A novel mutation of the erythroid-specific δ-aminolaevulinate synthase gene in a patient with X-linked sideroblastic anaemia
- 1 July 1999
- journal article
- case report
- Published by Wiley in British Journal of Haematology
- Vol. 106 (1) , 175-177
- https://doi.org/10.1046/j.1365-2141.1999.01479.x
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- X-linked sideroblastic anaemia due to a mutation in the erythroid 5-aminolaevulinate synthase gene leading to an arginine170 to leucine substitutionEuropean Journal of Haematology, 2009
- Identification of an arginine452 to histidine substitution in the erythroid 5-aminolaevulinate synthetase gene in a large pedigree with X-linked hereditary sideroblastic anaemiaEuropean Journal of Haematology, 2009
- R411C mutation of the ALAS2 gene encodes a pyridoxine‐responsive enzyme with low activityBritish Journal of Haematology, 1998
- Hereditary sideroblastic anaemia due to a mutation in exon 10 of the erythroid 5-aminolaevulinate synthase geneBritish Journal of Haematology, 1998
- Pyridoxine Refractory X-Linked Sideroblastic Anemia Caused by a Point Mutation in the Erythroid 5-Aminolevulinate Synthase GeneBlood, 1997
- Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts.Journal of Clinical Investigation, 1995
- Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemiaJournal of Bioenergetics and Biomembranes, 1995
- A new mutation of the ALAS2 gene in a large family with X-linked sideroblastic anemiaHuman Genetics, 1995
- X-linked Pyridoxine-Responsive Sideroblastic Anemia Due to a Thr388-to-Ser Substitution in Erythroid 5-Aminolevulinate SynthaseNew England Journal of Medicine, 1994
- Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency.Proceedings of the National Academy of Sciences, 1992