Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP)

The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability

(2012) Senkottuvelan Kadirvel et al.   EXPERIMENTAL HEMATOLOGY

X-linked Sideroblastic Anemia Due to Carboxyl-terminal ALAS2 Mutations That Cause Loss of Binding to the β-Subunit of Succinyl-CoA Synthetase (SUCLA2)

(2012) David F. Bishop et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria

(2011) J. To-Figueras et al.   BLOOD

Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria

(2011) Yongming Wang et al.   EXPERIMENTAL HEMATOLOGY

Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations

(2011) Sarah Ducamp et al.   HUMAN MUTATION

Hereditary sideroblastic anemia: pathophysiology and gene mutations

(2010) Hideo Harigae et al.   INTERNATIONAL JOURNAL OF HEMATOLOGY

Targeting the Active Site Gate to Yield Hyperactive Variants of 5-Aminolevulinate Synthase

(2010) Thomas Lendrihas et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Porphyrias

(2010) Hervé Puy et al.   LANCET

Comparison of methods for quantification of subtle splice variants

(2009) Stefanie Schindler et al.   ELECTROPHORESIS

C-Terminal Deletions in the ALAS2 Gene Lead to Gain of Function and Cause X-linked Dominant Protoporphyria without Anemia or Iron Overload

(2008) Sharon D. Whatley et al.   AMERICAN JOURNAL OF HUMAN GENETICS