| Key Genes FECH and ALAS2 under Acute High-Altitude Exposure: A Gene Expression and Network Analysis Based on Expression Profile Data. | Key Genes FECH and ALAS2 under Acute High-Altitude Exposure: A Gene Expression and Network Analysis Based on Expression Profile Data.
Zhao Y, Zhu L, Shi D, Gao J, Fan M., Free PMC Article | 10/9/2024 |
| Congenital sideroblastic anemia model due to ALAS2 mutation is susceptible to ferroptosis. | Congenital sideroblastic anemia model due to ALAS2 mutation is susceptible to ferroptosis.
Ono K, Fujiwara T, Saito K, Nishizawa H, Takahashi N, Suzuki C, Ochi T, Kato H, Ishii Y, Onodera K, Ichikawa S, Fukuhara N, Onishi Y, Yokoyama H, Yamada R, Nakamura Y, Igarashi K, Harigae H., Free PMC Article | 06/18/2022 |
| A synonymous coding variant that alters ALAS2 splicing and causes X-linked sideroblastic anemia. | A synonymous coding variant that alters ALAS2 splicing and causes X-linked sideroblastic anemia.
Oakley JH, Campagna DR, Sun L, Rockowitz S, Sliz P, Boudreaux J, Woods G, Fleming MD. | 03/5/2022 |
| Severe iron overload in a woman with homeostatic iron regulator (HFE) and a novel 5'-aminolevulinate synthase 2 (ALAS2) mutations: interactions of multiple genetic determinants. | Severe iron overload in a woman with homeostatic iron regulator (HFE) and a novel 5'-aminolevulinate synthase 2 (ALAS2) mutations: interactions of multiple genetic determinants.
de Gennes C, Lamoril J, Borgel A, Boi C, Yao R, Boileau C, Tchernitchko D. | 02/19/2022 |
| A mutation in the iron-responsive element of ALAS2 is a modifier of disease severity in a patient suffering from CLPX associated erythropoietic protoporphyria. | A mutation in the iron-responsive element of ALAS2 is a modifier of disease severity in a patient suffering from CLPX associated erythropoietic protoporphyria.
Ducamp S, Luscieti S, Ferrer-Cortès X, Nicolas G, Manceau H, Peoc'h K, Yien YY, Kannengiesser C, Gouya L, Puy H, Sanchez M., Free PMC Article | 08/7/2021 |
| Novel mutations in the ALAS2 gene from patients with X-linked sideroblastic anemia. | Novel mutations in the ALAS2 gene from patients with X-linked sideroblastic anemia.
Li J, Chen L, Lin Y, Ru K. | 01/23/2021 |
| [Knockdown of ALAS2 Affects Erythroid Differentiation by Down-regulating Mitophagy Receptor BNIP3L]. | [Knockdown of ALAS2 Affects Erythroid Differentiation by Down-regulating Mitophagy Receptor BNIP3L].
Hu ST, Li XY, Chen H, Xu LH, Fang JP. | 10/24/2020 |
| Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release. | Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release.
Bailey HJ, Bezerra GA, Marcero JR, Padhi S, Foster WR, Rembeza E, Roy A, Bishop DF, Desnick RJ, Bulusu G, Dailey HA Jr, Yue WW., Free PMC Article | 08/22/2020 |
| In erythropoietic protoporphyria, ALAS2 mRNA was increased both in absolute terms and in relation to deficiency in ferrochelatase mRNA as shown in this study. | Delta-aminolevulinic acid synthase 2 expression in combination with iron as modifiers of disease severity in erythropoietic protoporphyria.
Barman-Aksözen J, Halloy F, Iyer PS, Schümperli D, Minder AE, Hall J, Minder EI, Schneider-Yin X. | 05/30/2020 |
| A novel mutation, c.1108G > A (p.A370T, NM_000032), was found in the ALAS2 gene located in exon 8. A mother with X-linked sideroblastic anemia and her so-far asymptomatic daughter were heterozygous for this mutation. | Identification of a novel heterozygous ALAS2 mutation in a young Chinese female with X-linked sideroblastic anemia.
Qiu Y, Cai H, Cui L, Liu YX, Wang YN, Li J, Cao XX. | 02/8/2020 |
| Patients with porphyrias should always be assessed for the presence of the ALAS2 gain-of-function modifier variants identified here. A key region of the ALAS2 carboxyterminal region is identified by the truncation mutations, and the correlation of increased thermolability with activity suggests that increased molecular flexibility/active site openness is the mechanism of enhanced function of mutations in this region. | Molecular expression, characterization and mechanism of ALAS2 gain-of-function mutants.
Tchaikovskii V, Desnick RJ, Bishop DF., Free PMC Article | 08/17/2019 |
| we report that the dynamics of ALAS2 active site loop is anti-correlated with the dynamics of the C-terminal tail and that this anti-correlation can represent a molecular basis for the functional and dynamic asymmetry of the ALAS2 homodimer. | 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, Catena D, Kong MJ, Ferreira GC, Uversky VN., Free PMC Article | 10/27/2018 |
| report confirms the considerable variability in manifestations among patients with ALAS2 or SLC25A38 mutations and draws attention to differences in the assessment and the monitoring of iron overload and its complications | Non syndromic childhood onset congenital sideroblastic anemia: A report of 13 patients identified with an ALAS2 or SLC25A38 mutation.
Le Rouzic MA, Fouquet C, Leblanc T, Touati M, Fouyssac F, Vermylen C, Jäkel N, Guichard JF, Maloum K, Toutain F, Lutz P, Perel Y, Manceau H, Kannengiesser C, Vannier JP. | 08/25/2018 |
| A novel ALAS2 missense mutation in exon 9 affects the enzymatic activity of ALAS2 by affecting its interaction with the cofactor pyridoxal 5'-phosphate in X-linked sideroblastic anemia. | A Novel ALAS2 Mutation Resulting in Variable Phenotypes and Pyridoxine Response in a Family with X-linked Sideroblastic Anemia.
Lee JS, Gu J, Yoo HJ, Koh Y, Kim HK. | 04/7/2018 |
| a case of X-linked sideroblastic anemia caused by a novel homozygous deletional mutation in exon 10 of ALAS2 gene is presented | A Novel g.55040074delT in ALAS2 Gene Resulting in a Monomeric Protein and Severe Sideroblastic Anemia Phenotype.
Bhatia P, Singh A, Hedge A. | 09/30/2017 |
| int-1-GATA site should be examined in patients with XLSA in clinical settings when no known mutation is found in ALAS2 exons. | Intron 1 GATA site enhances ALAS2 expression indispensably during erythroid differentiation.
Zhang Y, Zhang J, An W, Wan Y, Ma S, Yin J, Li X, Gao J, Yuan W, Guo Y, Engel JD, Shi L, Cheng T, Zhu X., Free PMC Article | 06/24/2017 |
| From pH jump experiments, comparable rates for the denaturation of the tertiary structure and PLP-microenvironment were discerned, indicating that the catalytic active site geometry strongly depends on the stable tertiary structural organization. Lastly, we demonstrate that partially folded ALAS tends to self-associate into higher oligomeric species at moderate GuHCl concentrations. | The unfolding pathways of the native and molten globule states of 5-aminolevulinate synthase.
Stojanovski BM, Breydo L, Uversky VN, Ferreira GC. | 06/3/2017 |
| data indicate that the X-linked protoporphyria variants possess enhanced ALAS activity and ALA dissociation rates, as well as distinct structural properties from those of wild-type hALAS | Human Erythroid 5-Aminolevulinate Synthase Mutations Associated with X-Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release.
Fratz EJ, Clayton J, Hunter GA, Ducamp S, Breydo L, Uversky VN, Deybach JC, Gouya L, Puy H, Ferreira GC., Free PMC Article | 02/13/2016 |
| In this article we add a novel mutation to the previously described 61 different ALAS2 mutations identified in X-linked sideroblastic anaemia patients. | X-linked sideroblastic anaemia due to ALAS₂ mutations in the Netherlands: a disease in disguise.
Donker AE, Raymakers RA, Nieuwenhuis HK, Coenen MJ, Janssen MC, MacKenzie MA, Brons PP, Swinkels DW. | 09/5/2015 |
| the primary deficiency in ferrochelatase leads to a secondary increase in ALAS2 expression. | In ferrochelatase-deficient protoporphyria patients, ALAS2 expression is enhanced and erythrocytic protoporphyrin concentration correlates with iron availability.
Barman-Aksözen J, Minder EI, Schubiger C, Biolcati G, Schneider-Yin X. | 08/1/2015 |
| The ALAS2 Y365C mutation impairs pyridoxal 5'-phosphate binding to ALAS2, destabilizing the enzyme. X inactivation was not highly skewed in WBC from affected women. This X-linked dominant mutation perturbs erythropoiesis via cell-nonautonomous effects. | X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation.
Sankaran VG, Ulirsch JC, Tchaikovskii V, Ludwig LS, Wakabayashi A, Kadirvel S, Lindsley RC, Bejar R, Shi J, Lovitch SB, Bishop DF, Steensma DP., Free PMC Article | 07/4/2015 |
| the 130-base pair enhancer region located in the first intron of the ALAS2 gene should be examined in patients with congenital sideroblastic anemia in whom the gene responsible is unknown. | Identification of a novel erythroid-specific enhancer for the ALAS2 gene and its loss-of-function mutation which is associated with congenital sideroblastic anemia.
Kaneko K, Furuyama K, Fujiwara T, Kobayashi R, Ishida H, Harigae H, Shibahara S., Free PMC Article | 07/26/2014 |
| 5 families with X-linked sideroblastic anemia had mutations in a GATA transcription factor binding site located in a transcriptional enhancer element in intron 1 of the ALAS2 gene. | X-linked sideroblastic anemia due to ALAS2 intron 1 enhancer element GATA-binding site mutations.
Campagna DR, de Bie CI, Schmitz-Abe K, Sweeney M, Sendamarai AK, Schmidt PJ, Heeney MM, Yntema HG, Kannengiesser C, Grandchamp B, Niemeyer CM, Knoers NV, Swart S, Marron G, van Wijk R, Raymakers RA, May A, Markianos K, Bottomley SS, Swinkels DW, Fleming MD., Free PMC Article | 06/7/2014 |
| Loss-of-function FECH and gain-of-function erythroid-specific ALAS2 mutations causing erythropoietic protoporphyria and x-linked protoporphyria in North American patients reveal novel mutations and a high prevalence of X-linked protoporphyria. | 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, Doheny D, Bishop DF, Nazarenko I, Yasuda M, Dailey HA, Anderson KE, Bissell DM, Bloomer J, Bonkovsky HL, Phillips JD, Liu L, Desnick RJ, Porphyrias Consortium of the National Institutes of Health Rare Diseases Clinical Research Network., Free PMC Article | 12/28/2013 |
| ALAS2 gain-of-function mutations increas the specific activity (DeltaAT, DeltaAGTG and p.Q548X) or stability (DeltaG) of the enzyme, thereby leading to the increased erythroid protoporphyrin accumulation causing X-linked protoporphyria. | Molecular expression and characterization of erythroid-specific 5-aminolevulinate synthase gain-of-function mutations causing X-linked protoporphyria.
Bishop DF, Tchaikovskii V, Nazarenko I, Desnick RJ., Free PMC Article | 08/31/2013 |