| Year |
Citation |
Score |
| 2015 |
Lopalco A, Dalwadi G, Niu S, Schowen RL, Douglas J, Stella VJ. Mechanism of Decarboxylation of Pyruvic Acid in the Presence of Hydrogen Peroxide. Journal of Pharmaceutical Sciences. PMID 26422524 DOI: 10.1002/Jps.24653 |
0.319 |
|
| 2013 |
Anandarajah K, Schowen KB, Schowen RL. Isotope Effects and Temperature Dependences in the Action of the Glucose Dehydrogenase of the Mesophilic Bacterium Bacillus megaterium. Journal of Physical Organic Chemistry. 26. PMID 24298200 DOI: 10.1002/Poc.3166 |
0.304 |
|
| 2010 |
Limbach HH, Schowen KB, Schowen RL. Heavy atom motions and tunneling in hydrogen transfer reactions: The importance of the pre-tunneling state Journal of Physical Organic Chemistry. 23: 586-605. DOI: 10.1002/Poc.1663 |
0.343 |
|
| 2008 |
Li QS, Cai S, Fang J, Borchardt RT, Kuczera K, Middaugh CR, Schowen RL. Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 2. The role of helix 18 stability. Biochemistry. 47: 4983-91. PMID 18393535 DOI: 10.1021/Bi800175G |
0.343 |
|
| 2007 |
Schowen RL. Isotopic and other studies on the molecular origins of substrate regulation of some pyruvate decarboxylases: a reconsideration. Isotopes in Environmental and Health Studies. 43: 1-16. PMID 17454268 DOI: 10.1080/10256010600990393 |
0.333 |
|
| 2007 |
Li QS, Cai S, Borchardt RT, Fang J, Kuczera K, Middaugh CR, Schowen RL. Comparative kinetics of cofactor association and dissociation for the human and trypanosomal S-adenosylhomocysteine hydrolases. 1. Basic features of the association and dissociation processes. Biochemistry. 46: 5798-809. PMID 17447732 DOI: 10.1021/Bi700170M |
0.332 |
|
| 2007 |
Gradinaru R, Schowen R, Ghisla S. Solvent isotope effects in reactions of human medium-chain acyl-CoA dehydrogenase active site mutants Biochemistry. 46: 2497-2509. PMID 17286388 DOI: 10.1021/Bi0614582 |
0.388 |
|
| 2007 |
Schowen RL. The use of solvent isotope effects in the pursuit of enzyme mechanisms Journal of Labelled Compounds and Radiopharmaceuticals. 50: 1052-1062. DOI: 10.1002/Jlcr.1436 |
0.302 |
|
| 2006 |
Garoutte MP, Bibbs JA, Schowen RL. Solvent isotope effects and the question of quantum tunneling in hydrolytic enzyme action Journal of Nuclear Science and Technology. 43: 455-460. DOI: 10.1080/18811248.2006.9711123 |
0.314 |
|
| 2005 |
Wang M, Borchardt RT, Schowen RL, Kuczera K. Domain motions and the open-to-closed conformational transition of an enzyme: a normal mode analysis of S-adenosyl-L-homocysteine hydrolase. Biochemistry. 44: 7228-39. PMID 15882061 DOI: 10.1021/Bi047524M |
0.327 |
|
| 2005 |
Li B, Gorman EM, Moore KD, Williams T, Schowen RL, Topp EM, Borchardt RT. Effects of acidic N + 1 residues on asparagine deamidation rates in solution and in the solid state. Journal of Pharmaceutical Sciences. 94: 666-75. PMID 15668945 DOI: 10.1002/Jps.20263 |
0.306 |
|
| 2004 |
Romesberg FE, Schowen RL. Isotope effects and quantum tunneling in enzyme-catalyzed hydrogen transfer. Part I. The experimental basis Advances in Physical Organic Chemistry. 39: 27-77. DOI: 10.1016/S0065-3160(04)39002-7 |
0.331 |
|
| 2003 |
Parker NB, Yang X, Hanke J, Mason KA, Schowen RL, Borchardt RT, Yin DH. Trypanosoma cruzi: molecular cloning and characterization of the S-adenosylhomocysteine hydrolase. Experimental Parasitology. 105: 149-58. PMID 14969692 DOI: 10.1016/J.Exppara.2003.10.001 |
0.327 |
|
| 2003 |
Schowen RL. How an enzyme surmounts the activation energy barrier. Proceedings of the National Academy of Sciences of the United States of America. 100: 11931-2. PMID 14530397 DOI: 10.1073/Pnas.2235806100 |
0.375 |
|
| 2003 |
Li B, Borchardt RT, Topp EM, VanderVelde D, Schowen RL. Racemization of an asparagine residue during peptide deamidation. Journal of the American Chemical Society. 125: 11486-7. PMID 13129337 DOI: 10.1021/Ja0360992 |
0.305 |
|
| 2003 |
Hanson BA, Schowen RL, Stella VJ. A mechanistic and kinetic study of the E-ring hydrolysis and lactonization of a novel phosphoryloxymethyl prodrug of camptothecin. Pharmaceutical Research. 20: 1031-8. PMID 12880289 DOI: 10.1023/A:1024410322870 |
0.338 |
|
| 2003 |
Xie M, Shahrokh Z, Kadkhodayan M, Henzel WJ, Powell MF, Borchardt RT, Schowen RL. Asparagine deamidation in recombinant human lymphotoxin: hindrance by three-dimensional structures. Journal of Pharmaceutical Sciences. 92: 869-80. PMID 12661072 DOI: 10.1002/Jps.10342 |
0.311 |
|
| 2003 |
Yang X, Hu Y, Yin DH, Turner MA, Wang M, Borchardt RT, Howell PL, Kuczera K, Schowen RL. Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry. 42: 1900-9. PMID 12590576 DOI: 10.1021/Bi0262350 |
0.389 |
|
| 2002 |
Schowen RL. The elicitation of carboxylesterase activity in antibodies by reactive immunization with labile organophosphorus antigens: a role for flexibility. Journal of Immunological Methods. 269: 59-65. PMID 12379352 DOI: 10.1016/S0022-1759(02)00224-7 |
0.337 |
|
| 2002 |
Elrod P, Zhang J, Yang X, Yin D, Hu Y, Borchardt RT, Schowen RL. Contributions of active site residues to the partial and overall catalytic activities of human S-adenosylhomocysteine hydrolase. Biochemistry. 41: 8134-42. PMID 12069606 DOI: 10.1021/Bi025771P |
0.357 |
|
| 2002 |
Hopper CR, Schowen RL, Venkatasubban KS, Jayaraman H. Amide hydrolysis. VII. Proton inventories of transition states for solvation catalysis and proton-transfer catalysis. Decomposition of the tetrahedral intermediate in amide methanolysis Cheminform. 4. DOI: 10.1021/Ja00791A034 |
0.367 |
|
| 2001 |
Hu Y, Yang X, Yin DH, Mahadevan J, Kuczera K, Schowen RL, Borchardt RT. Computational characterization of substrate binding and catalysis in S-adenosylhomocysteine hydrolase. Biochemistry. 40: 15143-52. PMID 11735397 DOI: 10.1021/Bi015690D |
0.346 |
|
| 2000 |
Schowen KB, Limbach HH, Denisov GS, Schowen RL. Hydrogen bonds and proton transfer in general-catalytic transition-state stabilization in enzyme catalysis. Biochimica Et Biophysica Acta. 1458: 43-62. PMID 10812024 DOI: 10.1016/S0005-2728(00)00059-1 |
0.386 |
|
| 1999 |
Hajipour G, Schowen KB, Schowen RL. The linkage of catalysis and regulation in enzyme action: oxidative diversion in the hysteretically regulated yeast pyruvate decarboxylase. Bioorganic & Medicinal Chemistry. 7: 887-94. PMID 10400342 DOI: 10.1016/S0968-0896(98)00269-7 |
0.335 |
|
| 1999 |
Smirnov SN, Benedict H, Golubev NS, Denisov GS, Kreevoy MM, Schowen RL, Limbach HH. Exploring zero-point energies and hydrogen bond geometries along proton transfer pathways by low-temperature NMR Canadian Journal of Chemistry. 77: 943-949. DOI: 10.1139/V99-096 |
0.303 |
|
| 1999 |
Tian J, Tan J, Schowen KB, Schowen RL. The role of the medium in solvent isotope effects on serine protease action Canadian Journal of Chemistry. 77: 781-786. DOI: 10.1139/V99-054 |
0.357 |
|
| 1998 |
Hong J, Sun S, Derrick T, Larive C, Schowen KB, Schowen RL. Transition-state theoretical interpretation of the catalytic power of pyruvate decarboxylases: the roles of static and dynamical considerations. Biochimica Et Biophysica Acta. 1385: 187-200. PMID 9655907 DOI: 10.1016/S0167-4838(98)00068-5 |
0.35 |
|
| 1996 |
Nicolaou MG, Wolfe JL, Schowen RL, Borchardt RT. Facilitated Intramolecular Conjugate Addition of Amides of 3-(3',6'-Dioxo-2',4'-dimethyl-1',4'-cyclohexadienyl)-3,3-dimethylpropionic Acid. 2. Kinetics of Degradation. The Journal of Organic Chemistry. 61: 6633-6638. PMID 11667533 DOI: 10.1021/Jo961069L |
0.322 |
|
| 1996 |
Bryan CD, Schowen KB, Schowen RL. Solvent isotope effects as a probe of general catalysis and solvation in phosphoryl transfer Canadian Journal of Chemistry. 74: 931-938. DOI: 10.1139/V96-102 |
0.363 |
|
| 1995 |
Riley CM, Mummert MA, Zhou J, Schowen RL, Vander Velde DG, Morton MD, Slavik M. Hydrolysis of the prodrug, 2',3',5'-triacetyl-6-azauridine. Pharmaceutical Research. 12: 1361-70. PMID 8570536 DOI: 10.1023/A:1016238110533 |
0.307 |
|
| 1995 |
Alvarez FJ, Ermer J, Hübner G, Schellenberger A, Schowen RL. The linkage of catalysis and regulation in enzyme action. Solvent isotope effects as probes of protonic sites in the yeast pyruvate decarboxylase mechanism Journal of the American Chemical Society. 117: 1678-1683. DOI: 10.1021/Ja00111A002 |
0.339 |
|
| 1994 |
Xie M, Seravalli J, Huskey WP, Schowen KB, Schowen RL. Solvent isotope effects and the nature of electrophilic catalysis in the action of the lactate dehydrogenase of Bacillus stearothermophilus. Bioorganic & Medicinal Chemistry. 2: 691-5. PMID 7858977 DOI: 10.1016/0968-0896(94)85019-4 |
0.387 |
|
| 1994 |
Seravalli J, Huskey WP, Schowen KB, Schowen RL. Catalytic and regulatory strategies of thermophilic lactate dehydrogenase: Microscopic rate constants from kinetic isotope effects Pure and Applied Chemistry. 66: 695-702. DOI: 10.1351/Pac199466040695 |
0.36 |
|
| 1992 |
Huhta DW, Heckenthaler T, Alvarez FJ, Ermer J, Hübner G, Schellenberger A, Schowen RL. The catalytic power of pyruvate decarboxylase. A stochastic model for the molecular evolution of enzymes. Acta Chemica Scandinavica (Copenhagen, Denmark : 1989). 46: 778-88. PMID 1497997 DOI: 10.3891/Acta.Chem.Scand.46-0778 |
0.355 |
|
| 1992 |
Brandt W, Lehmann T, Hofmann T, Schowen RL, Barth A. The probable conformation of substrates recognized by dipeptidyl-peptidase IV and some aspects of the catalytic mechanism derived from theoretical investigations. Journal of Computer-Aided Molecular Design. 6: 159-74. PMID 1352539 DOI: 10.1007/Bf00129426 |
0.322 |
|
| 1990 |
Chokshi HP, Barbush M, Carlson RG, Givens RS, Kuwana T, Schowen RL. Oxalate/hydrogen peroxide chemiluminescence reaction. A 19F NMR probe of the reaction mechanism. Biomedical Chromatography : Bmc. 4: 96-9. PMID 2383698 DOI: 10.1002/Bmc.1130040304 |
0.314 |
|
| 1988 |
Kovach IM, Huber JHA, Schowen RL. Catalytic recruitment in the inactivation of acetylcholinesterase by soman: Temperature dependence of the solvent isotope effect Journal of the American Chemical Society. 110: 590-593. DOI: 10.1021/Ja00210A046 |
0.32 |
|
| 1988 |
Bibbs JA, Demuth HU, Huskey WP, Mordy CW, Schowen RL. On the role of quantum tunneling phenomena in the catalytic power of enzymes Journal of Molecular Catalysis. 47: 187-197. DOI: 10.1016/0304-5102(88)85042-9 |
0.383 |
|
| 1986 |
Wong OS, Sternson LA, Schowen RL. Correction. Reaction ofo-Phthalaldehyde with Alanine and Thiols: Kinetics and Mechanism Journal of the American Chemical Society. 108: 1361-1361. DOI: 10.1021/Ja00266A603 |
0.305 |
|
| 1986 |
Kovach IM, Larson M, Schowen RL. One-proton catalysis in the deacetylation of acetylcholinesterase Journal of the American Chemical Society. 108: 3054-3056. DOI: 10.1002/Chin.198641334 |
0.308 |
|
| 1985 |
Kovach IM, Belz M, Larson M, Rousy S, Schowen RL. Transition-state structures for ester aminolysis with and without rate-limiting proton transfer Journal of the American Chemical Society. 107: 7360-7365. DOI: 10.1002/Chin.198613089 |
0.334 |
|
| 1983 |
Stein RL, Elrod JP, Schowen RL. Correlative variations in enzyme-derived and substrate-derived structures of catalytic transition states. Implications for the catalytic strategy of acyl-transfer enzymes Journal of the American Chemical Society. 105: 2446-2452. DOI: 10.1021/Ja00346A056 |
0.34 |
|
| 1982 |
Rodgers J, Femec DA, Schowen RL. Isotopic mapping of transition-state structural features associated with enzymic catalysis of methyl transfer Journal of the American Chemical Society. 104: 3263-3268. DOI: 10.1021/Ja00376A003 |
0.302 |
|
| 1982 |
Barbara Schowen K, Schowen RL. [29] Solvent isotope effects on enzyme systems Methods in Enzymology. 87: 551-606. DOI: 10.1016/S0076-6879(82)87031-6 |
0.359 |
|
| 1981 |
Schowen KB, Schowen RL. The Use of Isotope Effects to Elucidate Enzyme Mechanisms Bioscience. 31: 826-831. DOI: 10.2307/1308680 |
0.338 |
|
| 1980 |
Hegazi M, Mata-Segreda JF, Schowen RL. Immature hydronium ion as a general transition-state catalytic entity in water reactions Journal of Organic Chemistry. 45: 307-310. DOI: 10.1021/Jo01290A021 |
0.31 |
|
| 1980 |
Kovach IM, Elrod JP, Schowen RL. Reaction progress at the transition state for nucleophilic attack on esters Journal of the American Chemical Society. 102: 7530-7534. DOI: 10.1021/Ja00545A023 |
0.321 |
|
| 1980 |
Quinn DM, Venkatasubban KS, Kise M, Schowen RL. Protonic reorganization and substrate structure in catalysis by amidohydrolases Journal of the American Chemical Society. 102: 5365-5369. DOI: 10.1021/Ja00536A041 |
0.316 |
|
| 1980 |
Quinn DM, Elrod JP, Ardis R, Friesen P, Schowen RL. Protonic reorganization in catalysis by serine proteases: Acylation by small substrates Journal of the American Chemical Society. 102: 5358-5365. DOI: 10.1021/Ja00536A040 |
0.332 |
|
| 1980 |
Elrod JP, Hogg JL, Quinn DM, Venkatasubban KS, Schowen RL. Protonic reorganization and substrate structure in catalysis by serine proteases Journal of the American Chemical Society. 102: 3917-3922. DOI: 10.1021/Ja00531A039 |
0.322 |
|
| 1980 |
Hogg JL, Elrod JP, Schowen RL. Transition-state properties and rate-limiting processes in the acetylation of acetylcholinesterase by natural and unnatural substrates Journal of the American Chemical Society. 102: 2082-2086. DOI: 10.1021/Ja00526A052 |
0.308 |
|
| 1980 |
Kovach IM, Hogg JL, Raben T, Halbert K, Rodgers J, Schowen RL. The .beta.-hydrogen secondary isotope effect in acyl transfer reactions. Origins, temperature dependence, and utility as a probe of transition-state structure Journal of the American Chemical Society. 102: 1991-1999. DOI: 10.1021/Ja00526A039 |
0.333 |
|
| 1979 |
Gray CH, Coward JK, Barbara Schowen K, Schowen RL. α-Deuterium and carbon-13 isotope effects for a simple, intermolecular sulfur-to-oxygen methyl-transfer reaction. Transition-state structures and isotope effects in transmethylation and transalkylation Journal of the American Chemical Society. 101: 4351-4358. DOI: 10.1021/Ja00509A051 |
0.301 |
|
| 1979 |
Mihel I, Knipe JO, Coward JK, Schowen RL. α-Deuterium isotope effects and transition-state structure in an intramolecular model system for methyl-transfer enzymes Journal of the American Chemical Society. 101: 4349-4351. DOI: 10.1021/Ja00509A050 |
0.357 |
|
| 1978 |
Gandour RD, Stella VJ, Coyne M, Schowen RL, Icaza EA. Secondary isotope effects in intramolecular catalysis. Mono-p-bromophenyl succinate hydrolysis Journal of Organic Chemistry. 43: 1705-1708. DOI: 10.1021/Jo00403A017 |
0.337 |
|
| 1975 |
Harmony JA, Himes RH, Schowen RL. The monovalent cation-induced association of formyltetrahydrofolate synthetase subunits: a solvent isotope effect. Biochemistry. 14: 5379-86. PMID 1191644 DOI: 10.1021/Bi00695A023 |
0.361 |
|
| 1975 |
Wang MS, Gandour RD, Rodgers J, Haslam JL, Schowen RL. Transition-state structure for a conformation change of ribonuclease Bioorganic Chemistry. 4: 392-406. DOI: 10.1016/0045-2068(75)90050-4 |
0.348 |
|
| 1974 |
Gandour RD, Schowen RL. Multiproton catalysis in the hydrolysis of 3,5-dinitroaspirin. Journal of the American Chemical Society. 96: 2231-4. PMID 4833644 DOI: 10.1021/Ja00814A038 |
0.352 |
|
| 1974 |
GANDOUR RD, SCHOWEN RL. ChemInform Abstract: CATALYSIS IN ESTER CLEAVAGE PART 6, MULTIPROTON CATALYSIS IN THE HYDROLYSIS OF 3,5-DINITROASPIRIN Chemischer Informationsdienst. 5: no-no. DOI: 10.1002/Chin.197424124 |
0.355 |
|
| 1973 |
Nakano NI, Smissman EE, Schowen RL. Nucleophilic and bifunctional catalysis. Mechanism, reactivity, and transition-state structure in the hydrolysis of 2-chloro-4-isopropylamino-6-cyclopropylamino-s-triazine by N-hydroxysuccinimide and 1-hydroxy-2-piperidone. The Journal of Organic Chemistry. 38: 4396-401. PMID 4782676 DOI: 10.1002/Chin.197413144 |
0.323 |
|
| 1973 |
Pollock E, Hogg JL, Schowen RL. One-proton catalysis in the deacetylation of acetyl- -chymotrypsin. Journal of the American Chemical Society. 95: 968-9. PMID 4688663 DOI: 10.1021/Ja00784A080 |
0.311 |
|
| 1973 |
Williams AE, Lee JK, Schowen RL. Catalysis in ester cleavage. V. Catalytic mechanism of intermolecularly carboxylate-assisted acyl transfer The Journal of Organic Chemistry. 38: 4053-4056. DOI: 10.1021/Jo00987A021 |
0.309 |
|
| 1973 |
Minor SS, Schowen RL. Catalysis in ester cleavage. IV. One-proton solvation bridge intramolecular carboxylate catalysis of ester hydrolysis Journal of the American Chemical Society. 95: 2279-2281. DOI: 10.1021/Ja00788A029 |
0.364 |
|
| 1973 |
Drake D, Schowen RL, Jayaraman H. Amide hydrolysis. VI. Diffusion-controlled proton transfer and heavy-atom reorganization in the general acid, specific base catalyzed hydrolysis of amides Journal of the American Chemical Society. 95: 454-458. DOI: 10.1021/Ja00783A024 |
0.301 |
|
| 1972 |
O'Donnell K, Bacon R, Chellappa KL, Schowen RL, Lee JK. Catalysis in organosilicon chemistry. III. Catalytic mode, solvent isotope effets, and transition-state structure in hydride expulsion from silicon Journal of the American Chemical Society. 94: 2500-2505. DOI: 10.1021/Ja00762A051 |
0.306 |
|
| 1972 |
Gandour RD, Schowen RL. Chapter 26. Intramolecular Catalysis in Medicinal Chemistry Annual Reports in Medicinal Chemistry. 7: 279-288. DOI: 10.1016/S0065-7743(08)60821-0 |
0.367 |
|
| 1971 |
Schowen RL, Kershner LD. Amide hydrolysis. IV. Proton transfer and heavy-atom reorganization in amide hydrolysis. Valence-isomeric transition states Journal of the American Chemical Society. 93: 2014-2024. DOI: 10.1021/Ja00737A029 |
0.332 |
|
| 1969 |
Mitton CG, Gresser M, Schowen RL. Catalysis in ester cleavage. III. Solvent isotope effects and transition-state solvation in the basic methanolysis of esters Journal of the American Chemical Society. 91: 2045-2047. DOI: 10.1021/Ja01036A030 |
0.334 |
|
| 1967 |
Schowen RL, Latham KS. The transition state for base-catalyzed cleavage of the silicon-oxygen bond Journal of the American Chemical Society. 89: 4677-4683. DOI: 10.1021/Ja00994A018 |
0.302 |
|
| 1966 |
Schowen RL, Jayaraman H, Kershner L, Zuorick GW. Solvent isotope effects in amide hydrolysis. Journal of the American Chemical Society. 88: 4008-12. PMID 5915154 DOI: 10.1021/Ja00969A020 |
0.315 |
|
| 1966 |
Schowen RL, Zuorick GW. Amide hydrolysis. Superimposed general base catalysis in the cleavage of anilides Journal of the American Chemical Society. 88: 1223-1225. DOI: 10.1021/Ja00958A025 |
0.305 |
|
| 1966 |
Schowen RL, Jayaraman H, Kershner L. Kinetic evidence for a two-step mechanism of amide hydrolysis Tetrahedron Letters. 7: 497-500. DOI: 10.1016/S0040-4039(00)72910-8 |
0.319 |
|
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