Year |
Citation |
Score |
1999 |
Burke JR, Witmer MR, Zusi FC, Gregor KR, Davern LB, Padmanabha R, Swann RT, Smith D, Tredup JA, Micanovic R, Manly SP, Villafranca JJ, Tramposch KM. Competitive, reversible inhibition of cytosolic phospholipase A2 at the lipid-water interface by choline derivatives that partially partition into the phospholipid bilayer. The Journal of Biological Chemistry. 274: 18864-71. PMID 10383382 DOI: 10.1074/Jbc.274.27.18864 |
0.349 |
|
1997 |
Emanuele JJ, Jin H, Yanchunas J, Villafranca JJ. Evaluation of the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase. Biochemistry. 36: 7264-71. PMID 9188728 DOI: 10.1021/Bi970266R |
0.38 |
|
1997 |
Burke JR, Guenther MG, Witmer MR, Tredup JA, Hail ME, Micanovic R, Villafranca JJ. Presence of glycerol masks the effects of phosphorylation on the catalytic efficiency of cytosolic phospholipase A2. Archives of Biochemistry and Biophysics. 341: 177-85. PMID 9143367 DOI: 10.1006/Abbi.1997.9974 |
0.428 |
|
1997 |
Axley MJ, Fairman R, Yanchunas J, Villafranca JJ, Robertson JG. Spectroscopic properties of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase. Biochemistry. 36: 812-22. PMID 9020779 DOI: 10.1021/Bi962260S |
0.418 |
|
1996 |
Emanuele JJ, Jin H, Jacobson BL, Chang CY, Einspahr HM, Villafranca JJ. Kinetic and crystallographic studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase. Protein Science : a Publication of the Protein Society. 5: 2566-74. PMID 8976565 DOI: 10.1002/Pro.5560051219 |
0.366 |
|
1996 |
Reynaldo LP, Villafranca JJ, Horrocks WD. Investigating the effects of posttranslational adenylylation on the metal binding sites of Escherichia coli glutamine synthetase using lanthanide luminescence spectroscopy. Protein Science : a Publication of the Protein Society. 5: 2532-44. PMID 8976562 DOI: 10.1002/Pro.5560051216 |
0.756 |
|
1996 |
Jin H, Emanuele JJ, Fairman R, Robertson JG, Hail ME, Ho HT, Falk PJ, Villafranca JJ. Structural studies of Escherichia coli UDP-N-acetylmuramate:L-alanine ligase. Biochemistry. 35: 1423-31. PMID 8634272 DOI: 10.1021/Bi952334K |
0.395 |
|
1995 |
Abell LM, Schineller J, Keck PJ, Villafranca JJ. Effect of metal-ligand mutations on phosphoryl transfer reactions catalyzed by Escherichia coli glutamine synthetase. Biochemistry. 34: 16695-702. PMID 8527443 DOI: 10.1021/bi00051a018 |
0.315 |
|
1995 |
Robertson JG, Yanchunas J, Villafranca JJ. Dimerization of native and C-terminally proteolyzed p56lck tyrosine kinase. Archives of Biochemistry and Biophysics. 317: 259-66. PMID 7872793 DOI: 10.1006/Abbi.1995.1161 |
0.389 |
|
1995 |
Witmer MR, Micanovic R, Tredup J, Lin W, Hail M, Villafranca JJ. Active recombinant human cytosolic phospholipase A2 is expressed in Escherichia coli. Archives of Biochemistry and Biophysics. 318: 430-8. PMID 7733674 DOI: 10.1006/Abbi.1995.1251 |
0.419 |
|
1995 |
Dhalla AM, Yanchunas J, Ho HT, Falk PJ, Villafranca JJ, Robertson JG. Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase. Biochemistry. 34: 5390-402. PMID 7727397 DOI: 10.1021/Bi00016A010 |
0.442 |
|
1995 |
Burke JR, Witmer MR, Tredup J, Micanovic R, Gregor KR, Lahiri J, Tramposch KM, Villafranca JJ. Cooperativity and binding in the mechanism of cytosolic phospholipase A2. Biochemistry. 34: 15165-74. PMID 7578131 DOI: 10.1021/Bi00046A024 |
0.419 |
|
1994 |
Kulathila R, Consalvo AP, Fitzpatrick PF, Freeman JC, Snyder LM, Villafranca JJ, Merkler DJ. Bifunctional peptidylglcine alpha-amidating enzyme requires two copper atoms for maximum activity. Archives of Biochemistry and Biophysics. 311: 191-5. PMID 8185317 DOI: 10.1006/Abbi.1994.1225 |
0.589 |
|
1994 |
Robertson JG, Adams GW, Medzihradszky KF, Burlingame AL, Villafranca JJ. Complete assignment of disulfide bonds in bovine dopamine beta-hydroxylase. Biochemistry. 33: 11563-75. PMID 7918370 DOI: 10.1021/Bi00204A019 |
0.325 |
|
1994 |
Dhalla AM, Li B, Alibhai MF, Yost KJ, Hemmingsen JM, Atkins WM, Schineller J, Villafranca JJ. Regeneration of catalytic activity of glutamine synthetase mutants by chemical activation: exploration of the role of arginines 339 and 359 in activity. Protein Science : a Publication of the Protein Society. 3: 476-81. PMID 7912599 DOI: 10.1002/Pro.5560030313 |
0.392 |
|
1994 |
Alibhai M, Villafranca JJ. Kinetic and mutagenic studies of the role of the active site residues Asp-50 and Glu-327 of Escherichia coli glutamine synthetase. Biochemistry. 33: 682-6. PMID 7904829 DOI: 10.1021/Bi00169A008 |
0.478 |
|
1994 |
Witmer MR, Palmieri-Young D, Villafranca JJ. Probing the catalytic roles of n2-site glutamate residues in Escherichia coli glutamine synthetase by mutagenesis. Protein Science : a Publication of the Protein Society. 3: 1746-59. PMID 7849593 DOI: 10.1002/Pro.5560031015 |
0.481 |
|
1994 |
Witmer MR, Palmieri-Young D, Villafranca JJ. Mutagenesis of n2-site Metal-Binding Glutamate Residues in E. coli Glutamine Synthetase Techniques in Protein Chemistry. 5: 321-329. DOI: 10.1016/B978-0-12-194710-1.50041-2 |
0.421 |
|
1993 |
Freeman JC, Nayar PG, Begley TP, Villafranca JJ. Stoichiometry and spectroscopic identity of copper centers in phenoxazinone synthase: a new addition to the blue copper oxidase family. Biochemistry. 32: 4826-30. PMID 8387816 DOI: 10.1021/Bi00069A018 |
0.327 |
|
1993 |
Robertson JG, Villafranca JJ. Characterization of metal ion activation and inhibition of CTP synthetase. Biochemistry. 32: 3769-77. PMID 8385490 DOI: 10.1021/Bi00065A032 |
0.461 |
|
1993 |
Liaw SH, Villafranca JJ, Eisenberg D. A model for oxidative modification of glutamine synthetase, based on crystal structures of mutant H269N and the oxidized enzyme. Biochemistry. 32: 7999-8003. PMID 8102250 DOI: 10.1021/Bi00082A022 |
0.434 |
|
1993 |
Atkins WM, Cader BM, Hemmingsen J, Villafranca JJ. Time-resolved fluorescence and computational studies of adenylylated glutamine synthetase: analysis of intersubunit interactions. Protein Science : a Publication of the Protein Society. 2: 800-13. PMID 8098638 DOI: 10.1002/Pro.5560020510 |
0.372 |
|
1993 |
Freeman JC, Villafranca JJ, Merkler DJ. Redox cycling of enzyme-bound copper during peptide amidation Journal of the American Chemical Society. 115: 4923-4924. DOI: 10.1021/Ja00064A077 |
0.321 |
|
1993 |
Reynaldo LP, Maruyama T, Horrocks WD, Villafranca J. Tb3+ luminescence studies of Escherichia coli glutamine synthetase provides metal ion binding constants. Journal of Inorganic Biochemistry. 51: 170. DOI: 10.1016/0162-0134(93)85206-N |
0.737 |
|
1992 |
Atkins WM, Villafranca JJ. Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes. Protein Science : a Publication of the Protein Society. 1: 342-55. PMID 1363912 DOI: 10.1002/Pro.5560010306 |
0.373 |
|
1992 |
Robertson JG, Sparvero LJ, Villafranca JJ. Inactivation and covalent modification of CTP synthetase by thiourea dioxide. Protein Science : a Publication of the Protein Society. 1: 1298-307. PMID 1303749 DOI: 10.1002/Pro.5560011009 |
0.409 |
|
1992 |
Villafranca JJ, Nowak T. 2 Metal Ions at Enzyme Active Sites Enzymes. 20: 63-94. DOI: 10.1016/S1874-6047(08)60020-7 |
0.447 |
|
1992 |
Villafranca JJ, Freeman J, Kotchevar A. Mechanisms of copper enzymes Journal of Inorganic Biochemistry. 47: 35. DOI: 10.1016/0162-0134(92)84106-W |
0.357 |
|
1991 |
Klinman JP, Dooley DM, Duine JA, Knowles PF, Mondovi B, Villafranca JJ. Status of the cofactor identity in copper oxidative enzymes. Febs Letters. 282: 1-4. PMID 1851106 DOI: 10.1016/0014-5793(91)80431-2 |
0.388 |
|
1991 |
Abell LM, Villafranca JJ. Investigation of the mechanism of phosphinothricin inactivation of Escherichia coli glutamine synthetase using rapid quench kinetic technique. Biochemistry. 30: 6135-41. PMID 1676298 DOI: 10.1021/Bi00239A008 |
0.469 |
|
1991 |
Lin WY, Dombrosky P, Atkins WM, Villafranca JJ. Terbium(III) luminescence study of tyrosine emission from Escherichia coli glutamine synthetase. Biochemistry. 30: 3427-31. PMID 1672823 DOI: 10.1021/Bi00228A011 |
0.399 |
|
1991 |
Lin WY, Eads CD, Villafranca JJ. Fluorescent probes for measuring the binding constants and distances between the metal ions bound to Escherichia coli glutamine synthetase. Biochemistry. 30: 3421-6. PMID 1672822 DOI: 10.1021/Bi00228A010 |
0.458 |
|
1991 |
McNemar LS, Lin WY, Eads CD, Atkins WM, Dombrosky P, Villafranca JJ. Terbium(III) luminescence study of the spatial relationship of tryptophan residues to the two metal ion binding sites of Escherichia coli glutamine synthetase. Biochemistry. 30: 3417-21. PMID 1672821 DOI: 10.1021/Bi00228A009 |
0.46 |
|
1991 |
Atkins WM, Stayton PS, Villafranca JJ. Time-resolved fluorescence studies of genetically engineered Escherichia coli glutamine synthetase. Effects of ATP on the tryptophan-57 loop. Biochemistry. 30: 3406-16. PMID 1672820 DOI: 10.1021/Bi00228A008 |
0.386 |
|
1991 |
Abell LM, Villafranca JJ. Effect of metal ions and adenylylation state on the internal thermodynamics of phosphoryl transfer in the Escherichia coli glutamine synthetase reaction. Biochemistry. 30: 1413-8. PMID 1671336 DOI: 10.1021/Bi00219A035 |
0.486 |
|
1991 |
Villafranca JJ. Metal-assisted catalysis Current Opinion in Structural Biology. 1: 821-825. DOI: 10.1016/0959-440X(91)90185-V |
0.413 |
|
1990 |
Robertson JG, Desai PR, Kumar A, Farrington GK, Fitzpatrick PF, Villafranca JJ. Primary amino acid sequence of bovine dopamine beta-hydroxylase. The Journal of Biological Chemistry. 265: 1029-35. PMID 2295597 |
0.462 |
|
1990 |
Logusch EW, Walker DM, McDonald JF, Franz JE, Villafranca JJ, DiIanni CL, Colanduoni JA, Li B, Schineller JB. Inhibition of Escherichia coli glutamine synthetase by alpha- and gamma-substituted phosphinothricins. Biochemistry. 29: 366-72. PMID 1967948 DOI: 10.1021/Bi00454A009 |
0.435 |
|
1989 |
Pember SO, Johnson KA, Villafranca JJ, Benkovic SJ. Mechanistic studies on phenylalanine hydroxylase from Chromobacterium violaceum. Evidence for the formation of an enzyme-oxygen complex. Biochemistry. 28: 2124-30. PMID 2719947 DOI: 10.1021/Bi00431A024 |
0.39 |
|
1989 |
Villafranca JJ. Positional isotope exchange using phosphorus-31 nuclear magnetic resonance. Methods in Enzymology. 177: 390-403. PMID 2607989 DOI: 10.1016/0076-6879(89)77022-1 |
0.383 |
|
1989 |
Villafranca JJ. Paramagnetic probes of macromolecules. Methods in Enzymology. 177: 403-13. PMID 2575205 DOI: 10.1016/0076-6879(89)77023-3 |
0.393 |
|
1989 |
Di Ianni CL, Villafranca JJ. Identification of amino acid residues modified by pyridoxal 5'-phosphate in Escherichia coli glutamine synthetase. The Journal of Biological Chemistry. 264: 8686-91. PMID 2566607 |
0.301 |
|
1989 |
Lewis DA, Villafranca JJ. Investigation of the mechanism of CTP synthetase using rapid quench and isotope partitioning methods. Biochemistry. 28: 8454-9. PMID 2532543 DOI: 10.1021/Bi00447A027 |
0.361 |
|
1988 |
Raushel FM, Villafranca JJ. Positional isotope exchange. Crc Critical Reviews in Biochemistry. 23: 1-26. PMID 3284712 |
0.453 |
|
1988 |
Kasprzak AA, Villafranca JJ. Interactive binding between the substrate and allosteric sites of carbamoyl-phosphate synthetase. Biochemistry. 27: 8050-6. PMID 3069127 DOI: 10.1021/Bi00421A012 |
0.434 |
|
1988 |
Eads CD, LoBrutto R, Kumar A, Villafranca JJ. Identification of nonprotein ligands to the metal ions bound to glutamine synthetase. Biochemistry. 27: 165-70. PMID 2894845 DOI: 10.1021/Bi00401A025 |
0.378 |
|
1988 |
McCracken J, Desai PR, Papadopoulos NJ, Villafranca JJ, Peisach J. Electron spin-echo studies of the copper(II) binding sites in dopamine beta-hydroxylase. Biochemistry. 27: 4133-7. PMID 2843225 DOI: 10.1021/Bi00411A034 |
0.353 |
|
1988 |
Wang HC, Ciskanik L, Dunaway-Mariano D, von der Saal W, Villafranca JJ. Investigations of the partial reactions catalyzed by pyruvate phosphate dikinase. Biochemistry. 27: 625-33. PMID 2831971 DOI: 10.1021/Bi00402A020 |
0.373 |
|
1988 |
McCracken J, Pember S, Benkovic SJ, Villafranca JJ, Miller RJ, Peisach J. Electron spin-echo studies of the copper binding site in phenylalanine hydroxylase from Chromobacterium violaceum Journal of the American Chemical Society. 110: 1069-1074. DOI: 10.1021/Ja00212A012 |
0.327 |
|
1988 |
Flory DR, Villafranca JJ. Characterization of 3-phenylpropenes as mechanism-based inhibitors of dopamine β-hydroxylase Bioorganic Chemistry. 16: 232-244. DOI: 10.1016/0045-2068(88)90012-0 |
0.327 |
|
1987 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors of dopamine beta-hydroxylase. Archives of Biochemistry and Biophysics. 257: 231-50. PMID 3662525 DOI: 10.1016/0003-9861(87)90563-7 |
0.483 |
|
1987 |
Colombo G, Papadopoulos NJ, Ash DE, Villafranca JJ. Characterization of highly purified dopamine beta-hydroxylase. Archives of Biochemistry and Biophysics. 252: 71-80. PMID 3101599 DOI: 10.1016/0003-9861(87)90009-9 |
0.44 |
|
1987 |
Colanduoni J, Nissan R, Villafranca JJ. Studies of the mechanism of glutamine synthetase utilizing pH-dependent behavior in catalysis and binding. The Journal of Biological Chemistry. 262: 3037-43. PMID 2880845 |
0.335 |
|
1987 |
Eads CD, Villafranca JJ. Interaction among substrates, inhibitors and Mn2+ bound to glutamine synthetase as studied by NMR relaxation rate measurements. Archives of Biochemistry and Biophysics. 252: 382-7. PMID 2880564 DOI: 10.1016/0003-9861(87)90044-0 |
0.466 |
|
1987 |
Pember SO, Benkovic SJ, Villafranca JJ, Pasenkiewicz-Gierula M, Antholine WE. Adduct formation between the cupric site of phenylalanine hydroxylase from Chromobacterium violaceum and 6,7-dimethyltetrahydropterin. Biochemistry. 26: 4477-83. PMID 2822093 DOI: 10.1021/Bi00388A045 |
0.404 |
|
1986 |
Fitzpatrick PF, Harpel MR, Villafranca JJ. Use of alternate substrates to probe the order of substrate addition to dopamine beta-hydroxylase. Archives of Biochemistry and Biophysics. 249: 70-5. PMID 3740855 DOI: 10.1016/0003-9861(86)90561-8 |
0.581 |
|
1986 |
Pember SO, Villafranca JJ, Benkovic SJ. Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme. Biochemistry. 25: 6611-9. PMID 3024714 DOI: 10.1021/Bi00369A042 |
0.426 |
|
1986 |
Fitzpatrick PF, Villafranca JJ. The mechanism of inactivation of dopamine beta-hydroxylase by hydrazines. The Journal of Biological Chemistry. 261: 4510-8. PMID 3007460 |
0.533 |
|
1986 |
DiIanni CL, Colanduoni JA, Villafranca JJ. Inactivation of Escherichia coli glutamine synthetase by thiourea trioxide Bioorganic Chemistry. 14: 242-248. DOI: 10.1016/0045-2068(86)90035-0 |
0.403 |
|
1986 |
Colanduoni JA, Villafranca JJ. Inhibition of Escherichia coli glutamine synthetase by phosphinothricin Bioorganic Chemistry. 14: 163-169. DOI: 10.1016/0045-2068(86)90026-X |
0.392 |
|
1985 |
Fitzpatrick PF, Flory DR, Villafranca JJ. 3-Phenylpropenes as mechanism-based inhibitors of dopamine beta-hydroxylase: evidence for a radical mechanism. Biochemistry. 24: 2108-14. PMID 3995005 DOI: 10.1021/Bi00330A003 |
0.555 |
|
1985 |
von der Saal W, Crysler CS, Villafranca JJ. Positional isotope exchange and kinetic experiments with Escherichia coli guanosine-5'-monophosphate synthetase. Biochemistry. 24: 5343-50. PMID 3907701 DOI: 10.1021/Bi00341A011 |
0.369 |
|
1985 |
Eads CD, Mulqueen P, Horrocks WD, Villafranca JJ. Comparative study of glutamine synthetase bound lanthanide(III) ions using NMR relaxation and lanthanide(III) luminescence techniques. Biochemistry. 24: 1221-6. PMID 2869779 DOI: 10.1021/Bi00326A025 |
0.429 |
|
1985 |
Villafranca JJ, Ransom SC, Gibbs EJ. Biophysical studies of Escherichia coli glutamine synthetase. Current Topics in Cellular Regulation. 26: 207-19. PMID 2866935 DOI: 10.1016/B978-0-12-152826-3.50023-1 |
0.494 |
|
1985 |
Clark DD, Villafranca JJ. Isotope-exchange enhancement studies of Escherichia coli glutamine synthetase. Biochemistry. 24: 5147-52. PMID 2866792 DOI: 10.1021/Bi00340A029 |
0.441 |
|
1985 |
Ransom SC, Colanduoni JA, Eads CD, Gibbs EJ, Villafranca JJ. Affinity labeling of Escherichia coli glutamine synthetase by beta, gamma-Cr(III)(H2O)4ATP. Biochemical and Biophysical Research Communications. 130: 418-25. PMID 2862863 DOI: 10.1016/0006-291X(85)90433-4 |
0.455 |
|
1985 |
Colanduoni JA, Villafranca JJ. Labeling of a specific arginine residue at the active site of glutamine synthetase (E.coli). Biochemical and Biophysical Research Communications. 126: 412-8. PMID 2857563 DOI: 10.1016/0006-291X(85)90621-7 |
0.454 |
|
1985 |
Kasprzyk PG, Whalen-Pederson E, Anderson PM, Villafranca JJ. Spatial relationships among the active and allosteric sites of carbamoyl-phosphate synthetase Bioorganic Chemistry. 13: 98-109. DOI: 10.1016/0045-2068(85)90012-4 |
0.418 |
|
1985 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors of dopamine β-hydroxylase containing acetylenic or cyclopropyl groups Journal of the American Chemical Society. 107: 5022-5023. DOI: 10.1002/Chin.198549099 |
0.489 |
|
1985 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors for dopamine β-hydroxylase containing vinyl, acetylenic, or cyclopropyl substituents: Evidence for a radical mechanism Federation Proceedings. 44: No. 5777. |
0.439 |
|
1984 |
Rajashekhar B, Fitzpatrick PF, Colombo G, Villafranca JJ. Synthesis of several 2-substituted 3-(p-hydroxyphenyl)-1-propenes and their characterization as mechanism-based inhibitors of dopamine beta-hydroxylase. The Journal of Biological Chemistry. 259: 6925-30. PMID 6547138 |
0.511 |
|
1984 |
Colombo G, Rajashekhar B, Giedroc DP, Villafranca JJ. Mechanism-based inhibitors of dopamine beta-hydroxylase: inhibition by 2-bromo-3-(p-hydroxyphenyl)-1-propene. Biochemistry. 23: 3590-8. PMID 6477886 DOI: 10.1021/Bi00311A004 |
0.393 |
|
1984 |
Gibbs EJ, Ransom SC, Cuppett S, Villafranca JJ. Mn-Mn interaction in adenylylated and unadenylylated glutamine synthetase. Biochemical and Biophysical Research Communications. 120: 939-45. PMID 6145412 DOI: 10.1016/S0006-291X(84)80197-7 |
0.43 |
|
1984 |
Knight WB, Dunaway-Mariano D, Ransom SC, Villafranca JJ. Investigations of the metal ion-binding sites of yeast inorganic pyrophosphatase. The Journal of Biological Chemistry. 259: 2886-95. PMID 6142048 |
0.367 |
|
1983 |
Pasternack RF, Gibbs EJ, Villafranca JJ. Interactions of porphyrins with nucleic acids. Biochemistry. 22: 2406-14. PMID 6860636 DOI: 10.1021/Bi00279A016 |
0.336 |
|
1983 |
Kasprzyk PG, Anderson PM, Villafranca JJ. Fluorescence energy transfer experiments with Escherichia coli carbamoyl-phosphate synthetase. Biochemistry. 22: 1877-82. PMID 6342671 DOI: 10.1021/Bi00277A021 |
0.37 |
|
1983 |
Raushel FM, Anderson PM, Villafranca JJ. A nuclear magnetic resonance study of the topography of binding sites of Escherichia coli carbamoyl-phosphate synthetase. Biochemistry. 22: 1872-6. PMID 6342670 DOI: 10.1021/Bi00277A020 |
0.6 |
|
1983 |
Viola RE, Shaw RW, Ransom SC, Villafranca JJ. Solvent proton relaxation studies of cytochrome c oxidase solutions. Archives of Biochemistry and Biophysics. 220: 106-15. PMID 6299195 DOI: 10.1016/0003-9861(83)90392-2 |
0.654 |
|
1983 |
Villafranca J, Ransom S, Gibbs E, Knight W, Dunaway-Mariano D. Metalmetal interactions in enzymes: EPR and NMR investigations Inorganica Chimica Acta. 79: 18. DOI: 10.1016/S0020-1693(00)95036-9 |
0.499 |
|
1982 |
Villafranca JJ, Raushel FM. The monovalent cation site of pyruvate kinase and other enzymes: NMR investigations. Federation Proceedings. 41: 2961-5. PMID 7140996 |
0.553 |
|
1982 |
Meek TD, Johnson KA, Villafranca JJ. Escherichia coli glutamine synthetase. Determination of rate-limiting steps by rapid-quench and isotope partitioning experiments. Biochemistry. 21: 2158-67. PMID 6124275 DOI: 10.1021/Bi00538A027 |
0.324 |
|
1981 |
Cunningham BA, Raushel FM, Villafranca JJ, Benkovic SJ. Distances between structural metal ion, substrates, and allosteric modifier of fructose bisphosphatase. Biochemistry. 20: 359-62. PMID 6258638 DOI: 10.1021/Bi00505A020 |
0.599 |
|
1980 |
Raushel FM, Villafranca JJ. A multinuclear nuclear magnetic resonance study of the monovalent-divalent cation sites of pyruvate kinase. Biochemistry. 19: 5481-5. PMID 7193048 DOI: 10.1021/Bi00565A003 |
0.61 |
|
1980 |
Raushel FM, Villafranca JJ. Phosphorus-31 nuclear magnetic resonance application to positional isotope exchange reactions catalyzed by Escherichia coli carbamoyl-phosphate synthetase: analysis of forward and reverse enzymatic reactions. Biochemistry. 19: 3170-4. PMID 6996701 DOI: 10.1021/Bi00555A009 |
0.508 |
|
1980 |
Pillai RP, Marshall M, Villafranca JJ. Substrate and metal ion binding to carbamate kinase: NMR and EPR studies. Archives of Biochemistry and Biophysics. 199: 21-7. PMID 6243908 DOI: 10.1016/0003-9861(80)90251-9 |
0.442 |
|
1980 |
Pillai RP, Marshall M, Villafranca JJ. Modification of an essential arginine of carbamate kinase. Archives of Biochemistry and Biophysics. 199: 16-20. PMID 6243907 DOI: 10.1016/0003-9861(80)90250-7 |
0.469 |
|
1980 |
Meek TD, Villafranca JJ. Kinetic mechanism of Escherichia coli glutamine synthetase. Biochemistry. 19: 5513-9. PMID 6109545 DOI: 10.1021/Bi00565A008 |
0.324 |
|
1980 |
Villafranca JJ, Raushel FM. Biophysical applications of NMR to phosphoryl transfer enzymes and metal nuclei of metalloproteins. Annual Review of Biophysics and Bioengineering. 9: 363-92. PMID 6104944 DOI: 10.1146/annurev.bb.09.060180.002051 |
0.513 |
|
1980 |
Pillai RP, Raushel FM, Villafranca JJ. Stereochemistry of binding of thiophosphate analogs of ATP and ADP to carbamate kinase, glutamine synthetase, and carbamoyl-phosphate synthetase. Archives of Biochemistry and Biophysics. 199: 7-15. PMID 6101943 DOI: 10.1016/0003-9861(80)90249-0 |
0.589 |
|
1980 |
Raushel FM, Villafranca JJ. A direct NMR method for the determination of correlation times in enzyme complexes involving monovalent cations and paramagnetic centers Journal of the American Chemical Society. 102: 6618-6619. DOI: 10.1021/Ja00541A067 |
0.555 |
|
1979 |
Raushel FM, Rawding CJ, Anderson PM, Villafranca JJ. Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry. 18: 5562-6. PMID 229896 DOI: 10.1021/Bi00592A006 |
0.576 |
|
1979 |
Raushel FM, Villafranca JJ. Determination of rate-limiting steps of Escherichia coli carbamoyl-phosphate synthase. Rapid quench and isotope partitioning experiments. Biochemistry. 18: 3424-9. PMID 223631 DOI: 10.1021/Bi00582A033 |
0.536 |
|
1979 |
Villafranca JJ, Balakrishnan MS. Glutamine synthetase: biophysical studies of structure-function-control relationships. The International Journal of Biochemistry. 10: 565-71. PMID 38153 DOI: 10.1016/0020-711X(79)90016-8 |
0.493 |
|
1979 |
Viola RE, Hartzell CR, Villafranca JJ. Copper(II) complexes of carnosine, glycylglycine, and glycylglycine-imidazole mixtures Journal of Inorganic Biochemistry. 10: 293-307. DOI: 10.1016/S0162-0134(00)80196-8 |
0.589 |
|
1978 |
Raushel FM, Anderson PM, Villafranca JJ. Kinetic mechanism of Escherichia coli carbamoyl-phosphate synthetase. Biochemistry. 17: 5587-91. PMID 215204 DOI: 10.1021/Bi00619A001 |
0.575 |
|
1978 |
Raushel FM, Anderson PM, Villafranca JJ. Carbamyl phosphate synthetase of Escherichia coli uses the same diastereomer of adenosine-5'-[2-thiotriphosphate] at both ATP sites. The Journal of Biological Chemistry. 253: 6627-9. PMID 211124 |
0.5 |
|
1978 |
Balakrishnan MS, Sharp TR, Villafranca JJ. Kinetic studies of 18O exchange from inorganic phosphate catalyzed by Mg2+-activated unadenylylated glutamine synthetase (E. coli w). Biochemical and Biophysical Research Communications. 85: 991-8. PMID 32887 DOI: 10.1016/0006-291X(78)90641-1 |
0.336 |
|
1978 |
Balakrishnan MS, Villafranca JJ. Distance determinations between the metal ion sites of Escherichia coli glutamine synthetase by electron paramagnetic resonance using Cr(III)--nucleotides as paramagnetic substrate analogues. Biochemistry. 17: 3531-8. PMID 28753 DOI: 10.1021/Bi00610A017 |
0.435 |
|
1977 |
Villafranca JJ, Levy RS, Kernich J, Vickroy T. TPN and Mn-isocitrate protect isocitrate dehydrogenase against inactivation but increase the number of modified sulfhydryl groups. Biochemical and Biophysical Research Communications. 77: 457-63. PMID 20091 DOI: 10.1016/S0006-291X(77)80002-8 |
0.404 |
|
1977 |
Balakrishnan MS, Villafranca JJ, Brenchley JE. Glutamine synthetase from Salmonella typhimurium: manganese(II), substrate, and inhibitor interaction with the unadenylylated enzyme. Archives of Biochemistry and Biophysics. 181: 603-15. PMID 20051 DOI: 10.1016/0003-9861(77)90267-3 |
0.49 |
|
1977 |
Levy RS, Villafranca JJ. Structure-function relationships in TPN-dependent isocitrate dehydrogenase. II. Determination of the paramagnetic relaxation rates of water protons in complexes of enzyme, Mn(II), substrates, cofactors, and inhibitors. Biochemistry. 16: 3301-9. PMID 19045 DOI: 10.1021/Bi00634A004 |
0.392 |
|
1977 |
Levy RS, Villafranca JJ. Structure-function relationships in TPN-dependent isocitrate dehydrogenase. I. Electron paramagnetic resonance studies of the interaction of enzyme-bound Mn(II) with substrates, cofactors, and substrate analogues. Biochemistry. 16: 3293-31. PMID 19044 DOI: 10.1021/Bi00634A003 |
0.456 |
|
1977 |
Villafranca JJ, Balakrishnan MS, Wedler FC. Determination of metal-metal distances in E. coli glutamine synthetase by EPR. Biochemical and Biophysical Research Communications. 75: 464-71. PMID 15566 DOI: 10.1016/0006-291X(77)91065-8 |
0.447 |
|
1976 |
Villafranca JJ, Ash DE, Wedler FC. Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). I. Temperature and frequency dependent nuclear magnetic resonance studies. Biochemistry. 15: 536-43. PMID 766828 DOI: 10.1021/Bi00648A013 |
0.484 |
|
1976 |
Villafranca JJ, Pillai RP, Woodworth RC. Magnetic resonance studies of Mn(II)-, Mn(III)-, and Fe(III)-conalbumin complexes. Bioinorganic Chemistry. 6: 233-45. PMID 233741 DOI: 10.1016/S0006-3061(00)80230-6 |
0.361 |
|
1976 |
Villafranca JJ, Ash DE, Wedler FC. Manganese (II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli w). II. Electron paramagnetic resonance and nuclear magnetic resonance studies of enzyme-bound manganese(II) with substrates and a potential transition-state analogue, methionine sulfoximine. Biochemistry. 15: 544-53. PMID 3200 DOI: 10.1021/Bi00648A014 |
0.463 |
|
1976 |
Viola RE, Hartzell CR, Villafranca JJ. Temperature Dependence of the EPR Spectrum of Copper(II)- carnosine Journal of Coordination Chemistry. 6: 119-121. DOI: 10.1080/00958977608079895 |
0.551 |
|
1975 |
Villafranca JJ, Ash DE, Wedler FC. Evidence for methionine sulfoximine as a transition-state analog for glutamine synthetase from NMR and EPR data Biochemical and Biophysical Research Communications. 66: 1003-1010. PMID 241345 DOI: 10.1016/0006-291X(75)90739-1 |
0.492 |
|
1975 |
Libby CB, Frey WA, Villafranca JJ, Benkovic SJ. Kinetic and binding studies of Mn (II) and fructose 1,6-bisphosphate with rabbit liver hexosebisphosphatase. The Journal of Biological Chemistry. 250: 7564-73. PMID 240832 |
0.415 |
|
1974 |
Villafranca JJ, Platus E. Fluorocitrate inhibition of aconitase. Reversibility of the inactivation. Biochemical and Biophysical Research Communications. 55: 1197-207. PMID 4771993 DOI: 10.1016/S0006-291X(73)80021-X |
0.372 |
|
1974 |
Villafranca JJ, Viola RE. Proton nuclear magnetic resonance studies of the manganese (II) binding site of concanavalin A. Effect of saccharides on the solvent relaxation rates. Archives of Biochemistry and Biophysics. 165: 51-9. PMID 4441085 DOI: 10.1016/0003-9861(74)90140-4 |
0.6 |
|
1974 |
Villafranca JJ, Viola RE. The use of 13C spin lattice relaxation times to study the interaction of alpha-methyl-D-glucopyranoside with concanavalin A. Archives of Biochemistry and Biophysics. 160: 465-8. PMID 4364767 DOI: 10.1016/0003-9861(74)90422-6 |
0.581 |
|
1974 |
Benkovic SJ, Frey WA, Libby CB, Villafranca JJ. The role of tryptophan in neutral fructose diphosphatase. Biochemical and Biophysical Research Communications. 57: 196-203. PMID 4364002 DOI: 10.1016/S0006-291X(74)80376-1 |
0.364 |
|
1974 |
Villafranca JJ, Colman RF. Frequency and temperature dependence of the proton relaxation rates of solvent and substrate interaction with isocitrate dehydrogenase bound Mn(II). Biochemistry. 13: 1152-60. PMID 4360780 DOI: 10.1021/Bi00703A016 |
0.341 |
|
1974 |
Villafranca JJ, Wedler FC. Nuclear magnetic resonance study of the complexes of manganese(II) and fully adenylated glutamine synthetase (Escherichia coli W). Frequency, temperature, and substrate dependence of water proton relaxation rates. Biochemistry. 13: 3286-91. PMID 4152181 DOI: 10.1021/Bi00713A017 |
0.34 |
|
1973 |
Benkovic SJ, Villafranca JJ, Kleinschuster JJ. 31 P and 13 C nmr measurements of a fructose-1-phosphate, Mn (II) and fructose 1,6-diphosphatase complex. Archives of Biochemistry and Biophysics. 155: 458-63. PMID 4350254 DOI: 10.1016/0003-9861(73)90137-9 |
0.349 |
|
1971 |
Villafranca JJ, Axelrod B. Heptulose synthesis from nonphosphorylated aldoses and ketoses by spinach transketolase. The Journal of Biological Chemistry. 246: 3126-31. PMID 5574390 |
0.414 |
|
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