References
- Marengo-Rowe AJ. Structure-function relations of human hemoglobins. Proceedings. 2006;19(3):239–245.
- Thom CS, Dickson CF, Gell DA, et al. Hemoglobin variants: biochemical properties and clinical correlates. Cold Spring Harb Perspect Med. 2013;3(3):a011858.
- Vinogradov SN, Hoogewijs D, Bailly X, et al. A model of globin evolution. Gene. 2007;398(1–2):132–142.
- Thein SL. Is it dominantly inherited β thalassaemia or just a β-chain variant that is highly unstable? Br J Haematol. 1999;107(1):12–21.
- Thein SL. Pathophysiology of β thalassemia–a guide to molecular therapies. Hematol Am Soc Hematol Educ Program. 2005;2005(1):31–37.
- Mettananda S, Higgs DR. Molecular basis and genetic modifiers of thalassemia. Hematol Oncol Clin North Am. 2018;32(2):177–191.
- Modell B, Darlison M. Global epidemiology of haemoglobin disorders and derived service indicators. Bull World Health Organ. 2008;86(6):480–487.
- Ma J, Wang S, Zhao F, et al. Protein threading using context-specific alignment potential. Bioinformatics. 2013;29(13):i257–i265.
- Adzhubei IA, Schmidt S, Peshkin L, et al. A method and server for predicting damaging missense mutations. Nat Methods. 2010;7(4):248–249.
- Sim N-L, Kumar P, Hu J, et al. SIFT web server: predicting effects of amino acid substitutions on proteins. Nucleic Acids Res. 2012;40(W1):W452–W457.
- Vaser R, Adusumalli S, Leng SN, et al. SIFT missense predictions for genomes. Nat Protoc. 2016;11(1):1–9.
- Schwarz JM, Cooper DN, Schuelke M, et al. MutationTaster2: mutation prediction for the deep-sequencing age. Nat Methods. 2014;11(4):361–362.
- Richards S, Aziz N, Bale S, et al. Standards and guidelines for the interpretation of sequence variants: a joint consensus recommendation of the American College of Medical Genetics and Genomics and the Association for Molecular Pathology. Genet Med. 2015;17(5):405–424.
- Giardine BM, Joly P, Pissard S, et al. Clinically relevant updates of the HbVar database of human hemoglobin variants and thalassemia mutations. Nucleic Acids Res. 2021;49(D1):D1192–D1196.
- Hollender A, Lorkin PA, Lehmann H, et al. New unstable haemoglobin borås: β 88 (F4) leucine-arginine. Nature. 1969;222(5197):953–955.
- Fais A, Sollaino MC, Barella S, et al. A new β chain hemoglobin variant with increased oxygen affinity: Hb Santa Giusta Sardegna [β93(F9)Cys→Trp; HBB c.282T>G]. Hemoglobin. 2012;36(2):151–156.
- Angastiniotis M, Modell B. Global epidemiology of hemoglobin disorders. Ann NY Acad Sci. 1998;850:251–269.
- Ojodu J, Hulihan MM, Pope SN, et al. Incidence of sickle cell trait. MMWR Morb Mortal Wkly Rep. 2010;63(49):1155–1158.
- Perea FJ, Magaña MT, Cobián JG, et al. Molecular spectrum of β-thalassemia in the Mexican population. Blood Cells Mol Dis. 2004;33(2):150–152.
- Cobián JG, Sánchez-López JY, Magaña MT, et al. Types and frequencies of hemoglobin disorders in the pacific coast of four states of Mexico. Rev Invest Clin. 2009;61(5):399–404.
- Thein SL. The molecular basis of β-thalassemia. Cold Spring Harb Perspect Med. 2013;3(5):a011700.
- Schoenberg DR, Maquat LE. Regulation of cytoplasmic mRNA decay. Nat Rev Genet. 2012;13(4):246–259.
- Hall GW, Thein S. Nonsense codon mutations in the terminal exon of the β-globin gene are not associated with a reduction in β-mRNA accumulation: a mechanism for the phenotype of dominant β-thalassemia. Blood. 1994;83(8):2031–2037.
- Stamler JS, Jia L, Eu JP, et al. Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient. Science. 1997;276(5321):2034–2037.
- Chan NL, Rogers PH, Arnone A. Crystal structure of the S-nitroso form of liganded human hemoglobin. Biochemistry. 1998;37(47):16459–16464.
- Jia L, Bonaventura C, Bonaventura J, et al. S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 1996;380(6571):221–226.