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Molecular basis of α-thalassemia

Farashi, Samaneh, Harteveld, Cornelis L.·2018·Blood Cells, Molecules, and Diseases
DOI 10.1016/j.bcmd.2017.09.004
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CC-BY-NC-ND · From the PDF
Fig. 1 Schematic presentation of the chromosomal location of the α - and β -globin gene clusters on 16p and 11p respectively. The embryonic and foetal genes are indicated as open boxes. The genes which remain active throughout postnatal life in grey and black. The di ff erent hemoglobins expressed during the embryonic period are shown, from left to right Hb Gower-1 ( ζ 2 ε 2), Hb Gower-2 ( α 2 ε 2) and Hb Portland ( ζ 2 γ 2), foetal period (HbF) and postnatal period (HbA and HbA2).
Fig. 1 Schematic presentation of the chromosomal location of the α - and β -globin gene clusters on 16p and 11p respectively. The embryonic and foetal genes are indicated as open boxes. The genes which remain active throughout postnatal life in grey and black. The di ff erent hemoglobins expressed during the embryonic period are shown, from left to right Hb Gower-1 ( ζ 2 ε 2), Hb Gower-2 ( α 2 ε 2) and Hb Portland ( ζ 2 γ 2), foetal period (HbF) and postnatal period (HbA and HbA2).CC-BY-NC-ND · From the PDF
Fig. 2 Classi fi cation of α -thalassemia defects and phenotypic expression.
Fig. 2 Classi fi cation of α -thalassemia defects and phenotypic expression.CC-BY-NC-ND · From the PDF
Fig. 3 Deletions that cause α + -thalassemia. The homologous duplication units X, Y and Z in which the α -globin genes are embedded are indicated as coloured boxes. A cross-over between the mis-paired Z boxes during meiosis gives rise to (a) the α 3.7 and ααα anti 3.7 chromosomes. (b) Cross-over between misaligned X-boxes give rise to α 4.2 and ααα anti 4.2 .
Fig. 3 Deletions that cause α + -thalassemia. The homologous duplication units X, Y and Z in which the α -globin genes are embedded are indicated as coloured boxes. A cross-over between the mis-paired Z boxes during meiosis gives rise to (a) the α 3.7 and ααα anti 3.7 chromosomes. (b) Cross-over between misaligned X-boxes give rise to α 4.2 and ααα anti 4.2 .CC-BY-NC-ND · From the PDF
Fig. 4 Schematic presentation of the α -globin gene cluster and surrounding genes on the telomeric end of chromosome 16p. The telomere is represented as an oval, genes are shown as boxes. The α -globin regulatory region (MCS-R 1 to 4) is indicated as vertical bars. The scale is in kilobases (kb). Below the α -gene cluster is shown enlarged with the traditional and HGVS gene annotation. The most common α -thalassemia ( α -thal) deletions are indicated as grey bars indicating the length of the deletion and the annotation and subdivided into α + - and α 0 -thalassemia deletions.
Fig. 4 Schematic presentation of the α -globin gene cluster and surrounding genes on the telomeric end of chromosome 16p. The telomere is represented as an oval, genes are shown as boxes. The α -globin regulatory region (MCS-R 1 to 4) is indicated as vertical bars. The scale is in kilobases (kb). Below the α -gene cluster is shown enlarged with the traditional and HGVS gene annotation. The most common α -thalassemia ( α -thal) deletions are indicated as grey bars indicating the length of the deletion and the annotation and subdivided into α + - and α 0 -thalassemia deletions.CC-BY-NC-ND · From the PDF
Fig. 5 Microscopic examination of the blood smear after staining with 1% Brilliant Cresyl Blue at 1000 fold magni fi cation. (a). Red cells of HbH disease patient showing Inclusion Body positive cells (1000×magni fi cation). (b). Red cells of α 0 -thalassemia carrier showing an occasional Inclusion Body positive cell after searching 10 -20 fi elds (1000×magni fi cation).
Fig. 5 Microscopic examination of the blood smear after staining with 1% Brilliant Cresyl Blue at 1000 fold magni fi cation. (a). Red cells of HbH disease patient showing Inclusion Body positive cells (1000×magni fi cation). (b). Red cells of α 0 -thalassemia carrier showing an occasional Inclusion Body positive cell after searching 10 -20 fi elds (1000×magni fi cation).CC-BY-NC-ND · From the PDF

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Research works printed but not linked: 100

  1. Shinar, 1989, Differing erythrocyte membrane skeletal protein defects in alpha and beta thalassemia, J. Clin. Invest., 83, 404, 10.1172/JCI113898 · DOI
  2. Yuan, 1995, The instability of the membrane skeleton in thalassemic red blood cells, Blood, 86, 3945, 10.1182/blood.V86.10.3945.bloodjournal86103945 · DOI
  3. Sankaran, 2010, Advances in the understanding of haemoglobin switching, Br. J. Haematol., 149, 181, 10.1111/j.1365-2141.2010.08105.x · DOI
  4. Sankaran, 2011, A functional element necessary for fetal hemoglobin silencing, N. Engl. J. Med., 365, 807, 10.1056/NEJMoa1103070 · DOI
  5. Galanello, 2011, Gene test review, Alpha-Thalassemia. Genet Med, 13, 83
  6. Farashi, 2015, Diagnostic pitfalls of less well recognized HbH disease, Blood Cells Mol. Dis., 55, 387, 10.1016/j.bcmd.2015.08.003 · DOI
  7. Wilkie, 1990, Clinical features and molecular analysis of the alpha thalassemia/mental retardation syndromes. I. Cases due to deletions involving chromosome band 16p13.3, Am. J. Hum. Genet., 46, 1112
  8. Pfeifer, 2000, The SOX8 gene is located within 700kb of the tip of chromosome 16p and is deleted in a patient with ATR-16 syndrome, Genomics, 63, 108, 10.1006/geno.1999.6060 · DOI
  9. Bezerra, 2008, The deletion of SOX8 is not associated with ATR-16 in an HbH family from Brazil, Br. J. Haematol., 10.1111/j.1365-2141.2008.07187.x · DOI
  10. Harteveld, 2010, Alpha-thalassaemia, Orphanet J. Rare Dis., 5, 13, 10.1186/1750-1172-5-13 · DOI · Paper page
  11. Gallego, 2005, ATR-16 due to a de novo complex rearrangement of chromosome 16, Hemoglobin, 29, 141, 10.1081/HEM-58585 · DOI
  12. Harteveld, 2007, Refinement of the genetic cause of ATR-16, Hum. Genet., 10.1007/s00439-007-0399-y · DOI
  13. Gibbons, 2006, Alpha thalassaemia-mental retardation, X linked, Orphanet J. Rare Dis., 1, 15, 10.1186/1750-1172-1-15 · DOI
  14. Gibbons, 2008, Mutations in the chromatin-associated protein ATRX, Hum. Mutat., 29, 796, 10.1002/humu.20734 · DOI
  15. Gibbons, 2003, Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS), Nat. Genet., 34, 446, 10.1038/ng1213 · DOI
  16. De La Fuente, 2011, Role of ATRX in chromatin structure and function: implications for chromosome instability and human disease, Reproduction, 142, 221, 10.1530/REP-10-0380 · DOI
  17. Higgs, 2005, Understanding alpha-globin gene regulation: Aiming to improve the management of thalassemia, Ann. N. Y. Acad. Sci., 1054, 92, 10.1196/annals.1345.012 · DOI
  18. Clynes, 2013, The chromatin remodeller ATRX: a repeat offender in human disease, Trends Biochem. Sci., 38, 461, 10.1016/j.tibs.2013.06.011 · DOI
  19. Law, 2010, ATR-X syndrome protein targets tandem repeats and influences allele-specific expression in a size-dependent manner, Cell, 143, 367, 10.1016/j.cell.2010.09.023 · DOI
  20. Steensma, 2005, Acquired alpha-thalassemia in association with myelodysplastic syndrome and other hematologic malignancies, Blood, 105, 443, 10.1182/blood-2004-07-2792 · DOI
  21. Steensma, 2004, Deletion of the alpha-globin gene cluster as a cause of acquired alpha-thalassemia in myelodysplastic syndrome, Blood, 103, 1518, 10.1182/blood-2003-09-3222 · DOI
  22. Steensma, 2004, Acquired somatic ATRX mutations in myelodysplastic syndrome associated with alpha thalassemia (ATMDS) convey a more severe hematologic phenotype than germline ATRX mutations, Blood, 103, 2019, 10.1182/blood-2003-09-3360 · DOI
  23. Weatherall, 2001, Inherited haemoglobin disorders: an increasing global health problem, Bull. World Health Organ., 79, 704
  24. Piel, 2014, Global migration and the changing distribution of sickle haemoglobin: a quantitative study of temporal trends between 1960 and 2000, Lancet Glob. Health, 2, e80, 10.1016/S2214-109X(13)70150-5 · DOI
  25. Piel, 2014, The alpha-thalassemias, N. Engl. J. Med., 371, 1908, 10.1056/NEJMra1404415 · DOI
  26. Traeger-Synodinos, 2015, EMQN Best Practice Guidelines for molecular and haematology methods for carrier identification and prenatal diagnosis of the haemoglobinopathies, Eur. J. Hum. Genet., 23, 426, 10.1038/ejhg.2014.131 · DOI
  27. Liebhaber, 1986, Human alpha-globin gene expression. The dominant role of the alpha 2-locus in mRNA and protein synthesis, J. Biol. Chem., 261, 15327, 10.1016/S0021-9258(18)66871-1 · DOI · Paper page
  28. Molchanova, 1994, The differences in quantities of alpha 2- and alpha 1-globin gene variants in heterozygotes, Br. J. Haematol., 88, 300, 10.1111/j.1365-2141.1994.tb05022.x · DOI
  29. Shakin, 1986, Translational profiles of alpha 1-, alpha 2-, and beta-globin messenger ribonucleic acids in human reticulocytes, J. Clin. Invest., 78, 1125, 10.1172/JCI112670 · DOI
  30. Smetanina, 1996, The relative levels of alpha 2-, alpha 1-, and zeta-mRNA in HB H patients with different deletional and nondeletional alpha-thalassemia determinants, Biochim. Biophys. Acta, 1316, 176, 10.1016/0925-4439(96)00024-5 · DOI
  31. Smetanina, 1996, The alpha/beta and alpha 2/alpha 1-globin mRNA ratios in different forms of alpha-thalassemia, Biochim. Biophys. Acta, 1315, 188, 10.1016/0925-4439(95)00123-9 · DOI
  32. Higgs, 1984, Independent recombination events between the duplicated human alpha globin genes; implications for their concerted evolution, Nucleic Acids Res., 12, 6965, 10.1093/nar/12.18.6965 · DOI
  33. Higgs, 2009, The alpha thalassaemias, Cell. Mol. Life Sci., 66, 1154, 10.1007/s00018-008-8529-9 · DOI
  34. Wajcman, 2008, Unstable and thalassemic alpha chain hemoglobin variants: a cause of Hb H disease and thalassemia intermedia, Hemoglobin, 32, 327, 10.1080/03630260802173833 · DOI
  35. Giardine, 2014, Updates of the HbVar database of human hemoglobin variants and thalassemia mutations, Nucleic Acids Res., 42, D1063, 10.1093/nar/gkt911 · DOI
  36. Giardine, 2011, Systematic documentation and analysis of human genetic variation in hemoglobinopathies using the microattribution approach, Nat. Genet., 43, 295, 10.1038/ng.785 · DOI
  37. Proudfoot, 1986, Transcriptional interference and termination between duplicated alpha-globin gene constructs suggests a novel mechanism for gene regulation, Nature, 322, 562, 10.1038/322562a0 · DOI
  38. Whitelaw, 1986, Alpha-thalassaemia caused by a poly(A) site mutation reveals that transcriptional termination is linked to 3′ end processing in the human alpha 2 globin gene, EMBO J., 5, 2915, 10.1002/j.1460-2075.1986.tb04587.x · DOI
  39. van BS Giardine, 2007, HbVar database of human hemoglobin variants and thalassemia mutations, Hum. Mutat., 2007, 206, 10.1002/humu.9479 · DOI
  40. Aksu, 2014, Homozygosity for HBA1: c.179G>A: Hb Adana in an infant, Hemoglobin, 38, 449, 10.3109/03630269.2014.969373 · DOI
  41. Megawati, 2014, Severe alpha-thalassemia intermedia due to a compound heterozygosity for the highly unstable Hb Adana (HBA2: c.179G>A) and a novel codon 24 (HBA2: c.75T>A) mutation, Hemoglobin, 38, 149, 10.3109/03630269.2013.863206 · DOI
  42. Nainggolan, 2010, Hydrops fetalis associated with homozygosity for Hb Adana [alpha59(E8)Gly–>Asp (alpha2)], Hemoglobin, 34, 394, 10.3109/03630269.2010.493405 · DOI
  43. Douna, 2008, A rare thalassemic syndrome caused by interaction of Hb Adana [alpha59(E8)Gly–>Asp] with an alpha±thalassemia deletion: clinical aspects in two cases, Hemoglobin, 32, 361, 10.1080/03630260802173890 · DOI
  44. Chan, 1997, Molecular defects in Hb H hydrops fetalis, Br. J. Haematol., 96, 224, 10.1046/j.1365-2141.1997.d01-2017.x · DOI
  45. Tan, 2016, George E. DNA studies are necessary for accurate patient diagnosis in compound heterozygosity for Hb Adana (HBA2:c.179>A) with deletional or nondeletional alpha-thalassaemia, Sci Rep, 6, 26994, 10.1038/srep26994 · DOI
  46. Lee, 2016, Analysis of alpha1 and alpha2 globin genes among patients with hemoglobin Adana in Malaysia, Genet. Mol. Res., 15, 10.4238/gmr.15027400 · DOI
  47. Higgs, 2013, The molecular basis of alpha-thalassemia, Cold Spring Harb. Perspect. Med., 3, a011718, 10.1101/cshperspect.a011718 · DOI · Paper page
  48. Phylipsen, 2011, A novel alpha(0) -thalassemia deletion in a Greek patient with HbH disease and beta-thalassemia trait, Eur. J. Haematol., 10.1111/j.1600-0609.2012.01748.x · DOI
  49. Nicholls, 1987, Recombination at the human alpha-globin gene cluster: sequence features and topological constraints, Cell, 49, 369, 10.1016/0092-8674(87)90289-3 · DOI
  50. Lauer, 1980, The chromosomal arrangement of human alpha-like globin genes: sequence homology and alpha-globin gene deletions, Cell, 20, 119, 10.1016/0092-8674(80)90240-8 · DOI
  51. Hughes, 2005, Annotation of cis-regulatory elements by identification, subclassification, and functional assessment of multispecies conserved sequences, Proc. Natl. Acad. Sci. U. S. A., 102, 9830, 10.1073/pnas.0503401102 · DOI
  52. Vernimmen, 2014, Uncovering enhancer functions using the alpha-globin locus, PLoS Genet., 10, 10.1371/journal.pgen.1004668 · DOI
  53. Sollaino, 2010, Homozygous deletion of the major alpha-globin regulatory element (MCS-R2) responsible for a severe case of hemoglobin H disease, Blood, 116, 2193, 10.1182/blood-2010-04-281345 · DOI
  54. Coelho, 2010, Novel large deletions in the human alpha-globin gene cluster: Clarifying the HS-40 long-range regulatory role in the native chromosome environment, Blood Cells Mol. Dis., 45, 147, 10.1016/j.bcmd.2010.05.010 · DOI
  55. Tufarelli, 2003, Transcription of antisense RNA leading to gene silencing and methylation as a novel cause of human genetic disease, Nat. Genet., 34, 157, 10.1038/ng1157 · DOI · Paper page
  56. Higgs, 2008, Long-range regulation of alpha globin gene expression during erythropoiesis, Curr. Opin. Hematol., 15, 176, 10.1097/MOH.0b013e3282f734c4 · DOI
  57. Ferreira, 2005, GATA1 function, a paradigm for transcription factors in hematopoiesis, Mol. Cell. Biol., 25, 1215, 10.1128/MCB.25.4.1215-1227.2005 · DOI
  58. De Gobbi, 2006, A regulatory SNP causes a human genetic disease by creating a new transcriptional promoter, Science, 312, 1215, 10.1126/science.1126431 · DOI
  59. Kihm, 2002, An abundant erythroid protein that stabilizes free alpha-haemoglobin, Nature, 417, 758, 10.1038/nature00803 · DOI
  60. Kowalczyk, 2012, Molecular biology: RNA discrimination, Nature, 482, 310, 10.1038/482310a · DOI
  61. Lam, 2007, Processes of de novo duplication of human alpha-globin genes, Proc. Natl. Acad. Sci. U. S. A., 104, 10950, 10.1073/pnas.0703856104 · DOI
  62. Lam, 2006, Processes of copy-number change in human DNA: the dynamics of {alpha}-globin gene deletion, Proc. Natl. Acad. Sci. U. S. A., 103, 8921, 10.1073/pnas.0602690103 · DOI
  63. Harteveld, 2008, Segmental duplications involving the alpha-globin gene cluster are causing beta-thalassemia intermedia phenotypes in beta-thalassemia heterozygous patients, Blood Cells Mol. Dis., 40, 312, 10.1016/j.bcmd.2007.11.006 · DOI
  64. Clark, 2016, Beta thalassaemia intermedia due to co-inheritance of three unique alpha globin cluster duplications characterised by next generation sequencing analysis, Br. J. Haematol.
  65. Fichera, 1997, Molecular basis of alpha-thalassemia in Sicily, Hum. Genet., 99, 381, 10.1007/s004390050376 · DOI
  66. Giordano, 1999, Haemoglobinopathy analyses in the Netherlands: a report of an in vitro globin chain biosynthesis survey using a rapid, modified method, Clin. Lab. Haematol., 21, 247, 10.1046/j.1365-2257.1999.00197.x · DOI
  67. Clark, 2017, Next-generation sequencing as a tool for breakpoint analysis in rearrangements of the globin gene clusters, Int. J. Lab. Hematol., 39, 111, 10.1111/ijlh.12680 · DOI
  68. Tan, 2001, A rapid and reliable 7-deletion multiplex polymerase chain reaction assay for alpha-thalassemia, Blood, 98, 250, 10.1182/blood.V98.1.250 · DOI
  69. Traeger-Synodinos, 2014, Advances in technologies for screening and diagnosis of hemoglobinopathies, Biomark. Med, 8, 119, 10.2217/bmm.13.103 · DOI · Paper page
  70. Thein, 2017, Molecular basis of beta thalassemia and potential therapeutic targets, Blood Cells Mol. Dis.
  71. Gambari, 2012, Alternative options for DNA-based experimental therapy of beta-thalassemia, Expert. Opin. Biol. Ther., 12, 443, 10.1517/14712598.2012.665047 · DOI
  72. Chou, 2015, Pharmacological induction of human fetal globin gene in hydroxyurea-resistant primary adult erythroid cells, Mol. Cell. Biol., 35, 2541, 10.1128/MCB.00035-15 · DOI
  73. Guda, 2015, miRNA-embedded shRNAs for Lineage-specific BCL11A knockdown and hemoglobin F induction, Mol. Ther., 23, 1465, 10.1038/mt.2015.113 · DOI
  74. Bauer, 2015, Hemoglobin switching's surprise: the versatile transcription factor BCL11A is a master repressor of fetal hemoglobin, Curr. Opin. Genet. Dev., 33, 62, 10.1016/j.gde.2015.08.001 · DOI · Paper page
  75. Huang, 2015, Production of gene-corrected adult beta globin protein in human erythrocytes differentiated from patient ipscs after genome editing of the sickle point mutation, Stem Cells, 33, 1470, 10.1002/stem.1969 · DOI
  76. Xu, 2015, Both TALENs and CRISPR/Cas9 directly target the HBB IVS2-654 (C>T) mutation in beta-thalassemia-derived iPSCs, Sci Rep, 5, 12065, 10.1038/srep12065 · DOI
  77. Hoban, 2015, Correction of the sickle cell disease mutation in human hematopoietic stem/progenitor cells, Blood, 125, 2597, 10.1182/blood-2014-12-615948 · DOI · Paper page
  78. Negre, 2016, Gene therapy of the beta-hemoglobinopathies by Lentiviral transfer of the beta(A(T87Q))-globin gene, Hum. Gene Ther., 27, 148, 10.1089/hum.2016.007 · DOI · Paper page
  79. Mettananda, 2016, Understanding alpha-globin gene regulation and implications for the treatment of beta-thalassemia, Ann. N. Y. Acad. Sci., 1368, 16, 10.1111/nyas.12988 · DOI
  80. Mettananda, 2015, alpha-Globin as a molecular target in the treatment of beta-thalassemia, Blood, 125, 3694, 10.1182/blood-2015-03-633594 · DOI
  81. Mettananda, 2017, Selective silencing of alpha-globin by the histone demethylase inhibitor IOX1: a potentially new pathway for treatment of beta-thalassemia, Haematologica, 102, e80, 10.3324/haematol.2016.155655 · DOI
  82. Urnov, 2005, Highly efficient endogenous human gene correction using designed zinc-finger nucleases, Nature, 435, 646, 10.1038/nature03556 · DOI
  83. Mahfouz, 2011, De novo-engineered transcription activator-like effector (TALE) hybrid nuclease with novel DNA binding specificity creates double-strand breaks, Proc. Natl. Acad. Sci. U. S. A., 108, 2623, 10.1073/pnas.1019533108 · DOI
  84. Niu, 2016, Combining Single Strand Oligodeoxynucleotides and CRISPR/Cas9 to Correct Gene Mutations in beta-Thalassemia-induced Pluripotent Stem Cells, J. Biol. Chem., 291, 16576, 10.1074/jbc.M116.719237 · DOI
  85. Xie, 2014, Seamless gene correction of beta-thalassemia mutations in patient-specific iPSCs using CRISPR/Cas9 and piggyBac, Genome Res., 24, 1526, 10.1101/gr.173427.114 · DOI · Paper page
  86. Song, 2015, Improved hematopoietic differentiation efficiency of gene-corrected beta-thalassemia induced pluripotent stem cells by CRISPR/Cas9 system, Stem Cells Dev., 24, 1053, 10.1089/scd.2014.0347 · DOI
  87. Hu, 2016, CRISPR/Cas9 system and its applications in human hematopoietic cells, Blood Cells Mol. Dis., 62, 6, 10.1016/j.bcmd.2016.09.003 · DOI
  88. Grispo, 2012, Gene duplication and the evolution of hemoglobin isoform differentiation in birds, J. Biol. Chem., 287, 37647, 10.1074/jbc.M112.375600 · DOI
  89. Opazo, 2015, Gene turnover in the avian globin gene families and evolutionary changes in hemoglobin isoform expression, Mol. Biol. Evol., 32, 871, 10.1093/molbev/msu341 · DOI
  90. Cooper, 2006, The mammalian alphaD-globin gene lineage and a new model for the molecular evolution of alpha-globin gene clusters at the stem of the mammalian radiation, Mol. Phylogenet. Evol., 38, 439, 10.1016/j.ympev.2005.05.014 · DOI
  91. Chen, 2005, Intrachromosomal serial replication slippage in trans gives rise to diverse genomic rearrangements involving inversions, Hum. Mutat., 26, 362, 10.1002/humu.20230 · DOI
  92. Brown, 1974, Structural studies on chick embryonic hemoglobins, J. Biol. Chem., 249, 3960, 10.1016/S0021-9258(19)42568-4 · DOI
  93. Hardison, 1986, A previously undetected pseudogene in the human alpha globin gene cluster, Nucleic Acids Res., 14, 1903, 10.1093/nar/14.4.1903 · DOI
  94. Cirotto, 1987, The minor haemoglobins of primitive and definitive erythrocytes of the chicken embryo. Evidence for haemoglobin L, Development, 101, 805, 10.1242/dev.101.4.805 · DOI
  95. Alev, 2008, BetaA, the major beta globin in definitive red blood cells, is present from the onset of primitive erythropoiesis in chicken, Dev. Dyn., 237, 1193, 10.1002/dvdy.21510 · DOI
  96. Alev, 2009, Genomic organization of zebra finch alpha and beta globin genes and their expression in primitive and definitive blood in comparison with globins in chicken, Dev. Genes Evol., 219, 353, 10.1007/s00427-009-0294-8 · DOI
  97. Knapp, 1999, The structural and functional analysis of the hemoglobin D component from chicken, J. Biol. Chem., 274, 6411, 10.1074/jbc.274.10.6411 · DOI
  98. Tchernitchko, 2004, In silico prediction of the deleterious effect of a mutation: proceed with caution in clinical genetics, Clin. Chem., 50, 1974, 10.1373/clinchem.2004.036053 · DOI
  99. Farashi, 2015, Mutations on the alpha2-globin gene that may trigger alpha(+)-thalassemia, Hemoglobin, 39, 398, 10.3109/03630269.2015.1075890 · DOI
  100. Farashi, 2016, Identification of mutations causing aberrant termination and deficient splice donor site on the HBA1 gene, Hemoglobin, 40, 38, 10.3109/03630269.2015.1088456 · DOI

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Metadata

Authors
Farashi, S., & Harteveld, C. L.
Venue
Blood Cells, Molecules, and Diseases
Publisher
Elsevier BV
Published
2018-05
Volume
70
Pages
43-53
ISSN
1079-9796
DOI
10.1016/j.bcmd.2017.09.004
Cited by
227
References
7
Language
en
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Farashi, S., & Harteveld, C. L. (2018). Molecular basis of α-thalassemia. Blood Cells, Molecules, and Diseases. https://doi.org/10.1016/j.bcmd.2017.09.004