| Year |
Citation |
Score |
| 2013 |
Reinhardt LA, Thoden JB, Peters GS, Holden HM, Cleland WW. pH-rate profiles support a general base mechanism for galactokinase (Lactococcus lactis). Febs Letters. 587: 2876-81. PMID 23872454 DOI: 10.1016/J.Febslet.2013.07.017 |
0.438 |
|
| 2012 |
Adina-Zada A, Sereeruk C, Jitrapakdee S, Zeczycki TN, St Maurice M, Cleland WW, Wallace JC, Attwood PV. Roles of Arg427 and Arg472 in the binding and allosteric effects of acetyl CoA in pyruvate carboxylase. Biochemistry. 51: 8208-17. PMID 22985389 DOI: 10.1021/Bi301060D |
0.322 |
|
| 2012 |
Adina-Zada A, Zeczycki TN, St Maurice M, Jitrapakdee S, Cleland WW, Attwood PV. Allosteric regulation of the biotin-dependent enzyme pyruvate carboxylase by acetyl-CoA. Biochemical Society Transactions. 40: 567-72. PMID 22616868 DOI: 10.1042/Bst20120041 |
0.378 |
|
| 2012 |
Saylor BT, Reinhardt LA, Lu Z, Shukla MS, Nguyen L, Cleland WW, Angerhofer A, Allen KN, Richards NG. A structural element that facilitates proton-coupled electron transfer in oxalate decarboxylase. Biochemistry. 51: 2911-20. PMID 22404040 DOI: 10.1021/Bi300001Q |
0.329 |
|
| 2012 |
Smith BC, Anderson MA, Hoadley KA, Keck JL, Cleland WW, Denu JM. Structural and kinetic isotope effect studies of nicotinamidase (Pnc1) from Saccharomyces cerevisiae. Biochemistry. 51: 243-56. PMID 22229411 DOI: 10.1021/Bi2015508 |
0.425 |
|
| 2011 |
Zeczycki TN, Menefee AL, Jitrapakdee S, Wallace JC, Attwood PV, St Maurice M, Cleland WW. Activation and inhibition of pyruvate carboxylase from Rhizobium etli. Biochemistry. 50: 9694-707. PMID 21958066 DOI: 10.1021/Bi201276R |
0.348 |
|
| 2011 |
Zeczycki TN, Menefee AL, Adina-Zada A, Jitrapakdee S, Surinya KH, Wallace JC, Attwood PV, St Maurice M, Cleland WW. Novel insights into the biotin carboxylase domain reactions of pyruvate carboxylase from Rhizobium etli. Biochemistry. 50: 9724-37. PMID 21957995 DOI: 10.1021/Bi2012788 |
0.389 |
|
| 2011 |
Adina-Zada A, Hazra R, Sereeruk C, Jitrapakdee S, Zeczycki TN, St Maurice M, Cleland WW, Wallace JC, Attwood PV. Probing the allosteric activation of pyruvate carboxylase using 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate as a fluorescent mimic of the allosteric activator acetyl CoA. Archives of Biochemistry and Biophysics. 509: 117-26. PMID 21426897 DOI: 10.1016/J.Abb.2011.03.006 |
0.369 |
|
| 2010 |
Duangpan S, Jitrapakdee S, Adina-Zada A, Byrne L, Zeczycki TN, St Maurice M, Cleland WW, Wallace JC, Attwood PV. Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis. Biochemistry. 49: 3296-304. PMID 20230056 DOI: 10.1021/Bi901894T |
0.399 |
|
| 2010 |
Van Vleet J, Kleeb A, Kast P, Hilvert D, Cleland WW. 13C isotope effect on the reaction catalyzed by prephenate dehydratase. Biochimica Et Biophysica Acta. 1804: 752-4. PMID 19948253 DOI: 10.1016/J.Bbapap.2009.11.018 |
0.347 |
|
| 2009 |
Zeczycki TN, St Maurice M, Jitrapakdee S, Wallace JC, Attwood PV, Cleland WW. Insight into the carboxyl transferase domain mechanism of pyruvate carboxylase from Rhizobium etli. Biochemistry. 48: 4305-13. PMID 19341298 DOI: 10.1021/Bi9003759 |
0.39 |
|
| 2008 |
Jitrapakdee S, St Maurice M, Rayment I, Cleland WW, Wallace JC, Attwood PV. Structure, mechanism and regulation of pyruvate carboxylase. The Biochemical Journal. 413: 369-87. PMID 18613815 DOI: 10.1042/Bj20080709 |
0.34 |
|
| 2008 |
Adina-Zada A, Jitrapakdee S, Surinya KH, McIldowie MJ, Piggott MJ, Cleland WW, Wallace JC, Attwood PV. Insights into the mechanism and regulation of pyruvate carboxylase by characterisation of a biotin-deficient mutant of the Bacillus thermodenitrificans enzyme. The International Journal of Biochemistry & Cell Biology. 40: 1743-52. PMID 18272421 DOI: 10.1016/J.Biocel.2008.01.001 |
0.442 |
|
| 2008 |
Van Vleet JL, Reinhardt LA, Miller BG, Sievers A, Cleland WW. Carbon isotope effect study on orotidine 5'-monophosphate decarboxylase: support for an anionic intermediate. Biochemistry. 47: 798-803. PMID 18081312 DOI: 10.1021/Bi701664N |
0.484 |
|
| 2007 |
St Maurice M, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I. Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme. Science (New York, N.Y.). 317: 1076-9. PMID 17717183 DOI: 10.1126/Science.1144504 |
0.368 |
|
| 2007 |
Ralph EC, Hirschi JS, Anderson MA, Cleland WW, Singleton DA, Fitzpatrick PF. Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase. Biochemistry. 46: 7655-64. PMID 17542620 DOI: 10.1021/Bi700482H |
0.428 |
|
| 2007 |
Jitrapakdee S, Adina-Zada A, Besant PG, Surinya KH, Cleland WW, Wallace JC, Attwood PV. Differential regulation of the yeast isozymes of pyruvate carboxylase and the locus of action of acetyl CoA. The International Journal of Biochemistry & Cell Biology. 39: 1211-23. PMID 17478118 DOI: 10.1016/J.Biocel.2007.03.016 |
0.336 |
|
| 2007 |
Svedruzić D, Liu Y, Reinhardt LA, Wroclawska E, Cleland WW, Richards NG. Investigating the roles of putative active site residues in the oxalate decarboxylase from Bacillus subtilis. Archives of Biochemistry and Biophysics. 464: 36-47. PMID 17459326 DOI: 10.1016/J.Abb.2007.03.016 |
0.367 |
|
| 2006 |
Rawlings J, Cleland WW, Hengge AC. Metal-catalyzed phosphodiester cleavage: secondary 18O isotope effects as an indicator of mechanism. Journal of the American Chemical Society. 128: 17120-5. PMID 17177465 DOI: 10.1021/Ja065931A |
0.681 |
|
| 2006 |
Ralph EC, Anderson MA, Cleland WW, Fitzpatrick PF. Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase. Biochemistry. 45: 15844-52. PMID 17176107 DOI: 10.1021/Bi061894O |
0.402 |
|
| 2006 |
Cleland WW, Hengge AC. Enzymatic mechanisms of phosphate and sulfate transfer. Chemical Reviews. 106: 3252-78. PMID 16895327 DOI: 10.1021/Cr050287O |
0.611 |
|
| 2006 |
Anderson MA, Cleland WW, Huang DT, Chan C, Shojaei M, Christopherson RI. 13C and 15N isotope effects for conversion of L-dihydroorotate to N-carbamyl-L-aspartate using dihydroorotase from hamster and Bacillus caldolyticus. Biochemistry. 45: 7132-9. PMID 16752903 DOI: 10.1021/Bi0604025 |
0.419 |
|
| 2006 |
Poyner RR, Anderson MA, Bandarian V, Cleland WW, Reed GH. Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Journal of the American Chemical Society. 128: 7120-1. PMID 16734439 DOI: 10.1021/Ja060710Q |
0.353 |
|
| 2005 |
Wright SK, DeClue MS, Mandal A, Lee L, Wiest O, Cleland WW, Hilvert D. Isotope effects on the enzymatic and nonenzymatic reactions of chorismate. Journal of the American Chemical Society. 127: 12957-64. PMID 16159290 DOI: 10.1021/Ja052929V |
0.41 |
|
| 2005 |
Templeton MD, Reinhardt LA, Collyer CA, Mitchell RE, Cleland WW. Kinetic analysis of the L-ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola that is resistant to the transition state analogue (R)-N delta-(N'-sulfodiaminophosphinyl)-L-ornithine. Biochemistry. 44: 4408-15. PMID 15766270 DOI: 10.1021/Bi047432X |
0.358 |
|
| 2005 |
Koropatkin NM, Cleland WW, Holden HM. Kinetic and structural analysis of alpha-D-Glucose-1-phosphate cytidylyltransferase from Salmonella typhi. The Journal of Biological Chemistry. 280: 10774-80. PMID 15634670 DOI: 10.1074/Jbc.M414111200 |
0.369 |
|
| 2005 |
Cleland WW. The use of isotope effects to determine enzyme mechanisms. Archives of Biochemistry and Biophysics. 433: 2-12. PMID 15581561 DOI: 10.1016/J.Abb.2004.08.027 |
0.382 |
|
| 2004 |
Allard ST, Cleland WW, Holden HM. High resolution X-ray structure of dTDP-glucose 4,6-dehydratase from Streptomyces venezuelae. The Journal of Biological Chemistry. 279: 2211-20. PMID 14570895 DOI: 10.1074/Jbc.M310134200 |
0.369 |
|
| 2003 |
Cleland WW. The use of isotope effects to determine enzyme mechanisms. The Journal of Biological Chemistry. 278: 51975-84. PMID 14583616 DOI: 10.1074/Jbc.X300005200 |
0.392 |
|
| 2003 |
Wright SK, Rishavy MA, Cleland WW. 2H, 13C, and 15N kinetic isotope effects on the reaction of the ammonia-rescued K258A mutant of aspartate aminotransferase. Biochemistry. 42: 8369-76. PMID 12846586 DOI: 10.1021/Bi030092F |
0.374 |
|
| 2003 |
Sims PA, Larsen TM, Poyner RR, Cleland WW, Reed GH. Reverse protonation is the key to general acid-base catalysis in enolase. Biochemistry. 42: 8298-306. PMID 12846578 DOI: 10.1021/Bi0346345 |
0.45 |
|
| 2003 |
Reinhardt LA, Svedruzic D, Chang CH, Cleland WW, Richards NG. Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis. Journal of the American Chemical Society. 125: 1244-52. PMID 12553826 DOI: 10.1021/Ja0286977 |
0.353 |
|
| 2003 |
Rawlings J, Cleland WW, Hengge AC. Metal ion catalyzed hydrolysis of ethyl p-nitrophenyl phosphate. Journal of Inorganic Biochemistry. 93: 61-5. PMID 12538053 DOI: 10.1016/S0162-0134(02)00435-X |
0.663 |
|
| 2002 |
Snider MJ, Reinhardt L, Wolfenden R, Cleland WW. 15N kinetic isotope effects on uncatalyzed and enzymatic deamination of cytidine. Biochemistry. 41: 415-21. PMID 11772041 DOI: 10.1021/Bi011410I |
0.353 |
|
| 2001 |
Rishavy MA, Yang Z, Tong L, Cleland WW. Determination of the mechanism of human malic enzyme with natural and alternate dinucleotides by isotope effects. Archives of Biochemistry and Biophysics. 396: 43-8. PMID 11716460 DOI: 10.1006/Abbi.2001.2598 |
0.448 |
|
| 2001 |
Anderson MA, Shim H, Raushel FM, Cleland WW. Hydrolysis of phosphotriesters: determination of transition states in parallel reactions by heavy-atom isotope effects. Journal of the American Chemical Society. 123: 9246-53. PMID 11562204 DOI: 10.1021/Ja011025G |
0.634 |
|
| 2001 |
Neidhart D, Wei Y, Cassidy C, Lin J, Cleland WW, Frey PA. Correlation of low-barrier hydrogen bonding and oxyanion binding in transition state analogue complexes of chymotrypsin. Biochemistry. 40: 2439-47. PMID 11327865 DOI: 10.1021/Bi002535A |
0.381 |
|
| 2001 |
Gerratana B, Frey PA, Cleland WW. Characterization of the transition-state structure of the reaction of kanamycin nucleotidyltransferase by heavy-atom kinetic isotope effects. Biochemistry. 40: 2972-7. PMID 11258909 DOI: 10.1021/Bi002557X |
0.312 |
|
| 2000 |
Rishavy MA, Hengge AC, Cleland WW. Lanthanide Catalyzed Cyclization of Uridine 3'-p-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 283-292. PMID 11133147 DOI: 10.1006/Bioo.2000.1179 |
0.669 |
|
| 2000 |
Hengge AC, Bruzik KS, Tobin AE, Cleland WW, Tsai MD. Kinetic Isotope Effects and Stereochemical Studies on a Ribonuclease Model: Hydrolysis Reactions of Uridine 3'-Nitrophenyl Phosphate. Bioorganic Chemistry. 28: 119-133. PMID 10915550 DOI: 10.1006/Bioo.2000.1170 |
0.669 |
|
| 2000 |
Rishavy MA, Cleland WW. 13C and (15)N kinetic isotope effects on the reaction of aspartate aminotransferase and the tyrosine-225 to phenylalanine mutant. Biochemistry. 39: 7546-51. PMID 10858304 DOI: 10.1021/Bi000458D |
0.44 |
|
| 2000 |
Rishavy MA, Cleland WW, Lusty CJ. 15N isotope effects in glutamine hydrolysis catalyzed by carbamyl phosphate synthetase: evidence for a tetrahedral intermediate in the mechanism. Biochemistry. 39: 7309-15. PMID 10852731 DOI: 10.1021/Bi000435Z |
0.478 |
|
| 2000 |
Gerratana B, Sowa GA, Cleland WW. Characterization of the transition-state structures and mechanisms for the isomerization and cleavage reactions of uridine 3′-m-nitrobenzyl phosphate Journal of the American Chemical Society. 122: 12615-12621. DOI: 10.1021/ja003400v |
0.328 |
|
| 1999 |
Rishavy MA, Cleland W. 13C, 15N, and 18O equilibrium isotope effects and fractionation factors Canadian Journal of Chemistry. 77: 967-977. DOI: 10.1139/Cjc-77-5-6-967 |
0.305 |
|
| 1999 |
Cassidy CS, Reinhardt LA, Cleland WW, Frey PA. Hydrogen bonding in complexes of carboxylic acids with 1-alkylimidazoles: Steric and isotopic effects on low barrier hydrogen bonding Journal of the Chemical Society. Perkin Transactions 2. 635-641. DOI: 10.1039/A806387G |
0.31 |
|
| 1998 |
CLELAND WW. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection. Biochimica Et Biophysica Acta. 67: 188-96. PMID 14021669 DOI: 10.1016/0006-3002(63)91816-X |
0.35 |
|
| 1998 |
Lin J, Westler WM, Cleland WW, Markley JL, Frey PA. Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin. Proceedings of the National Academy of Sciences of the United States of America. 95: 14664-8. PMID 9843946 DOI: 10.1073/Pnas.95.25.14664 |
0.494 |
|
| 1998 |
Hess RA, Hengge AC, Cleland WW. Isotope effects on enzyme-catalyzed acyl transfer from p-nitrophenyl acetate: Concerted mechanisms and increased hyperconjugation in the transition state Journal of the American Chemical Society. 120: 2703-2709. DOI: 10.1021/Ja973413H |
0.588 |
|
| 1997 |
Gerlt JA, Kreevoy MM, Cleland W, Frey PA. Understanding enzymic catalysis: the importance of short, strong hydrogen bonds. Chemistry & Biology. 4: 259-67. PMID 9195866 DOI: 10.1016/S1074-5521(97)90069-7 |
0.329 |
|
| 1997 |
Hess RA, Hengge AC, Cleland WW. Kinetic isotope effects for acyl transfer from p-nitrophenyl acetate to hydroxylamine show a pH-dependent change in mechanism Journal of the American Chemical Society. 119: 6980-6983. DOI: 10.1021/Ja970648K |
0.651 |
|
| 1997 |
Sowa GA, Hengge AC, Cleland WW. 18O isotope effects support a concerted mechanism for ribonuclease A Journal of the American Chemical Society. 119: 2319-2320. DOI: 10.1021/ja963974t |
0.563 |
|
| 1997 |
Rawlings J, Hengge AC, Cleland WW. Heavy-atom isotope effects on reactions of Co(III)-bound p-nitrophenyl phosphate: Nucleophilic displacements of p-nitrophenol and dissociation of p-nitrophenyl phosphate Journal of the American Chemical Society. 119: 542-549. DOI: 10.1021/Ja962448Z |
0.59 |
|
| 1996 |
Sculley MJ, Morrison JF, Cleland WW. Slow-binding inhibition: the general case. Biochimica Et Biophysica Acta. 1298: 78-86. PMID 8948491 DOI: 10.1016/S0167-4838(96)00118-5 |
0.403 |
|
| 1995 |
Cleland WW, Hengge AC. Mechanisms of phosphoryl and acyl transfer. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1585-94. PMID 8529838 DOI: 10.1096/Fasebj.9.15.8529838 |
0.667 |
|
| 1995 |
Cleland WW. Isotope effects: determination of enzyme transition state structure. Methods in Enzymology. 249: 341-73. PMID 7791618 DOI: 10.1016/0076-6879(95)49041-8 |
0.452 |
|
| 1995 |
Cleland WW. Kinetic method for determination of dissociation constants of metal ion-nucleotide complexes. Methods in Enzymology. 249: 181-8. PMID 7791611 DOI: 10.1016/0076-6879(95)49035-3 |
0.356 |
|
| 1995 |
Hengge AC, Tobin AE, Cleland WW. Studies of Transition-State Structures in Phosphoryl Transfer Reactions of Phosphodiesters of p-Nitrophenol Journal of the American Chemical Society. 117: 5919-5926. DOI: 10.1021/Ja00127A003 |
0.618 |
|
| 1994 |
Waldrop GL, Braxton BF, Urbauer JL, Cleland WW, Kiick DM. Secondary 18O and primary 13C isotope effects as a probe of transition-state structure for enzymatic decarboxylation of oxalacetate. Biochemistry. 33: 5262-7. PMID 8172901 DOI: 10.1021/Bi00183A032 |
0.663 |
|
| 1994 |
Cleland WW, Kreevoy MM. Low-barrier hydrogen bonds and enzymic catalysis. Science (New York, N.Y.). 264: 1887-90. PMID 8009219 DOI: 10.1126/Science.8009219 |
0.39 |
|
| 1992 |
Parmentier LE, O'Leary MH, Schachman HK, Cleland WW. 13C isotope effect studies of Escherichia coli aspartate transcarbamylase in the presence of the bisubstrate analog N-(phosphonoacetyl)-L-aspartate. Biochemistry. 31: 6598-602. PMID 1633172 DOI: 10.1021/Bi00143A033 |
0.322 |
|
| 1992 |
Waldrop GL, Turnbull JL, Parmentier LE, Lee S, O'Leary MH, Cleland WW, Schachman HK. The contribution of threonine 55 to catalysis in aspartate transcarbamoylase. Biochemistry. 31: 6592-7. PMID 1633171 DOI: 10.1021/Bi00143A032 |
0.662 |
|
| 1992 |
Waldrop GL, Turnbull JL, Parmentier LE, O'Leary MH, Cleland WW, Schachman HK. Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine. Biochemistry. 31: 6585-91. PMID 1633170 DOI: 10.1021/Bi00143A031 |
0.685 |
|
| 1992 |
Parmentier LE, Weiss PM, O'Leary MH, Schachman HK, Cleland WW. 13C and 15N isotope effects as a probe of the chemical mechanism of Escherichia coli aspartate transcarbamylase. Biochemistry. 31: 6577-84. PMID 1633169 DOI: 10.1021/Bi00143A030 |
0.365 |
|
| 1992 |
Parmentier LE, O'Leary MH, Schachman HK, Cleland WW. 13C isotope effects as a probe of the kinetic mechanism and allosteric properties of Escherichia coli aspartate transcarbamylase. Biochemistry. 31: 6570-6. PMID 1633168 DOI: 10.1021/Bi00143A029 |
0.367 |
|
| 1992 |
Janc JW, Cleland WW, O'Leary MH. Mechanistic studies of phosphoenolpyruvate carboxylase from Zea mays utilizing formate as an alternate substrate for bicarbonate. Biochemistry. 31: 6441-6. PMID 1321659 DOI: 10.1021/Bi00143A012 |
0.326 |
|
| 1992 |
Waldrop GL, Urbauer JL, Cleland WW. Nitrogen-15 isotope effects on nonenzymic and aspartate transcarbamylase catalyzed reactions of carbamyl phosphate Journal of the American Chemical Society. 114: 5941-5945. DOI: 10.1021/Ja00041A006 |
0.669 |
|
| 1991 |
Weiss PM, Gavva SR, Harris BG, Urbauer JL, Cleland WW, Cook PF. Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction. Biochemistry. 30: 5755-63. PMID 2043615 DOI: 10.1021/Bi00237A018 |
0.351 |
|
| 1991 |
Jones JP, Weiss PM, Cleland WW. Secondary 18O isotope effects for hexokinase-catalyzed phosphoryl transfer from ATP. Biochemistry. 30: 3634-9. PMID 2015221 |
0.325 |
|
| 1991 |
Canellas PF, Cleland WW. Carbon-13 and deuterium isotope effects on the reaction catalyzed by glyceraldehyde-3-phosphate dehydrogenase. Biochemistry. 30: 8871-6. PMID 1888744 |
0.351 |
|
| 1991 |
Turnbull J, Morrison JF, Cleland WW. Kinetic studies on chorismate mutase-prephenate dehydrogenase from Escherichia coli: models for the feedback inhibition of prephenate dehydrogenase by L-tyrosine. Biochemistry. 30: 7783-8. PMID 1868056 DOI: 10.1021/Bi00245A017 |
0.309 |
|
| 1991 |
Turnbull J, Cleland WW, Morrison JF. pH dependency of the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Escherichia coli. Biochemistry. 30: 7777-82. PMID 1868055 DOI: 10.1021/Bi00245A016 |
0.32 |
|
| 1991 |
Caldwell SR, Raushel FM, Weiss PM, Cleland WW. Transition-state structures for enzymatic and alkaline phosphotriester hydrolysis. Biochemistry. 30: 7444-50. PMID 1649629 DOI: 10.1021/Bi00244A011 |
0.486 |
|
| 1991 |
Hengge AC, Cleland WW. Mechanism of phosphodiester cleavage with .beta.-cyclodextrin The Journal of Organic Chemistry. 56: 1972-1974. DOI: 10.1021/Jo00005A064 |
0.552 |
|
| 1991 |
Hengge AC, Cleland WW. Phosphoryl-transfer reactions of phosphodiesters: characterization of transition states by heavy-atom isotope effects Journal of the American Chemical Society. 113: 5835-5841. DOI: 10.1021/Ja00015A043 |
0.664 |
|
| 1991 |
Caldwell SR, Raushel FM, Weiss PM, Cleland WW. Primary and secondary oxygen-18 isotope effects in the alkaline and enzyme-catalyzed hydrolysis of phosphotriesters Journal of the American Chemical Society. 113: 730-732. DOI: 10.1021/Ja00002A083 |
0.517 |
|
| 1991 |
Speckhard DC, Rawlings J, Pecoraro VL, Cleland W. Triamminechromium(III) complexes of tripolyphosphate and adenosine tri- and diphosphate Journal of Inorganic Biochemistry. 41: 105-116. DOI: 10.1016/0162-0134(91)80004-2 |
0.416 |
|
| 1990 |
Anderson VE, Cleland WW. Phosphonate analogue substrates for enolase. Biochemistry. 29: 10498-503. PMID 2271661 |
0.601 |
|
| 1990 |
Turnbull J, Cleland WW, Morrison JF. Chorismate mutase-prephenate dehydrogenase from Escherichia coli. 1. Kinetic characterization of the dehydrogenase reaction by use of alternative substrates. Biochemistry. 29: 10245-54. PMID 2271652 DOI: 10.1021/Bi00496A014 |
0.331 |
|
| 1990 |
Cleland WW. Secondary 18O isotope effects as a tool for studying reactions of phosphate mono-, di-, and triesters. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 4: 2899-905. PMID 2199287 DOI: 10.1096/Fasebj.4.11.2199287 |
0.431 |
|
| 1990 |
Hengge AC, Cleland WW. Direct measurement of transition-state bond cleavage in hydrolysis of phosphate esters of p-nitrophenol Journal of the American Chemical Society. 112: 7421-7422. DOI: 10.1021/Ja00176A067 |
0.616 |
|
| 1989 |
Cleland WW. Enzyme kinetics revisited: a commentary on 'The Kinetics of Enzyme-Catalyzed Reactions With Two or More Substrates or Products'. Biochimica Et Biophysica Acta. 1000: 209-12. PMID 2673368 DOI: 10.1016/S0006-3002(89)80019-8 |
0.407 |
|
| 1988 |
Grissom CB, Cleland WW. Isotope effect studies of the chemical mechanism of pig heart NADP isocitrate dehydrogenase. Biochemistry. 27: 2934-43. PMID 3401457 |
0.684 |
|
| 1988 |
Grissom CB, Cleland WW. Isotope effect studies of chicken liver NADP malic enzyme: role of the metal ion and viscosity dependence. Biochemistry. 27: 2927-34. PMID 3401456 |
0.707 |
|
| 1988 |
Weiss PM, Garcia GA, Kenyon GL, Cleland WW, Cook PF. Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues. Biochemistry. 27: 2197-205. PMID 3378056 DOI: 10.1021/bi00406a058 |
0.378 |
|
| 1988 |
Tipton PA, Cleland WW. Carbon-13 and deuterium isotope effects on the catalytic reactions of biotin carboxylase. Biochemistry. 27: 4325-31. PMID 3048384 DOI: 10.1021/bi00412a020 |
0.356 |
|
| 1988 |
Tipton PA, Cleland WW. Catalytic mechanism of biotin carboxylase: steady-state kinetic investigations. Biochemistry. 27: 4317-25. PMID 2971391 DOI: 10.1021/bi00412a019 |
0.356 |
|
| 1988 |
Tipton PA, Cleland WW. Carbon-13 isotope effects on reactions involving carbamate and carbamoyl phosphate. Archives of Biochemistry and Biophysics. 260: 273-6. PMID 2829730 DOI: 10.1016/0003-9861(88)90450-X |
0.318 |
|
| 1988 |
Speckhard DC, Pecoraro VL, Knight WB, Cleland WW. Determination of the absolute configurations of the isomers of triamminecobalt(III) adenosine triphosphate [Erratum to document cited in CA105(3):20891F] Journal of the American Chemical Society. 110: 2349-2349. DOI: 10.1021/Ja00215A081 |
0.378 |
|
| 1987 |
Attwood PV, Cleland WW. Decarboxylation of oxalacetate by pyruvate carboxylase. Biochemistry. 25: 8191-6. PMID 3814578 DOI: 10.1021/bi00373a011 |
0.344 |
|
| 1987 |
Weiss PM, Cook PF, Hermes JD, Cleland WW. Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase Biochemistry. 26: 7378-7384. PMID 3427079 DOI: 10.1021/Bi00397A027 |
0.346 |
|
| 1987 |
Grissom CB, Cleland WW. 2-Keto-3-fluoroglutarate: a useful mechanistic probe of 2-keto-glutarate-dependent enzyme systems. Biochimica Et Biophysica Acta. 916: 437-45. PMID 2891378 DOI: 10.1016/0167-4838(87)90190-7 |
0.662 |
|
| 1987 |
Cleland WW. The use of isotope effects in the detailed analysis of catalytic mechanisms of enzymes Bioorganic Chemistry. 15: 283-302. DOI: 10.1016/0045-2068(87)90026-5 |
0.396 |
|
| 1987 |
GRISSOM CB, CLELAND WW. ChemInform Abstract: 13C Carbon Isotope Effects on the Metal Ion Catalyzed Decarboxylationof Oxalacetate Cheminform. 18. DOI: 10.1002/chin.198702116 |
0.653 |
|
| 1986 |
Dougherty TM, Cleland WW. pH studies on the chemical mechanism of rabbit muscle pyruvate kinase. 2. Physiological substrates and phosphoenol-alpha-ketobutyrate. Biochemistry. 24: 5875-80. PMID 3878724 DOI: 10.1021/bi00342a028 |
0.317 |
|
| 1986 |
Grissom CB, Cleland WW. Carbon isotope effects on the metal ion catalyzed decarboxylation of oxalacetate Journal of the American Chemical Society. 108: 5582-5583. DOI: 10.1021/ja00278a036 |
0.647 |
|
| 1986 |
Speckhard DC, Pecoraro VL, Knight WB, Cleland WW. Determination of the absolute configurations of the isomers of triamminecobalt(III) adenosine triphosphate Journal of the American Chemical Society. 108: 4167-4171. DOI: 10.1021/Ja00274A053 |
0.428 |
|
| 1986 |
SPECKHARD DC, PECORARO VL, KNIGHT WB, CLELAND WW. ChemInform Abstract: Determination of the Absolute Configurations of the Isomers of Triamminecobalt(III) Adenosine Triphosphate. Chemischer Informationsdienst. 17. DOI: 10.1002/Chin.198646061 |
0.429 |
|
| 1985 |
Scharschmidt M, Fisher MA, Cleland WW. Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 1. Liver alcohol dehydrogenase with benzyl alcohol and yeast aldehyde dehydrogenase with benzaldehyde. Biochemistry. 23: 5471-8. PMID 6391543 DOI: 10.1021/bi00318a015 |
0.302 |
|
| 1985 |
Grissom CB, Cleland WW. Use of intermediate partitioning to calculate intrinsic isotope effects for the reaction catalyzed by malic enzyme. Biochemistry. 24: 944-8. PMID 3995001 |
0.724 |
|
| 1985 |
Hermes JD, Weiss PM, Cleland WW. Use of nitrogen-15 and deuterium isotope effects to determine the chemical mechanism of phenylalanine ammonia-lyase Biochemistry. 24: 2959-2967. PMID 3893533 DOI: 10.1021/bi00333a023 |
0.333 |
|
| 1985 |
Pecoraro VL, Rendina AR, Cleland WW. Determination of the screw sense specificity of bovine liver fructokinase. Biochemistry. 24: 1619-22. PMID 2988605 DOI: 10.1021/Bi00328A008 |
0.498 |
|
| 1984 |
Pecoraro VL, Rawlings J, Cleland WW. Investigation of substrate specificity of creatine kinase using chromium (III) and cobalt(III) complexes of adenosine 5'-diphosphate. Biochemistry. 23: 153-8. PMID 6546349 DOI: 10.1021/Bi00296A025 |
0.498 |
|
| 1984 |
Hermes JD, Tipton PA, Fisher MA, O'Leary MH, Morrison JF, Cleland WW. Mechanisms of enzymatic and acid-catalyzed decarboxylations of prephenate. Biochemistry. 23: 6263-75. PMID 6395898 DOI: 10.1021/Bi00320A057 |
0.35 |
|
| 1984 |
Rendina AR, Hermes JD, Cleland WW. Use of multiple isotope effects to study the mechanism of 6-phosphogluconate dehydrogenase Biochemistry. 23: 6257-6262. PMID 6395897 DOI: 10.1021/bi00320a056 |
0.331 |
|
| 1984 |
Hermes JD, Morrical SW, O'Leary MH, Cleland WW. Variation of transition-state structure as a function of the nucleotide in reactions catalyzed by dehydrogenases. 2. Formate dehydrogenase Biochemistry. 23: 5479-5488. PMID 6391544 DOI: 10.1021/Bi00318A016 |
0.35 |
|
| 1984 |
Anderson VE, Weiss PM, Cleland WW. Reaction intermediate analogues for enolase. Biochemistry. 23: 2779-86. PMID 6380574 DOI: 10.1021/Bi00307A038 |
0.534 |
|
| 1984 |
Pecoraro VL, Hermes JD, Cleland WW. Stability constants of Mg2+ and Cd2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP. Biochemistry. 23: 5262-71. PMID 6334536 |
0.445 |
|
| 1984 |
Rendina AR, Hermes JD, Cleland WW. A novel method for determining rate constants for dehydration of aldehyde hydrates Biochemistry. 23: 5148-5156. PMID 6095890 DOI: 10.1021/bi00317a011 |
0.315 |
|
| 1983 |
Cleland WW. The use of isotope effects to determine transition-state structure for enzymic reactions. Methods in Enzymology. 87: 625-41. PMID 7176928 DOI: 10.1016/S0076-6879(82)87033-X |
0.415 |
|
| 1983 |
Cleland WW. The use of pH studies to determine chemical mechanisms of enzyme-catalyzed reactions. Methods in Enzymology. 87: 390-405. PMID 7176923 DOI: 10.1016/S0076-6879(82)87024-9 |
0.452 |
|
| 1983 |
Cleland WW. An analysis of Haldane Relationships. Methods in Enzymology. 87: 366-9. PMID 7176921 DOI: 10.1016/S0076-6879(82)87022-5 |
0.375 |
|
| 1983 |
Cleland WW. Preparation of chromium(III) and cobalt(III) nucleotides as chirality probes and inhibitors. Methods in Enzymology. 87: 159-79. PMID 7176917 DOI: 10.1016/S0076-6879(82)87013-4 |
0.36 |
|
| 1983 |
Cleland WW. Use of isotope effects to elucidate enzyme mechanisms. Crc Critical Reviews in Biochemistry. 13: 385-428. PMID 6759038 DOI: 10.3109/10409238209108715 |
0.379 |
|
| 1983 |
Cleland WW. Determination of equilibrium isotope effects by the equilibrium perturbation method. Methods in Enzymology. 87: 641-6. PMID 6757652 DOI: 10.1016/S0076-6879(82)87034-1 |
0.413 |
|
| 1983 |
Taylor KB, Cook PF, Cleland WW. Solvent isotope effects on the reaction catalyzed by yeast hexokinase. European Journal of Biochemistry. 134: 571-4. PMID 6349994 DOI: 10.1111/J.1432-1033.1983.Tb07604.X |
0.368 |
|
| 1983 |
Morrison JF, Cleland WW. Lanthanide-adenosine 5'-triphosphate complexes: determination of their dissociation constants and mechanism of action as inhibitors of yeast hexokinase Biochemistry. 22: 5507-5513. DOI: 10.1021/Bi00293A009 |
0.334 |
|
| 1983 |
Pecoraro V, Rawlings J, Cleland W. The use of chromium(III) and cobalt(III) complexes of adenosine diphosphate to elucidate the catalytic mechanisms of creatine kinase Inorganica Chimica Acta. 79: 241. DOI: 10.1016/S0020-1693(00)95281-2 |
0.445 |
|
| 1982 |
Viola RE, Cleland WW. Initial velocity analysis for terreactant mechanisms. Methods in Enzymology. 87: 353-66. PMID 7176920 DOI: 10.1016/S0076-6879(82)87021-3 |
0.584 |
|
| 1982 |
Ainslie GR, Cleland WW. The effect of oligomeric environment on the kinetics of lactate dehydrogenase subunits. Archives of Biochemistry and Biophysics. 216: 101-4. PMID 7103501 DOI: 10.1016/0003-9861(82)90193-X |
0.316 |
|
| 1982 |
Viola RE, Raushel FM, Rendina AR, Cleland WW. Substrate synergism and the kinetic mechanism of yeast hexokinase. Biochemistry. 21: 1295-302. PMID 7041974 DOI: 10.1021/Bi00535A029 |
0.677 |
|
| 1982 |
Grimshaw CE, Cook PF, Cleland WW. Use of isotope effects and pH studies to determine the chemical mechanism of Bacillus subtilis L-alanine dehydrogenase. Biochemistry. 20: 5655-61. PMID 6794612 DOI: 10.1021/Bi00523A003 |
0.39 |
|
| 1981 |
Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 2. Isotope-dependent step not pH dependent. Kinetic mechanism of alcohol dehydrogenase. Biochemistry. 20: 1805-16. PMID 7013801 DOI: 10.1021/Bi00510A015 |
0.32 |
|
| 1981 |
Cook PF, Cleland WW. pH variation of isotope effects in enzyme-catalyzed reactions. 1. Isotope- and pH-dependent steps the same. Biochemistry. 20: 1797-805. PMID 7013800 DOI: 10.1021/Bi00510A014 |
0.318 |
|
| 1981 |
Cook PF, Cleland WW. Mechanistic deductions from isotope effects in multireactant enzyme mechanisms. Biochemistry. 20: 1790-6. PMID 7013799 DOI: 10.1021/Bi00510A013 |
0.32 |
|
| 1980 |
Blanchard JS, Cleland WW. Use of isotope effects to deduce the chemical mechanism of fumarase. Biochemistry. 19: 4506-13. PMID 7407088 |
0.573 |
|
| 1980 |
Morrison JF, Cleland WW. A kinetic method for determining dissociation constants for metal complexes of adenosine 5'-triphosphate and adenosine 5'-diphosphate. Biochemistry. 19: 3127-31. PMID 7407034 DOI: 10.1021/Bi00555A002 |
0.392 |
|
| 1980 |
Cleland WW. Measurement of isotope effects by the equilibrium perturbation technique. Methods in Enzymology. 64: 104-25. PMID 7374451 DOI: 10.1016/S0076-6879(80)64007-5 |
0.394 |
|
| 1980 |
Cook PF, Blanchard JS, Cleland WW. Primary and secondary deuterium isotope effects on equilibrium constants for enzyme-catalyzed reactions. Biochemistry. 19: 4853-8. PMID 7000186 DOI: 10.1021/Bi00562A023 |
0.476 |
|
| 1980 |
Blanchard JS, Cleland WW. Kinetic and chemical mechanisms of yeast formate dehydrogenase. Biochemistry. 19: 3543-50. PMID 6996706 |
0.518 |
|
| 1980 |
Viola RE, Morrison JF, Cleland WW. Interaction of metal(III)-adenosine 5'-triphosphate complexes with yeast hexokinase. Biochemistry. 19: 3131-7. PMID 6996699 DOI: 10.1021/Bi00555A003 |
0.635 |
|
| 1980 |
Viola RE, Cleland WW. Aldehyde-induced adenosine triphosphatase activities of fructose 6-phosphate and fructose kinases. Biochemistry. 19: 1861-6. PMID 6246937 DOI: 10.1021/Bi00550A600 |
0.561 |
|
| 1980 |
Cleland WW. Statistical analysis of enzyme kinetic data. Methods in Enzymology. 63: 103-38. PMID 502857 DOI: 10.1016/0076-6879(79)63008-2 |
0.323 |
|
| 1979 |
Gallopo AR, Cleland WW. Properties of 3-hydroxypropionaldehyde 3-phosphate. Archives of Biochemistry and Biophysics. 195: 152-4. PMID 475381 DOI: 10.1016/0003-9861(79)90337-0 |
0.337 |
|
| 1979 |
Viola RE, Cook PF, Cleland WW. Stereoselective preparation of deuterated reduced nicotinamide adenine nucleotides and substrates by enzymatic synthesis. Analytical Biochemistry. 96: 334-40. PMID 224725 DOI: 10.1016/0003-2697(79)90590-6 |
0.595 |
|
| 1979 |
Cleland WW. [20] Substrate inhibition Methods in Enzymology. 63: 500-513. DOI: 10.1016/0076-6879(79)63022-7 |
0.301 |
|
| 1978 |
Viola RE, Cleland WW. Use of pH studies to elucidate the chemical mechanism of yeast hexokinase. Biochemistry. 17: 4111-7. PMID 30473 DOI: 10.1021/Bi00613A001 |
0.586 |
|
| 1977 |
Meloche HP, Monti CT, Cleland WW. Magnitude of the equilibrium isotope effect on carbon-tritium bond synthesis. Biochimica Et Biophysica Acta. 480: 517-9. PMID 836851 DOI: 10.1016/0005-2744(77)90047-X |
0.352 |
|
| 1977 |
Raushel FM, Cleland WW. Bovine liver fructokinase: purification and kinetic properties. Biochemistry. 16: 2169-75. PMID 193556 DOI: 10.1021/Bi00629A020 |
0.516 |
|
| 1977 |
Cleland WW. Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Advances in Enzymology and Related Areas of Molecular Biology. 45: 273-387. PMID 21524 DOI: 10.1002/9780470122907.ch4 |
0.323 |
|
| 1977 |
Raushel FM, Cleland WW. Determination of the rate-limiting steps and chemical mechanism of fructokinase by isotope exchange, isotope partitioning, and pH studies. Biochemistry. 16: 2176-81. PMID 16640 DOI: 10.1021/Bi00629A021 |
0.632 |
|
| 1977 |
Schimerlik MI, Grimshaw CE, Cleland WW. Determination of the rate-limiting steps for malic enzyme by the use of isotope effects and other kinetic studies. Biochemistry. 16: 571-6. PMID 13820 DOI: 10.1021/Bi00623A002 |
0.352 |
|
| 1976 |
Cleland WW, Northrop DB. Comprehensive enzyme tome Trends in Biochemical Sciences. 1: 215. DOI: 10.1016/S0968-0004(76)80035-7 |
0.321 |
|
| 1975 |
Schimerlik MI, Rife JE, Cleland WW. Equilibrium perturbation by isotope substitution. Biochemistry. 14: 5347-54. PMID 1191642 DOI: 10.1021/Bi00695A020 |
0.319 |
|
| 1973 |
DePamphilis ML, Cleland WW. Preparation and properties of chromium (3)-nucleotide complexes for use in the study of enzyme mechanisms. Biochemistry. 12: 3714-24. PMID 4596147 DOI: 10.1021/bi00743a022 |
0.533 |
|
| 1973 |
Raushel FM, Cleland WW. The substrate and anomeric specificity of fructokinase. The Journal of Biological Chemistry. 248: 8174-7. PMID 4356621 |
0.453 |
|
| 1972 |
Orsi BA, Cleland WW. Inhibition kinetics of D-glyceraldehyde 3-phosphate dehydrogenase. The Biochemical Journal. 125: 112P-113P. PMID 4335538 DOI: 10.1042/Bj1250112Pb |
0.322 |
|
| 1969 |
Zahler WL, Cleland WW. Studies on the microsomal acylation of L-glycerol-3-phosphate. 3. Time course of the reaction. Biochimica Et Biophysica Acta. 176: 699-703. PMID 5797084 DOI: 10.1016/0005-2760(69)90250-1 |
0.4 |
|
| 1969 |
Sánchez de Jiménez E, Cleland WW. Studies of the microsomal acylation of L-glycerol-3-phosphate. I. The specificity of the rat brain enzyme. Biochimica Et Biophysica Acta. 176: 685-91. PMID 5797083 DOI: 10.1016/0005-2760(69)90248-3 |
0.316 |
|
| 1969 |
Abou-Issa HM, Cleland WW. Studies on the microsomal acylation of L-glycerol-3-phosphate. II. The specificity and properties of the rat liver enzyme. Biochimica Et Biophysica Acta. 176: 692-8. PMID 4978799 DOI: 10.1016/0005-2760(69)90249-5 |
0.33 |
|
| 1956 |
CLELAND WW, JOHNSON MJ. Studies on the formation of oxalic acid by Aspergillus niger. The Journal of Biological Chemistry. 220: 595-606. PMID 13331918 |
0.445 |
|
| 1954 |
CLELAND WW, JOHNSON MJ. Tracer experiments on the mechanism of citric acid formation by Aspergillus niger. The Journal of Biological Chemistry. 208: 679-89. PMID 13174578 |
0.466 |
|
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