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A New Hemoglobin Variant with Sickling Properties
New England Journal of Medicine, 1963THE red-cell sickling tendency of certain persons has long been a matter of great interest. Study of this problem by Pauling and his associates1 led to the suggestion of a genetic change in hemoglobin formation that resulted in synthesis of different globin fractions for normal and sickle-cell hemoglobin.
L E, PIERCE, C E, RATH, K, McCOY
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Ultrastructural Features of Erythrocyte and Hemoglobin Sickling
Archives of Internal Medicine, 1974Hemoglobin polymerization develops from a process of condensation, molecular interaction, aggregation, and assembly. Molecular organization of structures formed during polymerization depends on the type of hemoglobin, its specific defect, and its state of oxygenation. Sickling exemplifies hemoglobin polymerization.
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Screening for sickle hemoglobin??? a review
The American Journal of the Medical Sciences, 1973D W, Westring, S, Grand
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Stereospecific Inhibitors of the Gelation of Sickle Hemoglobin
Hemoglobin, 1980During the last decade there have been major advances in understanding the structure of the gel of deoxyhemoglobin S and the mechanism of its formation. These advances have allowed the development of a new strategy for the inhibition of gelation, i.e., stereospecific competitive inhibitors of the polymerization process.
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Neonatal Screening for Sickle Hemoglobin
American Journal of Clinical Pathology, 1979G, Serjeant, B, Serjeant
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Filter failures with sickling hemoglobin
Transfusion, 2009Eapen K, Jacob +4 more
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Structural analysis of polymers of sickle cell hemoglobin. I. Sickle hemoglobin fibers.
Journal of molecular biology, 1988The structure of fibers of deoxyhemoglobin S has been under investigation for several years and a number of different models have been proposed for the arrangement of molecules within the particles. We have used reconstruction and modeling techniques in our analysis of these structures.
B, Carragher +4 more
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