Year |
Citation |
Score |
2007 |
Hu XV, Chen X, Han KC, Mildvan AS, Liu JO. Kinetic and mutational studies of the number of interacting divalent cations required by bacterial and human methionine aminopeptidases. Biochemistry. 46: 12833-43. PMID 17929833 DOI: 10.1021/Bi701127X |
0.418 |
|
2006 |
Gabelli SB, Azurmendi HF, Bianchet MA, Amzel LM, Mildvan AS. X-ray, NMR, and mutational studies of the catalytic cycle of the GDP-mannose mannosyl hydrolase reaction. Biochemistry. 45: 11290-303. PMID 16981689 DOI: 10.1021/Bi061239G |
0.486 |
|
2006 |
Mildvan AS, Xia Z, Azurmendi HF, Legler PM, Balfour MR, Lairson LL, Withers SG, Gabelli SB, Bianchet MA, Amzel LM. Hydrogen bonding in the mechanism of GDP-mannose mannosyl hydrolase Journal of Molecular Structure. 790: 160-167. DOI: 10.1016/J.Molstruc.2005.09.024 |
0.722 |
|
2005 |
Xia Z, Azurmendi HF, Mildvan AS. Transient state kinetic studies of the MutT-catalyzed nucleoside triphosphate pyrophosphohydrolase reaction. Biochemistry. 44: 15334-44. PMID 16285737 DOI: 10.1021/Bi0513599 |
0.4 |
|
2005 |
Xia Z, Azurmendi HF, Lairson LL, Withers SG, Gabelli SB, Bianchet MA, Amzel LM, Mildvan AS. Mutational, structural, and kinetic evidence for a dissociative mechanism in the GDP-mannose mannosyl hydrolase reaction. Biochemistry. 44: 8989-97. PMID 15966723 DOI: 10.1021/Bi050583V |
0.413 |
|
2005 |
Azurmendi HF, Miller SG, Whitman CP, Mildvan AS. Half-of-the-sites binding of reactive intermediates and their analogues to 4-oxalocrotonate tautomerase and induced structural asymmetry of the enzyme. Biochemistry. 44: 7725-37. PMID 15909987 DOI: 10.1021/Bi0502590 |
0.466 |
|
2005 |
Mildvan AS, Xia Z, Azurmendi HF, Saraswat V, Legler PM, Massiah MA, Gabelli SB, Bianchet MA, Kang LW, Amzel LM. Structures and mechanisms of Nudix hydrolases. Archives of Biochemistry and Biophysics. 433: 129-43. PMID 15581572 DOI: 10.1016/J.Abb.2004.08.017 |
0.715 |
|
2004 |
Mildvan AS. Inverse thinking about double mutants of enzymes. Biochemistry. 43: 14517-20. PMID 15544321 DOI: 10.1021/Bi048052E |
0.394 |
|
2004 |
Gabelli SB, Bianchet MA, Azurmendi HF, Xia Z, Sarawat V, Mildvan AS, Amzel LM. Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus. Structure (London, England : 1993). 12: 927-35. PMID 15274914 DOI: 10.1016/J.Str.2004.03.028 |
0.463 |
|
2004 |
Azurmendi HF, Wang SC, Massiah MA, Poelarends GJ, Whitman CP, Mildvan AS. The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis. Biochemistry. 43: 4082-91. PMID 15065850 DOI: 10.1021/Bi030241U |
0.486 |
|
2004 |
Saraswat V, Azurmendi HF, Mildvan AS. Mutational, NMR, and NH exchange studies of the tight and selective binding of 8-oxo-dGMP by the MutT pyrophosphohydrolase. Biochemistry. 43: 3404-14. PMID 15035612 DOI: 10.1021/Bi030216O |
0.454 |
|
2004 |
Massiah MA, Saraswat V, Azurmendi HF, Mildvan AS. Solution structure, mutagenesis, and NH exchange studies of the MutT enzyme-Mg2+-8-oxo-dGMP complex Journal of Molecular Structure. 700: 247-254. DOI: 10.1016/J.Molstruc.2003.12.060 |
0.428 |
|
2003 |
Massiah MA, Saraswat V, Azurmendi HF, Mildvan AS. Solution structure and NH exchange studies of the MutT pyrophosphohydrolase complexed with Mg(2+) and 8-oxo-dGMP, a tightly bound product. Biochemistry. 42: 10140-54. PMID 12939141 DOI: 10.1021/Bi030105P |
0.43 |
|
2002 |
Saraswat V, Massiah MA, Lopez G, Amzel LM, Mildvan AS. Interactions of the products, 8-oxo-dGMP, dGMP, and pyrophosphate with the MutT nucleoside triphosphate pyrophosphohydrolase. Biochemistry. 41: 15566-77. PMID 12501185 DOI: 10.1021/Bi020552P |
0.442 |
|
2002 |
Legler PM, Massiah MA, Mildvan AS. Mutational, kinetic, and NMR studies of the mechanism of E. coli GDP-mannose mannosyl hydrolase, an unusual Nudix enzyme. Biochemistry. 41: 10834-48. PMID 12196023 DOI: 10.1021/Bi020362E |
0.737 |
|
2002 |
Bolton EC, Mildvan AS, Boeke JD. Inhibition of reverse transcription in vivo by elevated manganese ion concentration. Molecular Cell. 9: 879-89. PMID 11983178 DOI: 10.1016/S1097-2765(02)00495-1 |
0.36 |
|
2002 |
Legler PM, Lee HC, Peisach J, Mildvan AS. Kinetic and magnetic resonance studies of the role of metal ions in the mechanism of Escherichia coli GDP-mannose mannosyl hydrolase, an unusual nudix enzyme. Biochemistry. 41: 4655-68. PMID 11926828 DOI: 10.1021/Bi012118D |
0.744 |
|
2002 |
Mildvan AS, Massiah MA, Harris TK, Marks GT, Harrison DHT, Viragh C, Reddy PM, Kovach IM. Short, strong hydrogen bonds on enzymes: NMR and mechanistic studies Journal of Molecular Structure. 615: 163-175. DOI: 10.1016/S0022-2860(02)00212-0 |
0.378 |
|
2001 |
Marks GT, Harris TK, Massiah MA, Mildvan AS, Harrison DH. Mechanistic implications of methylglyoxal synthase complexed with phosphoglycolohydroxamic acid as observed by X-ray crystallography and NMR spectroscopy. Biochemistry. 40: 6805-18. PMID 11389594 DOI: 10.1021/Bi0028237 |
0.419 |
|
2001 |
Massiah MA, Viragh C, Reddy PM, Kovach IM, Johnson J, Rosenberry TL, Mildvan AS. Short, strong hydrogen bonds at the active site of human acetylcholinesterase: proton NMR studies. Biochemistry. 40: 5682-90. PMID 11341833 DOI: 10.1021/Bi010243J |
0.474 |
|
2001 |
Czerwinski RM, Harris TK, Massiah MA, Mildvan AS, Whitman CP. The structural basis for the perturbed pKa of the catalytic base in 4-oxalocrotonate tautomerase: kinetic and structural effects of mutations of Phe-50. Biochemistry. 40: 1984-95. PMID 11329265 DOI: 10.1021/Bi0024714 |
0.441 |
|
2000 |
Viragh C, Harris TK, Reddy PM, Massiah MA, Mildvan AS, Kovach IM. NMR evidence for a short, strong hydrogen bond at the active site of a cholinesterase. Biochemistry. 39: 16200-5. PMID 11123949 DOI: 10.1021/Bi0022644 |
0.446 |
|
2000 |
Legler PM, Massiah MA, Bessman MJ, Mildvan AS. GDP-mannose mannosyl hydrolase catalyzes nucleophilic substitution at carbon, unlike all other Nudix hydrolases. Biochemistry. 39: 8603-8. PMID 10913267 DOI: 10.1021/Bi000537P |
0.699 |
|
2000 |
Conyers GB, Wu G, Bessman MJ, Mildvan AS. Metal requirements of a diadenosine pyrophosphatase from Bartonella bacilliformis: magnetic resonance and kinetic studies of the role of Mn2+. Biochemistry. 39: 2347-54. PMID 10694402 DOI: 10.1021/bi992458n |
0.769 |
|
2000 |
Harris TK, Wu G, Massiah MA, Mildvan AS. Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase. Biochemistry. 39: 1655-74. PMID 10677214 DOI: 10.1021/Bi9918745 |
0.487 |
|
2000 |
Harris TK, Zhao Q, Mildvan AS. NMR studies of strong hydrogen bonds in enzymes and in a model compound Journal of Molecular Structure. 552: 97-109. DOI: 10.1016/S0022-2860(00)00469-5 |
0.333 |
|
1999 |
Mildvan AS, Harris TK, Abeygunawardana C. Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds on enzymes. Methods in Enzymology. 308: 219-45. PMID 10507007 DOI: 10.1016/S0076-6879(99)08012-X |
0.372 |
|
1999 |
Czerwinski RM, Harris TK, Johnson WH, Legler PM, Stivers JT, Mildvan AS, Whitman CP. Effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase on the pKa values of active site residues and on the pH dependence of catalysis. Biochemistry. 38: 12358-66. PMID 10493803 DOI: 10.1021/Bi9911177 |
0.72 |
|
1999 |
Harris TK, Czerwinski RM, Johnson WH, Legler PM, Abeygunawardana C, Massiah MA, Stivers JT, Whitman CP, Mildvan AS. Kinetic, stereochemical, and structural effects of mutations of the active site arginine residues in 4-oxalocrotonate tautomerase. Biochemistry. 38: 12343-57. PMID 10493802 DOI: 10.1021/Bi991116E |
0.733 |
|
1999 |
Massiah MA, Ko YH, Pedersen PL, Mildvan AS. Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation. Biochemistry. 38: 7453-61. PMID 10360942 DOI: 10.1021/Bi9903603 |
0.357 |
|
1999 |
Harris TK, Mildvan AS. High-precision measurement of hydrogen bond lengths in proteins by nuclear magnetic resonance methods. Proteins. 35: 275-82. PMID 10328262 DOI: 10.1002/(Sici)1097-0134(19990515)35:3<275::Aid-Prot1>3.0.Co;2-V |
0.349 |
|
1999 |
Mildvan AS, Weber DJ, Abeygunawardana C. Solution structure and mechanism of the MutT pyrophosphohydrolase. Advances in Enzymology and Related Areas of Molecular Biology. 73: 183-207. PMID 10218109 DOI: 10.1002/9780470123195.Ch6 |
0.606 |
|
1998 |
Harris TK, Cole RN, Comer FI, Mildvan AS. Proton transfer in the mechanism of triosephosphate isomerase. Biochemistry. 37: 16828-38. PMID 9843453 DOI: 10.1021/Bi982089F |
0.335 |
|
1997 |
Mildvan AS. Mechanisms of signaling and related enzymes. Proteins. 29: 401-16. PMID 9408938 DOI: 10.1002/(Sici)1097-0134(199712)29:4<401::Aid-Prot1>3.0.Co;2-B |
0.394 |
|
1997 |
Harris TK, Abeygunawardana C, Mildvan AS. NMR studies of the role of hydrogen bonding in the mechanism of triosephosphate isomerase. Biochemistry. 36: 14661-75. PMID 9398185 DOI: 10.1021/Bi972039V |
0.396 |
|
1997 |
Zhao Q, Abeygunawardana C, Gittis AG, Mildvan AS. Hydrogen bonding at the active site of delta 5-3-ketosteroid isomerase. Biochemistry. 36: 14616-26. PMID 9398180 DOI: 10.1021/Bi971549M |
0.438 |
|
1997 |
Czerwinski RM, Johnson WH, Whitman CP, Harris TK, Abeygunawardana C, Mildvan AS. Kinetic and structural effects of mutations of the catalytic amino- terminal proline in 4-oxalocrotonate tautomerase Biochemistry. 36: 14551-14560. PMID 9398173 DOI: 10.1021/Bi971545H |
0.418 |
|
1997 |
Stivers JT, Harris TK, Mildvan AS. Vaccinia DNA topoisomerase I: evidence supporting a free rotation mechanism for DNA supercoil relaxation. Biochemistry. 36: 5212-22. PMID 9136883 DOI: 10.1021/Bi962880T |
0.324 |
|
1997 |
Zhao Q, Abeygunawardana C, Mildvan AS. NMR studies of the secondary structure in solution and the steroid binding site of delta5-3-ketosteroid isomerase in complexes with diamagnetic and paramagnetic steroids. Biochemistry. 36: 3458-72. PMID 9131995 DOI: 10.1021/Bi962844U |
0.339 |
|
1997 |
Lin J, Abeygunawardana C, Frick DN, Bessman MJ, Mildvan AS. Solution structure of the quaternary MutT-M2+-AMPCPP-M2+ complex and mechanism of its pyrophosphohydrolase action. Biochemistry. 36: 1199-211. PMID 9063868 DOI: 10.1021/Bi962619C |
0.483 |
|
1996 |
Stivers JT, Abeygunawardana C, Mildvan AS. 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding. Biochemistry. 35: 16036-47. PMID 8973173 DOI: 10.1021/Bi961834Q |
0.399 |
|
1996 |
Stivers JT, Abeygunawardana C, Whitman CP, Mildvan AS. 4-Oxalocrotonate tautomerase, a 41-kDa homohexamer: backbone and side-chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy. Protein Science : a Publication of the Protein Society. 5: 729-41. PMID 8845763 DOI: 10.1002/Pro.5560050418 |
0.383 |
|
1996 |
O'Handley SF, Frick DN, Bullions LC, Mildvan AS, Bessman MJ. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. The Journal of Biological Chemistry. 271: 24649-54. PMID 8798731 DOI: 10.1074/Jbc.271.40.24649 |
0.386 |
|
1996 |
Zhao Q, Abeygunawardana C, Talalay P, Mildvan AS. NMR evidence for the participation of a low-barrier hydrogen bond in the mechanism of delta 5-3-ketosteroid isomerase. Proceedings of the National Academy of Sciences of the United States of America. 93: 8220-4. PMID 8710850 DOI: 10.1073/Pnas.93.16.8220 |
0.386 |
|
1996 |
Lin J, Abeygunawardana C, Frick DN, Bessman MJ, Mildvan AS. The role of Glu 57 in the mechanism of the Escherichia coli MutT enzyme by mutagenesis and heteronuclear NMR. Biochemistry. 35: 6715-26. PMID 8639622 DOI: 10.1021/Bi953071X |
0.49 |
|
1996 |
Zhao Q, Abeygunawardana C, Mildvan AS. 13C NMR relaxation studies of backbone and side chain motion of the catalytic tyrosine residue in free and steroid-bound delta 5-3-ketosteroid isomerase. Biochemistry. 35: 1525-32. PMID 8634283 DOI: 10.1021/Bi9525381 |
0.363 |
|
1996 |
Sekiguchi J, Stivers JT, Mildvan AS, Shuman S. Mechanism of inhibition of vaccinia DNA topoisomerase by novobiocin and coumermycin. The Journal of Biological Chemistry. 271: 2313-22. PMID 8567695 DOI: 10.1074/Jbc.271.4.2313 |
0.352 |
|
1996 |
Stivers JT, Abeygunawardana C, Mildvan AS, Hajipour G, Whitman CP. 4-Oxalocrotonate tautomerase: pH dependence of catalysis and pKa values of active site residues. Biochemistry. 35: 814-23. PMID 8547261 DOI: 10.1021/Bi9510789 |
0.392 |
|
1996 |
Stivers JT, Abeygunawardana C, Mildvan AS, Hajipour G, Whitman CP, Chen LH. Catalytic role of the amino-terminal proline in 4-oxalocrotonate tautomerase: affinity labeling and heteronuclear NMR studies. Biochemistry. 35: 803-13. PMID 8547260 DOI: 10.1021/Bi951077G |
0.415 |
|
1995 |
Zhao Q, Mildvan AS, Talalay P. Enzymatic and nonenzymatic polarizations of alpha,beta-unsaturated ketosteroids and phenolic steroids. Implications for the roles of hydrogen bonding in the catalytic mechanism of delta 5-3-ketosteroid isomerase. Biochemistry. 34: 426-34. PMID 7819234 DOI: 10.1021/Bi00002A006 |
0.378 |
|
1995 |
Chuang WJ, Abeygunawardana C, Gittis AG, Pedersen PL, Mildvan AS. Solution structure and function in trifluoroethanol of PP-50, an ATP-binding peptide from F1ATPase. Archives of Biochemistry and Biophysics. 319: 110-22. PMID 7771774 DOI: 10.1006/Abbi.1995.1272 |
0.404 |
|
1995 |
Zhao Q, Li YK, Mildvan AS, Talalay P. Ultraviolet spectroscopic evidence for decreased motion of the active site tyrosine residue of delta 5-3-ketosteroid isomerase by steroid binding. Biochemistry. 34: 6562-72. PMID 7756287 DOI: 10.1021/Bi00019A038 |
0.424 |
|
1995 |
Frick DN, Weber DJ, Abeygunawardana C, Gittis AG, Bessman MJ, Mildvan AS. NMR studies of the conformations and location of nucleotides bound to the Escherichia coli MutT enzyme. Biochemistry. 34: 5577-86. PMID 7727419 DOI: 10.1021/Bi00016A032 |
0.576 |
|
1995 |
Austin JC, Zhao Q, Jordan T, Talalay P, Mildvan AS, Spiro TG. Ultraviolet resonance Raman spectroscopy of delta 5-3-ketosteroid isomerase revisited: substrate polarization by active-site residues. Biochemistry. 34: 4441-7. PMID 7703258 DOI: 10.1021/Bi00013A037 |
0.405 |
|
1995 |
Abeygunawardana C, Weber DJ, Gittis AG, Frick DN, Lin J, Miller AF, Bessman MJ, Mildvan AS. Solution structure of the MutT enzyme, a nucleoside triphosphate pyrophosphohydrolase. Biochemistry. 34: 14997-5005. PMID 7578113 DOI: 10.1021/Bi00046A006 |
0.53 |
|
1994 |
Frick DN, Weber DJ, Gillespie JR, Bessman MJ, Mildvan AS. Dual divalent cation requirement of the MutT dGTPase. Kinetic and magnetic resonance studies of the metal and substrate complexes. The Journal of Biological Chemistry. 269: 1794-803. PMID 8294428 |
0.512 |
|
1994 |
Stivers JT, Shuman S, Mildvan AS. Vaccinia DNA topoisomerase I: single-turnover and steady-state kinetic analysis of the DNA strand cleavage and ligation reactions. Biochemistry. 33: 327-39. PMID 8286354 DOI: 10.1021/Bi00167A043 |
0.384 |
|
1994 |
Chuang WJ, Gittis AG, Mildvan AS. Magnetic resonance studies of the binding of oligonucleotide substrates to mutants of staphylococcal nuclease. Proteins. 18: 68-80. PMID 8146123 DOI: 10.1002/Prot.340180109 |
0.468 |
|
1994 |
Weber DJ, Libson AM, Gittis AG, Lebowitz MS, Mildvan AS. NMR docking of a substrate into the X-ray structure of the Asp-21-->Glu mutant of staphylococcal nuclease. Biochemistry. 33: 8017-28. PMID 8025106 DOI: 10.1021/Bi00192A005 |
0.592 |
|
1994 |
Stivers JT, Shuman S, Mildvan AS. Vaccinia DNA topoisomerase I: kinetic evidence for general acid-base catalysis and a conformational step. Biochemistry. 33: 15449-58. PMID 7803409 DOI: 10.1021/Bi00255A027 |
0.387 |
|
1993 |
Mullen GP, Vaughn JB, Mildvan AS. Sequential proton NMR resonance assignments, circular dichroism, and structural properties of a 50-residue substrate-binding peptide from DNA polymerase I. Archives of Biochemistry and Biophysics. 301: 174-83. PMID 8442659 DOI: 10.1006/Abbi.1993.1130 |
0.363 |
|
1993 |
Li YK, Kuliopulos A, Mildvan AS, Talalay P. Environments and mechanistic roles of the tyrosine residues of delta 5-3-ketosteroid isomerase. Biochemistry. 32: 1816-24. PMID 8439542 DOI: 10.1021/Bi00058A016 |
0.439 |
|
1993 |
Weber DJ, Abeygunawardana C, Bessman MJ, Mildvan AS. Secondary structure of the MutT enzyme as determined by NMR. Biochemistry. 32: 13081-8. PMID 8241162 DOI: 10.1021/Bi00211A018 |
0.521 |
|
1993 |
Abeygunawardana C, Weber DJ, Frick DN, Bessman MJ, Mildvan AS. Sequence-specific assignments of the backbone 1H, 13C, and 15N resonances of the MutT enzyme by heteronuclear multidimensional NMR. Biochemistry. 32: 13071-80. PMID 8241161 DOI: 10.1021/Bi00211A017 |
0.528 |
|
1993 |
Chuang WJ, Weber DJ, Gittis AG, Mildvan AS. Mutational tests of the NMR-docked structure of the staphylococcal nuclease-metal-3',5'-pdTp complex. Proteins. 17: 36-48. PMID 8234243 DOI: 10.1002/Prot.340170107 |
0.567 |
|
1993 |
Weber DJ, Serpersu EH, Gittis AG, Lattman EE, Mildvan AS. NMR docking of the competitive inhibitor thymidine 3',5'-diphosphate into the X-ray structure of staphylococcal nuclease. Proteins. 17: 20-35. PMID 8234242 DOI: 10.1002/Prot.340170106 |
0.547 |
|
1993 |
Martínez A, Abeygunawardana C, Haavik J, Flatmark T, Mildvan AS. Conformation and interaction of phenylalanine with the divalent cation at the active site of human recombinant tyrosine hydroxylase as determined by proton NMR. Biochemistry. 32: 6381-90. PMID 8100148 DOI: 10.1021/Bi00076A011 |
0.385 |
|
1993 |
Martínez A, Abeygunawardana C, Haavik J, Flatmark T, Mildvan AS. Interaction of substrate and pterin cofactor with the metal of human tyrosine hydroxylase as determined by 1H-NMR. Advances in Experimental Medicine and Biology. 338: 77-80. PMID 7905701 DOI: 10.1007/978-1-4615-2960-6_15 |
0.358 |
|
1992 |
Mildvan AS, Weber DJ, Kuliopulos A. Quantitative interpretations of double mutations of enzymes. Archives of Biochemistry and Biophysics. 294: 327-40. PMID 1567189 DOI: 10.1016/0003-9861(92)90692-P |
0.513 |
|
1992 |
Weber DJ, Gittis AG, Mullen GP, Abeygunawardana C, Lattman EE, Mildvan AS. NMR docking of a substrate into the X-ray structure of staphylococcal nuclease. Proteins. 13: 275-87. PMID 1518799 DOI: 10.1002/Prot.340130402 |
0.611 |
|
1992 |
Chuang WJ, Abeygunawardana C, Pedersen PL, Mildvan AS. Two-dimensional NMR, circular dichroism, and fluorescence studies of PP-50, a synthetic ATP-binding peptide from the beta-subunit of mitochondrial ATP synthase. Biochemistry. 31: 7915-21. PMID 1387322 DOI: 10.1021/Bi00149A024 |
0.373 |
|
1992 |
Austin JC, Kuliopulos A, Mildvan AS, Spiro TG. Substrate polarization by residues in delta 5-3-ketosteroid isomerase probed by site-directed mutagenesis and UV resonance Raman spectroscopy. Protein Science : a Publication of the Protein Society. 1: 259-70. PMID 1339027 DOI: 10.1002/Pro.5560010208 |
0.432 |
|
1992 |
Weber DJ, Bhatnagar SK, Bullions LC, Bessman MJ, Mildvan AS. NMR and isotopic exchange studies of the site of bond cleavage in the MutT reaction. The Journal of Biological Chemistry. 267: 16939-42. PMID 1324915 |
0.472 |
|
1991 |
Xue LA, Kuliopulos A, Mildvan AS, Talalay P. Catalytic mechanism of an active-site mutant (D38N) of delta 5-3-ketosteroid isomerase. Direct spectroscopic evidence for dienol intermediates. Biochemistry. 30: 4991-7. PMID 2036366 DOI: 10.1021/Bi00234A022 |
0.42 |
|
1991 |
Kuliopulos A, Mullen GP, Xue L, Mildvan AS. Stereochemistry of the concerted enolization catalyzed by delta 5-3-ketosteroid isomerase. Biochemistry. 30: 3169-78. PMID 2009258 DOI: 10.1021/Bi00227A003 |
0.485 |
|
1991 |
Xue LA, Talalay P, Mildvan AS. Studies of the catalytic mechanism of an active-site mutant (Y14F) of delta 5-3-ketosteroid isomerase by kinetic deuterium isotope effects. Biochemistry. 30: 10858-65. PMID 1932008 DOI: 10.1021/Bi00109A008 |
0.421 |
|
1991 |
Weber DJ, Mullen GP, Mildvan AS. Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR. Biochemistry. 30: 7425-37. PMID 1854746 DOI: 10.1021/Bi00244A009 |
0.565 |
|
1991 |
Weber DJ, Meeker AK, Mildvan AS. Interactions of the acid and base catalysts on staphylococcal nuclease as studied in a double mutant. Biochemistry. 30: 6103-14. PMID 1676297 DOI: 10.1021/Bi00239A004 |
0.575 |
|
1991 |
Han H, Rifkind JM, Mildvan AS. Role of divalent cations in the 3',5'-exonuclease reaction of DNA polymerase I. Biochemistry. 30: 11104-8. PMID 1657160 DOI: 10.1021/Bi00110A012 |
0.398 |
|
1990 |
Kuliopulos A, Talalay P, Mildvan AS. Combined effects of two mutations of catalytic residues on the ketosteroid isomerase reaction. Biochemistry. 29: 10271-80. PMID 2271654 DOI: 10.1021/Bi00496A017 |
0.434 |
|
1990 |
Xue LA, Talalay P, Mildvan AS. Studies of the mechanism of the delta 5-3-ketosteroid isomerase reaction by substrate, solvent, and combined kinetic deuterium isotope effects on wild-type and mutant enzymes. Biochemistry. 29: 7491-500. PMID 2223781 DOI: 10.1021/Bi00484A019 |
0.41 |
|
1990 |
Mullen GP, Serpersu EH, Ferrin LJ, Loeb LA, Mildvan AS. Metal binding to DNA polymerase I, its large fragment, and two 3',5'-exonuclease mutants of the large fragment. The Journal of Biological Chemistry. 265: 14327-34. PMID 2201684 |
0.308 |
|
1990 |
Mullen GP, Vaughn JB, Shenbagamurthi P, Mildvan AS. NMR studies of the active site of DNA polymerase I and of a 50-residue peptide fragment of the enzyme. Biochemical Pharmacology. 40: 69-81. PMID 2196883 DOI: 10.1016/0006-2952(90)90181-J |
0.447 |
|
1990 |
Urbina JA, Ysern X, Mildvan AS. Involvement of a divalent cation in the binding of fructose 6-phosphate to Trypanosoma cruzi phosphofructokinase: kinetic and magnetic resonance studies. Archives of Biochemistry and Biophysics. 278: 187-94. PMID 2138869 DOI: 10.1016/0003-9861(90)90247-V |
0.48 |
|
1990 |
Weber DJ, Serpersu EH, Shortle D, Mildvan AS. Diverse interactions between the individual mutations in a double mutant at the active site of staphylococcal nuclease. Biochemistry. 29: 8632-42. PMID 1702994 DOI: 10.1021/Bi00489A020 |
0.551 |
|
1989 |
Kuliopulos A, Mildvan AS, Shortle D, Talalay P. Kinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomerase. Biochemistry. 28: 149-59. PMID 2706241 DOI: 10.1021/Bi00427A022 |
0.467 |
|
1989 |
Mildvan AS. NMR studies of the interactions of substrates with enzymes and their peptide fragments. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 3: 1705-14. PMID 2649401 DOI: 10.1096/Fasebj.3.6.2649401 |
0.445 |
|
1989 |
Cachau RE, Serpersu EH, Mildvan AS, August JT, Amzel LM. Recognition in cell adhesion. A comparative study of the conformations of RGD-containing peptides by Monte Carlo and NMR methods. Journal of Molecular Recognition : Jmr. 2: 179-86. PMID 2637044 DOI: 10.1002/Jmr.300020407 |
0.329 |
|
1989 |
Rosevear PR, Mildvan AS. Ligand conformations and ligand-enzyme interactions as studied by the nuclear Overhauser effect. Methods in Enzymology. 177: 333-58. PMID 2607987 DOI: 10.1016/0076-6879(89)77019-1 |
0.356 |
|
1989 |
Serpersu EH, Hibler DW, Gerlt JA, Mildvan AS. Kinetic and magnetic resonance studies of the glutamate-43 to serine mutant of staphylococcal nuclease. Biochemistry. 28: 1539-48. PMID 2566322 DOI: 10.1021/Bi00430A018 |
0.454 |
|
1989 |
Kuby SA, Hamada M, Johnson MS, Russell GA, Manship M, Palmieri RH, Fleming G, Bredt DS, Mildvan AS. Studies on adenosine triphosphate transphosphorylases. XVIII. Synthesis and preparation of peptides and peptide fragments of rabbit muscle ATP-AMP transphosphorylase (adenylate kinase) and their nucleotide-binding properties. Journal of Protein Chemistry. 8: 549-62. PMID 2553049 DOI: 10.1007/Bf01026438 |
0.345 |
|
1988 |
Serpersu EH, McCracken J, Peisach J, Mildvan AS. Electron spin echo modulation and nuclear relaxation studies of staphylococcal nuclease and its metal-coordinating mutants. Biochemistry. 27: 8034-44. PMID 2852950 DOI: 10.1021/Bi00421A010 |
0.424 |
|
1987 |
Serpersu EH, Shortle D, Mildvan AS. Kinetic and magnetic resonance studies of active-site mutants of staphylococcal nuclease: factors contributing to catalysis. Biochemistry. 26: 1289-300. PMID 3567171 DOI: 10.1021/Bi00379A014 |
0.487 |
|
1987 |
Mildvan AS, Fry DC. NMR studies of the mechanism of enzyme action. Advances in Enzymology and Related Areas of Molecular Biology. 59: 241-313. PMID 3544711 DOI: 10.1002/9780470123058.Ch6 |
0.391 |
|
1987 |
Rosevear PR, Powers VM, Dowhan D, Mildvan AS, Kenyon GL. Nuclear overhauser effect studies on the conformation of magnesium adenosine 5'-triphosphate bound to rabbit muscle creatine kinase. Biochemistry. 26: 5338-44. PMID 3499934 DOI: 10.1021/Bi00391A018 |
0.343 |
|
1987 |
Rosevear PR, Fox TL, Mildvan AS. Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase. Biochemistry. 26: 3487-93. PMID 3498511 DOI: 10.1021/Bi00386A036 |
0.404 |
|
1987 |
Fry DC, Kuby SA, Mildvan AS. NMR studies of the AMP-binding site and mechanism of adenylate kinase. Biochemistry. 26: 1645-55. PMID 3036205 DOI: 10.1021/Bi00380A024 |
0.473 |
|
1987 |
Mildvan AS. Role of magnesium and other divalent cations in ATP-utilizing enzymes. Magnesium. 6: 28-33. PMID 3029516 |
0.339 |
|
1987 |
Kuliopulos A, Westbrook EM, Talalay P, Mildvan AS. Positioning of a spin-labeled substrate analogue into the structure of delta 5-3-ketosteroid isomerase by combined kinetic, magnetic resonance, and X-ray diffraction methods. Biochemistry. 26: 3927-37. PMID 2888482 DOI: 10.1021/Bi00387A028 |
0.449 |
|
1986 |
Ferrin LJ, Mildvan AS. NMR studies of conformations and interactions of substrates and ribonucleotide templates bound to the large fragment of DNA polymerase I. Biochemistry. 25: 5131-45. PMID 3533145 DOI: 10.1021/Bi00366A023 |
0.424 |
|
1986 |
Serpersu EH, Shortle D, Mildvan AS. Kinetic and magnetic resonance studies of effects of genetic substitution of a Ca2+-liganding amino acid in staphylococcal nuclease. Biochemistry. 25: 68-77. PMID 3513826 DOI: 10.1021/Bi00349A011 |
0.458 |
|
1986 |
Fry DC, Kuby SA, Mildvan AS. ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins. Proceedings of the National Academy of Sciences of the United States of America. 83: 907-11. PMID 2869483 DOI: 10.1073/Pnas.83.4.907 |
0.373 |
|
1985 |
Beckman RA, Mildvan AS, Loeb LA. On the fidelity of DNA replication: manganese mutagenesis in vitro. Biochemistry. 24: 5810-7. PMID 3910084 DOI: 10.1021/Bi00342A019 |
0.392 |
|
1985 |
Ferrin LJ, Mildvan AS. Nuclear Overhauser effect studies of the conformations and binding site environments of deoxynucleoside triphosphate substrates bound to DNA polymerase I and its large fragment. Biochemistry. 24: 6904-13. PMID 3907705 DOI: 10.1021/Bi00345A024 |
0.422 |
|
1985 |
Fry DC, Fox T, Lane MD, Mildvan AS. NMR studies of the exchange of the amide protons of d-biotin and its derivatives. Annals of the New York Academy of Sciences. 447: 140-51. PMID 3860170 DOI: 10.1111/J.1749-6632.1985.Tb18434.X |
0.32 |
|
1985 |
Mildvan AS, Rosevear PR, Fry DC, Bramson HN, Kaiser ET. NMR studies of the mechanism of action and regulation of protein kinase. Current Topics in Cellular Regulation. 27: 133-44. PMID 3004816 DOI: 10.1016/B978-0-12-152827-0.50018-9 |
0.391 |
|
1985 |
Fry DC, Kuby SA, Mildvan AS. NMR studies of the MgATP binding site of adenylate kinase and of a 45-residue peptide fragment of the enzyme. Biochemistry. 24: 4680-94. PMID 2998457 DOI: 10.1021/Bi00338A030 |
0.418 |
|
1985 |
Rosevear PR, Fry DC, Mildvan AS. Temperature dependence of the longitudinal relaxation rates and exchange rates of the amide protons in peptide substrates of protein kinase Journal of Magnetic Resonance (1969). 61: 102-115. DOI: 10.1016/0022-2364(85)90271-9 |
0.361 |
|
1985 |
Fry DC, Fox TL, Lane MD, Mildvan AS. Exchange characteristics of the amide protons of d-biotin and derivatives: Implications for the mechanism of biotin enzymes and the role of sulfur in biotin Journal of the American Chemical Society. 107: 7659-7665. DOI: 10.1002/Chin.198613134 |
0.394 |
|
1984 |
Garcia-Iniguez L, Powers L, Chance B, Sellin S, Mannervik B, Mildvan AS. X-ray absorption studies of the Zn2+ site of glyoxalase I. Biochemistry. 23: 685-9. PMID 6712919 DOI: 10.1021/Bi00299A016 |
0.343 |
|
1984 |
Rosevear PR, Sellin S, Mannervik B, Kuntz ID, Mildvan AS. NMR and computer modeling studies of the conformations of glutathione derivatives at the active site of glyoxalase I. The Journal of Biological Chemistry. 259: 11436-47. PMID 6547959 |
0.323 |
|
1984 |
Rosevear PR, Fry DC, Mildvan AS, Doughty M, O'Brian C, Kaiser ET. NMR studies of the backbone protons and secondary structure of pentapeptide and heptapeptide substrates bound to bovine heart protein kinase. Biochemistry. 23: 3161-73. PMID 6466636 DOI: 10.1021/Bi00309A009 |
0.466 |
|
1984 |
Mildvan AS, Kaiser ET, Rosevear PR, Bramson HN. NMR studies of the mechanism of cyclic AMP-dependent protein kinase. Federation Proceedings. 43: 2634-9. PMID 6086412 |
0.341 |
|
1983 |
Mildvan AS, Rosevear PR, Granot J, O'Brian CA, Bramson HN, Kaiser ET. Use of NMR and EPR to study cAMP-dependent protein kinase. Methods in Enzymology. 99: 93-119. PMID 6316105 DOI: 10.1016/0076-6879(83)99045-6 |
0.454 |
|
1982 |
Smith GM, Mildvan AS. Nuclear magnetic resonance studies of the nucleotide binding sites of porcine adenylate kinase. Biochemistry. 21: 6119-23. PMID 6295455 DOI: 10.1021/Bi00267A014 |
0.491 |
|
1981 |
Rosevear PR, Desmeules P, Kenyon GL, Mildvan AS. Nuclear magnetic resonance studies of the role of histidine residues at the active site of rabbit muscle creatine kinase. Biochemistry. 20: 6155-64. PMID 7306503 DOI: 10.1021/Bi00524A038 |
0.367 |
|
1981 |
Granot J, Mildvan AS, Bramson HN, Thomas N, Kaiser ET. Nuclear magnetic resonance studies of the conformation and kinetics of the peptide-substrate at the active site of bovine heart protein kinase. Biochemistry. 20: 602-10. PMID 7213597 DOI: 10.1021/Bi00506A024 |
0.386 |
|
1981 |
Smith GM, Mildvan AS. Nuclear magnetic resonance and chemical modification studies of the role of the metal in yeast aldolase Biochemistry. 20: 4340-4346. PMID 7025896 DOI: 10.1021/Bi00518A017 |
0.344 |
|
1981 |
Mildvan AS. Conformations and arrangement of substrates at active sites of ATP-utilizing enzymes Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 293: 65-74. PMID 6115425 DOI: 10.1098/Rstb.1981.0061 |
0.44 |
|
1981 |
Meshitsuka S, Smith GM, Mildvan AS. Proton NMR studies of the histidine residues and of bound ATP on rabbit muscle pyruvate kinase International Journal of Quantum Chemistry. 20: 241-245. DOI: 10.1002/Qua.560200721 |
0.496 |
|
1980 |
Gupta RK, Mildvan AS, Schonbaum GR. Water proton relaxation studies of the heme-environment in Mn(III)-substituted and native horseradish peroxidases Archives of Biochemistry and Biophysics. 202: 1-7. PMID 7396528 DOI: 10.1016/0003-9861(80)90398-7 |
0.395 |
|
1980 |
Granot J, Mildvan AS, Bramson HN, Kaiser ET. Magnetic resonance measurements of intersubstrate distances at the active site of protein kinase using substitution-inert cobalt(III) and chromium(III) complexes of adenosine 5'-(beta, gamma-methylenetriphosphate). Biochemistry. 19: 3537-43. PMID 6893273 |
0.421 |
|
1980 |
Mincey T, Tayrien G, Mildvan AS, Abeles RH. Presence of a flavin semiquinone in methanol oxidase. Proceedings of the National Academy of Sciences of the United States of America. 77: 7099-101. PMID 6261238 DOI: 10.1073/Pnas.77.12.7099 |
0.397 |
|
1980 |
Granot J, Mildvan AS, Kaiser ET. Studies of the mechanism of action and regulation of cAMP-dependent protein kinase. Archives of Biochemistry and Biophysics. 205: 1-17. PMID 6255875 DOI: 10.1016/0003-9861(80)90078-8 |
0.486 |
|
1979 |
Granot J, Kondo H, Armstrong RN, Mildvan AS, Kaiser ET. Nuclear magnetic resonance studies of the conformation of tetraamminecobalt (III)--ATP bound at the active site of bovine heart protein kinase. Biochemistry. 18: 2339-45. PMID 444460 DOI: 10.1021/Bi00578A032 |
0.393 |
|
1979 |
Mildvan AS. The role of metals in enzyme-catalyzed substitutions at each of the phosphorus atoms of ATP Advances in Enzymology and Related Areas of Molecular Biology. 49: 103-126. PMID 233740 DOI: 10.1002/9780470122945.Ch3 |
0.354 |
|
1979 |
Gupta RK, Mildvan AS, Schonbaum GR. Heme-environment of horseradish peroxidase as observed by oxygen-17 superhyperfine interaction in EPR Biochemical and Biophysical Research Communications. 89: 1334-1340. PMID 227384 DOI: 10.1016/0006-291X(79)92155-7 |
0.34 |
|
1979 |
Li TM, Switzer RL, Mildvan AS. Kinetic and magnetic resonance studies of the interaction of the Cr-ATP complex with phosphoribosylpyrophosphate synthetase from Salmonella typhimurium Archives of Biochemistry and Biophysics. 193: 1-13. PMID 222212 DOI: 10.1016/0003-9861(79)90001-8 |
0.432 |
|
1979 |
Armstrong RN, Kondo H, Granot J, Kaiser ET, Mildvan AS. Magnetic resonance and kinetic studies of the manganese(II) ion and substrate complexes of the catalytic subunit of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart. Biochemistry. 18: 1230-8. PMID 218617 DOI: 10.1021/Bi00574A018 |
0.404 |
|
1978 |
Mildvan AS, Gupta RK. [15] Nuclear relaxation measurements of the geometry of enzyme-bound substrates and analogs Methods in Enzymology. 49: 322-359. PMID 651672 DOI: 10.1016/S0076-6879(78)49017-2 |
0.467 |
|
1978 |
Stein PJ, Mildvan AS. Magnetic resonance and kinetic studies of initiator-substrate distances on RNA polymerase from Escherichia coli Biochemistry. 17: 2675-2684. PMID 354694 DOI: 10.1021/Bi00606A034 |
0.344 |
|
1977 |
Bean BL, Koren R, Mildvan AS. Magnetic resonance studies of the conformation of enzyme-bound adenylyl(3′→5′)uridine and adenosine 5′-triphosphate on RNA polymerase from Escherichia coli Biochemistry. 16: 3322-3333. PMID 329869 DOI: 10.1021/Bi00634A007 |
0.392 |
|
1977 |
Koren R, Mildvan AS. Magnetic resonance and kinetic studies of the role of the divalent cation activator of RNA polymerase from Escherichia coli Biochemistry. 16: 241-249. PMID 189795 |
0.381 |
|
1977 |
Mildvan AS. Magnetic resonance studies of the conformations of enzyme-bound substrates Accounts of Chemical Research. 10: 246-252. DOI: 10.1021/Ar50115A003 |
0.437 |
|
1976 |
Fung CH, Feldmann RJ, Mildvan AS. 1H and 31P fourier transform magnetic resonance studies of the conformation of enzyme-bound propionyl coenzyme A on transcarboxylase Biochemistry. 15: 75-84. PMID 1247514 DOI: 10.1021/Bi00646A013 |
0.394 |
|
1976 |
Hsu RY, Mildvan AS, Chang GG, Fung CH. Mechanism of malic enzyme from pigeon liver. Magnetic resonance and kinetic studies of the role of Mn2+ Journal of Biological Chemistry. 251: 6574-6583. PMID 988026 |
0.373 |
|
1976 |
Mildvan AS, Sloan DL, Fung CH, Gupta RK, Melamud E. Arrangement and conformations of substrates at the active site of pyruvate kinase from model building studies based on magnetic resonance data Journal of Biological Chemistry. 251: 2431-2434. PMID 944185 |
0.318 |
|
1976 |
Gupta RK, Fung CH, Mildvan AS. Chromium(III) adenosine triphosphate as a paramagnetic probe to determine intersubstrate distances on pyruvate kinase. Detection of an active enzyme metal ATP metal complex Journal of Biological Chemistry. 251: 2421-2430. PMID 177415 |
0.313 |
|
1976 |
Sloan DL, Mildvan AS. Nuclear magnetic relaxation studies of the conformation of adenosine 5' triphosphate on pyruvate kinase from rabbit muscle Journal of Biological Chemistry. 251: 2412-2420. PMID 177414 |
0.345 |
|
1976 |
Fung CH, Gupta RK, Mildvan AS. Magnetic resonance studies of the proximity and spatial arrangement of propionyl coenzyme A and pyruvate on a biotin-metalloenzyme, transcarboxylase Biochemistry. 15: 85-92. PMID 174714 DOI: 10.1021/Bi00646A014 |
0.434 |
|
1976 |
Gupta RK, Oesterling RM, Mildvan AS. Dual divalent cation requirement for activation of pyruvate kinase: Essential roles of both enzyme-and nucleotide-bound metal ions Biochemistry. 15: 2881-2887. PMID 7293 DOI: 10.1021/Bi00658A028 |
0.469 |
|
1975 |
Young JM, Schray KJ, Mildvan AS. Proton magnetic relaxation studies of the interaction of D-xylose and xylitol with D-xylose isomerase. Characterization of metal enzyme substrate interactions Journal of Biological Chemistry. 250: 9021-9027. PMID 1194275 |
0.309 |
|
1975 |
Sloan DL, Loeb LA, Mildvan AS, Feldmann RJ. Conformation of deoxynucleoside triphosphate substrates on DNA polymerase I from Escherichia coli as determined by nuclear magnetic relaxation Journal of Biological Chemistry. 250: 8913-8920. PMID 1104609 |
0.318 |
|
1975 |
Travaglini EC, Mildvan AS, Loeb LA. Kinetic analysis of Escherichia coli deoxyribonucleic acid polymerase I Journal of Biological Chemistry. 250: 8647-8656. PMID 1102540 |
0.309 |
|
1975 |
Grisham CM, Mildvan AS. Magnetic resonance and kinetic studies of the mechanism of membrane-bound sodium and potassium ion- activated adenosine triphosphatase. Journal of Supramolecular Structure. 3: 304-13. PMID 171521 DOI: 10.1002/Jss.400030313 |
0.728 |
|
1975 |
Maggio ET, Kenyon GL, Mildvan AS, Hegeman GD. Mandelate racemase from Pseudomonas putida. Magnetic resonance and kinetic studies of the mechanism of catalysis Biochemistry. 14: 1131-1139. PMID 164210 DOI: 10.1021/Bi00677A006 |
0.503 |
|
1975 |
Maggio E, Kenyon G, Mildvan A, Hegeman G. Corrections - Mandelate Racemase from Psuedomonas putida. Magnetic Resonance and Kinetic Studies of the Mechanism of Catalysis. Biochemistry. 14: 3292-3292. DOI: 10.1021/Bi00685A602 |
0.351 |
|
1974 |
Grisham CM, Gupta RK, Barnett RE, Mildvan AS. Thallium 205 nuclear relaxation and kinetic studies of sodium and potassium ion activated adenosine triphosphatase Journal of Biological Chemistry. 249: 6738-6744. PMID 4371202 |
0.724 |
|
1974 |
Sloan DL, Mildvan AS. Magnetic resonance studies of the geometry of bound nicotinamide adenine dinucleotide and isobutyramide on spin-labeled alcohol dehydrogenase Biochemistry. 13: 1711-1718. PMID 4364709 DOI: 10.1021/Bi00705A024 |
0.306 |
|
1974 |
Grisham CM, Mildvan AS. Magnetic resonance and kinetic studies of the mechanism of sodium and potassium ion-activated adenosine triphosphatase. The Journal of Biological Chemistry. 249: 3187-97. PMID 4364418 |
0.648 |
|
1974 |
Fung CH, Mildvan AS, Leigh JS. Electron and nuclear magnetic resonance studies of the interaction of pyruvate with transcarboxylase Biochemistry. 13: 1160-1169. PMID 4360781 DOI: 10.1021/Bi00703A017 |
0.532 |
|
1974 |
Mildvan AS. Mechanism of enzyme action Annual Review of Biochemistry. 43: 357-399. PMID 4212156 DOI: 10.1146/Annurev.Bi.43.070174.002041 |
0.353 |
|
1973 |
Ray WJ, Mildvan AS, Long JW. Arrangement of the phosphate and metal binding subsites of phosphoglucomutase. Intersubsite relationships by means of inhibition patterns Biochemistry. 12: 3724-3732. PMID 4788309 DOI: 10.1021/Bi00743A023 |
0.305 |
|
1973 |
Scrutton MC, Reed GH, Mildvan AS. Application of physical methods to the study of enzymes containing bound manganese: problems and prospects Advances in Experimental Medicine and Biology. 40: 79-102. PMID 4769160 DOI: 10.1007/978-1-4684-3240-4_5 |
0.44 |
|
1973 |
Nowak T, Mildvan AS, Kenyon GL. Nuclear relaxation and kinetic studies of the role of Mn2+ in the mechanism of enolase Biochemistry. 12: 1690-1701. PMID 4572991 DOI: 10.1021/Bi00733A005 |
0.647 |
|
1973 |
Mildvan AS, Nowak T, Fung CH. Nuclear relaxation studies of the role of the divalent cation in the mechanism of pyruvate kinase and enolase: inner sphere and second sphere complexes Annals of the New York Academy of Sciences. 192-210. PMID 4522427 DOI: 10.1111/J.1749-6632.1973.Tb15261.X |
0.648 |
|
1972 |
Nowak T, Mildvan AS. Nuclear magnetic resonance studies of the function of potassium in the mechanism of pyruvate kinase. Biochemistry. 11: 2819-28. PMID 5064959 DOI: 10.1021/Bi00765A014 |
0.646 |
|
1972 |
Slater JP, Mildvan AS, Loeb LA. Zinc in DNA polymerases. Biochemical and Biophysical Research Communications. 44: 37-43. PMID 4940372 DOI: 10.1016/S0006-291X(71)80155-9 |
0.325 |
|
1972 |
Nowak T, Mildvan AS. Nuclear magnetic resonance studies of selectively hindered internal motion of substrate analogs at the active site of pyruvate kinase Biochemistry. 11: 2813-2818. PMID 4625313 DOI: 10.1021/Bi00765A013 |
0.669 |
|
1972 |
Mildvan AS, Engle JL. [29] Nuclear relaxation measurements of water protons and other ligands Methods in Enzymology. 26: 654-682. PMID 4376581 DOI: 10.1016/S0076-6879(72)26031-1 |
0.442 |
|
1972 |
Benkovic SJ, Engle JL, Mildvan AS. Magnetic resonance studies of the anomeric distribution and manganese binding properties of fructose phosphates Biochemical and Biophysical Research Communications. 47: 852-858. PMID 4337325 DOI: 10.1016/0006-291X(72)90571-2 |
0.355 |
|
1972 |
Foster DM, Mildvan AS. Preparation, physical properties, and effects of a Cr3+-ADP complex on phosphoryl transfer enzyme systems Bioinorganic Chemistry. 1: 133-139. DOI: 10.1016/S0006-3061(00)80119-2 |
0.419 |
|
1971 |
Ray WJ, Mildvan AS. Role of bivalent cations in the phosphoglucomutase system. IV. A study of the Mn2+ binding site by means of nuclear relaxation measurements on water protons. Biochemistry. 9: 3886-94. PMID 5501647 DOI: 10.1021/Bi00822A006 |
0.373 |
|
1971 |
Mildvan AS, Kobes RD, Rutter WJ. Magnetic resonance studies of the role of the divalent cation in the mechanism of yeast aldolase. Biochemistry. 10: 1191-204. PMID 4324205 DOI: 10.1021/Bi00783A016 |
0.352 |
|
1970 |
Scrutton MC, Mildvan AS. Pyruvate carboxylase: nuclear magnetic resonance studies of the enzyme-manganese-oxalacetate and enzyme-manganese-pyruvate bridge complexes. Archives of Biochemistry and Biophysics. 140: 131-51. PMID 5466117 DOI: 10.1016/0003-9861(70)90017-2 |
0.441 |
|
1970 |
Mildvan AS, Cohn M. Aspects of enzyme mechanisms studies by nuclear spin relazation induced by paramagnetic probes. Advances in Enzymology and Related Areas of Molecular Biology. 33: 1-70. PMID 4916855 |
0.488 |
|
1969 |
Mildvan AS, Weiner H. Interaction of a spin-labeled analog of nicotinamide-adenine dinucleotide with alcohol dehydrogenase. II. Proton relaxation rate and electron paramagnetic resonance studies of binary and ternary complexes. Biochemistry. 8: 552-62. PMID 4307409 DOI: 10.1021/Bi00830A014 |
0.321 |
|
1968 |
Scrutton MC, Mildvan AS. Pyruvate carboxylase. XI. Nuclear magnetic resonance studies of the properties of the bound manganese after interaction of the biotin residues with avidin. Biochemistry. 7: 1490-505. PMID 5677837 DOI: 10.1021/Bi00844A036 |
0.379 |
|
1967 |
Mildvan AS, Leigh JS, Cohn M. Kinetic and magnetic resonance studies of pyruvate kinase. 3. The enzyme-metal-phosphoryl bridge complex in the fluorokinase reaction. Biochemistry. 6: 1805-18. PMID 6035920 DOI: 10.1021/Bi00858A032 |
0.688 |
|
1966 |
Mildvan AS, Cohn M. Kinetic and magnetic resonance studies of the pyruvate kinase reaction. II. Complexes of enzyme, metal, and substrates. The Journal of Biological Chemistry. 241: 1178-93. PMID 5933875 |
0.565 |
|
1965 |
MILDVAN AS, COHN M. KINETIC AND MAGNETIC RESONANCE STUDIES OF THE PYRUVATE KINASE REACTION. I. DIVALENT METAL COMPLEXES OF PYRUVATE KINASE. The Journal of Biological Chemistry. 240: 238-46. PMID 14253420 |
0.511 |
|
1964 |
Mildvan A, Cohn M. Corrections - Magnetic Resonance Studies of the Interaction of the Manganous Ion with Bovine Serum Albumin Biochemistry. 3: 469-469. DOI: 10.1021/Bi00891A604 |
0.545 |
|
1963 |
MILDVAN AS, COHN M. MAGNETIC RESONANCE STUDIES OF THE INTERACTION OF THE MANGANOUS ION WITH BOVINE SERUM ALBUMIN. Biochemistry. 2: 910-9. PMID 14087380 DOI: 10.1021/Bi00905A003 |
0.544 |
|
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