Biochimica Et Biophysica Acta. 188: 216-21 |
Blum N, Maleknia N, Schapira G. (1969) [Free alpha-hemoglobin and hemoglobin biosynthesis]. Biochimica Et Biophysica Acta. 179: 448-63 |
Schapira G, Benrubi M, Dreyfus JC, et al. (1969) [Problem of ambiguity during hemoglobin synthesis in rabbits: demonstration of RNA messenger specifically translating hemoglobin]. Bulletin De La Sociã©Tã© De Chimie Biologique. 51: 1546-7 |
Maleknia N, Blum N, Schapira G. (1969) [On the existance of alpha, beta, and alpha-beta globin partially bound to hemoglobin]. Comptes Rendus Hebdomadaires Des Sã©Ances De L'Acadã©Mie Des Sciences. Sã©Rie D: Sciences Naturelles. 268: 2631-4 |
Schapira G, Benrubi M, Maleknia N, et al. (1969) Hemoglobine de lapin: une variante resultant d'un allelomorphisme et non d'une ambiguite: Hbα 29 Val → Leu Biochimica Et Biophysica Acta (Bba) - Protein Structure. 188: 216-221 |
Blum N, Maleknia N, Schapira G. (1969) α-Hémoglobine libre et biosynthèse de l'hémoglobine Biochimica Et Biophysica Acta (Bba) - Nucleic Acids and Protein Synthesis. 179: 448-463 |
Schapira G, Dreyfus JC, Maleknia N. (1968) The ambiguities in the rabbit hemoglobin: evidence for a messenger RNA translated specifically into hemoglobin. Biochemical and Biophysical Research Communications. 32: 558-61 |