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cysteic acid/hypoxia

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ČlanciKliničkim ispitivanjimaPatenti
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After reacting with hydrogen peroxide (H2O2), sickle-cell hemoglobin (HbS, βE6V) remains longer in a highly oxidizing ferryl form (HbFe4+=O) and induces irreversible oxidation of "hot-spot" amino acids, including βCys-93. To control the damaging ferryl

Antisickling Drugs Targeting βCys93 Reduce Iron Oxidation and Oxidative Changes in Sickle Cell Hemoglobin.

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Sickle cell disease is a genetic blood disorder caused by a single point mutation in the β globin gene where glutamic acid is replaced by valine at the sixth position of the β chain of hemoglobin (Hb). At low oxygen tension, the polymerization of deoxyHbS into fibers occurs in red blood cells (RBCs)
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