Regulation of 5-aminolevulinate synthase mRNA in different rat tissues.

DNA sequencing with chain-terminating inhibitors

Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572 · see citing works

A simple and very efficient method for generating cDNA libraries

Gubler, U., & Hoffman, B. J. (1983) · Gene · doi:10.1016/0378-1119(83)90230-5 · Cited by 4,461 · see citing works

The Induction in Vitro of the Synthesis of δ-Aminolevulinic Acid Synthetase in Chemical Porphyria: A Response to Certain Drugs, Sex Hormones, and Foreign Chemicals

Granick, S. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96783-9 · Cited by 765 · see citing works

Analysis of transcriptional regulatory signals of the HSV thymidine kinase gene: Identification of an upstream control region

McKnight, S. L., Gavis, E. R., Kingsbury, R., & Axel, R. (1981) · Cell · doi:10.1016/0092-8674(81)90057-x · Cited by 600 · see citing works

Two promoters of different strengths control the transcription of the mouse alpha-amylase gene Amy-1a in the parotid gland and the liver

Schibler, U., Hagenbüchle, O., Wellauer, P. K., & Pittet, A. C. (1983) · Cell · doi:10.1016/0092-8674(83)90431-2 · Cited by 450 · see citing works

CYTOMORPHOMETRY OF DEVELOPING RAT LIVER AND ITS APPLICATION TO ENZYMIC DIFFERENTIATION

Greengard, O., Federman, M., & Knox, W. E. (1972) · The Journal of Cell Biology · doi:10.1083/jcb.52.2.261 · Cited by 317 · see citing works

Glucocorticoid-mediated induction of alpha 1-acid glycoprotein: evidence for hormone-regulated RNA processing.

Vannice, J. L., Taylor, J. M., & RINGOLD, G. M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.14.4241 · Cited by 204 · see citing works

5′ end of hmg CoA reductase gene contains sequences responsible for cholesterol-mediated inhibition of transcription

Osborne, T. F., Goldstein, J. L., & BROWN, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80116-1 · Cited by 181 · see citing works

New Developments in the Regulation of Heme Metabolism and Their Implications

Maines, M. D., & Snyder, R. (1984) · Critical Reviews in Toxicology · doi:10.3109/10408448409021604 · Cited by 144 · see citing works

Nucleotide sequence of mouse 5-aminolevulinic acid synthase cDNA and expression of its gene in hepatic and erythroid tissues

Schoenhaut, D. S., & Curtis, P. J. (1986) · Gene · doi:10.1016/0378-1119(86)90351-3 · Cited by 84 · see citing works

Biological detection of specific mRNA molecules by microinjection.

Liu, C. P., Slate, D. L., Gravel, R. A., & Ruddle, F. H. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4503 · Cited by 78 · see citing works

Isolation of recombinant cDNAs encoding chicken erythroid delta-aminolevulinate synthase.

Yamamoto, M., Yew, N. S., Federspiel, M. J., Dodgson, J. B., Hayashi, N., & Engel, J. D. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.11.3702 · Cited by 71 · see citing works

Complete nucleotide sequence of hepatic 5-aminolaevulinate synthase precursor

Borthwick, I. A., Srivastava, G., Day, A., Pirola, B. A., Snoswell, M. A., May, B. K., & Elliott, W. H. (1985) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1985.tb09047.x · Cited by 70 · see citing works

Control of 5-Aminolevulinate Synthase in Animals

May, B. K., Borthwick, I. A., Srivastava, G., Pirola, B. A., & Elliott, W. H. (1986) · Current topics in cellular regulation · doi:10.1016/b978-0-12-152828-7.50008-1 · Cited by 69 · see citing works

Nudeotide sequence of the chicken 5-aminolevulinate synthase gene

Maguire, D. J., Day, A., Borthwick, I. A., Srivastava, G., Wigley, P. L., May, B. K., & Elliott, W. H. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.3.1379 · Cited by 63 · see citing works

Transcription of the β-like globin genes and pseudogenes of the goat in a cell-free system

Luse, D. S., Haynes, J. R., VanLeeuwen, D., Schon, E. A., Cleary, M. L., Shapiro, S. G., Lingrel, J. B., & Roeder, R. G. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.17.4339 · Cited by 61 · see citing works

Regulation of cytochrome P-45011 beta gene expression by adrenocorticotropin.

John, M. E., John, M. C., Simpson, E. R., & Waterman, M. R. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89087-1 · Cited by 59 · see citing works

Evidence for erythroid and nonerythroid forms of δ-aminolevulinate synthetase

Bishop, D. F., Kitchen, H., & Wood, W. A. (1981) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(81)90105-3 · Cited by 56 · see citing works

Synthesis of δ‐Aminolaevulinate Synthase in vitro Using Hepatic mRNA from Chick Embryos with Induced Porphyria

Brooker, J. D., May, B. K., & Elliott, W. H. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb05992.x · Cited by 53 · see citing works

δ-Aminolevulinate synthase isozymes in the liver and erythroid cells of chicken

Watanabe, N., Hayashi, N., & Kikuchi, G. (1983) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(83)91737-0 · Cited by 44 · see citing works

Haem control in experimental porphyria. The effect of haemin on the induction of δ-aminolaevulinate synthase in isolated chick-embryo liver cells

Srivastava, G., Brooker, J. D., May, B. K., & Elliott, W. H. (1980) · Biochemical Journal · doi:10.1042/bj1880781 · Cited by 40 · see citing works

Porphyrogenic effects and induction of heme oxygenase in vivo by δ-aminolevulinic acid

Andersson, K., Drummond, G. R., Freddara, U., Sardana, M. K., & Sassa, S. (1981) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(81)90162-8 · Cited by 31 · see citing works

Human argininosuccinate synthetase minigenes are subject to arginine-mediated repression but not to trans induction.

Boyce, F. M., Anderson, G. M., Rusk, C. D., & Freytag, S. O. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.4.1244 · Cited by 23 · see citing works

Purification of rat liver mitochondrial δ-aminolaevulinate synthase

Srivastava, G., Borthwick, I. A., Brooker, J. D., May, B. K., & Elliott, W. H. (1982) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(82)91721-1 · Cited by 22 · see citing works

A unique gene for 5-aminolevulinate synthase in chickens. Evidence for expression of an identical messenger RNA in hepatic and erythroid tissues.

Elferink, C. J., Srivastava, G., Maguire, D. J., Borthwick, I. A., May, B. K., & Elliott, W. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61300-6 · Cited by 21 · see citing works

Molecular cloning of hepatic 5‐aminolevulinate synthase

Borthwick, I. A., Srivastava, G., Hobbs, A. A., Pirola, B. A., Brooker, J. D., May, B. K., & Elliott, W. H. (1984) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1984.tb08435.x · Cited by 13 · see citing works

The phycobilisome, a light-harvesting complex responsive to environmental conditions

Grossman, A. R., Schaefer, M. R., Chiang, G. G., & Collier, J. L. (1993) · Microbiological Reviews · doi:10.1128/mr.57.3.725-749.1993 · Cited by 651 · see citing works

Tissue-Specific Regulation of Iron Metabolism and Heme Synthesis: Distinct Control Mechanisms in Erythroid Cells

Ponka, P. (1997) · Blood · doi:10.1182/blood.v89.1.1 · Cited by 544 · see citing works

Biosynthesis of heme in mammals

Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493 · see citing works

Human erythroid 5‐aminolevulinate synthase: promoter analysis and identification of an iron‐responsive element in the mRNA.

Cox, T. C., Bawden, M. J., Martin, A., & May, B. K. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07715.x · Cited by 360 · see citing works

Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: leader peptides cleaved by two matrix proteases share a three-amino acid motif.

Hendrick, J. P., Hodges, P. E., & Rosenberg, L. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.11.4056 · Cited by 305 · see citing works

LIGHT-HARVESTING COMPLEXES IN OXYGENIC PHOTOSYNTHESIS: Diversity, Control, and Evolution

Grossman, A. R., Bhaya, D., Apt, K. E., & Kehoe, D. M. (1995) · Annual Review of Genetics · doi:10.1146/annurev.ge.29.120195.001311 · Cited by 291 · see citing works

Aminolevulinic Acid (ALA) as a Prodrug in Photodynamic Therapy of Cancer

Wachowska, M., Muchowicz, A., Firczuk, M., Gabrysiak, M., Winiarska, M., Wańczyk, M., Bojarczuk, K., & Golab, J. (2011) · Molecules · doi:10.3390/molecules16054140 · Cited by 265 · see citing works

Transcriptional Activation of the Heme Oxygenase Gene by Heme and Cadmium in Mouse Hepatoma Cells

Alam, J., Shibahara, S., & Smith, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83358-0 · Cited by 226 · see citing works

Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long-chain base component of sphingolipids

Buede, R., Rinker-Schaeffer, C. W., Pinto, W. J., Lester, R. L., & Dickson, R. C. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.14.4325-4332.1991 · Cited by 190 · see citing works

Human δ-aminolevulinate synthase: Assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome

Bishop, D. F., Henderson, A. S., & Astrin, K. H. (1990) · Genomics · doi:10.1016/0888-7543(90)90542-3 · Cited by 166 · see citing works

Enzymatic defect in "X-linked" sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency.

Cotter, P. D., Baumann, M., & Bishop, D. F. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.9.4028 · Cited by 157 · see citing works

Molecular Regulation of Heme Biosynthesis in Higher Vertebrates

May, B. K., Dogra, S. C., Sadlon, T., Bhasker, C. R., Cox, T. C., & Bottomley, S. S. (1995) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(08)60875-2 · Cited by 148 · see citing works

Lon Peptidase 1 (LONP1)-dependent Breakdown of Mitochondrial 5-Aminolevulinic Acid Synthase Protein by Heme in Human Liver Cells

Tian, Q., Li, T., Hou, W., Zheng, J., Schrum, L. W., & Bonkovsky, H. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.215772 · Cited by 134 · see citing works

Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription

Hamilton, J. W., Bement, W. J., Sinclair, P. R., Sinclair, J. F., Alcedo, J., & Wetterhahn, K. E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90428-l · Cited by 114 · see citing works

Identification of the xenosensors regulating human 5-aminolevulinate synthase

Podvinec, M., Handschin, C., Looser, R., & Meyer, U. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401845101 · Cited by 107 · see citing works

Regulation of cytochrome P-450b/e and P-450p gene expression by growth hormone in adult rat hepatocytes cultured on a reconstituted basement membrane.

Schuetz, E. G., Schuetz, J. D., May, B. K., & Guzelian, P. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40176-2 · Cited by 106 · see citing works

X-linked sideroblastic anemia: identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley

Cotter, P., Rucknagel, D., & Bishop, D. (1994) · Blood · doi:10.1182/blood.v84.11.3915.bloodjournal84113915 · Cited by 98 · see citing works

5-Aminolevulinate synthase and the first step of heme biosynthesis

Ferreira, G. C., & Gong, J. (1995) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110030 · Cited by 90 · see citing works

Cytochrome P450 regulation: the interplay between its heme and apoprotein moieties in synthesis, assembly, repair, and disposal

Correia, M. A., Sinclair, P. R., & Matteis, F. D. (2010) · Drug Metabolism Reviews · doi:10.3109/03602532.2010.515222 · Cited by 88 · see citing works

Erythroid 5-aminolevulinate synthase is located on the X chromosome.

Cox, T. C., Bawden, M. J., Abraham, N. G., Bottomley, S. S., May, B. K., Baker, E. G., Chen, L. Z., & Sutherland, G. R. (1990) · Europe PMC (PubMed Central) · Cited by 86 · see citing works

The molecular biology and pyridoxine responsiveness of X-linked sideroblastic anaemia.

May, A. M., & Bishop, D. F. (1998) · PubMed · Cited by 84 · see citing works

Identification of regulatory sequences in the gene for 5-aminolevulinate synthase from rat.

Braidotti, G., Borthwick, I. A., & May, B. K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54048-5 · Cited by 84 · see citing works

Erythroleukemia differentiation. Distinctive responses of the erythroid-specific and the nonspecific delta-aminolevulinate synthase mRNA.

Fujita, H., Yamamoto, M. P., Yamagami, T., Hayashi, N., & Sassa, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47399-7 · Cited by 81 · see citing works

Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells

Alam, J., & Smith, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84616-1 · Cited by 80 · see citing works

Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemia

Bottomley, S. S., May, B. K., Cox, T. C., Cotter, P. D., & Bishop, D. F. (1995) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf02110031 · Cited by 78 · see citing works

Expression of 5-aminolaevulinate synthase and cytochrome P-450 mRNAs in chicken embryo hepatocytes in vivo and in culture. Effect of porphyrinogenic drugs and haem

Hamilton, J. W., Bement, W. J., Sinclair, P. R., Sinclair, J. F., & Wetterhahn, K. E. (1989) · Biochemical Journal · doi:10.1042/bj2570936 · Cited by 77 · see citing works

Heme-hemopexin-mediated induction of metallothionein gene expression.

Alam, J., & Smith, A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42013-3 · Cited by 76 · see citing works

Cerebroprotective Functions of HO-2

Parfenova, H., & Leffler, C. W. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208783597380 · Cited by 75 · see citing works

Cloning and characterization of the hemA region of the Bacillus subtilis chromosome

Petricek, M., Rutberg, L., Schröder, I., & Hederstedt, L. (1990) · Journal of Bacteriology · doi:10.1128/jb.172.5.2250-2258.1990 · Cited by 75 · see citing works

Heme biosynthesis in mammalian systems: Evidence of a schiff base linkage between the pyridoxal 5′‐phosphate cofactor and a lysine residue in 5‐aminolevulinate synthase

Ferreira, G. C., Neame, P. J., & Dailey, H. A. (1993) · Protein Science · doi:10.1002/pro.5560021117 · Cited by 72 · see citing works

Limited heme synthesis in porphobilinogen deaminase‐deficient mice impairs transcriptional activation of specific cytochrome P450 genes by phenobarbital

Jover, R., Hoffmann, F., Scheffler‐Koch, V., & Lindberg, R. L. P. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01815.x · Cited by 60 · see citing works

The heme synthesis-export system regulates the tricarboxylic acid cycle flux and oxidative phosphorylation

Fiorito, V., Allocco, A. L., Petrillo, S., Gazzano, E., Torretta, S., Marchi, S., Destefanis, F., Pacelli, C., Audrito, V., Provero, P., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109252 · Cited by 55 · see citing works

Transcriptional regulation of the tartrate-resistant acid phosphatase (TRAP) gene by iron

Alcantara, O., Reddy, S. V., Roodman, G. D., & Boldt, D. H. (1994) · Biochemical Journal · doi:10.1042/bj2980421 · Cited by 55 · see citing works

Synergistic effect of 2,2',4,4',5,5'-hexachlorobiphenyl and 2,3,7,8-tetrachlorodibenzo-p-dioxin on hepatic porphyrin levels in the rat.

van Birgelen, A. P. J. M., Fase, K. M., van der Kolk, J., Poiger, H., Brouwer, A., Seinen, W., & van den Berg, M. (1996) · Environmental Health Perspectives · doi:10.1289/ehp.96104550 · Cited by 54 · see citing works

Cytochrome P450 and its interactions with the heme biosynthetic pathway

Matteis, F. D., & Marks, G. S. (1996) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/cjpp-74-1-1 · Cited by 53 · see citing works

Regional assignment of the human uroporphyrinogen III synthase (UROS) gene to chromosome 10q25.2?q26.3

Astrin, K. H., Warner, C. A., Yoo, H., Goodfellow, P. J., Tsai, S., & Desnick, R. J. (1991) · Human Genetics · doi:10.1007/bf01213085 · Cited by 52 · see citing works

Isolation and nucleotide sequence of the hemA gene of Escherichia coli K12

Drolet, M., Péloquin, L., Echelard, Y., Cousineau, L., & Sasarman, A. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00334375 · Cited by 52 · see citing works

Chromatic adaptation and the events involved in phycobilisome biosynthesis

Grossman, A. R. (1990) · Plant Cell & Environment · doi:10.1111/j.1365-3040.1990.tb01081.x · Cited by 51 · see citing works

Sequence of a Chicken Phenobarbital-Inducible Cytochrome P450 cDNA: Regulation of Two P450 mRNAs Transcribed from Different Genes

Hansen, A. J., & May, B. K. (1989) · DNA · doi:10.1089/dna.1.1989.8.179 · Cited by 49 · see citing works

5-Aminolevulinate synthase mRNA levels in the Harderian gland of Syrian hamsters: Correlation with porphyrin concentrations and regulation by androgens and melatonin

Menéndez-Peláez, A., Rodrı́guez, C., & Dominguez, P. A. (1991) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(91)90154-k · Cited by 49 · see citing works

Heme production in animal tissues: The regulation of biogenesis of δ-aminolevulinate synthase

Ades, I. Z. (1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90032-x · Cited by 48 · see citing works

Synthesis, delivery and regulation of eukaryotic heme and Fe–S cluster cofactors

Barupala, D., Dzul, S. P., Riggs-Gelasco, P. J., & Stemmler, T. L. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.01.010 · Cited by 46 · see citing works

Structure of a mouse erythroid 5-aminolevulinate synthase gene and mapping of erythroid-specific DNAse I hypersensitive sites

Schoenhaut, D. S., & Curtis, P. J. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.17.7013 · Cited by 46 · see citing works

MPTP selectively induces haem oxygenase‐1 expression in striatal astrocytes

Fernandez‐Gonzalez, A., Pérez‐Otaño, I., & Morgan, J. I. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00044.x · Cited by 43 · see citing works

5'-Aminolevulinate synthase activity is decreased in skeletal muscle of anemic rats

McNabney, L. A., & Essig, D. A. (1992) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1992.263.2.c429 · Cited by 43 · see citing works

The inhibition of the iron responsive element RNA-protein interaction by heme does not mimic in vivo iron regulation.

Haile, D. J., Rouault, T. A., Harford, J. B., & Klausner, R. D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38227-4 · Cited by 42 · see citing works

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release

Bailey, H., Bezerra, G. A., Marcero, J. R., Padhi, S., Foster, W. R., Rembeza, E., Roy, A., Bishop, D. F., Desnick, R. J., Bulusu, G., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16586-x · Cited by 41 · see citing works

Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin

Zheng, J., Shan, Y., Lambrecht, R. W., Donohue, S. E., & Bonkovsky, H. L. (2008) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-008-9888-0 · Cited by 40 · see citing works

Mitochondrial Biogenesis in Striated Muscle

Hood, D. A., Balaban, A., Connor, M. K., Craig, E. E., Nishio, M. L., Rezvani, M., & Takahashi, M. T. (1994) · Canadian Journal of Applied Physiology · doi:10.1139/h94-002 · Cited by 39 · see citing works

Haem repression of the housekeeping 5-aminolaevulinic acid synthase gene in the hepatoma cell line LMH

Kolluri, S., Sadlon, T. J., May, B. K., & Bonkovsky, H. L. (2005) · Biochemical Journal · doi:10.1042/bj20050354 · Cited by 37 · see citing works

Nuclear Receptor 5A (NR5A) Family Regulates 5-Aminolevulinic Acid Synthase 1 (ALAS1) Gene Expression in Steroidogenic Cells

Ju, Y., Mizutani, T., Imamichi, Y., Yazawa, T., Matsumura, T., Kawabe, S., Kanno, M., Umezawa, A., Kangawa, K., & Miyamoto, K. (2012) · Endocrinology · doi:10.1210/en.2012-1334 · Cited by 35 · see citing works

Divergent effects of cycloheximide on the induction of Class II and Class III cytochrome P450 mRNAs in cultures of adult rat hepatocytes

Burger, H.-J., Schuetz, E. G., Schuetz, J. D., & Guzelian, P. S. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90433-y · Cited by 35 · see citing works

Indispensable function for embryogenesis, expression and regulation of the nonspecific form of the 5‐aminolevulinate synthase gene in mouse

Okano, S., Zhou, L., Kusaka, T., Shibata, K., Shimizu, K., Gao, X., Kikuchi, Y., Togashi, Y., Hosoya, T., Takahashi, S., et al. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01366.x · Cited by 33 · see citing works

Expression of c-myc and c-fms oncogenes in trophoblastic cells in hydatidiform mole and normal human placenta.

Cheung, A., Srivastava, G., Pittaluga, S., Man, T., Ngan, H., & Collins, R. J. (1993) · Journal of Clinical Pathology · doi:10.1136/jcp.46.3.204 · Cited by 34 · see citing works

Heme metabolism in nonerythroid cells

Dunaway, L. S., Loeb, S. A., Petrillo, S., Tolosano, E., & Isakson, B. E. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107132 · Cited by 33 · see citing works

Cloning and sequencing of some genes responsible for porphyrin biosynthesis from the anaerobic bacterium Clostridium josui

Fujino, E., Fujino, T., Karita, S., Sakka, K., & Ohmiya, K. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.17.5169-5175.1995 · Cited by 32 · see citing works

Regulation of the genes for heme pathway enzymes in erythroid and in non‐erythroid cells

Sassa, S. (1990) · The International Journal Of Cell Cloning · doi:10.1002/stem.5530080104 · Cited by 33 · see citing works

Heme regulates expression of phycobiliprotein photogenes in the unicellular rhodophyte, Cyanidium caldarium

Troxler, R. F., Lin, S., & Offner, G. D. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47104-4 · Cited by 33 · see citing works

Role of heme in phenobarbital induction of cytochromes P450 and 5-aminolevulinate synthase in cultured rat hepatocytes maintained on an extracellular matrix

Sinclair, P. R., Schuetz, E. G., Bement, W. J., Haugen, S. A., Sinclair, J. F., May, B. K., Li, D., & Guzelian, P. S. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90133-j · Cited by 33 · see citing works

Structure and Regulated Expression of the δ-Aminolevulinate Synthase Gene from Drosophila melanogaster

de Mena, I. R., Fernández‐Moreno, M. Á., Bornstein, B., Kaguni, L. S., & Garesse, R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37321 · Cited by 32 · see citing works

Porphyrin accumulation in the harderian glands of female Syrian hamster results in mitochondrial damage and cell death

Antolı́n, I., Urı́a, H., Tolivia, D., Rodríguez‐Colunga, M. J., Rodrı́guez, C., Kotler, M. L., & Menéndez-Peláez, A. (1994) · The Anatomical Record · doi:10.1002/ar.1092390402 · Cited by 31 · see citing works

Heme binding by a bacterial repressor protein, the gene product of the ferric uptake regulation (fur) gene ofEscherichia coli

Smith, A., Hooper, N. I., Shipulina, N., & Morgan, W. T. (1996) · Journal of Protein Chemistry · doi:10.1007/bf01908539 · Cited by 30 · see citing works

Hypoxic Induction of Human Erythroid-Specific δ-Aminolevulinate Synthase Mediated by Hypoxia-Inducible Factor 1

Zhang, F., Shen, G., Liu, X., Wang, F., Zhao, H.-L., Yu, J., & Zhang, J. (2011) · Biochemistry · doi:10.1021/bi101585c · Cited by 28 · see citing works

Effects of Metals on Gene Expression

Koropatnick, J. D., & Leibbrandt, M. E. I. (1995) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-79162-8_5 · Cited by 29 · see citing works

Regulation of 5-aminolevulinate synthase in mouse erythroleukemic cells is different from that in liver.

Elferink, C. J., Sassa, S., & May, B. K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37664-6 · Cited by 28 · see citing works

High penetrance of acute intermittent porphyria in a Spanish founder mutation population and CYP2D6 genotype as a susceptibility factor

Barreda‐Sánchez, M., Buendía-Martínez, J., Glover-López, G., Carazo-Díaz, C., Ballesta‐Martínez, M. J., López‐González, V., Sánchez-Soler, M. J., Rodríguez-Peña, L., Serrano-Antón, A. T., Gil-Ferrer, R., et al. (2019) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-019-1031-7 · Cited by 27 · see citing works

Identification of an arginine452 to histidine substitution in the erythroid 5‐aminolaevulinate synthetase gene in a large pedigree with X‐linked hereditary sideroblastic anaemia

Edgar, A. J., Losowsky, M. S., Noble, J. S., & Wickramasinghe, S. N. (1997) · European Journal Of Haematology · doi:10.1111/j.1600-0609.1997.tb01402.x · Cited by 26 · see citing works

Mitochondrial actaptations to chronic muscle use: Effect of iron deficiency

Hood, D. A., Kelton, R., & Nismo, M. L. (1992) · Comparative Biochemistry and Physiology Part A Physiology · doi:10.1016/0300-9629(92)90514-q · Cited by 25 · see citing works

Alternative splicing and tissue-specific transcription of human and rodent ubiquitous 5-aminolevulinate synthase (ALAS1) genes

Roberts, A., & Elder, G. H. (2001) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(01)00187-7 · Cited by 22 · see citing works

δ-Aminolaevulinate synthase expression in muscle after contractions and recovery

Takahashi, M., McCurdy, D. T., Essig, D. A., & Hood, D. A. (1993) · Biochemical Journal · doi:10.1042/bj2910219 · Cited by 22 · see citing works

Sex-related differences and thyroid hormone regulation of vasoactive intestinal peptide gene expression in the rat brain and pituitary

Lam, K. S. L., & Srivastava, G. (1990) · Brain Research · doi:10.1016/0006-8993(90)90259-e · Cited by 21 · see citing works

Androgen regulation of gene expression in the Syrian hamster Harderian gland

Dominguez, P. A., Antolı́n, I., Boga, J. A., Urı́a, H., & Menéndez-Peláez, A. (1994) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(94)90189-9 · Cited by 20 · see citing works

Heme may not be a positive regulator of cytochrome‐P450 gene expression

Srivastava, G., Bawden, M. J., Hansen, A. J., & May, B. K. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14499.x · Cited by 18 · see citing works

Cloning and nucleotide sequence of the hemA gene of Agrobacterium radiobacter

Drolet, M., & Sasarman, A. (1991) · Molecular and General Genetics MGG · doi:10.1007/bf00273610 · Cited by 18 · see citing works

An alternatively‐spliced exon in the 5′‐UTR of human ALAS1 mRNA inhibits translation and renders it resistant to haem‐mediated decay

Roberts, A., Redding, S. J., & Llewellyn, D. H. (2005) · FEBS Letters · doi:10.1016/j.febslet.2004.12.080 · Cited by 16 · see citing works

Effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on heme oxygenase-1, biliverdin IXα reductase and δ-aminolevulinic acid synthetase 1 in rats with wild-type or variant AH receptor

Niittynen, M., Tuomisto, J. T., & Pohjanvirta, R. (2008) · Toxicology · doi:10.1016/j.tox.2008.06.014 · Cited by 15 · see citing works

Age and food restriction alter the porphyrin concentration and mRNA levels for 5-aminolevulinate synthase in rat harderian gland

Rodrı́guez, C., Menéndez-Peláez, A., Howes, K. A., & Reiter, R. J. (1992) · Life Sciences · doi:10.1016/0024-3205(92)90041-m · Cited by 15 · see citing works

Drug induction of P450IIB1/IIB2 and 5-aminolevulinate synthase mRNAs in rat tissues

Srivastava, G., Bawden, M. J., Anderson, A., & May, B. K. (1989) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(89)90038-9 · Cited by 13 · see citing works

An examination of the immune system of the duck (Anas platyrhynchos) for factors resembling some defined mammalian cytokines

Higgins, D. A., Cromie, R., Srivastava, G., Herzbeck, H., Schlüter, C., Gerdes, J., Diamantstein, T., & Flad, H.-D. (1993) · Developmental & Comparative Immunology · doi:10.1016/0145-305x(93)90006-c · Cited by 13 · see citing works

Gender-associated differences in the development of 5-aminolevulinate synthase gene expression in the Harderian gland of Syrian hamsters

Rodrı́guez, C., Menéndez-Peláez, A., Vaughan, M. K., & Reiter, R. J. (1993) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(93)90120-9 · Cited by 11 · see citing works

Classification of likely functional class for ligand binding sites identified from fragment screening

Utgés, J. S., MacGowan, S. A., Ives, C. M., & Barton, G. J. (2024) · Communications Biology · doi:10.1038/s42003-024-05970-8 · Cited by 10 · see citing works

Tissue‐specific expression of ALA synthase‐1 and heme oxygenase‐1 and their expression in livers of rats chronically exposed to ethanol

Zheng, J., Tian, Q., Hou, W., Watts, J. A., Schrum, L. W., & Bonkovsky, H. L. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.047 · Cited by 9 · see citing works

Evidence That Protein Kinase C Is Involved in δ-Aminolevulinate Synthase Expression in Rat Hepatocytes

Varone, C. L., & Cánepa, E. T. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.9978 · Cited by 9 · see citing works

A reversible feedback mechanism regulating mitochondrial heme synthesis

Chitrakar, I., Roberson, A. B., Ayres-Galhardo, P. H., & Brown, B. L. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111089 · Cited by 7 · see citing works

Elevation of δ-aminolevulinic acid synthase and cytochrome PB1 P450 messenger RNA levels by dihydropyridines, dihydroquinolines, sydnones, and N-ethylprotoporphyrin IX

Mackie, J. E., Back, D. W., Hamilton, J. W., & Marks, G. S. (1991) · Biochemical Pharmacology · doi:10.1016/0006-2952(91)90308-r · Cited by 7 · see citing works

Induction of cytochrome P-450 RNA by porphyrogenic agents: On the nature of the coordinate induction with δ-aminolevulinate synthase in tissues of the chicken embryo

Drew, P. D., & Ades, I. Z. (1990) · International Journal of Biochemistry · doi:10.1016/0020-711x(90)90036-3 · Cited by 7 · see citing works

Effect of dexamethasone on mRNA levels for 5‐aminolevulinate synthase in different rat tissues

Srivastava, G., KWONG, S. K. Y., Lam, K. S. L., & May, B. K. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb19827.x · Cited by 7 · see citing works

cAMP regulation of phenobarbital-mediated induction of δ-aminolevulinate synthase mRNA in hepatocytes from normal and experimental diabetic rats

Varone, C. L., Cánepa, E. T., Llambías, E. B. C., & Grinstein, M. (1994) · Biochemistry and Cell Biology · doi:10.1139/o94-051 · Cited by 7 · see citing works

Induction of 5-aminolevulinate synthase by activators of steroid biosynthesis

Martini, C. N., Romero, D. G., Yanes, L. L., & Vila, M. D. C. (2007) · Life Sciences · doi:10.1016/j.lfs.2007.04.020 · Cited by 6 · see citing works

Regulation of the aminolevulinate synthase gene in the Syrian hamster Harderian gland: Changes during development and circadian rhythm and role of some hormones

Rodrı́guez, C., Kotler, M. L., Antolı́n, I., Sainz, R. M., & Menéndez-Peláez, A. (1996) · Microscopy Research and Technique · doi:10.1002/(sici)1097-0029(19960501)34:1 · Cited by 6 · see citing works

EFFECT OF HAEM ON CYTOCHROME P‐450 SYNTHESIS

May, B. K., & Hansen, A. J. (1989) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/j.1440-1681.1989.tb01594.x · Cited by 6 · see citing works

Regulation of biogenesis of liver δ-aminolevulinate synthase: Effects of structural modifications of heme on the enzyme's rna

Lorber, B. J., & Ades, I. Z. (1989) · International Journal of Biochemistry · doi:10.1016/0020-711x(89)90369-8 · Cited by 5 · see citing works

Regulation of production of δ-aminolaevulinate synthase in tissues of chick embryos. Effects of porphyrogenic agents and of haem precursors

Drew, P. D., & Ades, I. Z. (1989) · Biochemical Journal · doi:10.1042/bj2620815 · Cited by 5 · see citing works

Chapter 6 Disruption of Heme Synthesis by Polyhalogenated Aromatics

Smith, A. G., & Chernova, T. (2009) · Advances in molecular toxicology · doi:10.1016/s1872-0854(09)00006-x · Cited by 4 · see citing works

Heme in the treatment of heme deficiency states

Tenhunen, R. (1990) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.1080/00365519009085802 · Cited by 4 · see citing works

N-Methyl Protoporphyrin IX: An Understudied Porphyrin

Xu, L., Qi, Q., Zhu, J., & Ma, X. (2022) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.2c00214 · Cited by 3 · see citing works

William Herdman Elliott 1925–2012

Rogers, G. E. (2013) · Historical Records of Australian Science · doi:10.1071/hr12021 · Cited by 3 · see citing works

Chapter 7 The genes of tetrapyrrole biosynthesis

Jordan, P. M., & Mgbeje, B. L. (1991) · New comprehensive biochemistry · doi:10.1016/s0167-7306(08)60114-3 · Cited by 3 · see citing works

Structure and regulation of vertebrate δ‐aminolevulinate synthases

Yamamoto, M. P., Lim, K.-C., Nagai, T., Furuyama, K., & Engel, J. D. (1994) · Stem Cells · doi:10.1002/stem.5530120705 · Cited by 3 · see citing works

Comparison of the beluga whale (Delphinapterus leucas) expressed genes for 5-aminolevulinate synthase with those in other vertebrates.

Kreiling, J., Duncan, R., Faggart, M., & Cornell, N. W. (1999) · Comparative Biochemistry and Physiology Part B Comparative Biochemistry · doi:10.1016/s0305-0491(99)00052-8 · Cited by 2 · see citing works

Structure, turnover, and heme-mediated suppression of the level of mRNA encoding rat liver delta-aminolevulinate synthase.

Yamamoto, M. P., Kure, S., Engel, J. D., & Hiraga, K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37544-6 · Cited by 112 · see citing works

Regulation of 5-aminolevulinate synthase in mouse erythroleukemic cells is different from that in liver.

Elferink, C. J., Sassa, S., & May, B. K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37664-6 · Cited by 28 · see citing works

Heme regulates hepatic 5-aminolevulinate synthase mRNA expression by decreasing mRNA half-life and not by altering its rate of transcription

Hamilton, J. W., Bement, W. J., Sinclair, P. R., Sinclair, J. F., Alcedo, J., & Wetterhahn, K. E. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90428-l · Cited by 114 · see citing works

Hepatic 5‐Aminolevulinic Acid Synthase mRNA Stability is Modulated by Inhibitors of Heme Biosynthesis and by Metalloporphyrins

Cable, E. E., Gildemeister, O. S., Pepe, J. A., Donohue, S. E., Lambrecht, R. W., & Bonkovsky, H. L. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0112h.x · Cited by 20 · see citing works

Biogenesis of embryonic chick liver δ-aminolevulinate synthase: Regulation of the level of mRNA by hemin

Ades, I. Z., Stevens, T. M., & Drew, P. D. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90182-2 · Cited by 31 · see citing works