Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system.
Open Access
- 1 February 1981
- journal article
- abstracts
- Published by Elsevier
- Vol. 256 (3), 1138-1144
- https://doi.org/10.1016/s0021-9258(19)69939-4
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- Oxygen chiral phosphodiesters. 2. Enzymic synthesis and configurational analysis of [.alpha.-18O]-2'-deoxyadenosine 5'-diphosphateJournal of the American Chemical Society, 1980
- Stereochemical courses of nucleotidyltransferase and phosphotransferase action. Uridine diphosphate glucose pyrophosphorylase, galactose-1-phosphate uridylyltransferase, adenylate kinase, and nucleoside diphosphate kinaseBiochemistry, 1979
- Stereochemical course of the reaction catalyzed by 5'-nucleotide phosphodiesterase from snake venomBiochemistry, 1979
- Stereochemical course of thiophosphoryl group transfer catalyzed by adenylate kinaseJournal of the American Chemical Society, 1978
- Synthesis of nucleoside [18O]pyrophosphorothioates with chiral [18O]phosphorothioate groups of known configuration. Stereochemical orientations of enzymic phosphorylations of chiral [18O]phosphorothioatesJournal of the American Chemical Society, 1978
- Absolute configuration of the diastereomers of adenosine 5'-O-(1-thiotriphosphate): consequences for the stereochemistry of polymerization by DNA-dependent RNA polymerase from Escherichia coli.Proceedings of the National Academy of Sciences, 1978
- Substrate activity of (adenosine triphosphato)tetraamminecobalt(III) with yeast hexokinase and separation of diastereomers using the enzymeBiochemistry, 1978
- Phosphorus-31 NMR studies of complexes of adenosine triphosphate, adenosine diphosphate, tripolyphosphate, and pyrophosphate with cobalt(III) amminesInorganic Chemistry, 1977
- Synthesis and properties of diastereoisomers of adenosine 5'-(O-1-thiotriphosphate) and adenosine 5'-(O-2-thiotriphosphate)Biochemistry, 1976
- Adenosine 5'-phosphorothioate. A nucleotide analog that is a substrate, competitive inhibitor, or regulator of some enzymes that interact with adenosine 5'-phosphateBiochemistry, 1968