78 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

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  0.32
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  0.32
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  1
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  1
2012 Shultzaberger RK, Maerkl SJ, Kirsch JF, Eisen MB. Probing the informational and regulatory plasticity of a transcription factor DNA-binding domain. Plos Genetics. 8: e1002614. PMID 22496663 DOI: 10.1371/journal.pgen.1002614  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.36
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1996 Wolf A, Lee KC, Kirsch JF, Ames GF. Ligand-dependent conformational plasticity of the periplasmic histidine-binding protein HisJ. Involvement in transport specificity. The Journal of Biological Chemistry. 271: 21243-50. PMID 8702898 DOI: 10.1074/jbc.271.35.21243  1
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  0.76
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  0.84
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.88
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1991 Toney MD, Kirsch JF. Tyrosine 70 fine-tunes the catalytic efficiency of aspartate aminotransferase. Biochemistry. 30: 7456-61. PMID 1677269  1
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  1
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  0.4
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  1
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  1
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  1
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  0.4
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  1
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  1
1987 Kirsch JF. Analysis of site-directed mutagenesis experiments by linear free energy relationships Protein Engineering. 1: 148-150. PMID 3507701 DOI: 10.1093/protein/1.3.148  1
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  1
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  1
1984 Jansonius JN, Eichele G, Ford GC, Kirsch JF, Picot D, Thaller C, Vincent MG, Gehring H, Christen P. Three-dimensional structure of mitochondrial aspartate aminotransferase and some functional derivatives: implications for its mode of action. Biochemical Society Transactions. 12: 424-7. PMID 6734906 DOI: 10.1042/bst0120424  1
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  1
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  1
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  1
1979 Lin HJ, Kirsch JF. [51] A rapid, sensitive fluorometric assay for avidin and biotin Methods in Enzymology. 62: 287-289. DOI: 10.1016/0076-6879(79)62231-0  1
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  1
1977 Lin HJ, Kirsch JF. A sensitive fluorometric assay for avidin and biotin Analytical Biochemistry. 81: 442-446. PMID 907104 DOI: 10.1016/0003-2697(77)90715-1  1
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  1
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  1
1973 Kirsch JF. Mechanism of enzyme action Annual Review of Biochemistry. 42: 205-234. PMID 4354313 DOI: 10.1146/annurev.bi.42.070173.001225  1
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  1
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