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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

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

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

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

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

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

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

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

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

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

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

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

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

William Herdman Elliott 1925–2012

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

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

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

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

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

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

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

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

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