Nuclear magnetic resonance studies on the binding of substrate, coenzymes, and effectors to glutamate dehydrogenase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00598a003
Reference36 articles.
1. Magnetic resonance studies on glutamate dehydrogenase
2. Binding of succinate to aspartate transcarbamylase catalytic subunit. The pH and temperature dependence of nuclear magnetic resonance relaxation times
3. l-GLUTAMIC ACID DEHYDROGENASE: STRUCTURAL REQUIREMENTS FOR SUBSTRATE COMPETITION: EFFECT OF THYROXINE
4. Ultraviolet Spectrophotometric Characterization of a Glutamate Dehydrogenase-reduced Coenzyme-α-Ketoglutarate Complex
Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Dynamical structure of glutamate dehydrogenase as monitored by tryptophan phosphorescence;Journal of Molecular Biology;1989-05
2. Fluorescence stopped-flow studies on the binding of 1,N6-etheno-NAD to bovine liver glutamate dehydrogenase;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1988-08
3. Kinetic studies to determine the mechanism of regulation of bovine liver glutamate dehydrogenase by nucleotide effectors;Biochemistry;1982-01-05
4. NMR of Amino Acids, Peptides, and Proteins (1977–1979);Annual Reports on NMR Spectroscopy;1981
5. A Model for Drug-Receptor Interactions: The Opiate Receptor. A Preliminary Report;The Jerusalem Symposia on Quantum Chemistry and Biochemistry;1981
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