The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
δ-Aminolevulinic Acid Synthetase
Open accessAbstract
Administration of allylisopropylacetamide to rats causes a marked increase in the hepatic ribonucleic acid-dependent synthesis of &aminolevulinic acid synthetase as evidenced by the fact that this increase is markedly inhibited by administration of actinomycin D or S-fluorouracil.The half-life of hepatic 6aminolevulinic acid synthetase following puromycin administration is 67 to 72 mm and is independent of the level of the enzyme.The administration of actinomycin D or 5-fluorouracil to rats previously treated with allylisopropylacetamide results in a rapid decline of the hepatic levels of induced b-aminolevulinic acid synthetase.This suggests that the turnover of the messenger RNA for hepatic &aminolevulinic acid synthetase is considerably more rapid than the bulk of rat liver messenger RNA.Glucose markedly inhibits induction of hepatic &aminolevulinic acid synthetase and also the increase of &amino-Ievulinic acid dehydratase produced by ahyhsopropylacetamide administration.
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Citations
Cites
DETERMINATION OF SERUM PROTEINS BY MEANS OF THE BIURET REACTION
Gornall, A. G., Bardawill, C. J., & David, M. M. (1949) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)57021-6 · Cited by 16,158
A SPECTROPHOTOMETRIC METHOD FOR MEASURING THE BREAKDOWN OF HYDROGEN PEROXIDE BY CATALASE
Beers, R. F., & Sizer, I. W. (1952) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50881-x · Cited by 6,761
Genetic regulatory mechanisms in the synthesis of proteins.
Jacob, F., & Monod, J. (1961) · Journal of Molecular Biology · doi:10.1016/s0022-2836(61)80072-7 · Cited by 5,300
INTRACELLULAR DISTRIBUTION OF ENZYMES
Schneider, W. C. (1948) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51025-5 · Cited by 1,095
The Roles of Synthesis and Degradation in the Control of Rat Liver Tryptophan Pyrrolase
Schimke, R. T., Sweeney, E. W., & Berlin, C. M. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97652-0 · Cited by 594
Granick, S., & Urata, G. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81340-0 · Cited by 430
The Importance of Both Synthesis and Degradation in the Control of Arginase Levels in Rat Liver
SCHIMKE, R. T. (1964) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91209-3 · Cited by 395
Microsomal particles and protein synthesis
Roberts, R. B. (1958) · Cited by 390
Goldberg, I. H., Rabinowitz, M., & Reich, E. (1962) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.48.12.2094 · Cited by 372
The purification and properties of δ-aminolaevulic acid dehydrase
Gibson, K. D., Neuberger, A., & Scott, J. J. (1955) · Biochemical Journal · doi:10.1042/bj0610618 · Cited by 367
Cited by
Gross, N. J., Getz, G. S., & Rabinowitz, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91795-3 · Cited by 377
Beale, S. I., Gough, S. P., & Granick, S. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.7.2719 · Cited by 200
Sassa, S., & Kappas, A. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110809 · Cited by 145
Inhibition of delta-aminolevulinic acid dehydrase by 4,6-dioxoheptanoic acid.
Tschudy, D. P., Hess, R. A., & Frykholm, B. C. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68717-x · Cited by 113
Self-citation
Metadata
- Authors
- Marver, H. S., Collins, A., Tschudy, D. P., & Rechcigl, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1966-10
- Volume
- 241
- Issue
- 19
- Pages
- 4323-4329
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1665143716
- Cited by
- 290
- References
- 31
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.