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
Elucidating the Role of Human ALAS2 C-terminal Mutations Resulting in Loss of Function and Disease.
Taylor JL et al.
Biochemistry, 2024
Case report: A novel 11-bp deletion in exon 11 causing a frameshift in the C-terminal of the ALAS2 gene leading to X-linked sideroblastic anemia-a family study.
Al Kindi S et al.
Frontiers in Medicine, 2024
Structural basis for dysregulation of aminolevulinic acid synthase in human disease.
Taylor JL et al.
The Journal of Biological Chemistry, 2022
Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release.
Bailey HJ et al.
Nature Communications, 2020
X-linked Sideroblastic Anemia in a Malay Boy With ALAS2 S568G Mutation.
Susanto TAK et al.
Journal of Pediatric Hematology/oncology, 2017
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
Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP).
Ducamp S et al.
Human Molecular Genetics, 2013
Molecular expression and characterization of erythroid-specific 5-aminolevulinate synthase gain-of-function mutations causing X-linked protoporphyria.
Bishop DF et al.
Molecular Medicine (cambridge, Mass.), 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
The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability.
Kadirvel S et al.
Experimental Hematology, 2012
ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria.
To-Figueras J et al.
Blood, 2011
Hereditary sideroblastic anemia: pathophysiology and gene mutations.
Harigae H et al.
International Journal of Hematology, 2010
C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload.
Whatley SD et al.
American Journal of Human Genetics, 2008
A novel mutation of the erythroid-specific delta-aminolaevulinate synthase gene in a patient with X-linked sideroblastic anaemia.
Harigae H et al.
British Journal of Haematology, 1999
The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia.
May A et al.
Haematologica, 1998
Clinical and biochemical genetics of the lipidoses.
Kolodny EH
Seminars in Hematology, 1972