Interaction of salicylate at the AMP site of fructose 1,6‐bisphosphatase
- 1 November 1976
- journal article
- Published by Wiley in FEBS Letters
- Vol. 70 (1-2) , 159-162
- https://doi.org/10.1016/0014-5793(76)80748-x
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Predicted distribution of NAD domain among glycolytic enzymesNature, 1975
- Functional consequences of modifying highly reactive arginyl residues of fructose 1,6-bisphosphatase. Loss of monovalent cation activationBiochemistry, 1975
- Blue dextran-sepharose: an affinity column for the dinucleotide fold in proteins.Proceedings of the National Academy of Sciences, 1975
- The Evolution of Dehydrogenases and KinaseCRC Critical Reviews in Biochemistry, 1975
- Binding of Salicylate in the Adenosine‐Binding Pocket of DehydrogenasesEuropean Journal of Biochemistry, 1974
- Structure of horse muscle phosphoglycerate kinase: Some results on the chain conformation, substrate binding and evolution of the molecule from a 3 Å Fourier mapJournal of Molecular Biology, 1974
- Selective alteration of the regulatory properties of fructose 1,6-diphosphatase by modification with pyridoxal 5'-phosphateBiochemistry, 1972
- The effects of pyridoxal phosphate on rabbit liver and kidney fructose 1,6-diphosphatasesArchives of Biochemistry and Biophysics, 1969
- The mechanism of the inhibition of dehydrogenases by salicylateJournal of Pharmacy and Pharmacology, 1967
- Tissue sulfhydryl groupsArchives of Biochemistry and Biophysics, 1959