Associated Papers
The role of genetic testing in accurate diagnosis of X-linked sideroblastic anemia: novel ALAS2 mutations and the impact of X-chromosome inactivation.
Jové-Solavera D et al.
Scientific Reports, 2025
[From persistent "hypoxemia" to the diagnosis of an hemoglobinopathy].
García Rosolen N et al.
Medicina, 2025
Murine models of erythroid 5ALA synthesis disorders and their conditional synthetic lethal dependency on pyridoxine.
Ducamp S et al.
Blood, 2024
Elucidating the Role of Human ALAS2 C-terminal Mutations Resulting in Loss of Function and Disease.
Taylor JL et al.
Biochemistry, 2024
Structural basis for dysregulation of aminolevulinic acid synthase in human disease.
Taylor JL et al.
The Journal of Biological Chemistry, 2022
Novel frameshift variant (c.409dupG) in SLC25A38 is a common cause of congenital sideroblastic anaemia in the Indian subcontinent.
Ravindra N et al.
Journal of Clinical Pathology, 2021
Novel mutations in the ALAS2 gene from patients with X-linked sideroblastic anemia.
Li J et al.
International Journal of Laboratory Hematology, 2020
Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release.
Bailey HJ et al.
Nature Communications, 2020
A variant erythroferrone disrupts iron homeostasis in SF3B1-mutated myelodysplastic syndrome.
Bondu S et al.
Science Translational Medicine, 2019
SF3B1 mutant MDS-initiating cells may arise from the haematopoietic stem cell compartment.
Mian SA et al.
Nature Communications, 2015
MitoFates: improved prediction of mitochondrial targeting sequences and their cleavage sites.
Fukasawa Y et al.
Molecular & Cellular Proteomics : Mcp, 2015
Mutation spectrum in Chinese patients affected by congenital sideroblastic anemia and a search for a genotype-phenotype relationship.
Liu G et al.
Haematologica, 2013
Loss-of-function ferrochelatase and gain-of-function erythroid-specific 5-aminolevulinate synthase mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria.
Balwani M et al.
Molecular Medicine (cambridge, Mass.), 2013
Clinical and genetic characteristics of congenital sideroblastic anemia: comparison with myelodysplastic syndrome with ring sideroblast (MDS-RS).
Ohba R et al.
Annals of Hematology, 2013
X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2).
Bishop DF et al.
The Journal of Biological Chemistry, 2012
Sideroblastic anemia, iron overload, and ALAS2 R452S in African-American males: phenotype and genotype features of five unrelated patients.
Lee PL et al.
American Journal of Hematology, 2011
Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations.
Ducamp S et al.
Human Mutation, 2011
New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine.
Kucerova J et al.
Acta Haematologica, 2011
Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G.
Sussman NL et al.
Acta Haematologica, 2008
Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity.
Furuyama K et al.
European Journal of Haematology, 2006
Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans.
Astner I et al.
The Embo Journal, 2005
Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.
Cotter PD et al.
Blood, 1999
The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia.
May A et al.
Haematologica, 1998
Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemia.
Bottomley SS et al.
Journal of Bioenergetics and Biomembranes, 1995
Clinical and biochemical genetics of the lipidoses.
Kolodny EH
Seminars in Hematology, 1972
Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma.
Barton JC et al.
Blood Cells, Molecules & Diseases, 0