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Role of magnesium and other divalent cations in ATP-utilizing enzymes.
Mildvan AS. Mildvan AS. Magnesium. 1987;6(1):28-33. Magnesium. 1987. PMID: 3029516
Conformations and arrangement of substrates at active sites of ATP-utilizing enzymes.
Mildvan AS. Mildvan AS. Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):65-74. doi: 10.1098/rstb.1981.0061. Philos Trans R Soc Lond B Biol Sci. 1981. PMID: 6115425 Review.
Nuclear magnetic resonance studies of the nucleotide binding sites of porcine adenylate kinase.
Smith GM, Mildvan AS. Smith GM, et al. Among authors: mildvan as. Biochemistry. 1982 Nov 23;21(24):6119-23. doi: 10.1021/bi00267a014. Biochemistry. 1982. PMID: 6295455
Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase.
Rosevear PR, Fox TL, Mildvan AS. Rosevear PR, et al. Among authors: mildvan as. Biochemistry. 1987 Jun 16;26(12):3487-93. doi: 10.1021/bi00386a036. Biochemistry. 1987. PMID: 3498511
MgATP binds both at the active site (site 1) and at a secondary site (site 2) on each monomer of muscle pyruvate kinase as previously found by binding studies and by X-ray analysis. Interproton distances on MgATP bound at each site have been measured by the time-dependent …
MgATP binds both at the active site (site 1) and at a secondary site (site 2) on each monomer of muscle pyruvate kinase as previously …
Nuclear magnetic relaxation studies of the conformation of adenosine 5'-triphosphate on pyruvate kinase from rabbit muscle.
Sloan DL, Mildvan AS. Sloan DL, et al. Among authors: mildvan as. J Biol Chem. 1976 Apr 25;251(8):2412-20. J Biol Chem. 1976. PMID: 177414
The metal-gammaP distance of 5 A for pyruvate kinase-bound ATP is equal to that found for the phosphorous atom of phosphoenolpyruvate and cobalt(II) on pyruvate kinase (Melamud, E., and Mildvan, A. S. (1975) J. Biol. Chem. 250, 8193-8201), which is consistent with the over …
The metal-gammaP distance of 5 A for pyruvate kinase-bound ATP is equal to that found for the phosphorous atom of phosphoenolpyruvate and co …
Arrangement and conformations of substrates at the active site of pyruvate kinase from model building studies based on magnetic resonance data.
Mildvan AS, Sloan DL, Fung CH, Gupta RK, Melamud E. Mildvan AS, et al. J Biol Chem. 1976 Apr 25;251(8):2431-4. J Biol Chem. 1976. PMID: 944185
Chromium(III)-adenosine triphosphate as a paramagnetic probe to determine intersubstrate distances on pyruvate kinase. Detection of an active enzyme-metal-ATP-metal complex.
Gupta RK, Fung CH, Mildvan AS. Gupta RK, et al. Among authors: mildvan as. J Biol Chem. 1976 Apr 25;251(8):2421-30. J Biol Chem. 1976. PMID: 177415
NMR and computer modeling studies of the conformations of glutathione derivatives at the active site of glyoxalase I.
Rosevear PR, Sellin S, Mannervik B, Kuntz ID, Mildvan AS. Rosevear PR, et al. Among authors: mildvan as. J Biol Chem. 1984 Sep 25;259(18):11436-47. J Biol Chem. 1984. PMID: 6547959
NMR studies of the nucleotide conformation and the arrangement of substrates and activators on phosphoribosylpyrophosphate synthetase.
Granot J, Gibson KJ, Switzer RL, Mildvan AS. Granot J, et al. Among authors: mildvan as. J Biol Chem. 1980 Nov 25;255(22):10931-7. J Biol Chem. 1980. PMID: 6253492 No abstract available.
Magnetic resonance studies of the interaction of Co2+ and phosphoenolpyruvate with pyruvate kinase.
Melamud E, Mildvan AS. Melamud E, et al. Among authors: mildvan as. J Biol Chem. 1975 Oct 25;250(20):8193-201. J Biol Chem. 1975. PMID: 1236850
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