@article{prehu_hb_2007,
	title = {Hb {BARIKA} (a42({C7}){Tyr}→{His} (a2)) {LEADS} {TO} {AN} a + -{THALASSEMIA}-{LIKE} {SYNDROME}},
	abstract = {In human deoxyhemoglobin (deoxyHb), the hydrogen bond between Aspβ99(G1) and Tyrα42(C7), located in the α1β2 interface, is crucial for the stability of the T structure. All the variants that could arise from a single point mutation affecting codon β99 have already been observed, leading always to erythrocytosis. Conversely, up to now, Hb Barika is the only example found in a patient in whom the α42 is mutated. From a biochemical point of view, for theoretical reasons, this substitution has already been extensively studied on recombinant hemoglobin (rHb). In the patient, Hb Barika is expressed at a level lower than expected for an α2 gene variant and leads to an α + -thalassemic-like syndrome.},
	author = {Préhu, Claude and Riou, Jean and Wajcman, Henri},
	month = jan,
	year = {2007},
	note = {MAG ID: 2141000168},
}

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