RP Naik, C Haywood Jr - Hematology 2014, the American …, 2015 - ashpublications.org
The sickle hemoglobin (HbS) point mutation has independently undergone evolutionary selection at least five times in the world because of its overwhelming malarial protective …
In the new edition of this successful and authoritative book, the thalassaemias are reviewed in detail with respect to their clinical features, cellular pathology, molecular genetics …
MH Steinberg - The Scientific World Journal, 2009 - Wiley Online Library
The clinical course of patients with sickle cell anemia, a Mendelian trait, is characteristically highly variable. HbF concentration and the presence of a thalassemia are established …
SL Thein - British journal of haematology, 2008 - Wiley Online Library
Identification of the molecular basis of the β‐thalassaemias and sickle cell disease (SCD) has made it clear that patients with the same β‐globin genotypes can have very variable …
MH Steinberg, GP Rodgers - Seminars in hematology, 2001 - Elsevier
Sickle hemoglobin (HbS), caused by a point mutation in the β-globin gene of hemoglobin, polymerizes when deoxygenated. The pathophysiology of sickle cell disease results from …
GD Pule, S Mowla, N Novitzky… - Expert review of …, 2015 - Taylor & Francis
Aim: To report on molecular mechanisms of fetal hemoglobin (HbF) induction by hydroxyurea (HU) for the treatment of sickle cell disease. Study Design: Systematic review …
Sickle cell disease is caused by a mutation in the β-globin chain of the haemoglobin molecule. Sickle haemoglobin, the result of this mutation, has the singular property of …
L Quek, SL Thein - British journal of haematology, 2007 - Wiley Online Library
The β‐thalassaemias have a major global impact on health and mortality. Allogeneic haemopoietic stem cell transplantation is the only approach that may lead to a cure but this …
L Manca, B Masala - IUBMB life, 2008 - Wiley Online Library
Fetal hemoglobin (HbF), the predominant hemoglobin in the fetus, is a mixture of two molecular species (α2Gγ2 and α2Aγ2) that differ only at position 136 reflecting the products …