Michael J. McLeish

2.9k total citations
93 papers, 2.4k citations indexed

About

Michael J. McLeish is a scholar working on Biochemistry, Molecular Biology and Clinical Biochemistry. According to data from OpenAlex, Michael J. McLeish has authored 93 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 38 papers in Biochemistry, 36 papers in Molecular Biology and 33 papers in Clinical Biochemistry. Recurrent topics in Michael J. McLeish's work include Biochemical Acid Research Studies (34 papers), Metabolism and Genetic Disorders (33 papers) and Alcoholism and Thiamine Deficiency (31 papers). Michael J. McLeish is often cited by papers focused on Biochemical Acid Research Studies (34 papers), Metabolism and Genetic Disorders (33 papers) and Alcoholism and Thiamine Deficiency (31 papers). Michael J. McLeish collaborates with scholars based in United States, Australia and Germany. Michael J. McLeish's co-authors include George L. Kenyon, Malea M. Kneen, Alejandra Yep, Pan‐Fen Wang, Gary L. Grunewald, Patricia C. Babbitt, Miriam S. Hasson, Frank Jordan, Forest H. Andrews and Gregory A. Petsko and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

Michael J. McLeish

92 papers receiving 2.4k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Michael J. McLeish United States 28 1.3k 796 479 420 273 93 2.4k
Kai Tittmann Germany 37 1.7k 1.3× 1.8k 2.3× 1.1k 2.3× 970 2.3× 436 1.6× 102 3.6k
Jung‐Ja P. Kim United States 36 2.2k 1.7× 231 0.3× 491 1.0× 728 1.7× 126 0.5× 70 3.3k
Roberto Contestabile Italy 29 1.6k 1.2× 733 0.9× 128 0.3× 371 0.9× 149 0.5× 93 2.4k
Martino L. di Salvo Italy 30 1.5k 1.2× 718 0.9× 131 0.3× 445 1.1× 153 0.6× 82 2.4k
Zheng Cui United States 27 1.8k 1.3× 468 0.6× 58 0.1× 208 0.5× 136 0.5× 60 2.9k
Vladimir I. Muronetz Russia 29 2.0k 1.5× 133 0.2× 184 0.4× 342 0.8× 102 0.4× 185 2.8k
David Maltby United States 33 2.5k 1.9× 380 0.5× 41 0.1× 603 1.4× 397 1.5× 67 3.9k
Frank E. Frerman United States 39 3.4k 2.6× 421 0.5× 97 0.2× 1.9k 4.6× 114 0.4× 107 4.4k
Subramanyam Swaminathan United States 27 1.4k 1.0× 237 0.3× 1.2k 2.4× 118 0.3× 104 0.4× 80 2.6k
James K Stoops United States 30 2.4k 1.8× 611 0.8× 41 0.1× 313 0.7× 163 0.6× 67 3.4k

Countries citing papers authored by Michael J. McLeish

Since Specialization
Citations

This map shows the geographic impact of Michael J. McLeish's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Michael J. McLeish with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Michael J. McLeish more than expected).

Fields of papers citing papers by Michael J. McLeish

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Michael J. McLeish. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Michael J. McLeish. The network helps show where Michael J. McLeish may publish in the future.

Co-authorship network of co-authors of Michael J. McLeish

This figure shows the co-authorship network connecting the top 25 collaborators of Michael J. McLeish. A scholar is included among the top collaborators of Michael J. McLeish based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Michael J. McLeish. Michael J. McLeish is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Sheng, Xiang, et al.. (2018). A Theoretical Study of the Benzoylformate Decarboxylase Reaction Mechanism. Frontiers in Chemistry. 6. 205–205. 20 indexed citations
2.
Andrews, Forest H., et al.. (2016). Mechanistic and Structural Insight to an Evolved Benzoylformate Decarboxylase with Enhanced Pyruvate Decarboxylase Activity. Publisher.
3.
Andrews, Forest H. & Michael J. McLeish. (2011). Substrate specificity in thiamin diphosphate-dependent decarboxylases. Bioorganic Chemistry. 43. 26–36. 33 indexed citations
4.
Kneen, Malea M., et al.. (2011). Characterization of a thiamin diphosphate‐dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae. FEBS Journal. 278(11). 1842–1853. 43 indexed citations
5.
Wu, Qian, et al.. (2009). The reaction mechanism of phenylethanolamine N-methyltransferase: A density functional theory study. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794(12). 1831–1837. 22 indexed citations
6.
Wang, Pan‐Fen, Alejandra Yep, George L. Kenyon, & Michael J. McLeish. (2008). Using directed evolution to probe the substrate specificity of mandelamide hydrolase. Protein Engineering Design and Selection. 22(2). 103–110. 4 indexed citations
7.
Rojanarata, Theerasak, et al.. (2007). 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 (BBA) - General Subjects. 1770(11). 1585–1592. 19 indexed citations
8.
Müller, Michael, et al.. (2006). Characterization of benzaldehyde lyase from Pseudomonas fluorescens: A versatile enzyme for asymmetric C–C bond formation. Bioorganic Chemistry. 34(6). 345–361. 70 indexed citations
9.
Wang, Pan‐Fen, Allen Flynn, Michael J. McLeish, & George L. Kenyon. (2005). Loop Movement and Catalysis in Creatine Kinase. IUBMB Life. 57(4-5). 355–362. 8 indexed citations
10.
McLeish, Michael J. & George L. Kenyon. (2005). Relating Structure to Mechanism in Creatine Kinase. Critical Reviews in Biochemistry and Molecular Biology. 40(1). 1–20. 165 indexed citations
11.
Gee, Christine L., Amanda Nourse, Qian Wu, et al.. (2005). Disulfide-linked dimers of human adrenaline synthesizing enzyme PNMT are catalytically active. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1750(1). 82–92. 4 indexed citations
12.
Wu, Qian, Kevin R. Criscione, Gary L. Grunewald, & Michael J. McLeish. (2004). Phenylethanolamine N-methyltransferase inhibition: re-evaluation of kinetic data. Bioorganic & Medicinal Chemistry Letters. 14(16). 4217–4220. 11 indexed citations
13.
Lazoura, Eliada, M.I. Aguilar, & Michael J. McLeish. (2000). Studies on the conformational properties of CP‐1042−55, the hinge region of CP‐10, using circular dichroism and RP‐HPLC. Journal of Peptide Research. 55(6). 411–418. 2 indexed citations
14.
Caine, Joanne M., Ian Macreadie, Gary L. Grunewald, & Michael J. McLeish. (1996). Recombinant Human PhenylethanolamineN-Methyltransferase: Overproduction inEscherichia coli,Purification, and Characterization. Protein Expression and Purification. 8(2). 160–166. 21 indexed citations
15.
McLeish, Michael J., et al.. (1996). Determination of ((R)-(+)- and (S)-(−)-isomers of thiopentone in plasma by chiral high-performance liquid chromatography. Journal of Chromatography B Biomedical Sciences and Applications. 675(1). 174–179. 12 indexed citations
16.
Craik, David J., et al.. (1995). 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 Enzymology. 1250(2). 163–170. 10 indexed citations
17.
McLeish, Michael J., et al.. (1994). Conformation of a Peptide Corresponding to T4 Lysozyme Residues 59-81 by NMR and CD Spectroscopy. Biochemistry. 33(37). 11174–11183. 24 indexed citations
18.
Wilson, Jennifer C., et al.. (1994). A Determination of the Solution Conformation of the Nonmammalian Tachykinin Eledoisin by NMR and CD Spectroscopy. Biochemistry. 33(22). 6802–6811. 21 indexed citations
19.
McLeish, Michael J., Douglas Julin, & Jack F. Kirsch. (1989). Aspartate aminotransferase catalyzed oxygen exchange with solvent from oxygen-18-enriched .alpha.-ketoglutarate: evidence for slow exchange of enzyme-bound water. Biochemistry. 28(9). 3821–3825. 3 indexed citations
20.
Sitaram, Balvant R., et al.. (1987). Gas chromatographic—mass spectroscopic characterisation of the psychotomimetic indolealkylamines and their in vivo metabolites. Journal of Chromatography B Biomedical Sciences and Applications. 422. 13–23. 7 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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