Associated Papers
The GLYT1 inhibitor bitopertin mitigates erythroid PPIX production and liver disease in erythroid protoporphyria.
Ducamp S et al.
The Journal of Clinical Investigation, 2025
Murine models of erythroid 5ALA synthesis disorders and their conditional synthetic lethal dependency on pyridoxine.
Ducamp S et al.
Blood, 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 dominant protoporphyria in a Chinese pedigree reveals a four-based deletion of ALAS2.
Wang T et al.
Annals of Translational Medicine, 2020
Molecular expression, characterization and mechanism of ALAS2 gain-of-function mutants.
Tchaikovskii V et al.
Molecular Medicine (cambridge, Mass.), 2019
Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase.
Na I et al.
International Journal of Molecular Sciences, 2018
Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients.
Fratz-Berilla EJ et al.
Biochimica Et Biophysica Acta. Molecular Basis of Disease, 2017
X-linked dominant protoporphyria: The first reported Japanese case.
Ninomiya Y et al.
The Journal of Dermatology, 2016
X-chromosomal inactivation directly influences the phenotypic manifestation of X-linked protoporphyria.
Brancaleoni V et al.
Clinical Genetics, 2016
Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.
Fratz EJ et al.
Biochemistry, 2015
Late-onset X-linked dominant protoporphyria: an etiology of photosensitivity in the elderly.
Livideanu CB et al.
The Journal of Investigative Dermatology, 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
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
Annular elastolytic giant cell granuloma associated to late-onset X-linked dominant protoporphyria.
García-Martínez FJ et al.
Dermatology (basel, Switzerland), 2013