| Year |
Citation |
Score |
| 2016 |
Srouji JR, Xu A, Park A, Kirsch JF, Brenner SE. The Evolution of Function within the Nudix homology Clan. Proteins. PMID 27936487 DOI: 10.1002/Prot.25223 |
0.332 |
|
| 2016 |
Nguyen VN, Park A, Xu A, Srouji JR, Brenner SE, Kirsch JF. Substrate specificity characterization for eight putative Nudix hydrolases. Evaluation of criteria for substrate identification within the Nudix family. Proteins. PMID 27618147 DOI: 10.1002/Prot.25163 |
0.469 |
|
| 2013 |
Muratore KE, Engelhardt BE, Srouji JR, Jordan MI, Brenner SE, Kirsch JF. Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: recurrence of tyrosine aminotransferase activity in the Iα subfamily. Proteins. 81: 1593-609. PMID 23671031 DOI: 10.1002/Prot.24318 |
0.776 |
|
| 2013 |
Xu A, Desai AM, Brenner SE, Kirsch JF. A continuous fluorescence assay for the characterization of Nudix hydrolases. Analytical Biochemistry. 437: 178-84. PMID 23481913 DOI: 10.1016/J.Ab.2013.02.023 |
0.429 |
|
| 2011 |
Deu E, Kirsch JF. Engineering homooligomeric proteins to detect weak intersite allosteric communication: aminotransferases, a case study. Protein Science : a Publication of the Protein Society. 20: 1991-2003. PMID 21936010 DOI: 10.1002/Pro.741 |
0.398 |
|
| 2011 |
Hanes MS, Reynolds KA, McNamara C, Ghosh P, Bonomo RA, Kirsch JF, Handel TM. Specificity and cooperativity at β-lactamase position 104 in TEM-1/BLIP and SHV-1/BLIP interactions. Proteins. 79: 1267-76. PMID 21294157 DOI: 10.1002/Prot.22961 |
0.752 |
|
| 2010 |
Shultzaberger RK, Malashock DS, Kirsch JF, Eisen MB. The fitness landscapes of cis-acting binding sites in different promoter and environmental contexts. Plos Genetics. 6: e1001042. PMID 20686658 DOI: 10.1371/Journal.Pgen.1001042 |
0.757 |
|
| 2010 |
Sankararaman S, Sha F, Kirsch JF, Jordan MI, Sjölander K. Active site prediction using evolutionary and structural information. Bioinformatics (Oxford, England). 26: 617-24. PMID 20080507 DOI: 10.1093/Bioinformatics/Btq008 |
0.413 |
|
| 2009 |
Deu E, Dhoot J, Kirsch JF. The partially folded homodimeric intermediate of Escherichia coli aspartate aminotransferase contains a "molten interface" structure. Biochemistry. 48: 433-41. PMID 19099423 DOI: 10.1021/Bi801431X |
0.403 |
|
| 2008 |
Reynolds KA, Hanes MS, Thomson JM, Antczak AJ, Berger JM, Bonomo RA, Kirsch JF, Handel TM. Computational redesign of the SHV-1 beta-lactamase/beta-lactamase inhibitor protein interface. Journal of Molecular Biology. 382: 1265-75. PMID 18775544 DOI: 10.1016/J.Jmb.2008.05.051 |
0.75 |
|
| 2008 |
Ma E, MacRae IJ, Kirsch JF, Doudna JA. Autoinhibition of human dicer by its internal helicase domain. Journal of Molecular Biology. 380: 237-43. PMID 18508075 DOI: 10.1016/J.Jmb.2008.05.005 |
0.387 |
|
| 2008 |
Muratore KE, Srouji JR, Chow MA, Kirsch JF. Recombinant expression of twelve evolutionarily diverse subfamily Ialpha aminotransferases. Protein Expression and Purification. 57: 34-44. PMID 17964807 DOI: 10.1016/J.Pep.2007.09.002 |
0.785 |
|
| 2008 |
Kirsch JF. Enzyme kinetics and mechanism, by Paul F. Cook and W.W. Cleland Protein Science. 17: 380-381. DOI: 10.1110/Ps.073353008 |
0.476 |
|
| 2007 |
Yin Y, Kirsch JF. Identification of functional paralog shift mutations: conversion of Escherichia coli malate dehydrogenase to a lactate dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 104: 17353-7. PMID 17947381 DOI: 10.1073/Pnas.0708265104 |
0.412 |
|
| 2007 |
Deu E, Kirsch JF. Cofactor-directed reversible denaturation pathways: the cofactor-stabilized Escherichia coli aspartate aminotransferase homodimer unfolds through a pathway that differs from that of the apoenzyme. Biochemistry. 46: 5819-29. PMID 17441730 DOI: 10.1021/Bi602632D |
0.36 |
|
| 2007 |
Deu E, Kirsch JF. The unfolding pathway for Apo Escherichia coli aspartate aminotransferase is dependent on the choice of denaturant. Biochemistry. 46: 5810-8. PMID 17425331 DOI: 10.1021/Bi602621T |
0.317 |
|
| 2006 |
Reynolds KA, Thomson JM, Corbett KD, Bethel CR, Berger JM, Kirsch JF, Bonomo RA, Handel TM. Structural and computational characterization of the SHV-1 beta-lactamase-beta-lactamase inhibitor protein interface. The Journal of Biological Chemistry. 281: 26745-53. PMID 16809340 DOI: 10.1074/Jbc.M603878200 |
0.738 |
|
| 2006 |
Krishnaswamy SR, Williams ER, Kirsch JF. Free energies of protein-protein association determined by electrospray ionization mass spectrometry correlate accurately with values obtained by solution methods. Protein Science : a Publication of the Protein Society. 15: 1465-75. PMID 16731980 DOI: 10.1110/Ps.062083406 |
0.303 |
|
| 2006 |
Sivaraman S, Kirsch JF. The narrow substrate specificity of human tyrosine aminotransferase--the enzyme deficient in tyrosinemia type II. The Febs Journal. 273: 1920-9. PMID 16640556 DOI: 10.1111/J.1742-4658.2006.05202.X |
0.48 |
|
| 2005 |
Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grütter MG. Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine. Febs Letters. 579: 2458-62. PMID 15848188 DOI: 10.1016/J.Febslet.2005.03.048 |
0.777 |
|
| 2005 |
Aitken SM, Kirsch JF. The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity. Archives of Biochemistry and Biophysics. 433: 166-75. PMID 15581575 DOI: 10.1016/J.Abb.2004.08.024 |
0.482 |
|
| 2004 |
Chow MA, McElroy KE, Corbett KD, Berger JM, Kirsch JF. Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase. Biochemistry. 43: 12780-7. PMID 15461450 DOI: 10.1021/Bi0487544 |
0.372 |
|
| 2004 |
McCarter JD, Stephens D, Shoemaker K, Rosenberg S, Kirsch JF, Georgiou G. Substrate specificity of the Escherichia coli outer membrane protease OmpT. Journal of Bacteriology. 186: 5919-25. PMID 15317797 DOI: 10.1128/Jb.186.17.5919-5925.2004 |
0.38 |
|
| 2004 |
Eliot AC, Kirsch JF. Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations. Annual Review of Biochemistry. 73: 383-415. PMID 15189147 DOI: 10.1146/Annurev.Biochem.73.011303.074021 |
0.792 |
|
| 2004 |
Aitken SM, Kirsch JF. Role of active-site residues Thr81, Ser82, Thr85, Gln157, and Tyr158 in yeast cystathionine beta-synthase catalysis and reaction specificity. Biochemistry. 43: 1963-71. PMID 14967036 DOI: 10.1021/Bi035496M |
0.47 |
|
| 2004 |
Rothman SC, Voorhies M, Kirsch JF. Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase. Protein Science : a Publication of the Protein Society. 13: 763-72. PMID 14767072 DOI: 10.1110/Ps.03117204 |
0.432 |
|
| 2004 |
Sandmark J, Eliot AC, Famm K, Schneider G, Kirsch JF. Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis. Biochemistry. 43: 1213-22. PMID 14756557 DOI: 10.1021/Bi0358059 |
0.825 |
|
| 2004 |
Ko S, Eliot AC, Kirsch JF. S-methylmethionine is both a substrate and an inactivator of 1-aminocyclopropane-1-carboxylate synthase. Archives of Biochemistry and Biophysics. 421: 85-90. PMID 14678788 DOI: 10.1016/J.Abb.2003.10.017 |
0.798 |
|
| 2003 |
Eliot AC, Kirsch JF. Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection. Accounts of Chemical Research. 36: 757-65. PMID 14567709 DOI: 10.1021/Ar0202767 |
0.806 |
|
| 2003 |
Aitken SM, Kim DH, Kirsch JF. Escherichia coli cystathionine gamma-synthase does not obey ping-pong kinetics. Novel continuous assays for the elimination and substitution reactions. Biochemistry. 42: 11297-306. PMID 14503880 DOI: 10.1021/Bi035107O |
0.388 |
|
| 2003 |
Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grütter MG. Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding. Biochimica Et Biophysica Acta. 1647: 55-60. PMID 12686108 DOI: 10.1016/S1570-9639(03)00049-9 |
0.798 |
|
| 2003 |
Rothman SC, Kirsch JF. How does an enzyme evolved in vitro compare to naturally occurring homologs possessing the targeted function? Tyrosine aminotransferase from aspartate aminotransferase. Journal of Molecular Biology. 327: 593-608. PMID 12634055 DOI: 10.1016/S0022-2836(03)00095-0 |
0.491 |
|
| 2003 |
Aitken SM, Kirsch JF. Kinetics of the yeast cystathionine beta-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction. Biochemistry. 42: 571-8. PMID 12525186 DOI: 10.1021/Bi026681N |
0.436 |
|
| 2002 |
Shaffer WA, Luong TN, Rothman SC, Kirsch JF. Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase. Protein Science : a Publication of the Protein Society. 11: 2848-59. PMID 12441383 DOI: 10.1110/Ps.0221902 |
0.416 |
|
| 2002 |
Eliot AC, Sandmark J, Schneider G, Kirsch JF. The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Biochemistry. 41: 12582-9. PMID 12379100 DOI: 10.1021/Bi026339A |
0.808 |
|
| 2002 |
Pons J, Stratton JR, Kirsch JF. How do two unrelated antibodies, HyHEL-10 and F9.13.7, recognize the same epitope of hen egg-white lysozyme? Protein Science : a Publication of the Protein Society. 11: 2308-15. PMID 12237453 DOI: 10.1110/Ps.0209102 |
0.311 |
|
| 2002 |
Capitani G, McCarthy DL, Gut H, Grütter MG, Kirsch JF. Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate. The Journal of Biological Chemistry. 277: 49735-42. PMID 12228256 DOI: 10.1074/Jbc.M208427200 |
0.399 |
|
| 2002 |
Deu E, Koch KA, Kirsch JF. The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants. Protein Science : a Publication of the Protein Society. 11: 1062-73. PMID 11967363 DOI: 10.1110/Ps.0200902 |
0.409 |
|
| 2002 |
Eliot AC, Kirsch JF. Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Biochemistry. 41: 3836-42. PMID 11888303 DOI: 10.1021/Bi016084L |
0.781 |
|
| 2002 |
Capitani G, McCarthy DL, Gut H, Gruetter MG, Kirsch JF. Apple 1-Aminocyclopropane-1-carboxylate Synthase in Complex with the Inhibitor L-Aminoethoxyvinylglycine Journal of Biological Chemistry. 277: 49735-49742. DOI: 10.2210/Pdb1M7Y/Pdb |
0.304 |
|
| 2001 |
McCarthy DL, Capitani G, Feng L, Gruetter MG, Kirsch JF. Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant. Biochemistry. 40: 12276-84. PMID 11591146 DOI: 10.1021/Bi011050Z |
0.478 |
|
| 2001 |
Stratton JR, Pelton JG, Kirsch JF. A novel engineered subtilisin BPN' lacking a low-barrier hydrogen bond in the catalytic triad. Biochemistry. 40: 10411-6. PMID 11523982 DOI: 10.1021/Bi015542N |
0.435 |
|
| 2001 |
Hardy LW, Kirsch JF. pH dependence and solvent deuterium oxide kinetic isotope effects on Bacillus cereus beta-lactamase I catalyzed reactions. Biochemistry. 23: 1282-7. PMID 11494985 DOI: 10.1021/Bi00301A041 |
0.37 |
|
| 2001 |
Hardy LW, Kirsch JF. Diffusion-limited component of reactions catalyzed by Bacillus cereus beta-lactamase I. Biochemistry. 23: 1275-82. PMID 11491129 DOI: 10.1021/Bi00301A040 |
0.355 |
|
| 2001 |
Hardy LW, Nishida CH, Kirsch JF. Anomalous pH dependence of the reactions of carbenicillin and sulbenicillin with Bacillus cereus beta-lactamase I. Influence of the alpha-substituent charge on the kinetic parameters. Biochemistry. 23: 1288-94. PMID 11491128 DOI: 10.1021/Bi00301A042 |
0.395 |
|
| 2001 |
Koch KA, Capitani G, Gruetter MG, Kirsch JF. The human cDNA for a homologue of the plant enzyme 1-aminocyclopropane-1-carboxylate synthase encodes a protein lacking that activity Gene. 272: 75-84. PMID 11470512 DOI: 10.1016/S0378-1119(01)00533-9 |
0.425 |
|
| 2001 |
Luong TN, Kirsch JF. A general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular association. Protein Science : a Publication of the Protein Society. 10: 581-91. PMID 11344326 DOI: 10.1110/Ps.24101 |
0.364 |
|
| 2000 |
Feng L, Geck MK, Eliot AC, Kirsch JF. Aminotransferase activity and bioinformatic analysis of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry. 39: 15242-9. PMID 11106504 DOI: 10.1021/Bi002092A |
0.802 |
|
| 2000 |
Feng L, Kirsch JF. L-Vinylglycine is an alternative substrate as well as a mechanism-based inhibitor of 1-aminocyclopropane-1-carboxylate synthase. Biochemistry. 39: 2436-44. PMID 10704193 DOI: 10.1021/Bi9922704 |
0.448 |
|
| 1999 |
Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN. Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene. Journal of Molecular Biology. 294: 745-56. PMID 10610793 DOI: 10.1006/Jmbi.1999.3255 |
0.466 |
|
| 1999 |
Geck MK, Kirsch JF. A novel, definitive test for substrate channeling illustrated with the aspartate aminotransferase/malate dehydrogenase system. Biochemistry. 38: 8032-7. PMID 10387047 DOI: 10.1021/Bi983029C |
0.42 |
|
| 1999 |
Pons J, Rajpal A, Kirsch JF. Energetic analysis of an antigen/antibody interface: alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction. Protein Science : a Publication of the Protein Society. 8: 958-68. PMID 10338006 DOI: 10.1110/Ps.8.5.958 |
0.39 |
|
| 1998 |
Rajpal A, Taylor MG, Kirsch JF. Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: free energies and kinetics. Protein Science : a Publication of the Protein Society. 7: 1868-74. PMID 9761468 DOI: 10.1002/Pro.5560070903 |
0.357 |
|
| 1998 |
Taylor MG, Rajpal A, Kirsch JF. Kinetic epitope mapping of the chicken lysozyme.HyHEL-10 Fab complex: delineation of docking trajectories. Protein Science : a Publication of the Protein Society. 7: 1857-67. PMID 9761467 DOI: 10.1002/Pro.5560070902 |
0.38 |
|
| 1998 |
Li Y, Feng L, Kirsch JF. Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase. Biochemistry. 36: 15477-88. PMID 9398277 DOI: 10.1021/Bi971625L |
0.487 |
|
| 1998 |
Feng L, Li Y, Kirsch JF. Genetic engineering approaches to enzyme design and mechanism Journal of Physical Organic Chemistry. 11: 536-539. DOI: 10.1002/(Sici)1099-1395(199808/09)11:8/9<536::Aid-Poc62>3.0.Co;2-B |
0.494 |
|
| 1997 |
Luong TN, Kirsch JF. A continuous coupled spectrophotometric assay for tyrosine aminotransferase activity with aromatic and other nonpolar amino acids. Analytical Biochemistry. 253: 46-9. PMID 9356140 DOI: 10.1006/Abio.1997.2344 |
0.451 |
|
| 1997 |
Park Y, Luo J, Schultz PG, Kirsch JF. Noncoded amino acid replacement probes of the aspartate aminotransferase mechanism. Biochemistry. 36: 10517-25. PMID 9265632 DOI: 10.1021/Bi970298E |
0.452 |
|
| 1997 |
Ramjee MK, Petithory JR, McElver J, Weber SC, Kirsch JF. A novel yeast expression/secretion system for the recombinant plant thiol endoprotease propapain. Protein Engineering. 9: 1055-61. PMID 8961359 DOI: 10.1093/Protein/9.11.1055 |
0.381 |
|
| 1996 |
Gloss LM, Spencer DE, Kirsch JF. Cysteine-191 in aspartate aminotransferases appears to be conserved due to the lack of a neutral mutation pathway to the functional equivalent, alanine-191 Proteins: Structure, Function and Genetics. 24: 195-208. PMID 8820486 DOI: 10.1002/(Sici)1097-0134(199602)24:2<195::Aid-Prot6>3.0.Co;2-I |
0.414 |
|
| 1996 |
Matsumura I, Kirsch JF. Synergistic contributions of asparagine 46 and aspartate 52 to the catalytic mechanism of chicken egg white lysozyme. Biochemistry. 35: 1890-6. PMID 8639671 DOI: 10.1021/Bi951672I |
0.723 |
|
| 1996 |
Matsumura I, Kirsch JF. Is aspartate 52 essential for catalysis by chicken egg white lysozyme? The role of natural substrate-assisted hydrolysis. Biochemistry. 35: 1881-9. PMID 8639670 DOI: 10.1021/Bi951671Q |
0.741 |
|
| 1996 |
Goldberg JM, Kirsch JF. The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrolysis. Biochemistry. 35: 5280-91. PMID 8611515 DOI: 10.1021/Bi952138D |
0.421 |
|
| 1996 |
Onuffer JJ, Ton BT, Klement I, Kirsch JF. The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. Protein Science : a Publication of the Protein Society. 4: 1743-9. PMID 8528072 DOI: 10.1002/Pro.5560040909 |
0.497 |
|
| 1995 |
Shih P, Kirsch JF. Design and structural analysis of an engineered thermostable chicken lysozyme Protein Science. 4: 2063-2072. PMID 8535242 DOI: 10.1002/Pro.5560041011 |
0.37 |
|
| 1995 |
Shih P, Holland DR, Kirsch JF. Thermal stability determinants of chicken egg-white lysozyme core mutants: Hydrophobicity, packing volume, and conserved buried water molecules Protein Science. 4: 2050-2062. PMID 8535241 DOI: 10.1002/Pro.5560041010 |
0.347 |
|
| 1995 |
Onuffer JJ, Kirsch JF. Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis Protein Science. 4: 1750-1757. PMID 8528073 DOI: 10.1002/Pro.5560040910 |
0.499 |
|
| 1995 |
Furumo NC, Kirsch JF. Accumulation of the quinonoid intermediate in the reaction catalyzed by aspartate aminotransferase with cysteine sulfinic acid. Archives of Biochemistry and Biophysics. 319: 49-54. PMID 7771805 DOI: 10.1006/Abbi.1995.1265 |
0.457 |
|
| 1995 |
Gloss LM, Kirsch JF. Use of site-directed mutagenesis and alternative substrates to assign the prototropic groups important to catalysis by Escherichia coli aspartate aminotransferase Biochemistry. 34: 3999-4007. PMID 7696265 DOI: 10.1021/Bi00012A018 |
0.408 |
|
| 1995 |
Gloss LM, Kirsch JF. Decreasing the basicity of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with γ-thialysine Biochemistry. 34: 3990-3998. PMID 7696264 DOI: 10.1021/Bi00012A017 |
0.47 |
|
| 1995 |
Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN. Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase. Nature Structural Biology. 2: 548-53. PMID 7664122 DOI: 10.1038/Nsb0795-548 |
0.458 |
|
| 1994 |
Onuffer JJ, Kirsch JF. Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change Protein Engineering, Design and Selection. 7: 413-424. PMID 8177890 DOI: 10.1093/Protein/7.3.413 |
0.49 |
|
| 1994 |
Hohenester E, White MF, Kirsch JF, Jansonius JN. Crystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene. Journal of Molecular Biology. 243: 947-9. PMID 7966311 DOI: 10.1006/Jmbi.1994.1695 |
0.314 |
|
| 1994 |
White MF, Vasquez J, Yang SF, Kirsch JF. Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: Kinetic characterization of wild-type and active-site mutant forms Proceedings of the National Academy of Sciences of the United States of America. 91: 12428-12432. PMID 7809054 DOI: 10.1073/Pnas.91.26.12428 |
0.486 |
|
| 1993 |
Toney MD, Kirsch JF. Lysine 258 in aspartate aminotransferase: enforcer of the Circe effect for amino acid substrates and general-base catalyst for the 1,3-prototropic shift. Biochemistry. 32: 1471-9. PMID 8431426 DOI: 10.1021/Bi00057A010 |
0.692 |
|
| 1993 |
Goldberg JM, Zheng J, Deng H, Chen YQ, Callender R, Kirsch JF. Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy. Biochemistry. 32: 8092-7. PMID 8347609 DOI: 10.1021/Bi00083A006 |
0.37 |
|
| 1993 |
Shih P, Malcolm BA, Rosenberg S, Kirsch JF, Wilson AC. Reconstruction and testing of ancestral proteins. Methods in Enzymology. 224: 576-90. PMID 8264412 DOI: 10.1016/0076-6879(93)24043-T |
0.528 |
|
| 1993 |
Kam-Morgan LN, Lavoie TB, Smith-Gill SJ, Kirsch JF. Site-directed mutagenesis in analysis of protein-protein interactions. Methods in Enzymology. 224: 503-16. PMID 8264405 DOI: 10.1016/0076-6879(93)24037-U |
0.379 |
|
| 1993 |
Kam-Morgan LN, Smith-Gill SJ, Taylor MG, Zhang L, Wilson AC, Kirsch JF. High-resolution mapping of the HyHEL-10 epitope of chicken lysozyme by site-directed mutagenesis. Proceedings of the National Academy of Sciences of the United States of America. 90: 3958-62. PMID 7683415 DOI: 10.1073/Pnas.90.9.3958 |
0.569 |
|
| 1993 |
Deng H, Goldberg JM, Kirsch JF, Callender R. Elucidation of the solution structure of the Escherichia coli aspartate aminotransferase-.alpha.-methyl-L-aspartate complex by isotope-edited Raman difference spectroscopy Journal of the American Chemical Society. 115: 8869-8870. DOI: 10.1021/Ja00072A062 |
0.324 |
|
| 1992 |
Gloss LM, Planas A, Kirsch JF. Contribution to catalysis and stability of the five cysteines in Escherichia coli aspartate aminotransferase. Preparation and properties of a cysteine-free enzyme Biochemistry. 31: 32-39. PMID 1731883 DOI: 10.1021/Bi00116A007 |
0.357 |
|
| 1992 |
Toney MD, Kirsch JF. Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant. Protein Science : a Publication of the Protein Society. 1: 107-19. PMID 1339023 DOI: 10.1002/Pro.5560010111 |
0.698 |
|
| 1992 |
White PW, Kirsch JF. Sequential site-directed mutagenesis and chemical modification to convert the active site arginine 292 of aspartate aminotransferase to homoarginine Journal of the American Chemical Society. 114: 3567-3568. DOI: 10.1021/Ja00035A068 |
0.351 |
|
| 1991 |
Goldberg JM, Swanson RV, Goodman HS, Kirsch JF. The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km. Biochemistry. 30: 305-12. PMID 1988027 DOI: 10.1021/Bi00215A041 |
0.482 |
|
| 1991 |
Planas A, Kirsch JF. Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteine. Biochemistry. 30: 8268-76. PMID 1907854 DOI: 10.1021/Bi00247A023 |
0.447 |
|
| 1991 |
Toney MD, Kirsch JF. The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate. The Journal of Biological Chemistry. 266: 23900-3. PMID 1748661 |
0.667 |
|
| 1991 |
Toney MD, Kirsch JF. Kinetics and equilibria for the reactions of coenzymes with wild type and the Y70F mutant of Escherichia coli aspartate aminotransferase. Biochemistry. 30: 7461-6. PMID 1677270 DOI: 10.1021/Bi00244A014 |
0.67 |
|
| 1991 |
Toney MD, Kirsch JF. Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase. Biochemistry. 30: 7456-61. PMID 1677269 DOI: 10.1021/Bi00244A013 |
0.683 |
|
| 1991 |
Petithory JR, Masiarz FR, Kirsch JF, Santi DV, Malcolm BA. A rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus. Proceedings of the National Academy of Sciences of the United States of America. 88: 11510-4. PMID 1662396 DOI: 10.1073/Pnas.88.24.11510 |
0.383 |
|
| 1990 |
Malcolm BA, Wilson KP, Matthews BW, Kirsch JF, Wilson AC. Ancestral lysozymes reconstructed, neutrality tested, and thermostability linked to hydrocarbon packing. Nature. 345: 86-9. PMID 2330057 DOI: 10.1038/345086A0 |
0.552 |
|
| 1990 |
Planas A, Kirsch JF. Sequential protection-modification method for selective sulfhydryl group derivatization in proteins having more than one cysteine. Protein Engineering. 3: 625-8. PMID 2217135 DOI: 10.1093/Protein/3.7.625 |
0.422 |
|
| 1990 |
Kirsch JF, Toney MD. Brønsted analysis of enzymatic proton transfer reactions through site-directed mutagenesis. Annals of the New York Academy of Sciences. 585: 48-57. PMID 2162646 DOI: 10.1111/J.1749-6632.1990.Tb28040.X |
0.63 |
|
| 1990 |
Shih P, Malcolm BA, Kirsch JF. Engineering Enzymes for Enhanced Thermostability Mrs Proceedings. 218. DOI: 10.1557/Proc-218-37 |
0.407 |
|
| 1989 |
Hardy LW, Kirsch JF. Isolation of a Staphylococcus aureus beta-lactamase-dicloxacillin complex and kinetic studies on the reactivation of the enzyme. Archives of Biochemistry and Biophysics. 268: 338-48. PMID 2783544 DOI: 10.1016/0003-9861(89)90595-X |
0.427 |
|
| 1989 |
Julin DA, Wiesinger H, Toney MD, Kirsch JF. Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C alpha-labeled amino acids with solvent. Biochemistry. 28: 3815-21. PMID 2665809 DOI: 10.1021/Bi00435A029 |
0.659 |
|
| 1989 |
McLeish MJ, Julin DA, Kirsch JF. Aspartate aminotransferase catalyzed oxygen exchange with solvent from oxygen-18-enriched alpha-ketoglutarate: evidence for slow exchange of enzyme-bound water. Biochemistry. 28: 3821-5. PMID 2568851 DOI: 10.1021/Bi00435A030 |
0.642 |
|
| 1989 |
Malcolm BA, Rosenberg S, Corey MJ, Allen JS, de Baetselier A, Kirsch JF. Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proceedings of the National Academy of Sciences of the United States of America. 86: 133-7. PMID 2563161 DOI: 10.1073/Pnas.86.1.133 |
0.48 |
|
| 1989 |
Julin DA, Kirsch JF. Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism. Biochemistry. 28: 3825-33. PMID 2546582 DOI: 10.1021/Bi00435A031 |
0.332 |
|
| 1989 |
Toney MD, Kirsch JF. Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science (New York, N.Y.). 243: 1485-8. PMID 2538921 DOI: 10.1126/Science.2538921 |
0.709 |
|
| 1988 |
Cronin CN, Kirsch JF. Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis. Biochemistry. 27: 4572-9. PMID 3167000 DOI: 10.1021/Bi00412A052 |
0.494 |
|
| 1987 |
Toney MD, Kirsch JF. Tyrosine 70 increases the coenzyme affinity of aspartate aminotransferase. A site-directed mutagenesis study. The Journal of Biological Chemistry. 262: 12403-5. PMID 3305507 |
0.679 |
|
| 1987 |
Cronin CN, Malcolm BA, Kirsch JF. Reversal of substrate charge specificity by site-directed mutagenesis of aspartate aminotransferase Journal of the American Chemical Society. 109: 2222-2223. DOI: 10.1021/Ja00241A072 |
0.355 |
|
| 1986 |
Bazelyansky M, Robey E, Kirsch JF. Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry. 25: 125-30. PMID 3954986 DOI: 10.1021/Bi00349A019 |
0.386 |
|
| 1985 |
Malcolm BA, Kirsch JF. Site-directed mutagenesis of aspartate aminotransferase from E. coli. Biochemical and Biophysical Research Communications. 132: 915-21. PMID 3907632 DOI: 10.1016/0006-291X(85)91894-7 |
0.356 |
|
| 1984 |
Kirsch JF, Eichele G, Ford GC, Vincent MG, Jansonius JN, Gehring H, Christen P. Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure. Journal of Molecular Biology. 174: 497-525. PMID 6143829 DOI: 10.1016/0022-2836(84)90333-4 |
0.505 |
|
| 1982 |
Brouwer AC, Kirsch JF. Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation Biochemistry. 21: 1302-1307. PMID 7074086 DOI: 10.1021/Bi00535A030 |
0.385 |
|
| 1981 |
Rosenberg S, Kirsch JF. Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 2. Lysozyme and beta-glucosidase: acid and alkaline hydrolysis. Biochemistry. 20: 3196-204. PMID 6788083 DOI: 10.1021/Bi00514A032 |
0.391 |
|
| 1981 |
Rosenberg S, Kirsch JF. Oxygen-18 leaving group kinetic isotope effects on the hydrolysis of nitrophenyl glycosides. 1. beta-galactosidease-catalyzed hydrolysis. Biochemistry. 20: 3189-96. PMID 6788082 DOI: 10.1021/Bi00514A031 |
0.459 |
|
| 1980 |
Thomas RA, Kirsch JF. Kinetics and mechanism of inhibition of Escherichia coli alkaline phosphatase by permanganate ion Biochemistry. 19: 5328-5334. PMID 7004485 DOI: 10.1021/Bi00564A028 |
0.455 |
|
| 1978 |
Zannis VI, Kirsch JF. Effects of substituents on the rates of deacylation of substituted benzoyl papains. Role of a carboxylate residue in the catalytic mechanism Biochemistry. 17: 2669-2674. PMID 28148 DOI: 10.1021/Bi00606A033 |
0.38 |
|
| 1977 |
Gilmer PJ, Kirsch JF. Pyridoxamine-pyruvate transaminase. 2. Temperature-jump and stopped-flow kinetic investigation of the rates and mechanism of the reaction of 5′-deoxypyridoxal with the enzyme Biochemistry. 16: 5246-5253. PMID 21681 DOI: 10.1021/Bi00643A014 |
0.444 |
|
| 1977 |
Gilmer PJ, McIntire WS, Kirsch JF. Pyridoxamine-pyruvate transaminase. 1. Determination of the active site stoichiometry and the pH dependence of the dissociation constant for 5′-deoxypyridoxal Biochemistry. 16: 5241-5246. PMID 21680 DOI: 10.1021/Bi00643A013 |
0.373 |
|
| 1975 |
Sawyer CB, Kirsch JF. Letter: Kinetic isotope effects for the chymotrypsin catalyzed hydrolysis of ethoxyl-18 O labeled specific ester substrates. Journal of the American Chemical Society. 97: 1963-4. PMID 1133404 DOI: 10.1021/Ja00840A065 |
0.343 |
|
| 1975 |
BILKADI Z, DE LORIMIER R, KIRSCH JF. ChemInform Abstract: SECONDARY ALPHA-DEUTERIUM KINETIC ISOTOPE EFFECTS AND TRANSITION-STATE STRUCTURES FOR THE HYDROLYSIS AND HYDRAZINOLYSIS REACTIONS OF FORMATE ESTERS Chemischer Informationsdienst. 6. DOI: 10.1002/Chin.197541146 |
0.343 |
|
| 1973 |
Sawyer CB, Kirsch JF. Kinetic isotope effects for reactions of methyl formate-methoxyl-18O Journal of the American Chemical Society. 95: 7375-7381. DOI: 10.1021/Ja00803A027 |
0.336 |
|
| 1972 |
Hubbard CD, Kirsch JF. Acylation of chymotrypsin by active esters of nonspecific substrates. Evidence for a transient acylimidazole intermediate. Biochemistry. 11: 2483-93. PMID 5040654 DOI: 10.1021/Bi00763A016 |
0.401 |
|
| 1971 |
Hinkle PM, Kirsch JF. Demonstration of a change in the rate-determining step in papain- and ficin-catalyzed acyl-transfer reactions. Biochemistry. 10: 2717-26. PMID 5558694 DOI: 10.1021/Bi00790A010 |
0.334 |
|
| 1970 |
Kirsch JF, Hinkle PM. Evidence for conformational restrictions within the active site of acyl papains which influence the rates of hydrolysis Biochemistry. 9: 4633-4644. DOI: 10.1021/Bi00826A003 |
0.348 |
|
| 1969 |
Klein IB, Kirsch JF. The mechanism of the activation of papain. Biochemical and Biophysical Research Communications. 34: 575-81. PMID 5777776 DOI: 10.1016/0006-291X(69)90776-1 |
0.408 |
|
| 1969 |
Kirsch JF, Kline A. Acyl substituent effects in the general base catalyzed ammonolysis reactions of esters Journal of the American Chemical Society. 91: 1841-1847. DOI: 10.1021/Ja01035A041 |
0.329 |
|
| 1968 |
Wolfenden RV, Kirsch JF. Enzymatic displacement of oxygen and sulfur from purines. Journal of the American Chemical Society. 90: 6849-50. PMID 5687711 DOI: 10.1021/Ja01026A054 |
0.484 |
|
| 1968 |
Hubbard CD, Kirsch JF. The presteady-state kinetics of the papain-catalyzed hydrolysis of isomeric nitrophenyl esters of carbobenzoxyglycine. Biochemistry. 7: 2569-73. PMID 5660074 DOI: 10.1021/Bi00847A018 |
0.34 |
|
| 1966 |
Kirsch JF, Igelström M. The kinetics of the papain-catalyzed hydrolysis of esters of carbobenzoxyglycine. Evidence for an acyl-enzyme intermediate. Biochemistry. 5: 783-91. PMID 5940961 DOI: 10.1021/Bi00866A053 |
0.47 |
|
| 1964 |
Kirsch JF, Jencks WP. Nonlinear Structure-Reactivity Correlations. The Imidazole-Catalyzed Hydrolysis of Esters Journal of the American Chemical Society. 86: 837-846. DOI: 10.1021/Ja01059A019 |
0.505 |
|
| 1964 |
Kirsch JF, Jencks WP. Base Catalysis of Imidazole Catalysis of Ester Hydrolysis Journal of the American Chemical Society. 86: 833-837. DOI: 10.1021/Ja01059A018 |
0.563 |
|
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