| Year |
Citation |
Score |
| 2004 |
Rendle PM, Seger A, Rodrigues J, Oldham NJ, Bott RR, Jones JB, Cowan MM, Davis BG. Glycodendriproteins: a synthetic glycoprotein mimic enzyme with branched sugar-display potently inhibits bacterial aggregation. Journal of the American Chemical Society. 126: 4750-1. PMID 15080658 DOI: 10.1021/Ja031698U |
0.492 |
|
| 2003 |
Davis BG, Sala RF, Hodgson DR, Ullman A, Khumtaveeporn K, Estell DA, Sanford K, Bott RR, Jones JB. Selective protein degradation by ligand-targeted enzymes: towards the creation of catalytic antagonists. Chembiochem : a European Journal of Chemical Biology. 4: 533-7. PMID 12794865 DOI: 10.1002/Cbic.200300591 |
0.521 |
|
| 2003 |
Davis BG, Sala RF, Hodgson DRW, Ullman A, Khumtaveeporn K, Estell DA, Sanford K, Bott RR, Jones JB. Cover Picture: Selective Protein Degradation by Ligand-Targeted Enzymes: Towards the Creation of Catalytic Antagonists (ChemBioChem 6/2003) Chembiochem. 4: 457-457. DOI: 10.1002/Cbic.200390074 |
0.541 |
|
| 2003 |
Jones JB, Jakovac IJ. Preparation of Chiral, Nonracemic γ-Lactones by Enzymecatalyzed Oxidation of meso-Diols: ( + )-(1R,6S)-8-Oxabicyclo[4.3.0]Nonan-7-One Organic Syntheses. 10-10. DOI: 10.1002/0471264180.Os063.02 |
0.318 |
|
| 2002 |
Matsumoto K, Davis BG, Jones JB. Chemically modified "polar patch" mutants of subtilisin in peptide synthesis with remarkably broad substrate acceptance: designing combinatorial biocatalysts. Chemistry (Weinheim An Der Bergstrasse, Germany). 8: 4129-37. PMID 12298003 DOI: 10.1002/1521-3765(20020916)8:18<4129::Aid-Chem4129>3.0.Co;2-V |
0.577 |
|
| 2001 |
Matsumoto K, Davis BG, Jones JB. Glycosylation of the primary binding pocket of a subtilisin protease causes a remarkable broadening in stereospecificity in peptide synthesis Chemical Communications. 903-904. DOI: 10.1039/B010021H |
0.578 |
|
| 2001 |
Khumtaveeporn K, Ullmann A, Matsumoto K, Davis BG, Jones JB. Expanding the utility of proteases in synthesis: Broadening the substrate acceptance in non-coded amide bond formation using chemically modified mutants of subtilisin Tetrahedron Asymmetry. 12: 249-261. DOI: 10.1016/S0957-4166(01)00024-6 |
0.58 |
|
| 2000 |
Dickman M, Jones JB. Covalent modification of subtilisin Bacillus lentus cysteine mutants with enantiomerically pure chiral auxiliaries causes remarkable changes in activity. Bioorganic & Medicinal Chemistry. 8: 1957-1968. PMID 11003141 DOI: 10.1016/S0968-0896(00)00121-8 |
0.421 |
|
| 2000 |
Lloyd RC, Davis BG, Jones JB. Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity. Bioorganic & Medicinal Chemistry. 8: 1537-44. PMID 10976502 DOI: 10.1016/S0968-0896(00)00084-5 |
0.587 |
|
| 2000 |
Davis BG, Lloyd RC, Jones JB. Controlled site-selective protein glycosylation for precise glycan structure-catalytic activity relationships. Bioorganic & Medicinal Chemistry. 8: 1527-35. PMID 10976501 DOI: 10.1016/S0968-0896(00)00083-3 |
0.539 |
|
| 2000 |
DeSantis G, Paech C, Jones JB. Benzophenone boronic acid photoaffinity labeling of subtilisin CMMs to probe altered specificity. Bioorganic & Medicinal Chemistry. 8: 563-570. PMID 10732973 DOI: 10.1016/S0968-0896(99)00320-X |
0.37 |
|
| 2000 |
Davis BG, Maughan MAT, Green MP, Ullman A, Jones JB. Glycomethanethiosulfonates: Powerful reagents for protein glycosylation Tetrahedron Asymmetry. 11: 245-262. DOI: 10.1016/S0957-4166(99)00497-8 |
0.526 |
|
| 1999 |
Davis BG, Khumtaveeporn K, Bott RR, Jones JB. Altering the specificity of subtilisin Bacillus lentus through the introduction of positive charge at single amino acid sites. Bioorganic & Medicinal Chemistry. 7: 2303-11. PMID 10632040 DOI: 10.1016/S0968-0896(99)00168-6 |
0.556 |
|
| 1999 |
Davis BG, Shang X, DeSantis G, Bott RR, Jones JB. The controlled introduction of multiple negative charge at single amino acid sites in subtilisin Bacillus lentus. Bioorganic & Medicinal Chemistry. 7: 2293-301. PMID 10632039 DOI: 10.1016/S0968-0896(99)00167-4 |
0.546 |
|
| 1999 |
DeSantis G, Jones JB. Probing the altered specificity and catalytic properties of mutant subtilisin chemically modified at position S156C and S166C in the S1 pocket. Bioorganic & Medicinal Chemistry. 7: 1381-1387. PMID 10465412 DOI: 10.1016/S0968-0896(99)00068-1 |
0.381 |
|
| 1999 |
DeSantis G, Jones JB. Chemical modification of enzymes for enhanced functionality. Current Opinion in Biotechnology. 10: 324-330. PMID 10449313 DOI: 10.1016/S0958-1669(99)80059-7 |
0.416 |
|
| 1999 |
Davis BG, Jones JB. Glycoprotein Synthesis: From Glycobiological Tools to Tailor-made Catalysts Synlett. 1999: 1495-1507. DOI: 10.1055/S-1999-2865 |
0.462 |
|
| 1999 |
Plettner E, DeSantis G, Stabile MR, Jones JB. Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of cysteine mutants Journal of the American Chemical Society. 121: 4977-4981. DOI: 10.1021/Ja9902266 |
0.366 |
|
| 1999 |
Jones JB, DeSantis G. Toward Understanding and Tailoring the Specificity of Synthetically Useful Enzymes Accounts of Chemical Research. 32: 99-107. DOI: 10.1021/Ar960078D |
0.368 |
|
| 1999 |
Khumtaveeporn K, DeSantis G, Jones JB. Expanded structural and stereospecificity in peptide synthesis with chemically modified mutants of subtilisin Tetrahedron-Asymmetry. 10: 2563-2572. DOI: 10.1016/S0957-4166(99)00255-4 |
0.393 |
|
| 1998 |
Plettner E, Khumtaveeporn K, Shang X, Jones JB. A combinatorial approach to chemical modification of subtilisin Bacillus lentus Bioorganic & Medicinal Chemistry Letters. 8: 2291-2296. PMID 9873530 DOI: 10.1016/S0960-894X(98)00415-6 |
0.33 |
|
| 1998 |
Davis BG, Lloyd RC, Jones JB. Controlled site-selective glycosylation of proteins by a combined site- directed mutagenesis and chemical modification approach Journal of Organic Chemistry. 63: 9614-9615. DOI: 10.1021/Jo9816461 |
0.496 |
|
| 1998 |
and GD, Jones JB. Chemical Modifications at a Single Site Can Induce Significant Shifts in the pH Profiles of a Serine Protease Journal of the American Chemical Society. 120: 8582-8586. DOI: 10.1021/Ja980072E |
0.428 |
|
| 1998 |
Dickman M, Lloyd RC, Jones JB. Chemically modified mutants of subtilisin Bacillus lentus catalyze transesterification reactions better than wild type Tetrahedron-Asymmetry. 9: 4099-4102. DOI: 10.1016/S0957-4166(98)00450-9 |
0.373 |
|
| 1998 |
Lloyd RC, Dickman M, Jones JB. Probing the specificity of the S1′, leaving group, site of subtilisin Bacillus lentus using an enzyme-catalyzed transesterification reaction Tetrahedron-Asymmetry. 9: 551-561. DOI: 10.1016/S0957-4166(98)00022-6 |
0.352 |
|
| 1997 |
Martichonok V, Jones JB. Crysteine Proteases such as papain are not inhibited by substrate analogue peptidyl boronic acids Bioorganic & Medicinal Chemistry. 5: 679-684. PMID 9158866 DOI: 10.1016/S0968-0896(97)00008-4 |
0.34 |
|
| 1997 |
Ma GX, Batey RA, Tayler SD, Hum G, Jones JB. The Synthesis of Dienecarbamates as Adapt Prodrug Models Synthetic Communications. 27: 2445-2453. DOI: 10.1080/00397919708004108 |
0.313 |
|
| 1997 |
and TL, Jones JB. Probing the Abilities of Synthetically Useful Serine Proteases To Discriminate Remote Stereocenters. Chiral Naphthyl Aldehyde Inhibitors Journal of the American Chemical Society. 119: 10260-10268. DOI: 10.1021/Ja9708777 |
0.373 |
|
| 1997 |
Berglund P, DeSantis G, Stabile MR, Shang X, Gold M, Bott RR, Graycar TP, Lau TH, Mitchinson C, Jones JB. Chemical Modification of Cysteine Mutants of Subtilisin Bacillus lentus Can Create Better Catalysts Than the Wild-Type Enzyme Journal of the American Chemical Society. 119: 5265-5266. DOI: 10.1021/Ja970344Y |
0.334 |
|
| 1996 |
Strynadka NC, Martin R, Jensen SE, Gold M, Jones JB. Structure-based design of a potent transition state analogue for TEM-1 beta-lactamase. Nature Structural Biology. 3: 688-95. PMID 8756327 DOI: 10.1038/Nsb0896-688 |
0.313 |
|
| 1996 |
Bonneau PR, Martin R, Lee T, Sakowicz R, Martichonok V, Hogan JK, Gold M, Jones JB. Enzymes in Organics Synthesis. Present and Future Journal of the Brazilian Chemical Society. 7: 357-369. DOI: 10.5935/0103-5053.19960065 |
0.392 |
|
| 1996 |
Lee T, Sakowicz R, Martichonok V, Hogan JK, Gold M, Jones JB, Undheim K, Rosendahl CN, Haugg M, Trabesinger-Rüf N, Weinhold EG. Probing Enzymes Specificity Acta Chemica Scandinavica. 50: 697-706. DOI: 10.3891/Acta.Chem.Scand.50-0697 |
0.359 |
|
| 1996 |
and TL, Jones JB. Probing the Abilities of Synthetically Useful Serine Proteases To Discriminate between the Configurations of Remote Stereocenters Using Chiral Aldehyde Inhibitors Journal of the American Chemical Society. 118: 502-508. DOI: 10.1021/Ja952835T |
0.386 |
|
| 1996 |
and VM, Jones JB. Probing the Specificity of the Serine Proteases Subtilisin Carlsberg and α-Chymotrypsin with Enantiomeric 1-Acetamido Boronic Acids. An Unexpected Reversal of the Normal “l”-Stereoselectivity Preference Journal of the American Chemical Society. 118: 950-958. DOI: 10.1021/Ja952816J |
0.36 |
|
| 1996 |
Berglund P, Stabile MR, Gold M, Jones JB, Mitchinson C, Bott RR, Graycar TP. Altering the specificity of subtilisin B. lentus by combining site-directed mutagenesis and chemical modification Bioorganic and Medicinal Chemistry Letters. 6: 2507-2512. DOI: 10.1016/0960-894X(96)00467-2 |
0.42 |
|
| 1996 |
Stabile MR, Lai WG, DeSantis G, Gold M, Jones JB, Mitchinson C, Bott RR, Graycar TP, Liu CC. Probing the specificity of the S1 binding site of M222 mutants of subtilisin B. lentus with boronic acid inhibitors Bioorganic and Medicinal Chemistry Letters. 6: 2501-2506. DOI: 10.1016/0960-894X(96)00466-0 |
0.369 |
|
| 1996 |
Occhiato E, Jones JB. Probing enzyme stereospecificity. Inhibition of α-chymotrypsin and subtilisin Carlsberg by chiral amine- and aminoalcohol-derivatives Tetrahedron. 52: 4199-4214. DOI: 10.1016/0040-4020(96)00078-6 |
0.376 |
|
| 1995 |
Martichonok V, Jones JB. (Z)-Heptadec-8-enylboronic acid: a potential lipase inhibitor Journal of the Chemical Society-Perkin Transactions 1. 2927-2929. DOI: 10.1039/P19950002927 |
0.32 |
|
| 1995 |
Sakowicz R, Gold M, Jones JB. Partial Reversal Of The Substrate Stereospecificity Of An L-Lactate Dehydrogenase By Site-Directed Mutagenesis Journal of the American Chemical Society. 117: 2387-2394. DOI: 10.1021/Ja00114A002 |
0.348 |
|
| 1995 |
Martin R, Jones JB. Rational design and synthesis of a highly effective transition state analog inhibitor of the RTEM-1 β-lactamase Tetrahedron Letters. 36: 8399-8402. DOI: 10.1016/0040-4039(95)01799-N |
0.305 |
|
| 1995 |
Lee T, Jones JB. Probing enzyme stereospecificity. Evaluation of β-Alkoxy-α-amino acids with two stereocenters as inhibitors of serine proteases Tetrahedron. 51: 7331-7346. DOI: 10.1016/0040-4020(95)00382-I |
0.389 |
|
| 1994 |
Seufer-Wasserthal P, Martichonok V, Keller TH, Chin B, Martin R, Jones JB. Probing the specificity of the S1 binding site of subtilisin Carlsberg with boronic acids. Bioorganic & Medicinal Chemistry. 2: 35-48. PMID 7922119 DOI: 10.1016/S0968-0896(00)82200-2 |
0.351 |
|
| 1994 |
Provencher L, Jones JB. A Concluding Specification of the Dimensions of the Active Site Model of Pig Liver Esterase Journal of Organic Chemistry. 59: 2729-2732. DOI: 10.1021/Jo00089A015 |
0.372 |
|
| 1994 |
Martin R, Gold M, Jones J. Inhibition of the RTEM-1 β-lactamase by boronic acids Bioorganic & Medicinal Chemistry Letters. 4: 1229-1234. DOI: 10.1016/S0960-894X(01)80336-X |
0.324 |
|
| 1993 |
Kallwass HK, Surewicz WK, Parris W, Macfarlane EL, Luyten MA, Kay CM, Gold M, Jones JB. Single amino acid substitutions can further increase the stability of a thermophilic L-lactate dehydrogenase. Protein Engineering. 5: 769-74. PMID 1287656 DOI: 10.1093/Protein/5.8.769 |
0.403 |
|
| 1993 |
Jones JB. 1992 Alfred Bader Award Lecture Probing the specificity of synthetically useful enzymes Canadian Journal of Chemistry. 71: 1273-1282. DOI: 10.1139/V93-164 |
0.405 |
|
| 1993 |
Provencher L, Wynn H, Jones JB, Krawczyk AR. Enzymes in organic synthesis 51. Probing the dimensions of the large hydrophobic pocket of the active site of pig liver esterase Tetrahedron-Asymmetry. 4: 2025-2040. DOI: 10.1016/S0957-4166(00)82251-X |
0.381 |
|
| 1993 |
Kallwass HKW, Parris W, Macfariane ELA, Gold M, Jones JB. Site-specific immobilization of an L-lactate dehydrogenase via an engineered surface cysteine residue Biotechnology Letters. 15: 29-34. DOI: 10.1007/Bf00131548 |
0.397 |
|
| 1992 |
Sakowicz R, Kallwass H, Parris W, Gold M, Jones JB. THR246 mutations decrease substrate inhibition in lactate dehydrogenase Biochemical and Biophysical Research Communications. 182: 1309-1312. PMID 1540173 DOI: 10.1016/0006-291X(92)91875-Q |
0.38 |
|
| 1992 |
Hultin PG, Mueseler FJ, Jones JB. Enzymes in organic synthesis. 48. Pig liver esterase and porcine pancreatic lipase catalyzed hydrolyses of 3,4-(isopropylidenedioxy)-2,5-tetrahydrofuranyl diesters. [Erratum to document cited in CA115(13):135963e] The Journal of Organic Chemistry. 57: 2978-2978. DOI: 10.1021/Jo00036A051 |
0.366 |
|
| 1992 |
Kallwass HKW, Hogan JK, Macfarlane ELA, Martichonok V, Parris W, Kay CM, Gold M, Jones JB. On the factors controlling the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus: effects of Gln102.fwdarw.Arg and Arg171.fwdarw.Trp/Tyr double mutations Journal of the American Chemical Society. 114: 10704-10710. DOI: 10.1021/Ja00053A004 |
0.344 |
|
| 1992 |
Kallwass HKW, Luyten MA, Parris W, Gold M, Kay CM, Jones JB. Effects of Gln102Arg and Cys97Gly mutations on the structural specificity and stereospecificity of the L-lactate dehydrogenase from Bacillus stearothermophilus Journal of the American Chemical Society. 114: 4551-4557. DOI: 10.1021/Ja00038A016 |
0.345 |
|
| 1992 |
Simpelkamp J, Jones JB. Borinic acid inhibitors as probes of the factors involved in binding at the active sites of subtilisin carlsberg and α-chymotrypsin Bioorganic & Medicinal Chemistry Letters. 2: 1391-1394. DOI: 10.1016/S0960-894X(00)80519-3 |
0.392 |
|
| 1992 |
Hultin PG, Jones J. Dilemma regarding an active site model for porcine pancreatic lipase Tetrahedron Letters. 33: 1399-1402. DOI: 10.1016/S0040-4039(00)91631-9 |
0.348 |
|
| 1992 |
Hultin PG, Jones J. Probing trypsin specificity with basic 3-substituted glutarate diesters and related monoester substrate analogs: Evidence for allosteric activation of trypsin catalysis Bioorganic Chemistry. 20: 30-41. DOI: 10.1016/0045-2068(92)90023-V |
0.428 |
|
| 1992 |
Hoga JK, Parris W, Gold M, Jones JB. The substrate specificity of the muscle l-lactate dehydrogenase of spiny dogfish (Squalus acanthis) Bioorganic Chemistry. 20: 204-212. DOI: 10.1016/0045-2068(92)90013-S |
0.314 |
|
| 1991 |
Keller TH, Seufer-Wasserthal P, Jones JB. Probing the specificity of the S1 binding site of subtilisin Carlsberg with boronic acids Biochemical and Biophysical Research Communications. 176: 401-405. PMID 2018529 DOI: 10.1016/0006-291X(91)90938-4 |
0.335 |
|
| 1991 |
Hultin PG, Mueseler FJ, Jones JB. Enzymes in organic synthesis. 48. Pig liver esterase and porcine pancreatic lipase catalyzed hydrolyses of 3,4-(isopropylidenedioxy)-2,5-tetrahydrofuranyl diesters The Journal of Organic Chemistry. 56: 5375-5380. DOI: 10.1021/Jo00018A033 |
0.411 |
|
| 1991 |
Toone EJ, Jones JB. Enzymes in organic synthesis 50. Probing the dimensions of the large hydrophobic binding region of the active site of pig liver esterase using substituted aryl malonate substrates Tetrahedron: Asymmetry. 2: 1041-1052. DOI: 10.1016/S0957-4166(00)86155-8 |
0.67 |
|
| 1991 |
Toone EJ, Jones JB. Enzymes in organic synthesis 49. Resolutions of racemic monocyclic esters with pig liver esterase Tetrahedron: Asymmetry. 2: 207-222. DOI: 10.1016/S0957-4166(00)82360-5 |
0.665 |
|
| 1990 |
Toone EJ, Werth MJ, Jones JB. Enzymes in organic synthesis. 47. Active-site model for interpreting and predicting the specificity of pig liver esterase Journal of the American Chemical Society. 112: 4946-4952. DOI: 10.1021/Ja00168A047 |
0.64 |
|
| 1989 |
Bur D, Clarke T, Friesen JD, Gold M, Hart KW, Holbrook JJ, Jones JB, Luyten MA, Wilks HM. On the effect on specificity of Thr246→Gly mutation in L-lactate dehydrogenase of Bacillus stearothermophilus Biochemical and Biophysical Research Communications. 161: 59-63. PMID 2499337 DOI: 10.1016/0006-291X(89)91559-3 |
0.405 |
|
| 1989 |
Bur D, Luyten MA, Wynn H, Provencher LR, Jones JB, Gold M, Friesen JD, Clarke AR, Holbrook JJ. An evaluation of the substrate specificity and asymmetric synthesis potential of the cloned L-lactate dehydrogenase from Bacillusstearothermophilus Canadian Journal of Chemistry. 67: 1065-1070. DOI: 10.1139/V89-161 |
0.452 |
|
| 1989 |
Krawczyk AR, Jones JB. Enzymes in organic synthesis. 46. Regiospecific and stereoselective horse liver alcohol dehydrogenase catalyzed reductions of cis- and trans-bicyclo[4.3.0]nonanones Journal of Organic Chemistry. 54: 1795-1801. DOI: 10.1021/Jo00269A010 |
0.405 |
|
| 1989 |
Luyten MA, Bur D, Wynn H, Parris W, Gold M, Friesen JD, Jones JB. An evaluation of the substrate specificity, and of its modification by site-directed mutagenesis, of the cloned L-lactate dehydrogenase from Bacillus stearothermophilus Journal of the American Chemical Society. 111: 6800-6804. DOI: 10.1021/Ja00199A046 |
0.349 |
|
| 1988 |
Lam LK-, Jones JB. Enzymes in organic synthesis. 44. Stereoselective pig liver esterase-catalyzed hydrolyses of 3-substituted glutarate diesters of compactin-synthon interest Canadian Journal of Chemistry. 66: 1422-1424. DOI: 10.1139/V88-229 |
0.451 |
|
| 1988 |
Lam LKP, Jones JB. Enzymes in organic synthesis. 43. Investigation of the preferred orientations of ester groups in pig liver esterase catalyzed hydrolyses using conformationally rigid substrates Journal of Organic Chemistry. 53: 2637-2639. DOI: 10.1021/Jo00246A049 |
0.437 |
|
| 1988 |
Lam LKP, Gair IA, Jones JB. Enzymes in organic synthesis. 42. Stereoselective horse liver alcohol dehydrogenase catalyzed reductions of heterocyclic bicyclic ketones Journal of Organic Chemistry. 53: 1611-1615. DOI: 10.1021/Jo00243A004 |
0.426 |
|
| 1988 |
Lam LKP, Brown CM, De Jeso B, Lym L, Toone EJ, Jones JB. Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolysis of asymmetric synthetic value Journal of the American Chemical Society. 110: 4409-4411. DOI: 10.1021/Ja00221A049 |
0.639 |
|
| 1988 |
Dodds DR, Jones JB. Enzymes in organic synthesis. 38. Preparations of enantiomerically pure chiral hydroxydecalones via stereospecific horse liver alcohol dehydrogenase catalyzed reductions of decalindiones Journal of the American Chemical Society. 110: 577-583. DOI: 10.1021/Ja00210A044 |
0.431 |
|
| 1987 |
Jones JB. Some examples of enzymes in organic synthesis Annals of the New York Academy of Sciences. 501: 119-128. PMID 3475007 DOI: 10.1111/J.1749-6632.1987.Tb45696.X |
0.394 |
|
| 1987 |
Hart KW, Clarke AR, Wigley DB, Waldman AD, Chia WN, Barstow DA, Atkinson T, Jones JB, Holbrook JJ. A strong carboxylate-arginine interaction is important in substrate orientation and recognition in lactate dehydrogenase. Biochimica Et Biophysica Acta. 914: 294-8. PMID 3113484 DOI: 10.1016/0167-4838(87)90289-5 |
0.393 |
|
| 1987 |
Toone EJ, Jones JB. Enzymes in organic synthesis. 40. Evaluation of the enantioselectivity of the pig liver esterase catalyzed hydrolyses of racemic piperidine carboxylic acid esters Canadian Journal of Chemistry. 65: 2722-2726. DOI: 10.1139/V87-452 |
0.657 |
|
| 1987 |
Jones JB, Hinks RS. Enzymes in organic synthesis. 36. Synthesis of optically active civet constituent from an enzyme-generated chiral synthon Canadian Journal of Chemistry. 65: 704-707. DOI: 10.1139/V87-119 |
0.429 |
|
| 1987 |
Sabbioni G, Jones JB. Enzymes in organic synthesis. 39. Preparations of chiral cyclic acid-esters and bicyclic lactones via stereoselective pig liver esterase catalyzed hydrolyses of cyclic meso diesters Journal of Organic Chemistry. 52: 4565-4570. DOI: 10.1021/Jo00229A024 |
0.462 |
|
| 1986 |
Ramaswamy S, Hui RAHF, Jones JB. Enantiomerically selective pig liver esterase-catalysed hydrolyses of racemic allenic esters Journal of the Chemical Society, Chemical Communications. 1545-1546. DOI: 10.1039/C39860001545 |
0.385 |
|
| 1986 |
Lam LKP, Hui RAHF, Jones JB. Enzymes in organic synthesis. 35. Stereoselective pig liver esterase catalyzed hydrolyses of 3-substituted glutarate diesters. Optimization of enantiomeric excess via reaction conditions control Journal of Organic Chemistry. 51: 2047-2050. DOI: 10.1021/Jo00361A021 |
0.408 |
|
| 1985 |
Jones JB, Hinks RS, Hultin PG. Enzymes in organic synthesis. 33. Stereoselective pig liver esterase-catalyzed hydrolyses of meso cyclopentyl-, tetrahydrofuranyl-, and tetrahydrothiophenyl-1,3-diesters Canadian Journal of Chemistry. 63: 452-456. DOI: 10.1139/V85-074 |
0.416 |
|
| 1985 |
Kasel W, Hultin PG, Jones JB. Preparation of chiral hydroxyester synthons vis stereoselective porcine pancreatic lipase-catalysed hydrolyses of meso-diesters Journal of the Chemical Society, Chemical Communications. 1563-1564. DOI: 10.1039/C39850001563 |
0.326 |
|
| 1985 |
Lok KP, Jakovac IJ, Jones JB. Enzymes in organic synthesis. 34. Preparations of enantiomerically pure exo- and endo-bridged bicyclic [2.2.1] and [2.2.2] chiral lactones via stereospecific horse liver alcohol dehydrogenase catalyzed oxidations of meso diols Journal of the American Chemical Society. 107: 2521-2526. DOI: 10.1021/Ja00294A052 |
0.43 |
|
| 1984 |
Jones JB, Francis CJ. Enzymes in organic synthesis. 32. Stereospecific horse liver alcohol dehydrogenase-catalyzed oxidations of exo- and endo-oxabicyclic meso diols Canadian Journal of Chemistry. 62: 2578-2582. DOI: 10.1139/V84-440 |
0.403 |
|
| 1984 |
Jones JB, Takemura T. Enzymes in organic synthesis. 30. Reaction conditions – control of enantiomeric purities. Horse liver alcohol dehydrogenase-catalyzed reductions of 2-alkylcyclohexanones and their thiopyran analogs Canadian Journal of Chemistry. 62: 77-80. DOI: 10.1139/V84-015 |
0.407 |
|
| 1984 |
Francis CJ, Jones JB. Preparations of chiral δ-lactones via enantiotopically specific pig liver esterase-catalysed hydrolyses of 3-substituted glutaric acid diesters Journal of the Chemical Society, Chemical Communications. 579-580. DOI: 10.1039/C39840000579 |
0.378 |
|
| 1984 |
Sabbioni G, Shea ML, Jones JB. Preparations of bicyclic chiral lactone synthons via stereospecific pig liver esterase-catalysed hydrolyses of meso-diesters. Ring-size induced reversal of stereospecificity Journal of the Chemical Society, Chemical Communications. 236-238. DOI: 10.1039/C39840000236 |
0.345 |
|
| 1984 |
Bridges AJ, Raman PS, Ng GSY, Jones JB. Enzymes in organic synthesis. 31. Preparations of enantiomerically pure bicyclic [3.2.1] and [3.3.1] chiral lactones via stereospecific horse liver alcohol dehydrogenase catalyzed oxidations of meso diols Journal of the American Chemical Society. 106: 1461-1467. DOI: 10.1021/Ja00317A046 |
0.428 |
|
| 1983 |
Takemura T, Jones JB. Enzymes in organic synthesis. 27. Horse liver alcohol dehydrogenase-catalyzed oxidoreductions of 3-alkylthiopyran ketones and alcohols Journal of Organic Chemistry. 14: 791-796. DOI: 10.1021/Jo00154A007 |
0.368 |
|
| 1982 |
Jones JB, Takemura T. Enzymes in organic synthesis. 28. Reinvestigation of the horse liver alcohol dehydrogenase-catalyzed reductions of 2-alkylcyclohexanones.Identification of cis-alkylcyclohexanols as minor products Canadian Journal of Chemistry. 60: 2950-2956. DOI: 10.1139/V82-423 |
0.326 |
|
| 1982 |
Jones JB, Finch MAW, Jakovac IJ. Enzymes in organic synthesis. 26.Synthesis of enantiomerically pure grandisol from an enzyme-generated chiral synthon Canadian Journal of Chemistry. 60: 2007-2011. DOI: 10.1139/V82-283 |
0.409 |
|
| 1982 |
Jones JB, Schwartz HM. Enzymes in organic synthesis. 22. Effects of organic solvents on horse liver alcohol dehydrogenase-catalyzed reduction Canadian Journal of Chemistry. 60: 1030-1033. DOI: 10.1139/V82-051 |
0.359 |
|
| 1982 |
Jones JB, Jakovac IJ. A new cubic-space section model for predicting the specificity of horse liver alcohol dehydrogenase-catalyzed oxidoreductions Canadian Journal of Chemistry. 60: 19-28. DOI: 10.1139/V82-005 |
0.349 |
|
| 1982 |
Haslegrave JA, Jones JB. Enzymes in organic synthesis. 25. Heterocyclic ketones as substrates of horse liver alcohol dehydrogenase. Highly stereoselective reductions of 2-substituted tetrahydropyran-4-ones Journal of the American Chemical Society. 104: 4666-4671. DOI: 10.1021/Ja00381A025 |
0.442 |
|
| 1982 |
Jakovac IJ, Goodbrand HB, Lok KP, Jones JB. Enzymes in organic synthesis. 24. Preparations of enantiomerically pure chiral lactones via stereospecific horse liver alcohol dehydrogenase catalyzed oxidations of monocyclic meso diols Journal of the American Chemical Society. 104: 4659-4665. DOI: 10.1021/Ja00381A024 |
0.427 |
|
| 1981 |
Jones JB, Pliura DH. Effects of organic solvents on immobilized enzyme catalyses. Chymotrypsin immobilized on porous glass Canadian Journal of Chemistry. 59: 2921-2925. DOI: 10.1139/V81-423 |
0.325 |
|
| 1981 |
Jones JB, Schwartz HM. Enzymes in organic syntheses. 19. Evaluation of the stereoselectivities of horse liver alcohol dehydrogenase; catalyzed oxidoreductions of hydroxy- and ketothiolanes, -thianes, and -thiepanes Canadian Journal of Chemistry. 59: 1574-1579. DOI: 10.1139/V81-232 |
0.41 |
|
| 1980 |
Pliura DH, Jones JB. Effects of organic solvents on immobilized enzyme catalyses. Chymotrypsin immobilized on Sephadex Canadian Journal of Chemistry. 58: 2633-2640. DOI: 10.1139/V80-421 |
0.329 |
|
| 1980 |
Jakovac IJ, Ng G, Lok KP, Jones JB. Preparation of useful chiral lactone synthons via stereospecific enzyme-catalysed oxidations of meso-diols Journal of the Chemical Society, Chemical Communications. 515-516. DOI: 10.1039/C39800000515 |
0.411 |
|
| 1979 |
Jones JB, Dodds DR. Enzymes in organic synthesis 17. Oxidoreductions of alcohols, aldehydes, and ketones using chemically modified horse liver alcohol dehydrogenase Canadian Journal of Chemistry. 57: 2533-2538. DOI: 10.1139/V79-406 |
0.393 |
|
| 1979 |
Jones JB, Mehes MM. Effects of organic cosolvents on enzyme stereospecificity. The enantiomeric specificity of α-chymotrypsin is reduced by high organic solvent concentrations Canadian Journal of Chemistry. 57: 2245-2248. DOI: 10.1139/V79-359 |
0.383 |
|
| 1979 |
Jones JB, Lok KP. Enzymes in organic synthesis. 14. Stereoselective horse liver alcohol dehydrogenase catalyzed oxidations of diols containing a prochiral centre and of related hemiacetals Canadian Journal of Chemistry. 57: 1025-1032. DOI: 10.1139/V79-170 |
0.404 |
|
| 1979 |
Davies J, Jones JB. Enzymes in organic synthesis. 16. Heterocyclic ketones as substrates of horse liver alcohol dehydrogenase. Stereospecific reductions of 2-substituted tetrahydrothiopyran-4-ones Journal of the American Chemical Society. 101: 5405-5410. DOI: 10.1021/Ja00512A048 |
0.438 |
|
| 1978 |
Irwin AJ, Lok KP, Huang KW, Jones JB. Enzymes in organic synthesis. Influence of substrate structure on rates of horse liver alcohol dehydrogenase-catalysed oxidoreductions Journal of the Chemical Society-Perkin Transactions 1. 12: 1636-1642. PMID 570570 DOI: 10.1039/P19780001636 |
0.401 |
|
| 1977 |
Irwin AJ, Jones JB. Asymmetric syntheses via enantiotopically selective horse liver alcohol dehydrogenase catalyzed oxidations of diols containing a prochiral center Journal of the American Chemical Society. 99: 556-561. PMID 830692 DOI: 10.1021/Ja00444A040 |
0.409 |
|
| 1977 |
Irwin AJ, Jones JB. Regiospecific and enantioselective horse liver alcohol dehydrogenase catalyzed oxidations of some hydroxycyclopentanes Journal of the American Chemical Society. 99: 1625-1630. PMID 557066 DOI: 10.1021/Ja00447A057 |
0.356 |
|
| 1977 |
Jones JB, Goodbrand HB. Regiospecific horse liver alcohol dehydrogenase-catalyzed oxidations of some bishydroxycyclohexanes Canadian Journal of Chemistry. 55: 2685-2691. DOI: 10.1139/V77-374 |
0.327 |
|
| 1977 |
Jones JB, Taylor KE. Hydroxymethylbenzimidazole carboxylic acid models of the Asp-His-Ser charge relay system of serine proteases Canadian Journal of Chemistry. 55: 1653-1657. DOI: 10.1139/V77-233 |
0.375 |
|
| 1977 |
Goodbrand HB, Jones JB. Enzyme discrimination between conformational enantiomers as a means of effecting asymmetric syntheses Journal of the Chemical Society, Chemical Communications. 469-470. DOI: 10.1039/C39770000469 |
0.395 |
|
| 1977 |
Irwin AJ, Jones JB. Stereospecific thallium(III) nitrate mediated conversion of bicyclo[3.2.1]-2-octanone to exo-2-norbornanecarboxylic acid methyl ester Journal of Organic Chemistry. 42: 2176-2177. DOI: 10.1021/Jo00432A038 |
0.304 |
|
| 1977 |
Sih CJ, Abushanab E, Jones JB. Chapter 30. Biochemical Procedures in Organic Synthesis Annual Reports in Medicinal Chemistry. 12: 298-308. DOI: 10.1016/S0065-7743(08)61569-9 |
0.43 |
|
| 1976 |
Jones JB, Taylor KE. Nicotinamide coenzyme regeneration. Flavin mononucleotide (riboflavin phosphate) as an efficient, economical, and enzyme-compatible recycling agent Canadian Journal of Chemistry. 54: 2969-2973. DOI: 10.1139/V76-420 |
0.374 |
|
| 1974 |
Lin YY, Palmer DN, Jones JB. The Specificity of the Nucleophilic Site of α-Chymotrypsin and its Potential for the Resolution of Alcohols. Enzyme-catalyzed Hydrolyses of Some (+)-, (−)-, and (±)-2-Butyl, -2-Octyl, and -α-Phenethyl Esters Canadian Journal of Chemistry. 52: 469-476. DOI: 10.1139/V74-075 |
0.403 |
|
| 1974 |
Jones JB, Sneddon DW, Lewis AJ. Inhibition of alpha-chymotrypsin by hydroxymethyl analogues of D-and L-N-acetylphenylalanine and N-acetyltryptophan of potential affinity labeling value. Biochimica Et Biophysica Acta. 341: 284-290. DOI: 10.1016/0005-2744(74)90089-8 |
0.315 |
|
| 1974 |
Lin YY, Palmer DN, Jones JB. The Specificity Of The Nucleophilic Site Of Alpha-Chymotrypsin And Its Potential For The Resolution Of Alcohols, Enzyme-Catalyzed Hydrolyses Of Some (+)-, (-)-, And (+-)-2-Butyl, -2-Octyl, And -Alpha-Phenethyl Esters Cheminform. 5. DOI: 10.1002/Chin.197417129 |
0.34 |
|
| 1973 |
Jones JB, Baskevitch N. Steroids and steroidases XX (1). Aggregation in aqueous solution of steroids with stigmastane type C-17 side chains and its influence on their enzymic transformations Steroids. 22: 525-538. PMID 4355810 DOI: 10.1016/0039-128X(73)90008-1 |
0.354 |
|
| 1973 |
Jones JB, Taylor KE. Use of pyridinium and flavin derivatives for recycling of catalystic amounts of NAD<sup>+</sup> during preparative-scale horse liver alchohol dehydrogenase-catalysed oxidations of alcohols Journal of the Chemical Society, Chemical Communications. 205-206. DOI: 10.1039/C39730000205 |
0.351 |
|
| 1973 |
Jones JB, Marr PW. Illustrations of the potential of α-chymotrypsin for the resolution of alicyclic acids and esters Tetrahedron Letters. 14: 3165-3168. DOI: 10.1016/S0040-4039(00)79800-5 |
0.305 |
|
| 1972 |
Jones JB, Ship S. Inhibition of the 3-ketosteroid Δ5→Δ4-isomerase of Pseudomonas testosteroni by some bromo-3-ketosteroid derivatives Biochimica Et Biophysica Acta. 258: 800-809. PMID 5017704 DOI: 10.1016/0005-2744(72)90181-7 |
0.379 |
|
| 1972 |
Jones JB, Gordon KD. Steroids and Steroidases. XVI. An Evaluation of Synthetic Routes to Variously C-17-Substituted Δ5-3-Ketosteroids Canadian Journal of Chemistry. 50: 2712-2718. DOI: 10.1139/V72-435 |
0.33 |
|
| 1972 |
Jones JB, Lin YY. Evaluation of Some of the Factors Involved in the Selective Hydrolysis of Aromatic Ester Protecting Groups by α-Chymotrypsin Canadian Journal of Chemistry. 50: 2053-2058. DOI: 10.1139/V72-331 |
0.38 |
|
| 1972 |
Jones JB, Grayshan R. Steroids and Steroidases. XIII. Illustrations of the Potential of Lithiodithiane–Epoxide Reactions for the Stereospecific Introduction of Substituents into the Steroid Nucleus Canadian Journal of Chemistry. 50: 810-813. DOI: 10.1139/V72-126 |
0.314 |
|
| 1972 |
Jones JB, Sneddon DW, Higgins W, Lewis AJ. Preparative-scale reductions of cyclic ketones and aldehyde substrates of horse liver alcohol dehydrogenase with in situ sodium dithionite recycling of catalytic amounts of NAD Journal of the Chemical Society, Chemical Communications. 856-857. DOI: 10.1039/C39720000856 |
0.373 |
|
| 1971 |
Jones JB, Hysert DW. Alkylations of the Side-chain Nucleophiles of Cysteine, Methionine, Histidine, and Lysine Derivatives with Allyl Bromide, 1-Bromo-2-butyne, and 2-Bromoacetophenone Canadian Journal of Chemistry. 49: 3012-3019. DOI: 10.1139/V71-502 |
0.348 |
|
| 1971 |
Jones JB, Leman JD. Steroids and Steroidases. XI. Synthetic Approaches to C-17 Bis(2-hydroxyethyl)-amino Compounds as Potential Precursors of 17-Hydroxyandrostane Nitrogen Mustards Canadian Journal of Chemistry. 49: 2420-2426. DOI: 10.1139/V71-395 |
0.313 |
|
| 1971 |
Jones JB, Leman JD, Marr PW. Preparations of Some Tetrahydronaphthalenone and Dihydroindanone Derivatives of Potential Value as Intermediates for the Synthesis of Steroids and Related Compounds Canadian Journal of Chemistry. 49: 1604-1609. DOI: 10.1139/V71-262 |
0.3 |
|
| 1971 |
Jones JB, Marr PW. An Aspect of the Scope of the Phosphonic Acid Bis Amide – Carbonyl Method in the Synthesis of Exocyclic Olefins Canadian Journal of Chemistry. 49: 1300-1302. DOI: 10.1139/V71-212 |
0.365 |
|
| 1971 |
Jones JB, Hysert DW. Reactions of Some Allylic and Propargylic Halides with Nucleophiles Analogous to Those Present in Proteins and Nucleic Acids Canadian Journal of Chemistry. 49: 325-332. DOI: 10.1139/V71-052 |
0.363 |
|
| 1971 |
Jones JB, Hysert DW. Alkylierung Der Seitenketten-Nucleophile Von Cystein-, Methionin-, Histidin- Und Lysin-Derivaten Mit Allylbromid, 1-Brom-Butin-(2) Und 2-Brom-Acetophenon Cheminform. 2. DOI: 10.1002/Chin.197151383 |
0.335 |
|
| 1970 |
Jones JB, Barker JN. Carcinogenicity of lactones. V. The reactions of 4-hydroxypent-2-enoic acid lactone with α-toluenethiol, benzylamine, methylamine, imidazole, and guanidine Canadian Journal of Chemistry. 48: 1574-1578. DOI: 10.1139/V70-256 |
0.338 |
|
| 1970 |
Jones JB, Young JM. Carcinogenicity of lactones. IV. Alkylation of analogues of DNA guanine groups such as imidazole, N-methylimidazole, and guanosine by α, β-unsaturated acids Canadian Journal of Chemistry. 48: 1566-1573. DOI: 10.1139/V70-255 |
0.31 |
|
| 1969 |
Jones JB, Wigfield DC. Steroids and steroidases. IX. Activation parameters and the mechanism of base- and enzyme-catalyzed isomerizations of androst-5-ene-3,17-dione. The nature of the active center of the Δ5 → Δ4-3-ketosteroid isomerase of Pseudomonas testosteroni Canadian Journal of Chemistry. 47: 4459-4466. DOI: 10.1139/V69-735 |
0.395 |
|
| 1968 |
Jones JB, Wigfield DC. Steroids and steroidases. VI. On the C-17 specificity of the Δ5-3-ketoisomerase of Pseudomonas testosteroni and evidence for substrate micelle formation Canadian Journal of Chemistry. 46: 1459-1465. DOI: 10.1139/V68-241 |
0.42 |
|
| 1966 |
Jones JB, Wigfield DC. Steroids And Steroidases: Iii. Dicyclohexylcarbodiimide–Dimethyl Sulfoxide Oxidations Of Alcohols And Thiols Canadian Journal of Chemistry. 44: 2517-2523. DOI: 10.1139/V66-379 |
0.304 |
|
| Show low-probability matches. |
