2.3.1.37 5-aminolevulinate synthase deficiency http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1570328&form=6&db=m Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. causal interaction,ongoing research,unassigned 3,3,0 2.3.1.37 5-aminolevulinate synthase deficiency http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12393610&form=6&db=m Aberrant iron accumulation and oxidized status of erythroid-specific delta-aminolevulinate synthase (ALAS2)-deficient definitive erythroblasts. causal interaction,unassigned 3,0 2.3.1.37 5-aminolevulinate synthase deficiency http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29908199&form=6&db=m Establishment of a cell model of X-linked sideroblastic anemia using genome editing. causal interaction,unassigned 4,0 2.3.1.37 Alzheimer Disease http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19477221&form=6&db=m Down-regulation of aminolevulinate synthase, the rate-limiting enzyme for heme biosynthesis in Alzheimer's disease. causal interaction,ongoing research,unassigned 1,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=500806&form=6&db=m delta-Aminolevulinic acid synthetase in erythroblasts of patients with pyridoxine-responsive anemia. Hypercatabolism caused by the increased susceptibility to the controlling protease. therapeutic application,unassigned 1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=541749&form=6&db=m Developmental and convalescent changes of the anemia caused by excess methionine in the rat. causal interaction,diagnostic usage,unassigned 2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=934737&form=6&db=m Heme synthesis in hereditary hemolytic anemias: decreased delta-aminolevulinic acid synthetase in hemoglobin Köln disease. causal interaction,diagnostic usage,ongoing research,therapeutic application 4,2,3,1 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3197910&form=6&db=m Properties of chicken erythrocyte delta-aminolevulinate synthase. unassigned - 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3390396&form=6&db=m 5-Aminolaevulinic acid synthase activity in developing human erythroblasts. causal interaction,diagnostic usage,unassigned 1,3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7560104&form=6&db=m Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8107717&form=6&db=m X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. causal interaction,ongoing research,therapeutic application,unassigned 4,2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8154933&form=6&db=m Abnormal haem biosynthesis in the chronic anaemia of rheumatoid arthritis. causal interaction,unassigned 1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9226183&form=6&db=m Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene. causal interaction,ongoing research,unassigned 4,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9372069&form=6&db=m The molecular basis of the sideroblastic anemias. causal interaction,unassigned 3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15565468&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678585&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678586&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678587&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15885606&form=6&db=m Iron overload in an African American woman with SS hemoglobinopathy and a promoter mutation in the X-linked erythroid-specific 5-aminolevulinate synthase (ALAS2) gene. causal interaction,diagnostic usage,unassigned 4,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16446107&form=6&db=m Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. causal interaction,diagnostic usage,ongoing research,unassigned 3,2,3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16540354&form=6&db=m Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma. therapeutic application,unassigned 1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16735131&form=6&db=m X-linked sideroblastic anemia associated with a novel ALAS2 mutation and unfortunate skewed X-chromosome inactivation patterns. causal interaction,unassigned 4,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16838333&form=6&db=m Iron overload and prolonged ingestion of iron supplements: Clinical features and mutation analysis of hemochromatosis-associated genes in four cases. diagnostic usage,unassigned 1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18760763&form=6&db=m C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. causal interaction,unassigned 4,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18780836&form=6&db=m hem6: an ENU-induced recessive hypochromic microcytic anemia mutation in the mouse. unassigned - 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19066423&form=6&db=m Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19693999&form=6&db=m Novel human pathological mutations. Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,unassigned 2,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21296123&form=6&db=m A toxicogenomic approach for identifying biomarkers for myelosuppressive anemia in rats. causal interaction,diagnostic usage,ongoing research,unassigned 1,3,3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24829177&form=6&db=m X-linked sideroblastic anaemia due to ALAS? mutations in the Netherlands: a disease in disguise. causal interaction,unassigned 4,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25705881&form=6&db=m X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation. causal interaction,unassigned 3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28123038&form=6&db=m Intron 1 GATA site enhances ALAS2 expression indispensably during erythroid differentiation. causal interaction,unassigned 3,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31338833&form=6&db=m Genotype/phenotype correlations of childhood-onset congenital sideroblastic anaemia in a European cohort. causal interaction,diagnostic usage,unassigned 4,1,0 2.3.1.37 Anemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31895053&form=6&db=m X-linked macrocytic dyserythropoietic anemia in females with an ALAS2 mutation. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Dyserythropoietic, Congenital http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3390396&form=6&db=m 5-Aminolaevulinic acid synthase activity in developing human erythroblasts. causal interaction,diagnostic usage,unassigned 1,3,0 2.3.1.37 Anemia, Hemolytic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=14577161&form=6&db=m [Activity of key enzymes of heme metabolism and cytochrome P-450 content in the rat liver in experimental rhabdomyolysis and hemolytic anemia] ongoing research,unassigned 2,0 2.3.1.37 Anemia, Hemolytic, Congenital http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=934737&form=6&db=m Heme synthesis in hereditary hemolytic anemias: decreased delta-aminolevulinic acid synthetase in hemoglobin Köln disease. causal interaction,diagnostic usage,ongoing research,therapeutic application 4,2,3,1 2.3.1.37 Anemia, Macrocytic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9372069&form=6&db=m The molecular basis of the sideroblastic anemias. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Refractory http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7560104&form=6&db=m Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Anemia, Refractory http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21388451&form=6&db=m Lack of efficacy of pyridoxine (vitamin B6) treatment in acquired idiopathic sideroblastic anaemia, including refractory anaemia with ring sideroblasts. therapeutic application,unassigned 3,0 2.3.1.37 Anemia, Sickle Cell http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15885606&form=6&db=m Iron overload in an African American woman with SS hemoglobinopathy and a promoter mutation in the X-linked erythroid-specific 5-aminolevulinate synthase (ALAS2) gene. causal interaction,diagnostic usage,unassigned 4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=213624&form=6&db=m [A case of acquired sideroblastic anemia with reduced activity of either delta-aminolevulinic acid synthetase in erythroblasts or neutral protease and cytochrome oxidase in granulocytes (author's transl)] unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=987283&form=6&db=m [A family of hereditary refractory sideroblastic anemia with markedly reduced delta-aminolevulinic acid synthetase activity in bone marrow erythroblasts] therapeutic application,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1301172&form=6&db=m Identification of a highly polymorphic marker within intron 7 of the ALAS2 gene and suggestion of at least two loci for X-linked sideroblastic anemia. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1415186&form=6&db=m 5-Aminolevulinate synthase in sideroblastic anemias: mRNA and enzyme activity levels in bone marrow cells. diagnostic usage,ongoing research,unassigned 4,2,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1570328&form=6&db=m Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. causal interaction,ongoing research,unassigned 3,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1577484&form=6&db=m Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2347585&form=6&db=m Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3390396&form=6&db=m 5-Aminolaevulinic acid synthase activity in developing human erythroblasts. causal interaction,diagnostic usage,unassigned 1,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3414687&form=6&db=m 5-Aminolevulinate synthase is at 3p21 and thus not the primary defect in X-linked sideroblastic anemia. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4208577&form=6&db=m Delta-aminolevulinic acid synthetase activity in normal human bone marrow and in patients with idiopathic sideroblastic anemia. diagnostic usage,ongoing research,unassigned 2,4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4738994&form=6&db=m Aminolevulinic acid synthetase activity in erythroblasts of patients with primary sideroblastic anemia. diagnostic usage,ongoing research,unassigned 3,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4833846&form=6&db=m Bone marrow delta-aminolevulinic acid synthetase activity in experimental sideroblastic anemia. diagnostic usage,ongoing research,therapeutic application,unassigned 3,1,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5561051&form=6&db=m Delta-aminolevulinic acid synthetase activity in erythroblasts of patients with sideroblastic anemia. diagnostic usage,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7313498&form=6&db=m The activities of delta-aminolaevulinic acid synthase and haem synthase in experimental sideroblastic anaemia. Effect of mitochondrial iron excess on the enzyme activity in peripheral red blood cells. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7313623&form=6&db=m [Acquired, vitamin B6-responsive, primary sideroblastic anemia, an enzyme deficiency in heme synthesis] causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7336157&form=6&db=m Haem biosynthesis in refractory sideroblastic anaemia associated with the preleukaemic syndrome. causal interaction,diagnostic usage,therapeutic application,unassigned 1,2,2,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7560104&form=6&db=m Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7592562&form=6&db=m 5-Aminolevulinate synthase and the first step of heme biosynthesis. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7592563&form=6&db=m Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemia. diagnostic usage,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7705839&form=6&db=m A new mutation of the ALAS2 gene in a large family with X-linked sideroblastic anemia. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7912287&form=6&db=m Pyridoxine-refractory congenital sideroblastic anaemia with evidence for autosomal inheritance: exclusion of linkage to ALAS2 at Xp11.21 by polymorphism analysis. causal interaction,diagnostic usage,unassigned 3,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7949148&form=6&db=m X-linked sideroblastic anemia: identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley. causal interaction,unassigned 2,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8089650&form=6&db=m Erythroid 5-aminolevulinate synthase and X-linked sideroblastic anemia. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8107717&form=6&db=m X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. causal interaction,ongoing research,therapeutic application,unassigned 4,2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9226183&form=6&db=m Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene. causal interaction,ongoing research,unassigned 4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9423809&form=6&db=m Sideroblastic anemias: variations on imprecision in diagnostic criteria, proposal for an extended classification of sideroblastic anemias. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9446639&form=6&db=m Deficient heme and globin synthesis in embryonic stem cells lacking the erythroid-specific delta-aminolevulinate synthase gene. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9542324&form=6&db=m The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9806542&form=6&db=m Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10029606&form=6&db=m Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10496043&form=6&db=m [An infant case of sideroblastic anemia that responded to oral pyridoxine] causal interaction,diagnostic usage,ongoing research,therapeutic application 4,1,1,1 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10577279&form=6&db=m A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. ongoing research,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10582344&form=6&db=m Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis. causal interaction,ongoing research,unassigned 1,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11110715&form=6&db=m Familial-skewed X-chromosome inactivation as a predisposing factor for late-onset X-linked sideroblastic anemia in carrier females. causal interaction,diagnostic usage,unassigned 3,4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11877024&form=6&db=m [A novel mutation of the ALAS2 gene in a family with X-linked sideroblastic anemia] causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11929042&form=6&db=m Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12031592&form=6&db=m A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12382202&form=6&db=m The genetics of inherited sideroblastic anemias. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12393718&form=6&db=m Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12531813&form=6&db=m Late-onset X-linked sideroblastic anemia following hemodialysis. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12663458&form=6&db=m A promoter mutation in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causes X-linked sideroblastic anemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12686158&form=6&db=m 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. ongoing research,therapeutic application,unassigned 1,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12699240&form=6&db=m Mechanism of 5-aminolevulinate synthase and the role of the protein environment in controlling the cofactor chemistry. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15217771&form=6&db=m [Hereditary sideroblastic anemia: a rare diagnosis] causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15477213&form=6&db=m Onset of X-linked sideroblastic anemia in the fourth decade. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15498136&form=6&db=m [Construction of recombinant vector expressing ALAS2 gene in X-linked sideroblastic anemia.] causal interaction,ongoing research,therapeutic application,unassigned 3,1,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15506716&form=6&db=m [Genetics of hereditary iron overload] causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15565468&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678585&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678586&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15678587&form=6&db=m Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,therapeutic application,unassigned 2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15972158&form=6&db=m [Progress of study on sideroblastic anemia and its possible gene therapy--review] causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16446107&form=6&db=m Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. causal interaction,diagnostic usage,ongoing research,unassigned 3,2,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16540354&form=6&db=m Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma. therapeutic application,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16716198&form=6&db=m Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16735131&form=6&db=m X-linked sideroblastic anemia associated with a novel ALAS2 mutation and unfortunate skewed X-chromosome inactivation patterns. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16892088&form=6&db=m Mitochondria in hematopoiesis and hematological diseases. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16935983&form=6&db=m A novel mutation, Ile289Thr, in the ALAS2 gene in a family with pyridoxine responsive sideroblastic anaemia. causal interaction,ongoing research,unassigned 2,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=17240176&form=6&db=m In silico analyses of Fsf1 sequences, a new group of fungal proteins orthologous to the metazoan sideroblastic anemia-related sideroflexin family. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18637800&form=6&db=m Recent advances in the understanding of inherited sideroblastic anaemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18760763&form=6&db=m C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19066423&form=6&db=m Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19268008&form=6&db=m 5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19679982&form=6&db=m Congenital sideroblastic anemia: a report of two cases. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19693999&form=6&db=m Novel human pathological mutations. Gene symbol: ALAS2. Disease: sideroblastic anaemia. ongoing research,unassigned 2,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19731322&form=6&db=m Systematic molecular genetic analysis of congenital sideroblastic anemia: Evidence for genetic heterogeneity and identification of novel mutations. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19786205&form=6&db=m Hereditary sideroblastic anemias: pathophysiology, diagnosis, and treatment. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19907149&form=6&db=m Mitochondrial iron metabolism and sideroblastic anemia. ongoing research,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21252495&form=6&db=m New Mutation in Erythroid-Specific Delta-Aminolevulinate Synthase as the Cause of X-Linked Sideroblastic Anemia Responsive to Pyridoxine. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21309041&form=6&db=m Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of ten missense mutations. diagnostic usage,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21348241&form=6&db=m [Recent progress in iron metabolism and iron-related anemia]. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21388451&form=6&db=m Lack of efficacy of pyridoxine (vitamin B6) treatment in acquired idiopathic sideroblastic anaemia, including refractory anaemia with ring sideroblasts. therapeutic application,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21393332&form=6&db=m Missense SLC25A38 variations play an important role in autosomal recessive inherited sideroblastic anemia. causal interaction,diagnostic usage,ongoing research,unassigned 2,1,2,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21653323&form=6&db=m ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21800356&form=6&db=m Sideroblastic anemia, iron overload, and ALAS2 R452S in African-American males: Phenotype and genotype features of five unrelated patients. diagnostic usage,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22269113&form=6&db=m The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22740690&form=6&db=m X-linked Sideroblastic Anemia Due to Carboxyl-terminal ALAS2 Mutations That Cause Loss of Binding to the ?-Subunit of Succinyl-CoA Synthetase (SUCLA2). causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22983749&form=6&db=m Clinical and genetic characteristics of congenital sideroblastic anemia: comparison with myelodysplastic syndrome with ring sideroblast (MDS-RS). causal interaction,diagnostic usage,unassigned 3,4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23935018&form=6&db=m Identification of the novel erythroid-specific enhancer for ALAS2 gene and its loss-of-function mutation associated with congenital sideroblastic anemia. causal interaction,diagnostic usage,ongoing research,unassigned 2,4,3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24166784&form=6&db=m X-linked sideroblastic anemia due to ALAS2 intron 1 enhancer element GATA-binding site mutations. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24624355&form=6&db=m A Novel Hemizygous I418S Mutation in the ALAS2 Gene in a Young Korean Man with X-Linked Sideroblastic Anemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24829177&form=6&db=m X-linked sideroblastic anaemia due to ALAS? mutations in the Netherlands: a disease in disguise. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25232504&form=6&db=m Concomitant a novel ALAS2 mutation and GATA1 mutation in a newborn: a case report and review of the literature. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26637696&form=6&db=m Diagnosis and treatment of sideroblastic anemias: from defective heme synthesis to abnormal RNA splicing. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27247955&form=6&db=m Sideroblastic anemia: functional study of two novel missense mutations in ALAS2. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27292130&form=6&db=m Lethal ALAS2 mutation in males X-linked sideroblastic anaemia. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27346685&form=6&db=m Exome Genotyping Identifies Pleiotropic Variants Associated with Red Blood Cell Traits. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27838491&form=6&db=m Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients. causal interaction,therapeutic application,unassigned 1,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28123038&form=6&db=m Intron 1 GATA site enhances ALAS2 expression indispensably during erythroid differentiation. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28644307&form=6&db=m X-linked Sideroblastic Anemia in a Malay Boy With ALAS2 S568G Mutation. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28667034&form=6&db=m A Novel ALAS2 Mutation Resulting in Variable Phenotypes and Pyridoxine Response in a Family with X-linked Sideroblastic Anemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28731922&form=6&db=m A Novel g.55040074delT in ALAS2 Gene Resulting in a Monomeric Protein and Severe Sideroblastic Anemia Phenotype. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28772256&form=6&db=m Non syndromic childhood onset congenital sideroblastic anemia: A report of 13 patients identified with an ALAS2 or SLC25A38 mutation. causal interaction,diagnostic usage,unassigned 4,4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28840292&form=6&db=m A novel heterozygous ALAS2 mutation in a female with macrocytic sideroblastic anemia resembling myelodysplastic syndrome with ring sideroblasts: a case report and literature review. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29213171&form=6&db=m Congenital sideroblastic anemia of a Saudi child. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29743399&form=6&db=m [Successful treatment of X-linked sideroblastic anemia with ALAS2 R452H mutation using vitamin B6]. causal interaction,diagnostic usage,therapeutic application,unassigned 3,4,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29908199&form=6&db=m Establishment of a cell model of X-linked sideroblastic anemia using genome editing. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30660387&form=6&db=m GLRX5 mutations impair heme biosynthetic enzymes ALA synthase 2 and ferrochelatase in Human congenital sideroblastic anemia. causal interaction,unassigned 1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30670569&form=6&db=m Generation and Molecular Characterization of Human Ring Sideroblasts: A Key Role of Ferrous Iron in Terminal Erythroid Differentiation and Ring Sideroblast Formation. ongoing research,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30737140&form=6&db=m Regulation and tissue-specific expression of ?-aminolevulinic acid synthases in non-syndromic sideroblastic anemias and porphyrias. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31326287&form=6&db=m Heme biosynthesis and the porphyrias. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31395332&form=6&db=m Results of a pilot study of isoniazid in patients with erythropoietic protoporphyria. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31495138&form=6&db=m [A case report of X-linked sideroblastic anemia with novel ALAS2 gene mutation]. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31848684&form=6&db=m Identification of a novel heterozygous ALAS2 mutation in a young Chinese female with X-linked sideroblastic anemia. causal interaction,unassigned 3,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32297424&form=6&db=m Novel mutations in the ALAS2 gene from patients with X-linked sideroblastic anemia. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32605921&form=6&db=m Novel frameshift variant (c.409dupG) in SLC25A38 is a common cause of congenital sideroblastic anaemia in the Indian subcontinent. unassigned - 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33858445&form=6&db=m A hemizygous p.R204Q mutation in the ALAS2 gene underlies X-linked sideroblastic anemia in an adult Chinese Han man. causal interaction,unassigned 4,0 2.3.1.37 Anemia, Sideroblastic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34411431&form=6&db=m A synonymous coding variant that alters ALAS2 splicing and causes X-linked sideroblastic anemia. causal interaction,unassigned 3,0 2.3.1.37 Ataxia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1577484&form=6&db=m Assignment of human erythroid delta-aminolevulinate synthase (ALAS2) to a distal subregion of band Xp11.21 by PCR analysis of somatic cell hybrids containing X; autosome translocations. unassigned - 2.3.1.37 beta-Thalassemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11110715&form=6&db=m Familial-skewed X-chromosome inactivation as a predisposing factor for late-onset X-linked sideroblastic anemia in carrier females. causal interaction,diagnostic usage,unassigned 3,4,0 2.3.1.37 Carcinogenesis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1451437&form=6&db=m Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation. causal interaction,unassigned 1,0 2.3.1.37 Carcinoma http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2178097&form=6&db=m Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice--I. Effect of allyl-isopropylacetamide and veronal on delta-aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase. diagnostic usage,ongoing research,unassigned 1,3,0 2.3.1.37 Carcinoma http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24718052&form=6&db=m Expression of Murine 5-Aminolevulinate Synthase Variants Causes Protoporphyrin IX Accumulation and Light-Induced Mammalian Cell Death. causal interaction,diagnostic usage,ongoing research,unassigned 2,1,4,0 2.3.1.37 Carcinoma http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26472512&form=6&db=m Over-expression 5-aminolevulinic acid synthase 2 in nonerythroid cell may causes protoporphyrin IX accumulation. ongoing research,therapeutic application,unassigned 4,1,0 2.3.1.37 Carcinoma http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27777144&form=6&db=m Over expression of 5-aminolevulinic acid synthase 2 increased protoporphyrin IX in nonerythroid cells. ongoing research,therapeutic application,unassigned 4,1,0 2.3.1.37 Carcinoma, Ehrlich Tumor http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2416025&form=6&db=m Heme metabolism and turnover of cytochrome P-450 in tumor-bearing mouse livers. diagnostic usage,unassigned 3,0 2.3.1.37 Carcinoma, Hepatocellular http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9806796&form=6&db=m Insulin inhibits delta-aminolevulinate synthase gene expression in rat hepatocytes and human hepatoma cells. ongoing research,unassigned 4,0 2.3.1.37 Carcinoma, Hepatocellular http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12469218&form=6&db=m CYP2E1 overexpression up-regulates both non-specific delta-aminolevulinate synthase and heme oxygenase-1 in the human hepatoma cell line HLE/2E1. ongoing research,unassigned 4,0 2.3.1.37 Carcinoma, Hepatocellular http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16540354&form=6&db=m Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma. therapeutic application,unassigned 1,0 2.3.1.37 Cardiomyopathies http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31823667&form=6&db=m Identification of differential gene expression related to epirubicin-induced cardiomyopathy in breast cancer patients. causal interaction,diagnostic usage,therapeutic application,unassigned 4,4,4,0 2.3.1.37 Cardiotoxicity http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31823667&form=6&db=m Identification of differential gene expression related to epirubicin-induced cardiomyopathy in breast cancer patients. causal interaction,diagnostic usage,therapeutic application,unassigned 4,4,4,0 2.3.1.37 Cholestasis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6401253&form=6&db=m Effect of cholestasis produced by bile duct ligation on hepatic heme and hemoprotein metabolism in rats. causal interaction,therapeutic application,unassigned 1,1,0 2.3.1.37 cystathionine beta-synthase deficiency http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31551410&form=6&db=m Cystathionine ?-synthase (CBS) deficiency suppresses erythropoiesis by disrupting expression of heme biosynthetic enzymes and transporter. causal interaction,ongoing research,therapeutic application,unassigned 1,2,1,0 2.3.1.37 Friedreich Ataxia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15506716&form=6&db=m [Genetics of hereditary iron overload] causal interaction,unassigned 4,0 2.3.1.37 Genetic Diseases, Inborn http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15506716&form=6&db=m [Genetics of hereditary iron overload] causal interaction,unassigned 4,0 2.3.1.37 Hemochromatosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10029606&form=6&db=m Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. causal interaction,unassigned 3,0 2.3.1.37 Hemochromatosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11202050&form=6&db=m Porphyrins, porphyrin metabolism, porphyrias. III. Diagnosis, care and monitoring in porphyria cutanea tarda--suggestions for a handling programme. causal interaction,unassigned 3,0 2.3.1.37 Hemochromatosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16446107&form=6&db=m Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. causal interaction,diagnostic usage,ongoing research,unassigned 3,2,3,0 2.3.1.37 Hemoglobinopathies http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15885606&form=6&db=m Iron overload in an African American woman with SS hemoglobinopathy and a promoter mutation in the X-linked erythroid-specific 5-aminolevulinate synthase (ALAS2) gene. causal interaction,diagnostic usage,unassigned 4,1,0 2.3.1.37 Hepatitis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26349215&form=6&db=m [Peculiarities of the Structural-Functional State of the Cytochrome Part of Liver Mitochondrial Respiratory Chain under Conditions of Acetaminophen-induced Hepatitis against the Background of Alimentary Deprivation of Protein]. unassigned - 2.3.1.37 Hepatitis C http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18823803&form=6&db=m Severe iron overload with a novel aminolevulinate synthase mutation and hepatitis C infection. A case report. causal interaction,unassigned 4,0 2.3.1.37 Hepatitis C, Chronic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18823803&form=6&db=m Severe iron overload with a novel aminolevulinate synthase mutation and hepatitis C infection. A case report. causal interaction,unassigned 4,0 2.3.1.37 Homocystinuria http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31551410&form=6&db=m Cystathionine ?-synthase (CBS) deficiency suppresses erythropoiesis by disrupting expression of heme biosynthetic enzymes and transporter. causal interaction,ongoing research,therapeutic application,unassigned 1,2,1,0 2.3.1.37 Hypertension, Pulmonary http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16181105&form=6&db=m Increased pulmonary heme oxygenase-1 and delta-aminolevulinate synthase expression in monocrotaline-induced pulmonary hypertension. causal interaction,unassigned 4,0 2.3.1.37 Infections http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18823803&form=6&db=m Severe iron overload with a novel aminolevulinate synthase mutation and hepatitis C infection. A case report. causal interaction,unassigned 4,0 2.3.1.37 Iron Deficiencies http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25179834&form=6&db=m In ferrochelatase-deficient protoporphyria patients, ALAS2 expression is enhanced and erythrocytic protoporphyrin concentration correlates with iron availability. causal interaction,unassigned 1,0 2.3.1.37 Iron Deficiencies http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25972160&form=6&db=m Inducing iron deficiency improves erythropoiesis and photosensitivity in congenital erythropoietic porphyria. therapeutic application,unassigned 2,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6895846&form=6&db=m Control of delta-aminolaevulinate synthase and haem oxygenase in chronic-iron-overloaded rats. causal interaction,ongoing research,unassigned 3,3,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10029606&form=6&db=m Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. causal interaction,unassigned 3,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15506716&form=6&db=m [Genetics of hereditary iron overload] causal interaction,unassigned 4,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15885606&form=6&db=m Iron overload in an African American woman with SS hemoglobinopathy and a promoter mutation in the X-linked erythroid-specific 5-aminolevulinate synthase (ALAS2) gene. causal interaction,diagnostic usage,unassigned 4,1,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16446107&form=6&db=m Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. causal interaction,diagnostic usage,ongoing research,unassigned 3,2,3,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16540354&form=6&db=m Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma. therapeutic application,unassigned 1,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18637800&form=6&db=m Recent advances in the understanding of inherited sideroblastic anaemia. causal interaction,unassigned 4,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18760763&form=6&db=m C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. causal interaction,unassigned 4,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=18823803&form=6&db=m Severe iron overload with a novel aminolevulinate synthase mutation and hepatitis C infection. A case report. causal interaction,unassigned 4,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19066423&form=6&db=m Multi-organ iron overload in an African-American man with ALAS2 R452S and SLC40A1 R561G. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21800356&form=6&db=m Sideroblastic anemia, iron overload, and ALAS2 R452S in African-American males: Phenotype and genotype features of five unrelated patients. diagnostic usage,unassigned 3,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28772256&form=6&db=m Non syndromic childhood onset congenital sideroblastic anemia: A report of 13 patients identified with an ALAS2 or SLC25A38 mutation. causal interaction,diagnostic usage,unassigned 4,4,0 2.3.1.37 Iron Overload http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33281618&form=6&db=m A Novel ALAS2 Missense Mutation in Two Brothers With Iron Overload and Associated Alterations in Serum Hepcidin/Erythroferrone Levels. diagnostic usage,unassigned 1,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=57826&form=6&db=m Erythroid differentiation in cultured Friend leukemia cells treated with metabolic inhibitors. causal interaction,unassigned 4,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4525098&form=6&db=m Induction of delta-aminolevulinic acid synthetase during erythroid differentiation of cultured leukemia cells. ongoing research,unassigned 4,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4852413&form=6&db=m Induction of delta-aminolevulinic acid synthetase in cultured friend leukemia cells by dimethyl sulfoxide and human placental extract. causal interaction,ongoing research,unassigned 1,4,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5777627&form=6&db=m Effect of Friend leukemia virus infection upon polycythemia and delta-aminolevulinic acid synthetase activity in nurine spleen and liver. ongoing research,unassigned 1,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21296123&form=6&db=m A toxicogenomic approach for identifying biomarkers for myelosuppressive anemia in rats. causal interaction,diagnostic usage,ongoing research,unassigned 1,3,3,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26703568&form=6&db=m miR-218 Inhibits Erythroid Differentiation and Alters Iron Metabolism by Targeting ALAS2 in K562 Cells. causal interaction,ongoing research,unassigned 1,2,0 2.3.1.37 Leukemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31551410&form=6&db=m Cystathionine ?-synthase (CBS) deficiency suppresses erythropoiesis by disrupting expression of heme biosynthetic enzymes and transporter. causal interaction,ongoing research,therapeutic application,unassigned 1,2,1,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1536142&form=6&db=m Differential induction responses of delta-aminolevulinate synthase mRNAs during erythroid differentiation: use of nonradioactive in situ hybridization. ongoing research,unassigned 4,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1894633&form=6&db=m Erythroleukemia differentiation. Distinctive responses of the erythroid-specific and the nonspecific delta-aminolevulinate synthase mRNA. ongoing research,unassigned 2,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3464611&form=6&db=m Control of heme synthesis during Friend cell differentiation: role of iron and transferrin. causal interaction,unassigned 1,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8413301&form=6&db=m Biphasic ordered induction of heme synthesis in differentiating murine erythroleukemia cells: role of erythroid 5-aminolevulinate synthase. causal interaction,ongoing research,unassigned 1,3,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8843957&form=6&db=m The role of iron supply in the regulation of 5-aminolevulinate synthase mRNA levels in murine erythroleukemia cells. ongoing research,unassigned 3,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9106619&form=6&db=m Protein tyrosine phosphatase-dependent activation of beta-globin and delta-aminolevulinic acid synthase genes in the camptothecin-induced IW32 erythroleukemia cell differentiation. causal interaction,ongoing research,therapeutic application,unassigned 3,1,2,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12393745&form=6&db=m Hypoxic up-regulation of erythroid 5-aminolevulinate synthase. unassigned - 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23935018&form=6&db=m Identification of the novel erythroid-specific enhancer for ALAS2 gene and its loss-of-function mutation associated with congenital sideroblastic anemia. causal interaction,diagnostic usage,ongoing research,unassigned 2,4,3,0 2.3.1.37 Leukemia, Erythroblastic, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24718052&form=6&db=m Expression of Murine 5-Aminolevulinate Synthase Variants Causes Protoporphyrin IX Accumulation and Light-Induced Mammalian Cell Death. causal interaction,diagnostic usage,ongoing research,unassigned 2,1,4,0 2.3.1.37 Leukemia, Myeloid http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=9133617&form=6&db=m 5-Aminolevulinate synthase expression and hemoglobin synthesis in a human myelogenous leukemia cell line. diagnostic usage,ongoing research,unassigned 1,4,0 2.3.1.37 Liver Cirrhosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6848403&form=6&db=m Changes in aminolevulinate synthase and aminolevulinate dehydratase activity in cirrhotic liver. diagnostic usage,ongoing research,unassigned 2,3,0 2.3.1.37 Liver Cirrhosis http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16540354&form=6&db=m Disparate phenotypic expression of ALAS2 R452H (nt 1407 G --> A) in two brothers, one with severe sideroblastic anemia and iron overload, hepatic cirrhosis, and hepatocellular carcinoma. therapeutic application,unassigned 1,0 2.3.1.37 Liver Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3679087&form=6&db=m Hepatic heme synthesis in a new model of experimental hemochromatosis: studies in rats fed finely divided elemental iron. causal interaction,unassigned 1,0 2.3.1.37 Liver Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23348515&form=6&db=m Molecular Expression and Characterization of Erythroid-Specific 5-Aminolevulinate Synthase Gain-of-Function Mutations Causing X-Linked Protoporphyria. causal interaction,unassigned 3,0 2.3.1.37 Liver Failure, Acute http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15547665&form=6&db=m Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute liver failure. causal interaction,ongoing research,unassigned 4,3,0 2.3.1.37 Liver Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2317819&form=6&db=m Heme synthesis in normal mouse liver and mouse liver tumors. unassigned - 2.3.1.37 Malnutrition http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=228623&form=6&db=m [Activity of delta-aminolevulinic synthetase, cytochrome oxidase and levels of the mixed function oxidase system during experimental protein malnutrition. Response to re-alimentation] diagnostic usage,ongoing research,therapeutic application,unassigned 3,4,1,0 2.3.1.37 Mental Retardation, X-Linked http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16969374&form=6&db=m X-linked mental retardation: a comprehensive molecular screen of 47 candidate genes from a 7.4 Mb interval in Xp11. unassigned - 2.3.1.37 Muscular Atrophy http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33785075&form=6&db=m Muscle atrophy induced by overexpression of ALAS2 is related to muscle mitochondrial dysfunction. causal interaction,unassigned 1,0 2.3.1.37 Myelodysplastic Syndromes http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28840292&form=6&db=m A novel heterozygous ALAS2 mutation in a female with macrocytic sideroblastic anemia resembling myelodysplastic syndrome with ring sideroblasts: a case report and literature review. causal interaction,unassigned 4,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1526138&form=6&db=m Rhodanese and ALA-S in mammary tumor and liver from normal and tumor-bearing mice. diagnostic usage,ongoing research,unassigned 1,4,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1781034&form=6&db=m Sex comparison of heme pathway in rats bearing hepatic tumors. causal interaction,unassigned 2,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2178097&form=6&db=m Heme regulation in mouse mammary carcinoma and liver of tumor bearing mice--I. Effect of allyl-isopropylacetamide and veronal on delta-aminolevulinate synthetase, cytochrome P-450 and cytochrome oxidase. diagnostic usage,ongoing research,unassigned 1,3,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2416025&form=6&db=m Heme metabolism and turnover of cytochrome P-450 in tumor-bearing mouse livers. diagnostic usage,unassigned 3,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3802102&form=6&db=m Heme enzyme patterns in rat liver nodules and tumors. ongoing research,unassigned 3,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6548516&form=6&db=m Alterations of hepatic delta-aminolevulinic acid synthetase, heme oxygenase, microsomal cytochrome content and drug metabolism in rats bearing ascitic tumors AH 13, AH 66 and AH 414 and a 3-methylcholanthrene induced tumor. causal interaction,diagnostic usage,ongoing research,unassigned 3,1,3,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12444039&form=6&db=m Temporal and spatial patterns of ovarian gene transcription following an ovulatory dose of gonadotropin in the rat. causal interaction,therapeutic application,unassigned 3,1,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15797241&form=6&db=m Repression of 5-aminolevulinate synthase gene by the potent tumor promoter, TPA, involves multiple signal transduction pathways. ongoing research,therapeutic application,unassigned 1,1,0 2.3.1.37 Neoplasms http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27238205&form=6&db=m Microbial Synthesis of 5-Aminolevulinic Acid and Its Coproduction with Polyhydroxybutyrate. unassigned - 2.3.1.37 Obesity http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34258471&form=6&db=m Gene expression profile of peripheral blood mononuclear cells in mild to moderate obesity in dogs. causal interaction,diagnostic usage,unassigned 3,1,0 2.3.1.37 Pantothenate Kinase-Associated Neurodegeneration http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=15506716&form=6&db=m [Genetics of hereditary iron overload] causal interaction,unassigned 4,0 2.3.1.37 Pelger-Huet Anomaly http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3678479&form=6&db=m Impaired heme synthesis in a family with Pelger-Huët anomaly, recurrent abdominal pain attacks and impaired neutrophil motility in vitro. diagnostic usage,unassigned 1,0 2.3.1.37 Photosensitivity Disorders http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=24718052&form=6&db=m Expression of Murine 5-Aminolevulinate Synthase Variants Causes Protoporphyrin IX Accumulation and Light-Induced Mammalian Cell Death. causal interaction,diagnostic usage,ongoing research,unassigned 2,1,4,0 2.3.1.37 Polycythemia http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5777627&form=6&db=m Effect of Friend leukemia virus infection upon polycythemia and delta-aminolevulinic acid synthetase activity in nurine spleen and liver. ongoing research,unassigned 1,0 2.3.1.37 Porphyria Cutanea Tarda http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3679087&form=6&db=m Hepatic heme synthesis in a new model of experimental hemochromatosis: studies in rats fed finely divided elemental iron. causal interaction,unassigned 1,0 2.3.1.37 Porphyria Cutanea Tarda http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3872633&form=6&db=m Influence of chloroquine on the porphyrin metabolism. causal interaction,unassigned 3,0 2.3.1.37 Porphyria Cutanea Tarda http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6452153&form=6&db=m Rifampicin-induced porphyria cutanea tarda. unassigned - 2.3.1.37 Porphyria Cutanea Tarda http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22791288&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyria Cutanea Tarda http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23233556&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1296823&form=6&db=m Administration of the anesthetic isoflurane to mice: a model for acute intermittent porphyria? causal interaction,unassigned 4,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1397973&form=6&db=m Porphyrinogenic properties of the anesthetic enflurane. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3621613&form=6&db=m Clinical usefulness of cimetidine for the treatment of acute intermittent porphyria--a preliminary report. causal interaction,unassigned 1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6377248&form=6&db=m Acute intermittent porphyria: pathophysiology and treatment. causal interaction,unassigned 1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7957180&form=6&db=m Effects of mifepristone (RU-486) on heme metabolism and cytochromes P-450 in cultured chick embryo liver cells, possible implications for acute porphyria. causal interaction,unassigned 1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7957494&form=6&db=m Repression of ALA synthase by heme and zinc-mesoporphyrin in a chick embryo liver cell culture model of acute porphyria. ongoing research,unassigned 3,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=8040318&form=6&db=m Differential effects of metalloporphyrins on messenger RNA levels of delta-aminolevulinate synthase and heme oxygenase. Studies in cultured chick embryo liver cells. causal interaction,unassigned 1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10207164&form=6&db=m Motor neuropathy in porphobilinogen deaminase-deficient mice imitates the peripheral neuropathy of human acute porphyria. ongoing research,therapeutic application,unassigned 1,2,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=13949833&form=6&db=m Induction of the synthesis of delta-aminolevulinic acid synthetase in liver parenchyma cells in culture by chemical that induce acute porphyria. ongoing research,unassigned 2,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19656462&form=6&db=m Sevoflurane: its action on heme metabolism and Phase I drug metabolizing system. ongoing research,therapeutic application,unassigned 1,1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23720291&form=6&db=m Porphyrin and heme metabolism and the porphyrias. causal interaction,unassigned 4,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30726693&form=6&db=m Phase 1 Trial of an RNA Interference Therapy for Acute Intermittent Porphyria. causal interaction,ongoing research,unassigned 3,1,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30847674&form=6&db=m Genetic neuromuscular disorders: living the era of a therapeutic revolution. Part 1: peripheral neuropathies. causal interaction,therapeutic application,unassigned 1,4,0 2.3.1.37 Porphyria, Acute Intermittent http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32487371&form=6&db=m Hyperhomocysteinemia in patients with acute porphyrias: A potentially dangerous metabolic crossroad? causal interaction,unassigned 2,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3080960&form=6&db=m An immunochemical study of delta-aminolevulinate synthase and delta-aminolevulinate dehydratase in liver and erythroid cells of rat. unassigned - 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21653323&form=6&db=m ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23348515&form=6&db=m Molecular Expression and Characterization of Erythroid-Specific 5-Aminolevulinate Synthase Gain-of-Function Mutations Causing X-Linked Protoporphyria. causal interaction,unassigned 3,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=25615817&form=6&db=m X-chromosomal inactivation directly influences the phenotypic manifestation of X-linked protoporphyria. causal interaction,unassigned 3,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28118224&form=6&db=m Acute hepatic and erythropoietic porphyrias: from ALA synthases 1 and 2 to new molecular bases and treatments. causal interaction,therapeutic application,unassigned 3,3,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30454868&form=6&db=m Congenital erythropoietic porphyria and erythropoietic protoporphyria: Identification of 7 uroporphyrinogen III synthase and 20 ferrochelatase novel mutations. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30678654&form=6&db=m Molecular expression, characterization and mechanism of ALAS2 gain-of-function mutants. causal interaction,diagnostic usage,therapeutic application,unassigned 2,4,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=266732&form=6&db=m Postulated deficiency of hepatic heme and repair by hematin infusions in the "inducible" hepatic porphyrias. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=359965&form=6&db=m [Alcohol-induced changes of porphyrin metabolism (author's transl)] causal interaction,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1296823&form=6&db=m Administration of the anesthetic isoflurane to mice: a model for acute intermittent porphyria? causal interaction,unassigned 4,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=1397973&form=6&db=m Porphyrinogenic properties of the anesthetic enflurane. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=2283668&form=6&db=m Strain and sex differences in the response of mice to drugs that induce protoporphyria: role of porphyrin biosynthesis and removal. causal interaction,diagnostic usage,unassigned 1,2,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3058536&form=6&db=m Maturation of embryonic chick liver delta-aminolevulinate synthase: precursor pools and regulation by intra-cellularly produced heme. causal interaction,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3114913&form=6&db=m Role of inhibition of uroporphyrinogen decarboxylase in PCB-induced porphyria in mice. causal interaction,ongoing research,therapeutic application,unassigned 4,3,3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3621613&form=6&db=m Clinical usefulness of cimetidine for the treatment of acute intermittent porphyria--a preliminary report. causal interaction,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3662642&form=6&db=m Studies in laboratory animals to assess the safety of anti-inflammatory agents in acute porphyria. therapeutic application,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3679087&form=6&db=m Hepatic heme synthesis in a new model of experimental hemochromatosis: studies in rats fed finely divided elemental iron. causal interaction,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3872633&form=6&db=m Influence of chloroquine on the porphyrin metabolism. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=3981665&form=6&db=m The effect of tetrachlorohydroquinone on hexachlorobenzene-induced porphyria in Japanese quail. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4015737&form=6&db=m Influence of N-acetylcysteine on the hexachlorobenzene induced porphyria in rats. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4750745&form=6&db=m The effect of DL-propranolol on delta-aminolevulinic acid synthetase activity and urinary excretion of porphyrins in allylisopropylacetamide-induced experimental porphyria. therapeutic application,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5935350&form=6&db=m The induction in vitro of the synthesis of delta-aminolevulinic acid synthetase in chemical porphyria: a response to certain drugs, sex hormones, and foreign chemicals. ongoing research,unassigned 2,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6377248&form=6&db=m Acute intermittent porphyria: pathophysiology and treatment. causal interaction,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6452153&form=6&db=m Rifampicin-induced porphyria cutanea tarda. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6636202&form=6&db=m Studies on the porphyrinogenic action of 1,2,4-trichlorobenzene in birds. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6689267&form=6&db=m Effect of heme on allylisopropylacetamide-induced changes in heme and drug metabolism in the rhesus monkey (Macaca mulatta). unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6838217&form=6&db=m Aging-related decreases in hepatic mitochondrial and cytosolic delta-aminolevulinic acid synthase during experimental porphyria. ongoing research,unassigned 2,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10052016&form=6&db=m Retinoic acid in association with tin-metalloporphyrins influences heme metabolism in vivo in rats. causal interaction,unassigned 1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10692079&form=6&db=m Molecular aspects of the inherited porphyrias. diagnostic usage,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10729988&form=6&db=m Hematologic aspects of the porphyrias. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12369042&form=6&db=m [Nephrologists and porphyrias] causal interaction,diagnostic usage,unassigned 2,3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=12899439&form=6&db=m Acute porphyrias in the Argentinean population: a review. causal interaction,unassigned 4,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19656462&form=6&db=m Sevoflurane: its action on heme metabolism and Phase I drug metabolizing system. ongoing research,therapeutic application,unassigned 1,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21653323&form=6&db=m ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=21889565&form=6&db=m How porphyrinogenic drugs modeling acute porphyria impair the hormonal status that regulates glucose metabolism. Their relevance in the onset of this disease. causal interaction,unassigned 2,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22791288&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23105256&form=6&db=m Antagonistic effect of FePP on the ethanol mediated induction of hepatic, renal and splenic ?-amino levulinic acid synthase activityin vivo in rats. unassigned - 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23233556&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30391163&form=6&db=m Strong correlation of ferrochelatase enzymatic activity with Mitoferrin-1 mRNA in lymphoblasts of patients with protoporphyria. ongoing research,unassigned 4,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30678654&form=6&db=m Molecular expression, characterization and mechanism of ALAS2 gain-of-function mutants. causal interaction,diagnostic usage,therapeutic application,unassigned 2,4,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30726693&form=6&db=m Phase 1 Trial of an RNA Interference Therapy for Acute Intermittent Porphyria. causal interaction,ongoing research,unassigned 3,1,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30847674&form=6&db=m Genetic neuromuscular disorders: living the era of a therapeutic revolution. Part 1: peripheral neuropathies. causal interaction,therapeutic application,unassigned 1,4,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32499479&form=6&db=m Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release. causal interaction,therapeutic application,unassigned 4,4,0 2.3.1.37 Porphyrias http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33199206&form=6&db=m 5-Aminolevulinate dehydratase porphyria: Update on hepatic 5-aminolevulinic acid synthase induction and long-term response to hemin. causal interaction,diagnostic usage,ongoing research,unassigned 1,3,4,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=359965&form=6&db=m [Alcohol-induced changes of porphyrin metabolism (author's transl)] causal interaction,unassigned 3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=708789&form=6&db=m Effects of antihypertensive drugs on hepatic heme biosynthesis, and evaluation of ferrochelatase inhibitors to simplify testing of drugs for heme pathway induction. diagnostic usage,unassigned 2,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=4026834&form=6&db=m The effect of metalloporphyrins and heme liposomes on delta-aminolevulinate synthase activity in rat liver. unassigned - 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6800821&form=6&db=m Abnormal haem biosynthesis in chronic alcoholics. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=6870916&form=6&db=m Effect of hexachlorobenzene on the activities of hepatic alcohol metabolizing enzymes. unassigned - 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7252241&form=6&db=m Treatment of the porphyrias: mechanisms of action. causal interaction,therapeutic application,unassigned 4,4,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7426253&form=6&db=m Screening of certain anaesthetic agents for their ability to elicit acute porphyric phases in susceptible patients. unassigned - 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10787385&form=6&db=m Alcohol and porphyrin metabolism. causal interaction,diagnostic usage,unassigned 3,1,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=11343251&form=6&db=m Zinc mesoporphyrin represses induced hepatic 5-aminolevulinic acid synthase and reduces heme oxygenase activity in a mouse model of acute hepatic porphyria. ongoing research,unassigned 2,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22791288&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23233556&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23720291&form=6&db=m Porphyrin and heme metabolism and the porphyrias. causal interaction,unassigned 4,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28118224&form=6&db=m Acute hepatic and erythropoietic porphyrias: from ALA synthases 1 and 2 to new molecular bases and treatments. causal interaction,therapeutic application,unassigned 3,3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30737140&form=6&db=m Regulation and tissue-specific expression of ?-aminolevulinic acid synthases in non-syndromic sideroblastic anemias and porphyrias. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31443750&form=6&db=m Hypothesis: Metabolic targeting of 5-aminolevulinate synthase by tryptophan and inhibitors of heme utilisation by tryptophan 2,3-dioxygenase as potential therapies of acute hepatic porphyrias. causal interaction,ongoing research,therapeutic application,unassigned 1,2,3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=32521132&form=6&db=m Phase 3 Trial of RNAi Therapeutic Givosiran for Acute Intermittent Porphyria. causal interaction,unassigned 3,0 2.3.1.37 Porphyrias, Hepatic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=34510420&form=6&db=m A Drug-Drug Interaction Study Evaluating the Effect of Givosiran, a Small Interfering Ribonucleic Acid (siRNA), on Cytochrome P450 Activity in Liver. causal interaction,therapeutic application,unassigned 3,4,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5577033&form=6&db=m Hepatic and erythropoietic protoporphyria. Delta-aminolevulinic acid synthetase, fluorescence, and microfluorospectrophotometric study. ongoing research,unassigned 3,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=22791288&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23233556&form=6&db=m The porphyrias: advances in diagnosis and treatment. causal interaction,unassigned 3,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=23364466&form=6&db=m Loss-of-Function Ferrochelatase and Gain-of-Function Erythroid 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. causal interaction,unassigned 4,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27346685&form=6&db=m Exome Genotyping Identifies Pleiotropic Variants Associated with Red Blood Cell Traits. causal interaction,unassigned 4,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=30454868&form=6&db=m Congenital erythropoietic porphyria and erythropoietic protoporphyria: Identification of 7 uroporphyrinogen III synthase and 20 ferrochelatase novel mutations. causal interaction,therapeutic application,unassigned 4,1,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31076252&form=6&db=m Delta-aminolevulinic acid synthase 2 expression in combination with iron as modifiers of disease severity in erythropoietic protoporphyria. causal interaction,diagnostic usage,therapeutic application,unassigned 3,2,1,0 2.3.1.37 Protoporphyria, Erythropoietic http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=33596641&form=6&db=m A mutation in the iron-responsive element of ALAS2 is a modifier of disease severity in a patient suffering from CLPX associated erythropoietic protoporphyria. causal interaction,unassigned 3,0 2.3.1.37 Starvation http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=188376&form=6&db=m Studies on heme synthesis in the rat adrenal. unassigned - 2.3.1.37 Virus Diseases http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=5777627&form=6&db=m Effect of Friend leukemia virus infection upon polycythemia and delta-aminolevulinic acid synthetase activity in nurine spleen and liver. ongoing research,unassigned 1,0 2.3.1.37 Vitamin B 6 Deficiency http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=7275938&form=6&db=m Mechanism of thiamine-induced respiratory deficiency in Saccharomyces carlsbergensis. causal interaction,unassigned 4,0