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Michael J. McLeish, Ph.D. - Publications

Affiliations: 
1988-1998 Victorian College of Pharmacy Monash University, Parkville, Australia 
 1998-2008 Medicinal Chemistry University of Michigan, Ann Arbor, Ann Arbor, MI 
 2008- Chemistry and Chemical Biology IUPUI, Indianapolis, IN, United States 
Area:
Enzyme Mechanisms, Biochemistry, Molecular Biology,
Website:
https://science.iupui.edu/ppgenchemmcleish-michael
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Year Citation  Score
2019 Planas F, McLeish MJ, Himo F. Computational characterization of enzyme-bound thiamin diphosphate reveals a surprisingly stable tricyclic state: implications for catalysis. Beilstein Journal of Organic Chemistry. 15: 145-159. PMID 30745990 DOI: 10.3762/Bjoc.15.15  0.435
2019 Planas F, McLeish MJ, Himo F. Computational Study of Enantioselective Carboligation Catalyzed by Benzoylformate Decarboxylase Acs Catalysis. 9: 5657-5667. DOI: 10.1021/Acscatal.9B01084  0.381
2018 Planas F, Sheng X, McLeish MJ, Himo F. A Theoretical Study of the Benzoylformate Decarboxylase Reaction Mechanism. Frontiers in Chemistry. 6: 205. PMID 29998094 DOI: 10.3389/Fchem.2018.00205  0.386
2017 Pallitsch K, Rogers MP, Andrews FH, Hammerschmidt F, McLeish MJ. Phosphonodifluoropyruvate is a mechanism-based inhibitor of phosphonopyruvate decarboxylase from Bacteroides fragilis. Bioorganic & Medicinal Chemistry. PMID 28693916 DOI: 10.1016/J.Bmc.2017.06.013  0.761
2017 Zahniser MP, Prasad S, Kneen MM, Kreinbring CA, Petsko GA, Ringe D, McLeish MJ. Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily. Protein Engineering, Design & Selection : Peds. 1-8. PMID 28338942 DOI: 10.1093/Protein/Gzx015  0.363
2017 Adediran SA, Wang PF, Shilabin AG, Baron CA, McLeish MJ, R F Pratt. Specificity and mechanism of mandelamide hydrolase catalysis. Archives of Biochemistry and Biophysics. PMID 28129982 DOI: 10.1016/J.Abb.2017.01.010  0.456
2016 Andrews F, Wechsler C, Rogers M, Meyer D, Tittmann K, McLeish M. Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity Catalysts. 6: 190. DOI: 10.3390/Catal6120190  0.778
2015 Andrews FH, Horton JD, Shin D, Yoon HJ, Logsdon MG, Malik AM, Rogers MP, Kneen MM, Suh SW, McLeish MJ. The kinetic characterization and X-ray structure of a putative benzoylformate decarboxylase from M. smegmatis highlights the difficulties in the functional annotation of ThDP-dependent enzymes. Biochimica Et Biophysica Acta. 1854: 1001-9. PMID 25936776 DOI: 10.1016/J.Bbapap.2015.04.027  0.769
2014 Loschonsky S, Wacker T, Waltzer S, Giovannini PP, McLeish MJ, Andrade SL, Müller M. Extended reaction scope of thiamine diphosphate dependent cyclohexane-1,2-dione hydrolase: from C-C bond cleavage to C-C bond ligation. Angewandte Chemie (International Ed. in English). 53: 14402-6. PMID 25382418 DOI: 10.1002/Anie.201408287  0.342
2014 Andrews FH, Rogers MP, Paul LN, McLeish MJ. Perturbation of the monomer-monomer interfaces of the benzoylformate decarboxylase tetramer. Biochemistry. 53: 4358-67. PMID 24956165 DOI: 10.1021/Bi500081R  0.762
2014 Patel H, Nemeria NS, Andrews FH, McLeish MJ, Jordan F. Identification of charge transfer transitions related to thiamin-bound intermediates on enzymes provides a plethora of signatures useful in mechanistic studies. Biochemistry. 53: 2145-52. PMID 24628377 DOI: 10.1021/Bi4015743  0.75
2013 Wu Q, McLeish MJ. Kinetic and pH studies on human phenylethanolamine N-methyltransferase. Archives of Biochemistry and Biophysics. 539: 1-8. PMID 24018397 DOI: 10.1016/J.Abb.2013.08.019  0.333
2013 Andrews FH, McLeish MJ. Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes. The Febs Journal. 280: 6395-411. PMID 23895593 DOI: 10.1111/Febs.12459  0.786
2013 Andrews FH, Tom AR, Gunderman PR, Novak WR, McLeish MJ. A bulky hydrophobic residue is not required to maintain the V-conformation of enzyme-bound thiamin diphosphate. Biochemistry. 52: 3028-30. PMID 23607689 DOI: 10.1021/Bi400368J  0.777
2012 Andrews FH, McLeish MJ. Substrate specificity in thiamin diphosphate-dependent decarboxylases. Bioorganic Chemistry. 43: 26-36. PMID 22245019 DOI: 10.1016/J.Bioorg.2011.12.001  0.757
2011 Kneen MM, Stan R, Yep A, Tyler RP, Saehuan C, McLeish MJ. Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae. The Febs Journal. 278: 1842-53. PMID 21501384 DOI: 10.1111/J.1742-4658.2011.08103.X  0.443
2010 Pratt RF, McLeish MJ. Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: convergent evolution? Biochemistry. 49: 9688-97. PMID 20977193 DOI: 10.1021/Bi1012222  0.423
2010 Drinkwater N, Vu H, Lovell KM, Criscione KR, Collins BM, Prisinzano TE, Poulsen SA, McLeish MJ, Grunewald GL, Martin JL. Fragment-based screening by X-ray crystallography, MS and isothermal titration calorimetry to identify PNMT (phenylethanolamine N-methyltransferase) inhibitors. The Biochemical Journal. 431: 51-61. PMID 20642456 DOI: 10.1042/Bj20100651  0.313
2010 Brandt GS, Kneen MM, Petsko GA, Ringe D, McLeish MJ. Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition Journal of the American Chemical Society. 132: 438-439. PMID 20030408 DOI: 10.1021/Ja907064W  0.372
2009 Georgieva P, Wu Q, McLeish MJ, Himo F. The reaction mechanism of phenylethanolamine N-methyltransferase: a density functional theory study. Biochimica Et Biophysica Acta. 1794: 1831-7. PMID 19733262 DOI: 10.1016/J.Bbapap.2009.08.022  0.367
2009 Yep A, McLeish MJ. Engineering the substrate binding site of benzoylformate decarboxylase. Biochemistry. 48: 8387-95. PMID 19621900 DOI: 10.1021/Bi9008402  0.433
2009 Drinkwater N, Gee CL, Puri M, Criscione KR, McLeish MJ, Grunewald GL, Martin JL. Molecular recognition of physiological substrate noradrenaline by the adrenaline-synthesizing enzyme PNMT and factors influencing its methyltransferase activity. The Biochemical Journal. 422: 463-71. PMID 19570037 DOI: 10.1042/Bj20090702  0.489
2009 Brandt GS, Kneen MM, Chakraborty S, Baykal AT, Nemeria N, Yep A, Ruby DI, Petsko GA, Kenyon GL, McLeish MJ, Jordan F, Ringe D. Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57. PMID 19320438 DOI: 10.1021/Bi801950K  0.624
2009 Wu Q, Caine JM, Thomson SA, Slavica M, Grunewald GL, McLeish MJ. Time-dependent inactivation of human phenylethanolamine N-methyltransferase by 7-isothiocyanatotetrahydroisoquinoline. Bioorganic & Medicinal Chemistry Letters. 19: 1071-4. PMID 19171483 DOI: 10.1016/J.Bmcl.2009.01.014  0.752
2009 Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F. Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94. PMID 19140682 DOI: 10.1021/Bi801810H  0.617
2009 Wang PF, Yep A, Kenyon GL, McLeish MJ. Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein Engineering, Design & Selection : Peds. 22: 103-10. PMID 19074156 DOI: 10.1093/Protein/Gzn073  0.615
2008 Brandt GS, Nemeria N, Chakraborty S, McLeish MJ, Yep A, Kenyon GL, Petsko GA, Jordan F, Ringe D. Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43. PMID 18570438 DOI: 10.1021/Bi8004413  0.637
2008 Yeung CK, Yep A, Kenyon GL, McLeish MJ. Physical, kinetic and spectrophotometric studies of a NAD(P)-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Biochimica Et Biophysica Acta. 1784: 1248-55. PMID 18498778 DOI: 10.1016/J.Bbapap.2008.04.015  0.642
2008 Yep A, Kenyon GL, McLeish MJ. Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism. Proceedings of the National Academy of Sciences of the United States of America. 105: 5733-8. PMID 18398009 DOI: 10.1073/Pnas.0709657105  0.631
2008 Chakraborty S, Nemeria N, Yep A, McLeish MJ, Kenyon GL, Jordan F. Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects. Biochemistry. 47: 3800-9. PMID 18314961 DOI: 10.1021/Bi702302U  0.616
2007 Saehuan C, Rojanarata T, Wiyakrutta S, McLeish MJ, Meevootisom V. Isolation and characterization of a benzoylformate decarboxylase and a NAD+/NADP+-dependent benzaldehyde dehydrogenase involved in D-phenylglycine metabolism in Pseudomonas stutzeri ST-201. Biochimica Et Biophysica Acta. 1770: 1585-92. PMID 17916405 DOI: 10.1016/J.Bbagen.2007.08.007  0.333
2007 Gee CL, Drinkwater N, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL. Enzyme adaptation to inhibitor binding: a cryptic binding site in phenylethanolamine N-methyltransferase. Journal of Medicinal Chemistry. 50: 4845-53. PMID 17845018 DOI: 10.1021/Jm0703385  0.401
2007 Nemeria N, Korotchkina L, McLeish MJ, Kenyon GL, Patel MS, Jordan F. Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states. Biochemistry. 46: 10739-44. PMID 17715948 DOI: 10.1021/Bi700838Q  0.647
2007 Bera AK, Polovnikova LS, Roestamadji J, Widlanski TS, Kenyon GL, McLeish MJ, Hasson MS. Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme. Journal of the American Chemical Society. 129: 4120-1. PMID 17367138 DOI: 10.1021/Ja068636Z  0.632
2006 Janzen E, Müller M, Kolter-Jung D, Kneen MM, McLeish MJ, Pohl M. Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C-C bond formation. Bioorganic Chemistry. 34: 345-61. PMID 17078994 DOI: 10.1016/J.Bioorg.2006.09.002  0.41
2006 Yep A, Kenyon GL, McLeish MJ. Determinants of substrate specificity in KdcA, a thiamin diphosphate-dependent decarboxylase. Bioorganic Chemistry. 34: 325-36. PMID 17028071 DOI: 10.1016/J.Bioorg.2006.08.005  0.652
2006 Wang PF, Flynn AJ, Naor MM, Jensen JH, Cui G, Merz KM, Kenyon GL, McLeish MJ. Exploring the role of the active site cysteine in human muscle creatine kinase. Biochemistry. 45: 11464-72. PMID 16981706 DOI: 10.1021/Bi0607002  0.582
2006 Wang PF, Kenyon GL, McLeish MJ. Heterogeneity of Escherichia coli-expressed human muscle creatine kinase. Iubmb Life. 58: 421-8. PMID 16801217 DOI: 10.1080/15216540600779394  0.573
2006 Andricopulo AD, Akoachere MB, Krogh R, Nickel C, McLeish MJ, Kenyon GL, Arscott LD, Williams CH, Davioud-Charvet E, Becker K. Specific inhibitors of Plasmodium falciparum thioredoxin reductase as potential antimalarial agents. Bioorganic & Medicinal Chemistry Letters. 16: 2283-92. PMID 16458512 DOI: 10.1016/J.Bmcl.2006.01.027  0.541
2005 Gee CL, Tyndall JD, Grunewald GL, Wu Q, McLeish MJ, Martin JL. Mode of binding of methyl acceptor substrates to the adrenaline-synthesizing enzyme phenylethanolamine N-methyltransferase: implications for catalysis. Biochemistry. 44: 16875-85. PMID 16363801 DOI: 10.1021/Bi051636B  0.382
2005 Wu Q, Gee CL, Lin F, Tyndall JD, Martin JL, Grunewald GL, McLeish MJ. Structural, mutagenic, and kinetic analysis of the binding of substrates and inhibitors of human phenylethanolamine N-methyltransferase. Journal of Medicinal Chemistry. 48: 7243-52. PMID 16279783 DOI: 10.1021/Jm050568O  0.416
2005 Kneen MM, Pogozheva ID, Kenyon GL, McLeish MJ. Exploring the active site of benzaldehyde lyase by modeling and mutagenesis. Biochimica Et Biophysica Acta. 1753: 263-71. PMID 16226928 DOI: 10.1016/J.Bbapap.2005.08.025  0.642
2005 Wang PF, Flynn AJ, McLeish MJ, Kenyon GL. Loop movement and catalysis in creatine kinase. Iubmb Life. 57: 355-62. PMID 16036620 DOI: 10.1080/15216540500091999  0.618
2005 Siegert P, McLeish MJ, Baumann M, Iding H, Kneen MM, Kenyon GL, Pohl M. Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida. Protein Engineering, Design & Selection : Peds. 18: 345-57. PMID 15930043 DOI: 10.1093/Protein/Gzi035  0.65
2005 Gee CL, Nourse A, Hsin AY, Wu Q, Tyndall JD, Grunewald GL, McLeish MJ, Martin JL. Disulfide-linked dimers of human adrenaline synthesizing enzyme PNMT are catalytically active. Biochimica Et Biophysica Acta. 1750: 82-92. PMID 15893506 DOI: 10.1016/J.Bbapap.2005.03.006  0.391
2005 McLeish MJ, Kenyon GL. Relating structure to mechanism in creatine kinase. Critical Reviews in Biochemistry and Molecular Biology. 40: 1-20. PMID 15804623 DOI: 10.1080/10409230590918577  0.587
2004 Novak WR, Wang PF, McLeish MJ, Kenyon GL, Babbitt PC. Isoleucine 69 and valine 325 form a specificity pocket in human muscle creatine kinase. Biochemistry. 43: 13766-74. PMID 15504039 DOI: 10.1021/Bi049060Y  0.617
2004 Wu Q, Criscione KR, Grunewald GL, McLeish MJ. Phenylethanolamine N-methyltransferase inhibition: re-evaluation of kinetic data. Bioorganic & Medicinal Chemistry Letters. 14: 4217-20. PMID 15261273 DOI: 10.1016/J.Bmcl.2004.06.009  0.355
2004 Gopalakrishna KN, Stewart BH, Kneen MM, Andricopulo AD, Kenyon GL, McLeish MJ. Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family. Biochemistry. 43: 7725-35. PMID 15196015 DOI: 10.1021/Bi049907Q  0.613
2004 McMillan FM, Archbold J, McLeish MJ, Caine JM, Criscione KR, Grunewald GL, Martin JL. Molecular recognition of sub-micromolar inhibitors by the epinephrine-synthesizing enzyme phenylethanolamine N-methyltransferase. Journal of Medicinal Chemistry. 47: 37-44. PMID 14695818 DOI: 10.1021/Jm0205752  0.775
2003 Davioud-Charvet E, McLeish MJ, Veine DM, Giegel D, Arscott LD, Andricopulo AD, Becker K, Müller S, Schirmer RH, Williams CH, Kenyon GL. Mechanism-based inactivation of thioredoxin reductase from Plasmodium falciparum by Mannich bases. Implication for cytotoxicity. Biochemistry. 42: 13319-30. PMID 14609342 DOI: 10.1021/Bi0353629  0.609
2003 McLeish MJ, Kneen MM, Gopalakrishna KN, Koo CW, Babbitt PC, Gerlt JA, Kenyon GL. Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633. Journal of Bacteriology. 185: 2451-6. PMID 12670968 DOI: 10.1128/Jb.185.8.2451-2456.2003  0.533
2003 Polovnikova ES, McLeish MJ, Sergienko EA, Burgner JT, Anderson NL, Bera AK, Jordan F, Kenyon GL, Hasson MS. Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase. Biochemistry. 42: 1820-30. PMID 12590569 DOI: 10.1021/Bi026490K  0.642
2003 McLeish MJ, Kenyon GL. Approaches to the Rational Design of Enzyme Inhibitors Burger's Medicinal Chemistry and Drug Discovery. 715-779. DOI: 10.1002/0471266949.Bmc015  0.396
2002 Lahiri SD, Wang PF, Babbitt PC, McLeish MJ, Kenyon GL, Allen KN. The 2.1 A structure of Torpedo californica creatine kinase complexed with the ADP-Mg(2+)-NO(3)(-)-creatine transition-state analogue complex. Biochemistry. 41: 13861-7. PMID 12437342 DOI: 10.1021/Bi026655P  0.613
2002 Wang PF, Novak WR, Cantwell JS, Babbitt PC, McLeish MJ, Kenyon GL. Expression of Torpedo californica creatine kinase in Escherichia coli and purification from inclusion bodies. Protein Expression and Purification. 26: 89-95. PMID 12356475 DOI: 10.1016/S1046-5928(02)00512-0  0.591
2002 Begun J, McLeish MJ, Caine JM, Palant E, Grunewald GL, Martin JL. Crystallization of PNMT, the adrenaline-synthesizing enzyme, is critically dependent on a high protein concentration. Acta Crystallographica. Section D, Biological Crystallography. 58: 314-5. PMID 11807261 DOI: 10.1107/S090744490101962X  0.747
2001 Martin JL, Begun J, McLeish MJ, Caine JM, Grunewald GL. Getting the adrenaline going: crystal structure of the adrenaline-synthesizing enzyme PNMT. Structure (London, England : 1993). 9: 977-85. PMID 11591352 DOI: 10.1016/S0969-2126(01)00662-1  0.446
2001 Wang PF, McLeish MJ, Kneen MM, Lee G, Kenyon GL. An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry. 40: 11698-705. PMID 11570870 DOI: 10.1021/Bi011208F  0.57
2001 Grunewald GL, McLeish MJ, Criscione KR. Phenylethanolamine N-methyltransferase kinetics: bovine versus recombinant human enzyme. Bioorganic & Medicinal Chemistry Letters. 11: 1579-82. PMID 11412985 DOI: 10.1016/S0960-894X(01)00245-1  0.348
2001 Cantwell JS, Novak WR, Wang PF, McLeish MJ, Kenyon GL, Babbitt PC. Mutagenesis of two acidic active site residues in human muscle creatine kinase: implications for the catalytic mechanism. Biochemistry. 40: 3056-61. PMID 11258919 DOI: 10.1021/Bi0020980  0.61
2000 Sergienko EA, Wang J, Polovnikova L, Hasson MS, McLeish MJ, Kenyon GL, Jordan F. Spectroscopic detection of transient thiamin diphosphate-bound intermediates on benzoylformate decarboxylase. Biochemistry. 39: 13862-9. PMID 11076527 DOI: 10.1021/Bi001214W  0.615
2000 Montserret R, McLeish MJ, Böckmann A, Geourjon C, Penin F. Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding Biochemistry. 39: 8362-8373. PMID 10913242 DOI: 10.1021/Bi000208X  0.391
2000 Chen LH, White CB, Babbitt PC, McLeish MJ, Kenyon GL. A comparative study of human muscle and brain creatine kinases expressed in Escherichia coli. Journal of Protein Chemistry. 19: 59-66. PMID 10882173 DOI: 10.1023/A:1007047026691  0.56
2000 Najbar LV, Craik DJ, Wade JD, McLeish MJ. Identification of initiation sites for T4 lysozyme folding using CD and NMR spectroscopy of peptide fragments Biochemistry. 39: 5911-5920. PMID 10801343 DOI: 10.1021/Bi000070I  0.774
1999 Montserret R, Aubert-Foucher E, McLeish MJ, Hill JM, Ficheux D, Jaquinod M, van der Rest M, Deléage G, Penin F. Structural analysis of the heparin-binding site of the NC1 domain of collagen XIV by CD and NMR. Biochemistry. 38: 6479-88. PMID 10350466 DOI: 10.1021/Bi9900222  0.373
1998 Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D. The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry. 37: 9918-30. PMID 9665697 DOI: 10.1021/Bi973047E  0.647
1998 Kenvon QL, Hasson MS, Muscate A, McLeish MJ, Harris TK, Babbitt PC, Gerlt JA, Petsko GA, Rinye D. Structure and mechanism of benzoylformate decarboxylase, a thiamin dtthosphate-dependent enzyme Faseb Journal. 12: A1332.  0.316
1997 Najbar LV, Craik DJ, Wade JD, Salvatore D, McLeish MJ. Conformational analysis of LYS(11-36), a peptide derived from the β- sheet region of T4 lysozyme, in TFE and SDS Biochemistry. 36: 11525-11533. PMID 9298973 DOI: 10.1021/Bi970730S  0.765
1996 Caine JM, Macreadie IG, Grunewald GL, McLeish MJ. Recombinant human phenylethanolamine N-methyltransferase: overproduction in Escherichia coli, purification, and characterization. Protein Expression and Purification. 8: 160-6. PMID 8812853 DOI: 10.1006/Prep.1996.0088  0.39
1995 Najbar LV, Craik DJ, Wade JD, Lin F, McLeish MJ. CD and NMR determination of the solution structure of a peptide corresponding to T4 lysozyme residues 38-51 Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1250: 163-170. PMID 7632721 DOI: 10.1016/0167-4838(95)00045-V  0.772
1995 Wade JD, Perich JW, McLeish MJ, Otvos L, Tregear GW. Synthesis and conformational analysis of an O-phosphotyrosine-containing α-helical peptide Letters in Peptide Science. 2: 71-76. DOI: 10.1007/Bf00128500  0.364
1994 Wilson JC, Nielsen KJ, McLeish MJ, Craik DJ. A determination of the solution conformation of the nonmammalian tachykinin eledoisin by NMR and CD spectroscopy. Biochemistry. 33: 6802-11. PMID 8204614 DOI: 10.1021/Bi00188A008  0.413
1994 McLeish MJ, Nielsen KJ, Najbar LV, Wade JD, Lin F, Doughty MB, Craik DJ. Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy. Biochemistry. 33: 11174-83. PMID 7727368 DOI: 10.1021/Bi00203A013  0.772
1993 McLeish MJ, Nielsen KJ, Wade JD, Craik DJ. A peptide corresponding to the N-terminal 13 residues of T4 lysozyme forms an alpha-helix. Febs Letters. 315: 323-8. PMID 8422925 DOI: 10.1016/0014-5793(93)81187-5  0.387
1991 McLeish MJ, Caine JM. Chemical modification of PABA synthetase Biochemistry International. 24: 1033-1042. PMID 1781781  0.336
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  0.557
1983 Broxton TJ, McLeish MJ. Reactions of aryl diazonium salts and alkyl arylazo ethers. XI further evidence for the mechanism of dediazoniation in basic alcoholic solution Australian Journal of Chemistry. 36: 1031-1035. DOI: 10.1071/Ch9831031  0.65
1983 Broxton TJ, McLeish MJ. Reactions of Aryl Diazonium Salts and Alkyl Arylazo Ethers. X General Acid and Intramolecular Electrostatic Catalysis in the Ionization of Methyl (E)-2-Organyl-5-nitrophenylazo Ethers in Alcoholic Solvents† Australian Journal of Chemistry. 36: 55-66. DOI: 10.1071/Ch9830055  0.69
1983 Broxton TJ, McLeish MJ. Reactions of aryl diazonium salts and alkyl arylazo ethers. 9. Studies of the carbanionic and free radical mechanisms of dediazoniation of substituted 2-chlorobenzenediazonium salts Journal of Organic Chemistry. 48: 191-195. DOI: 10.1021/Jo00150A010  0.661
1982 Broxton TJ, McLeish MJ. Reactions of Aryl Diazonium Salts and Arylazo Alkyl Ethers. VI A Comparison of the Available Methods for the Measurement of the Rate of Ionization of (Z)-Arylazo Alkyl Ethers in Alcoholic Solvents Australian Journal of Chemistry. 35: 319-329. DOI: 10.1071/Ch9820319  0.646
1982 Broxton TJ, McLeish MJ. Reactions of aryl diazonium salts and arylazo alkyl ethers. 7. Kinetic studies of the decomposition of Z ethers derived from some substituted 2-nitrobenzene diazonium salts Journal of Organic Chemistry. 47: 3673-3679. DOI: 10.1021/Jo00140A017  0.668
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