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Year Number of Results
1983 3
1984 1
1985 3
1986 3
1987 8
1990 1
2020 0
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19 results
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Page 1
NMR studies of the mechanism of enzyme action.
Mildvan AS, Fry DC. Mildvan AS, et al. Adv Enzymol Relat Areas Mol Biol. 1987;59:241-313. doi: 10.1002/9780470123058.ch6. Adv Enzymol Relat Areas Mol Biol. 1987. PMID: 3544711 Review. No abstract available.
Renal metabolism and acute renal failure.
Dickman KG, Jacobs WR, Mandel LJ. Dickman KG, et al. Pediatr Nephrol. 1987 Jul;1(3):359-66. doi: 10.1007/BF00849235. Pediatr Nephrol. 1987. PMID: 3153300 Review.
ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins.
Fry DC, Kuby SA, Mildvan AS. Fry DC, et al. Proc Natl Acad Sci U S A. 1986 Feb;83(4):907-11. doi: 10.1073/pnas.83.4.907. Proc Natl Acad Sci U S A. 1986. PMID: 2869483 Free PMC article.
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
Nuclear Overhauser effect studies of the conformations and binding site environments of deoxynucleoside triphosphate substrates bound to DNA polymerase I and its large fragment.
Ferrin LJ, Mildvan AS. Ferrin LJ, et al. Biochemistry. 1985 Nov 19;24(24):6904-13. doi: 10.1021/bi00345a024. Biochemistry. 1985. PMID: 3907705
NMR studies of conformations and interactions of substrates and ribonucleotide templates bound to the large fragment of DNA polymerase I.
Ferrin LJ, Mildvan AS. Ferrin LJ, et al. Biochemistry. 1986 Sep 9;25(18):5131-45. doi: 10.1021/bi00366a023. Biochemistry. 1986. PMID: 3533145
NMR studies of the AMP-binding site and mechanism of adenylate kinase.
Fry DC, Kuby SA, Mildvan AS. Fry DC, et al. Biochemistry. 1987 Mar 24;26(6):1645-55. doi: 10.1021/bi00380a024. Biochemistry. 1987. PMID: 3036205
NMR studies of the backbone protons and secondary structure of pentapeptide and heptapeptide substrates bound to bovine heart protein kinase.
Rosevear PR, Fry DC, Mildvan AS, Doughty M, O'Brian C, Kaiser ET. Rosevear PR, et al. Biochemistry. 1984 Jul 3;23(14):3161-73. doi: 10.1021/bi00309a009. Biochemistry. 1984. PMID: 6466636
Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis.
Serpersu EH, Shortle D, Mildvan AS. Serpersu EH, et al. Biochemistry. 1987 Mar 10;26(5):1289-300. doi: 10.1021/bi00379a014. Biochemistry. 1987. PMID: 3567171
13C NMR studies of the product complex of glyoxalase I.
Rosevear PR, Chari RV, Kozarich JW, Sellin S, Mannervik B, Mildvan AS. Rosevear PR, et al. J Biol Chem. 1983 Jun 10;258(11):6823-6. J Biol Chem. 1983. PMID: 6853506 Free article.
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