Cadmium-113 and magnesium-25 NMR study of the divalent metal binding sites of isocitrate dehydrogenases from pig heart
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference49 articles.
1. Affinity labeling of NADP+-specific isocitrate dehydrogenase by a new fluorescent nucleotide analog, 2-[(4-bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 2',5'-bisphosphate
2. Role of Metal Ions in Reactions Catalyzed by Pig Heart Triphosphopyridine Nucleotide-dependent Isocitrate Dehydrogenase
3. Chemical characterization of distinct subunits of pig heart DPN-specific isocitrate dehydrogenase.
4. Re-evaluation of molecular weight of pig heart NAD-specific isocitrate dehydrogenase.
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1. In-cell NMR: Why and how?;Progress in Nuclear Magnetic Resonance Spectroscopy;2022-10
2. The β and γ subunits play distinct functional roles in the α2βγ heterotetramer of human NAD-dependent isocitrate dehydrogenase;Scientific Reports;2017-01-31
3. Use of 113Cd NMR to Probe the Native Metal Binding Sites in Metalloproteins: An Overview;Cadmium: From Toxicity to Essentiality;2012-11-03
4. Differential sensitivity to cadmium of key mitochondrial enzymes in the eastern oyster, Crassostrea virginica Gmelin (Bivalvia: Ostreidae);Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology;2008-07
5. Identification of Mn2+-binding Aspartates from α, β, and γ Subunits of Human NAD-dependent Isocitrate Dehydrogenase;Journal of Biological Chemistry;2006-07
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