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5-aminolevulinate synthetase - genetics (445) 445
humans (351) 351
animals (349) 349
5-aminolevulinate synthetase - metabolism (296) 296
male (209) 209
biochemistry & molecular biology (173) 173
index medicus (152) 152
heme - biosynthesis (148) 148
female (142) 142
molecular sequence data (129) 129
base sequence (128) 128
mutation (121) 121
mice (116) 116
heme (113) 113
5-aminolevulinate synthase (111) 111
5-aminolevulinate synthetase - biosynthesis (102) 102
anemia, sideroblastic - genetics (102) 102
delta-aminolevulinate synthase (101) 101
liver - enzymology (95) 95
rats (87) 87
amino acid sequence (82) 82
expression (78) 78
hematology (78) 78
rna, messenger - metabolism (77) 77
adult (74) 74
messenger-rna (71) 71
heme - metabolism (69) 69
gene (62) 62
enzymes (61) 61
rna, messenger - genetics (59) 59
liver - metabolism (58) 58
cell biology (57) 57
kinetics (57) 57
aminolevulinic acid - metabolism (56) 56
gene expression (56) 56
erythrocytes - enzymology (54) 54
iron - metabolism (53) 53
chick embryo (50) 50
identification (50) 50
5-aminolevulinate synthetase - chemistry (49) 49
biosynthesis (49) 49
cells, cultured (49) 49
liver - drug effects (49) 49
cloning, molecular (46) 46
heme-biosynthesis (45) 45
research article (45) 45
analysis (43) 43
middle aged (43) 43
transcription, genetic (43) 43
genes (42) 42
porphyrias - genetics (42) 42
microbiology (41) 41
gene expression regulation (39) 39
liver (39) 39
physiological aspects (39) 39
genetic diseases, x-linked - genetics (38) 38
genetics & heredity (38) 38
iron (38) 38
anemia (37) 37
biophysics (37) 37
escherichia coli - genetics (37) 37
porphyrias - enzymology (37) 37
research (37) 37
enzyme induction - drug effects (36) 36
porphyrins - biosynthesis (36) 36
erythroid 5-aminolevulinate synthase (35) 35
pedigree (35) 35
rna, messenger - biosynthesis (35) 35
saccharomyces cerevisiae - genetics (35) 35
genetic aspects (34) 34
porphyrias - metabolism (34) 34
promoter regions, genetic (34) 34
sideroblastic anemia (34) 34
porphyrins - metabolism (33) 33
5-aminolevulinate synthetase - blood (32) 32
biotechnology & applied microbiology (32) 32
escherichia-coli (32) 32
proteins (32) 32
gene-expression (31) 31
anemia, sideroblastic - enzymology (30) 30
article (30) 30
mitochondria (30) 30
porphobilinogen synthase - metabolism (30) 30
porphyria (30) 30
tumor cells, cultured (30) 30
enzyme induction (29) 29
erythropoiesis (29) 29
gene expression regulation, enzymologic (29) 29
hemin - pharmacology (28) 28
phenotype (28) 28
recombinant proteins - metabolism (28) 28
x chromosome (28) 28
aged (27) 27
alas2 (27) 27
ferrochelatase - metabolism (27) 27
mitochondria - metabolism (27) 27
cells (26) 26
induction (26) 26
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iron-responsive element (25) 25
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1. Full Text X-linked sideroblastic anemia due to carboxyl-terminal ALAS2 mutations that cause loss of binding to the β-subunit of succinyl-CoA synthetase (SUCLA2)
by Bishop, David F and Tchaikovskii, Vassili and Hoffbrand, A. Victor and Fraser, Marie E and Margolis, Steven
Journal of Biological Chemistry, ISSN 0021-9258, 08/2012, Volume 287, Issue 34, pp. 28943 - 28955
Mutations in the erythroid-specific aminolevulinic acid synthase gene (ALAS2) cause X-linked sideroblastic anemia (XLSA) by reducing mitochondrial enzymatic... 
SUBSTITUTION | ENZYME | HEME-BIOSYNTHESIS | GENE | PYRIDOXINE RESPONSIVENESS | BIOCHEMISTRY & MOLECULAR BIOLOGY | DELTA-AMINOLEVULINATE SYNTHASE | ERYTHROID 5-AMINOLEVULINATE SYNTHASE | NUCLEOSIDE-DIPHOSPHATE KINASE | ENCEPHALOMYOPATHY | IRON OVERLOAD | Succinate-CoA Ligases - genetics | Succinate-CoA Ligases - metabolism | Genetic Diseases, X-Linked - enzymology | Vitamin B 6 - metabolism | Humans | Male | Mutation, Missense | Vitamin B 6 - genetics | Anemia, Sideroblastic - genetics | Protoporphyria, Erythropoietic - genetics | Heme - genetics | Heme - biosynthesis | 5-Aminolevulinate Synthetase - genetics | Anemia, Sideroblastic - enzymology | Protein Binding | Adult | Genetic Diseases, X-Linked - genetics | 5-Aminolevulinate Synthetase - metabolism | Protoporphyria, Erythropoietic - enzymology | Enzyme Stability - genetics | Amino Acid Substitution | Enzyme Purification | Heme Biosynthesis | Molecular Bases of Disease | Positive Cooperativity | Hematology | Heme | Metabolic Diseases | Enzyme Mutation | Iron | Enzyme Kinetics | Pyridoxine-responsive
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2. Full Text Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP)
by Ducamp, Sarah and Schneider-Yin, Xiaoye and De Rooij, Felix and Clayton, Jerome and Fratz, Erica J and Rudd, Alice and Ostapowicz, George and Varigos, George and Lefebvre, Thibaud and Deybach, Jean-Charles and Gouya, Laurent and Wilson, Paul and Ferreira, Gloria C and Minder, Elisabeth I and Puy, Hervé
Human Molecular Genetics, ISSN 0964-6906, 04/2013, Volume 22, Issue 7, pp. 1280 - 1288
Frameshift mutations in the last coding exon of the 5-aminolevulinate synthase (ALAS) 2 gene were described to activate the enzyme causing increased levels of... 
MODIFIER | PROTEIN | VARIANTS | SUCCINYL-COA SYNTHETASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENETICS & HEREDITY | SIDEROBLASTIC ANEMIA | MUTATIONS | IRON OVERLOAD | ALAS2 GENE | DEFICIENCY | PORPHYRIA | 5-Aminolevulinate Synthetase - deficiency | Frameshift Mutation | Genetic Diseases, X-Linked - enzymology | Exons | Humans | Child, Preschool | Molecular Sequence Data | Infant | Protoporphyria, Erythropoietic - genetics | Young Adult | DNA Mutational Analysis | Base Sequence | Female | Genetic Diseases, X-Linked - genetics | 5-Aminolevulinate Synthetase - metabolism | Protoporphyria, Erythropoietic - enzymology | Protein Structure, Tertiary | Amino Acid Sequence | Mutagenesis, Site-Directed | Genetic Association Studies | 5-Aminolevulinate Synthetase - chemistry | Codon, Nonsense | Sequence Analysis, DNA | Pedigree | 5-Aminolevulinate Synthetase - genetics | Mosaicism | Kinetics | Nonsense mutant | Protoporphyrin | Enzymatic activity | Point mutation | X chromosome | Frameshift mutation | Amino acids | 5-Aminolevulinate synthase | C-Terminus
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3. Full Text ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria
by To-Figueras, Jordi and Ducamp, Sarah and Clayton, Jerome and Badenas, Celia and Delaby, Constance and Ged, Cecile and Lyoumi, Said and Gouya, Laurent and De Verneuil, Hubert and Beaumont, Carole and Ferreira, Gloria C and Deybach, Jean-Charles and Herrero, Carmen and Puy, Herve
Blood, ISSN 0006-4971, 08/2011, Volume 118, Issue 6, pp. 1443 - 1451
Mutations in the uroporphyrinogen III synthase (UROS) gene cause congenital erythropoietic porphyria (CEP), an autosomal-recessive inborn error of erythroid... 
PERFORMANCE LIQUID-CHROMATOGRAPHY | ENZYME | PROTOPORPHYRIA | DELTA-AMINOLEVULINATE SYNTHASE | MUTATION | LINKED SIDEROBLASTIC ANEMIA | UROPORPHYRINOGEN-III SYNTHASE | IDENTIFICATION | HEMATOLOGY | 5-AMINOLEVULINATE SYNTHASE | EXPRESSION | Humans | Child, Preschool | Molecular Sequence Data | Family Health | Infant | Male | Mutation, Missense | Anemia, Sideroblastic - metabolism | Protoporphyria, Erythropoietic - genetics | Uroporphyrinogens - metabolism | Porphyria, Erythropoietic - genetics | Base Sequence | Female | Genetic Diseases, X-Linked - genetics | 5-Aminolevulinate Synthetase - metabolism | Anemia, Sideroblastic - pathology | Porphyria, Erythropoietic - metabolism | Severity of Illness Index | Amino Acid Sequence | Electrophoresis, Polyacrylamide Gel | Uroporphyrinogen III Synthetase - genetics | Uroporphyrinogen III Synthetase - metabolism | Genotype | Porphyria, Erythropoietic - pathology | Genetic Diseases, X-Linked - metabolism | Anemia, Sideroblastic - genetics | Sequence Homology, Amino Acid | Protoporphyria, Erythropoietic - metabolism | Pedigree | 5-Aminolevulinate Synthetase - genetics | Kinetics | Spectrophotometry
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4. Full Text Structure of the Mitochondrial Aminolevulinic Acid Synthase, a Key Heme Biosynthetic Enzyme
by Brown, Breann L and Kardon, Julia R and Sauer, Robert T and Baker, Tania A and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Structure, ISSN 0969-2126, 04/2018, Volume 26, Issue 4, pp. 580 - 589.e4
5-Aminolevulinic acid synthase (ALAS) catalyzes the first step in heme biosynthesis. We present the crystal structure of a eukaryotic ALAS from . In this... 
ClpX | AAA+ unfoldase | porphyria | XLSA | XLPP | α-oxoamine family | sideroblastic anemia | BIOCHEMISTRY & MOLECULAR BIOLOGY | LINKED SIDEROBLASTIC ANEMIA | 5-AMINOLEVULINATE SYNTHASE | GLYCINE LOOP | FEATURES | CELL BIOLOGY | PHOSPHATE COFACTOR-BINDING | BIOPHYSICS | METABOLISM | SUCCINYL-COA SYNTHETASE | PURIFICATION | MUTATIONS | DOMINANT PROTOPORPHYRIA | Pyridoxal Phosphate - chemistry | Mitochondria - enzymology | Aminolevulinic Acid - chemistry | Saccharomyces cerevisiae - genetics | Protein Multimerization | Substrate Specificity | Crystallography, X-Ray | Protein Subunits - metabolism | Pyridoxal Phosphate - metabolism | Coenzymes - metabolism | Heme - chemistry | Mitochondria - genetics | Aminolevulinic Acid - metabolism | Heme - biosynthesis | Cloning, Molecular | Escherichia coli - metabolism | 5-Aminolevulinate Synthetase - metabolism | Protein Interaction Domains and Motifs | Coenzymes - chemistry | Mitochondria - chemistry | Protein Subunits - genetics | Recombinant Proteins - metabolism | Protein Conformation, alpha-Helical | Catalytic Domain | Gene Expression | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | 5-Aminolevulinate Synthetase - chemistry | Recombinant Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - chemistry | Amino Acid Motifs | Protein Conformation, beta-Strand | Escherichia coli - genetics | 5-Aminolevulinate Synthetase - genetics | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Protein Subunits - chemistry | Kinetics | Mutation | Amino Acid Substitution | Saccharomyces cerevisiae Proteins - chemistry | Phosphates | Enzymes | Anemia | Analysis | Heme | Crystals | Hemoglobin synthesis | Structure | AAA+ | unfoldase | Sideroblastic anemia
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5. Full Text Clinical, Biochemical, and Genetic Characterization of North American Patients With Erythropoietic Protoporphyria and X-linked Protoporphyria
by Balwani, Manisha and Naik, Hetanshi and Anderson, Karl E and Bissell, D. Montgomery and Bloomer, Joseph and Bonkovsky, Herbert L and Phillips, John D and Overbey, Jessica R and Wang, Bruce and Singal, Ashwani K and Liu, Lawrence U and Desnick, Robert J
JAMA Dermatology, ISSN 2168-6068, 08/2017, Volume 153, Issue 8, pp. 789 - 796
IMPORTANCE: Autosomal recessive erythropoietic protoporphyria (EPP) and X-linked protoporphyria (XLP) are rare photodermatoses presenting with variable degrees... 
SYNTHASE | DIAGNOSIS | LIVER-TRANSPLANTATION | PHOTOSENSITIVITY | AFAMELANOTIDE | PORPHYRIN | GAIN | CIMETIDINE | DERMATOLOGY | 5-Aminolevulinate Synthetase - deficiency | Prospective Studies | Humans | Middle Aged | Child, Preschool | Male | Protoporphyria, Erythropoietic - genetics | Young Adult | Protoporphyria, Erythropoietic - physiopathology | Adult | Female | Genetic Diseases, X-Linked - genetics | Child | Genetic Diseases, X-Linked - physiopathology | Severity of Illness Index | Liver Diseases - genetics | Genotype | Phenotype | 5-Aminolevulinate Synthetase - genetics | Adolescent | Quality of Life | Ferrochelatase - genetics | Aged | Liver Diseases - physiopathology | Mutation | Genetic aspects | Demographic aspects | Erythrohepatic porphyria | Risk factors | Online First | Original Investigation | Research
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6. Full Text Malaria Parasite-Synthesized Heme Is Essential in the Mosquito and Liver Stages and Complements Host Heme in the Blood Stages of Infection
by Nagaraj, Viswanathan Arun and Sundaram, Balamurugan and Varadarajan, Nandan Mysore and Subramani, Pradeep Annamalai and Kalappa, Devaiah Monnanda and Ghosh, Susanta Kumar and Padmanaban, Govindarajan
PLoS Pathogens, ISSN 1553-7366, 08/2013, Volume 9, Issue 8, p. e1003522
Heme metabolism is central to malaria parasite biology. The parasite acquires heme from host hemoglobin in the intraerythrocytic stages and stores it as... 
LOCALIZATION | DEHYDRATASE | VACCINE | MICROBIOLOGY | IDENTIFICATION | VACUOLE | IMPORT | TRANSMISSION | VIROLOGY | OXIDASE | PLASMODIUM-FALCIPARUM | BIOSYNTHESIS | PARASITOLOGY | Malaria, Falciparum - enzymology | Plasmodium falciparum - enzymology | Malaria, Falciparum - genetics | Hemeproteins - biosynthesis | Hemeproteins - genetics | Liver - pathology | Anopheles - parasitology | Humans | Plasmodium berghei - genetics | Oocysts - enzymology | Sporozoites - enzymology | Animals | Heme - genetics | Ferrochelatase - metabolism | Heme - biosynthesis | 5-Aminolevulinate Synthetase - genetics | Plasmodium berghei - enzymology | Plasmodium falciparum - genetics | Ferrochelatase - genetics | 5-Aminolevulinate Synthetase - metabolism | Mice | Liver - parasitology | Malaria | Liver | Heme | Physiological aspects | Host-parasite relationships | Biosynthesis | Research | Health aspects | Studies | Parasites | Blood
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7. Full Text C-Terminal Deletions in the ALAS2 Gene Lead to Gain of Function and Cause X-linked Dominant Protoporphyria without Anemia or Iron Overload
by Whatley, Sharon D and Ducamp, Sarah and Gouya, Laurent and Grandchamp, Bernard and Beaumont, Carole and Badminton, Michael N and Elder, George H and Holme, S. Alexander and Anstey, Alexander V and Parker, Michelle and Corrigall, Anne V and Meissner, Peter N and Hift, Richard J and Marsden, Joanne T and Ma, Yun and Mieli-Vergani, Giorgina and Deybach, Jean-Charles and Puy, Hervé
The American Journal of Human Genetics, ISSN 0002-9297, 2008, Volume 83, Issue 3, pp. 408 - 414
All reported mutations in , which encodes the rate-regulating enzyme of erythroid heme biosynthesis, cause X-linked sideroblastic anemia. We describe eight... 
ZINC PROTOPORPHYRIN | HEME-BIOSYNTHESIS | METABOLISM | ERYTHROPOIETIC PROTOPORPHYRIA | MUTATION | GENETICS & HEREDITY | MICE | SIDEROBLASTIC ANEMIA | DIFFERENTIATION | AMINOLEVULINATE SYNTHASE GENE | FAMILY | Chromosomes, Human, X - genetics | Heme - metabolism | Porphyrias, Hepatic - pathology | 5-Aminolevulinate Synthetase - genetics | Humans | Erythrocytes - metabolism | Female | Male | Protoporphyrins - blood | Mutation | Porphyrias, Hepatic - genetics | Genetic aspects | Gene expression | Prokaryotes | Analysis | Erythrohepatic porphyria | Report
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8. Full Text Human Erythroid 5‑Aminolevulinate Synthase Mutations Associated with X‑Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release
by Fratz, Erica J and Clayton, Jerome and Hunter, Gregory A and Ducamp, Sarah and Breydo, Leonid and Uversky, Vladimir N and Deybach, Jean-Charles and Gouya, Laurent and Puy, Hervé and Ferreira, Gloria C
Biochemistry, ISSN 0006-2960, 09/2015, Volume 54, Issue 36, pp. 5617 - 5631
Regulation of 5-aminolevulinate synthase (ALAS) is at the origin of balanced heme production in mammals. Mutations in the C-terminal region of human... 
SUBSTRATE-BINDING | ENZYME | PYRIDOXAL-PHOSPHATE COFACTOR | SUCCINYL-COA SYNTHETASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DELTA-AMINOLEVULINATE SYNTHASE | ESCHERICHIA-COLI | TERMINAL REGION | SIDEROBLASTIC ANEMIA | DOMINANT PROTOPORPHYRIA | ALAS2 GENE | 5-Aminolevulinate Synthetase - deficiency | Protein Structure, Tertiary | Aminolevulinic Acid - chemistry | Genetic Diseases, X-Linked - enzymology | Protein Structure, Secondary | Humans | Enzyme Stability | Protoporphyrins - metabolism | 5-Aminolevulinate Synthetase - chemistry | Escherichia coli - cytology | Hot Temperature | Protoporphyria, Erythropoietic - genetics | Thermodynamics | Aminolevulinic Acid - metabolism | 5-Aminolevulinate Synthetase - genetics | K562 Cells | Genetic Diseases, X-Linked - genetics | 5-Aminolevulinate Synthetase - metabolism | Protoporphyria, Erythropoietic - enzymology | HeLa Cells | Kinetics | Mutation | Protoporphyrins - chemistry | Proteins | Usage | Research | Gene mutations | Spectrum analysis | Erythrohepatic porphyria | tetrapyrrole | porphyrin | pyridoxal 5’-phosphate | porphyria | X-linked erythropoietic protoporphyria | Heme biosynthesis | 5-aminolevulinate | 5-aminolevulinate synthase
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9. Full Text The heme biosynthesis pathway is essential for Plasmodium falciparum development in mosquito stage but not in blood stages
by Ke, Hangjun and Sigala, Paul A and Miura, Kazutoyo and Morrisey, Joanne M and Mather, Michael W and Crowley, Jan R and Henderson, Jeffrey P and Goldberg, Daniel E and Long, Carole A and Vaidya, Akhil B
Journal of Biological Chemistry, ISSN 0021-9258, 12/2014, Volume 289, Issue 50, pp. 34827 - 34837
Background: Malaria parasites require heme for growth. Results: Genetic disruption of the P. falciparum heme biosynthesis pathway ablated growth in mosquitoes... 
DRUG | MALARIAL PARASITE | DECARBOXYLASE | ACID | Malaria | MECHANISM | BIOCHEMISTRY & MOLECULAR BIOLOGY | IRON | IDENTIFICATION | MASS-SPECTROMETRY | Mitochondria | METABOLISM | Heme | FERROCHELATASE | Insect | Mitochondrial Metabolism | 5-Aminolevulinate Synthetase - deficiency | Heme - metabolism | Anopheles - parasitology | Humans | Male | Gene Knockout Techniques | Tandem Mass Spectrometry | Animals | Heme - biosynthesis | 5-Aminolevulinate Synthetase - genetics | Plasmodium falciparum - genetics | Female | Ferrochelatase - genetics | Plasmodium falciparum - metabolism | Plasmodium falciparum - growth & development | Plasmodium falciparum - physiology | Erythrocytes - parasitology | Microbiology
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10. Full Text Phase 1 Trial of an RNA Interference Therapy for Acute Intermittent Porphyria
by Sardh, Eliane and Harper, Pauline and Balwani, Manisha and Stein, Penelope and Rees, David and Bissell, D. Montgomery and Desnick, Robert and Parker, Charles and Phillips, John and Bonkovsky, Herbert L and Vassiliou, Daphne and Penz, Craig and Chan-Daniels, Amy and He, Qiuling and Querbes, William and Fitzgerald, Kevin and Kim, Jae B and Garg, Pushkal and Vaishnaw, Akshay and Simon, Amy R and Anderson, Karl E
The New England Journal of Medicine, ISSN 0028-4793, 02/2019, Volume 380, Issue 6, pp. 549 - 558
Acute intermittent porphyria results in excess activity of ALA synthase and overproduction of neurotoxic metabolites that cause attacks of severe abdominal... 
GENOTYPE-PHENOTYPE CORRELATION | BIOCHEMICAL CHARACTERISTICS | MEDICINE, GENERAL & INTERNAL | ACUTE ATTACKS | LIVER-TRANSPLANTATION | GENE | DELTA-AMINOLEVULINIC-ACID | RECOMMENDATIONS | PORPHOBILINOGEN | PREVALENCE | CLINICAL MANAGEMENT | Porphobilinogen - blood | Drug Administration Schedule | Humans | Liver - metabolism | Middle Aged | Male | RNA, Messenger - urine | 5-Aminolevulinate Synthetase - antagonists & inhibitors | Molecular Targeted Therapy | RNA, Messenger - metabolism | Dose-Response Relationship, Drug | Porphyria, Acute Intermittent - drug therapy | 5-Aminolevulinate Synthetase - genetics | Injections, Subcutaneous | Amides - adverse effects | Adult | Female | 5-Aminolevulinate Synthetase - metabolism | RNAi Therapeutics | Amides - administration & dosage | Porphyria | Care and treatment | Analysis | Clinical trials | Genetic aspects | Research | Gene expression | RNA-mediated interference | Body weight | Diarrhea | Rhinopharyngitis | Aminolevulinic acid | Patients | Intermediates | Hereditary diseases | Neurotoxicity | Pain | Heme | Mutation | Pharmaceuticals | Index Medicus | Abridged Index Medicus
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11. Full Text X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation
by Sankaran, Vijay G and Ulirsch, Jacob C and Tchaikovskii, Vassili and Ludwig, Leif S and Wakabayashi, Aoi and Kadirvel, Senkottuvelan and Lindsley, R. Coleman and Bejar, Rafael and Shi, Jiahai and Lovitch, Scott B and Bishop, David F and Steensma, David P
Journal of Clinical Investigation, ISSN 0021-9738, 04/2015, Volume 125, Issue 4, pp. 1665 - 1669
Macrocytic anemia with abnormal erythropoiesis is a common feature of megaloblastic anemias, congenital dyserythropoietic anemias, and myelodysplastic... 
MEDICINE, RESEARCH & EXPERIMENTAL | GENE | CHROMOSOME-INACTIVATION PATTERNS | IRON | SIDEROBLASTIC ANEMIA | IDENTIFICATION | HEMATOLOGY | 5-AMINOLEVULINATE SYNTHASE | Humans | Molecular Sequence Data | Male | Mutation, Missense | Pregnancy Complications, Hematologic - genetics | Pyridoxal Phosphate - metabolism | Iron Overload - etiology | Genes, X-Linked | Genes, Dominant | Hemorrhage - etiology | Adult | Female | Genetic Diseases, X-Linked - genetics | 5-Aminolevulinate Synthetase - metabolism | Erythropoiesis - genetics | Genetic Diseases, X-Linked - blood | RNA, Messenger - genetics | Anemia, Dyserythropoietic, Congenital - genetics | Cells, Cultured | Models, Molecular | Reticulocytes - metabolism | Pregnancy | Point Mutation | Puerperal Disorders - etiology | Exome - genetics | 5-Aminolevulinate Synthetase - genetics | Protein Binding | Protein Conformation | Anemia, Macrocytic - genetics | X Chromosome Inactivation | Women | Gene mutations | Genetic research | Development and progression | Genetic aspects | Research | Health aspects | Macrocytic anemia | Mutation | Enzyme kinetics | Anemia | Biopsy | Genes | Brief Report
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12. Full Text Novel mechanisms for heme-dependent degradation of ALAS1 protein as a component of negative feedback regulation of heme biosynthesis
by Kubota, Yoshiko and Nomura, Kazumi and Katoh, Yasutake and Yamashita, Rina and Kaneko, Kiriko and Furuyama, Kazumichi
Journal of Biological Chemistry, ISSN 0021-9258, 09/2016, Volume 291, Issue 39, pp. 20516 - 20529
In eukaryotic cells, heme production is tightly controlled by heme itself through negative feedback-mediated regulation of nonspecific 5-aminolevulinate... 
post-translational modification (PTM) | LON PROTEASE | CELLS | RECOGNITION | heme | MITOCHONDRIAL | mitochondria | BIOCHEMISTRY & MOLECULAR BIOLOGY | DELTA-AMINOLEVULINATE SYNTHASE | SIDEROBLASTIC ANEMIA | MOTIF | ENZYME | GENE | ATP-dependent protease | 5-aminolevulinate synthase | protein degradation | mass spectrometry (MS) | Mitochondria - enzymology | ATP-Dependent Proteases - genetics | Heme - metabolism | Oxidation-Reduction | Humans | Endopeptidase Clp - genetics | Endopeptidase Clp - metabolism | Mitochondrial Proteins - genetics | Amino Acid Motifs | Hep G2 Cells | Heme - genetics | Mitochondria - genetics | Mitochondrial Proteins - metabolism | Proteolysis | 5-Aminolevulinate Synthetase - genetics | 5-Aminolevulinate Synthetase - metabolism | Binding Sites | ATP-Dependent Proteases - metabolism | Protein Synthesis and Degradation
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13. Full Text Lethal ALAS2 mutation in males X‐linked sideroblastic anaemia
by Rose, Christian and Callebaut, Isabelle and Pascal, Laurent and Oudin, Claire and Fournier, Martine and Gouya, Laurent and Lambilliotte, Anne and Kannengiesser, Caroline
British Journal of Haematology, ISSN 0007-1048, 08/2017, Volume 178, Issue 4, pp. 648 - 651
Red cells | ALAS2 | Haem | HEMATOLOGY | ONSET | Amino Acid Sequence | Humans | Models, Molecular | Erythrocyte Indices | Male | 5-Aminolevulinate Synthetase - chemistry | Genetic Diseases, X-Linked - diagnosis | Anemia, Sideroblastic - genetics | Genes, Lethal | Phenotype | Anemia, Sideroblastic - diagnosis | DNA Mutational Analysis | Pedigree | 5-Aminolevulinate Synthetase - genetics | Bone Marrow - pathology | Germ-Line Mutation | Female | Genetic Diseases, X-Linked - genetics | Heterozygote | Protein Conformation | Mutation | Anemia | Genetic aspects | Males
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14. Full Text Long non-coding RNA-dependent mechanism to regulate heme biosynthesis and erythrocyte development
by Liu, Jinhua and Li, Yapu and Tong, Jingyuan and Gao, Jie and Guo, Qing and Zhang, Lingling and Wang, Bingrui and Zhao, Hui and Wang, Hongtao and Jiang, Erlie and Kurita, Ryo and Nakamura, Yukio and Tanabe, Osamu and Engel, James Douglas and Bresnick, Emery H and Zhou, Jiaxi and Shi, Lihong
Nature Communications, ISSN 2041-1723, 12/2018, Volume 9, Issue 1, pp. 4386 - 15
In addition to serving as a prosthetic group for enzymes and a hemoglobin structural component, heme is a crucial homeostatic regulator of erythroid cell... 
BLADDER-CARCINOMA | HEMATOPOIESIS | CONGENITAL SIDEROBLASTIC ANEMIA | ERYTHROPOIESIS | MULTIDISCIPLINARY SCIENCES | DELTA-AMINOLEVULINATE SYNTHASE | GENE-EXPRESSION | DEGRADATION | DIFFERENTIATION | IDENTIFICATION | TRACT-BINDING-PROTEIN | Antigens, CD34 - metabolism | Heme - metabolism | Humans | Erythroid Cells - metabolism | Heterogeneous-Nuclear Ribonucleoproteins - metabolism | Polypyrimidine Tract-Binding Protein - metabolism | RNA, Long Noncoding - genetics | RNA, Messenger - metabolism | Stem Cells - metabolism | Erythropoiesis - physiology | Heterogeneous-Nuclear Ribonucleoproteins - genetics | Cell Differentiation - genetics | 5-Aminolevulinate Synthetase - genetics | Protein Binding | 5-Aminolevulinate Synthetase - metabolism | Cell Differentiation - physiology | RNA, Long Noncoding - metabolism | Erythropoiesis - genetics | Polypyrimidine Tract-Binding Protein - genetics | Prostheses | Post-transcription | Erythrocytes | mRNA | Biosynthesis | Metabolism | Ribonucleic acid--RNA | Erythroid cells | Proteins | RNA-binding protein | Red blood cells | Heme | Hemoglobin | Non-coding RNA
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15. Full Text RNAi-mediated silencing of hepatic Alas1 effectively prevents and treats the induced acute attacks in acute intermittent porphyria mice
by Makiko Yasuda and Lin Gan and Brenden Chen and Senkottuvelan Kadir