References
- Thein SL. The molecular basis of β-thalassemia. Cold Spring Harb Perspect Med. 2013;3(5):a011700. (hppt://www.ncbi.nlm.nih.gov/pubmed/23637309)
- Thom CS, Dickson CF, Gell DA, Weiss MJ. Hemoglobin variants: Biochemical properties and clinical correlates. Cold Spring Harb Perspect Med. 2013;3(3):a011858. (hppt://www.ncbi.nlm.nih.gov/pubmed/23388674)
- Kumar R, Tamhankar PM, Panigrahi I, et al. A novel β-globin mutation (HBB:c.107A > G; or codon 35 β (A→G)) at α-β interfaces. Ann Hematol. 2009;88(12):1269–1271
- Asakura T, Adachi K, Schwartz E, Wiley J. Molecular stability of Hb Philly (). The relationship of hemoglobin stability to ligand state as defined by heat and mechanical shaking tests. Hemoglobin. 1981;5(2):177–190
- Nakatsukasa T, Nomura N, Miyazaki G, et al. The artificial α1β1-contact mutant hemoglobin, Hb Phe-35β, shows only small functional abnormalities. FEBS Lett. 1998;441(1):93–96
- Kavanaugh JS, Weydert JA, Rogers PH, et al. Site-directed mutations of human hemoglobin at residue 35β: A residue at the intersection of the α1β1, α1β2, and α1α2 interfaces. Protein Sci. 2001;10(9):1847–1855