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Illuminating "the dark side of the HBB": Visualizing the full spectrum of Cas9 outcomes. [PDF]
Scalisi G, Laurent M, Amendola M.
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Sickle cell hemoglobin, primaquine sensitivity and their correlation. 1. Sickle cell hemoglobin.
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2020
Sickle cell hemoglobin (HbS) is an example of a genetic variant of human hemoglobin where a point mutation in the β globin gene results in substitution of glutamic acid to valine at sixth position of the β globin chain. Association between tetrameric hemoglobin molecules through noncovalent interactions between side chain residue of βVal6 and ...
Amit Kumar, Mandal +2 more
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Sickle cell hemoglobin (HbS) is an example of a genetic variant of human hemoglobin where a point mutation in the β globin gene results in substitution of glutamic acid to valine at sixth position of the β globin chain. Association between tetrameric hemoglobin molecules through noncovalent interactions between side chain residue of βVal6 and ...
Amit Kumar, Mandal +2 more
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Effect of piracetam on sickle erythrocytes and sickle hemoglobin
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1981Piracetam, 2-oxo-1-pyrrolidine acetamide, inhibits sickling of red cells containing sickle hemoglobin (Hb S). The concentration required for 50% inhibition is about 300 mM. Addition of piracetam into the supersaturated Hb S solution in concentrated phosphate buffer prolongs the delay time prior to gelation.
T, Asakura +6 more
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Alternative diaspirins for modification of hemoglobin and sickle hemoglobin
Archives of Biochemistry and Biophysics, 1984Studies of modification of hemoglobin and of sickle hemoglobin by alternative aspirins have been extended to a series of new bis esters with a variety of substituted bridging diacids and to a group of mono esters with polar acyl groups. Rates of hydrolysis of these alternative aspirins have also been examined, and they reveal that a careful balance ...
E J, Delaney +3 more
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Crowding and the polymerization of sickle hemoglobin
Journal of Molecular Recognition, 2004AbstractUnder physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A with a surface hydrophobic valine in place of a negatively charged glutamic acid, polymerizes at high volume occupancy. Equilibrium solubility of sickle hemoglobin entails activity coefficients that can approach 103 at high concentrations.
Frank A, Ferrone, Maria A, Rotter
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On the assembly of sickle hemoglobin fascicles
Journal of Molecular Biology, 1989Deoxyhemoglobin S fibers associate into bundles, or fascicles, that subsequently crystallize by a process of alignment and fusion. We have used electron microscopy to study the formation of fascicles and the changes in fiber packing that occur during the conversion of fascicles to crystals.
W A, McDade +3 more
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The interactions of sickle hemoglobin
Biochimie, 1972Resume Les interactions entre molecules d'hemoglobine qui conduisent a la falciformation des erythrocytes, aux crises micro-emboliques et a l'anemie chronique sont dues a la presence de la desoxyhemoglobine S (α 2 a β 2 6Val ). Au cours de la desoxygenation la viscosite des solutions concentrees d'hemoglobine S augmente progressivement; il y a ...
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