James H. McKie

826 total citations
28 papers, 747 citations indexed

About

James H. McKie is a scholar working on Molecular Biology, Public Health, Environmental and Occupational Health and Biochemistry. According to data from OpenAlex, James H. McKie has authored 28 papers receiving a total of 747 indexed citations (citations by other indexed papers that have themselves been cited), including 19 papers in Molecular Biology, 10 papers in Public Health, Environmental and Occupational Health and 5 papers in Biochemistry. Recurrent topics in James H. McKie's work include Research on Leishmaniasis Studies (10 papers), Insect and Pesticide Research (5 papers) and Phenothiazines and Benzothiazines Synthesis and Activities (5 papers). James H. McKie is often cited by papers focused on Research on Leishmaniasis Studies (10 papers), Insect and Pesticide Research (5 papers) and Phenothiazines and Benzothiazines Synthesis and Activities (5 papers). James H. McKie collaborates with scholars based in United Kingdom, France and Sweden. James H. McKie's co-authors include Kenneth T. Douglas, Alan H. Fairlamb, Rabih Jaouhari, Hong Yin, Cecil Chan, Adolfo Borges, John A. Parkinson, Seyed Esmaeil Sadat Ebrahimi, Simon L. Croft and Peter Speers and has published in prestigious journals such as Biochemistry, Biochemical Journal and FEBS Letters.

In The Last Decade

James H. McKie

28 papers receiving 730 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
James H. McKie United Kingdom	14	431	312	231	228	60	28	747
Annette L. Bodley United States	12	539 1.3×	239 0.8×	205 0.9×	91 0.4×	43 0.7×	13	833
S. Franceschini Italy	13	329 0.8×	198 0.6×	198 0.9×	145 0.6×	64 1.1×	14	701
Casimir Blonski France	17	580 1.3×	169 0.5×	323 1.4×	261 1.1×	75 1.3×	50	1.1k
Irene Hallyburton United Kingdom	15	317 0.7×	292 0.9×	296 1.3×	285 1.3×	43 0.7×	23	840
Marı́a Laura Uhrig Argentina	20	594 1.4×	216 0.7×	523 2.3×	161 0.7×	37 0.6×	53	920
Esther Jortzik Germany	17	388 0.9×	281 0.9×	71 0.3×	74 0.3×	28 0.5×	26	747
L.B. Tulloch United Kingdom	17	495 1.1×	275 0.9×	267 1.2×	307 1.3×	20 0.3×	28	820
Mithu Guha India	13	248 0.6×	353 1.1×	105 0.5×	69 0.3×	61 1.0×	19	858
Valérie Landry France	13	211 0.5×	163 0.5×	289 1.3×	194 0.9×	17 0.3×	22	622
Justin R. Harrison United Kingdom	16	304 0.7×	151 0.5×	511 2.2×	239 1.0×	18 0.3×	21	881

Countries citing papers authored by James H. McKie

Since Specialization

Citations

This map shows the geographic impact of James H. McKie'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 James H. McKie with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites James H. McKie more than expected).

Fields of papers citing papers by James H. McKie

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by James H. McKie. 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 James H. McKie. The network helps show where James H. McKie may publish in the future.

Co-authorship network of co-authors of James H. McKie

This figure shows the co-authorship network connecting the top 25 collaborators of James H. McKie. A scholar is included among the top collaborators of James H. McKie 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 James H. McKie. James H. McKie is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Chan, Cecil, Hong Yin, James H. McKie, Alan H. Fairlamb, & Kenneth T. Douglas. (2002). Peptoid inhibition of trypanothione reductase as a potential antitrypanosomal and antileishmanial drug lead. Amino Acids. 22(4). 297–308. 16 indexed citations

McKie, James H., Rabih Jaouhari, Cecil Chan, et al.. (2001). Specific peptide inhibitors of trypanothione reductase with backbone structures unrelated to that of substrate: potential rational drug design lead frameworks. Amino Acids. 20(2). 145–153. 15 indexed citations

Yuen, C-T., et al.. (1999). Synthesis and enzymology of modifiedN-benzyloxycarbonyl-L-cysteinylglycyl-3,3-dimethylaminopropylamide disulphides as alternative substrates for trypanothione reductase fromTrypanosoma crud: Part 3. Amino Acids. 17(2). 175–183. 3 indexed citations

Kennedy, Karen, Michel Baltas, Kenneth T. Douglas, et al.. (1999). Rational Inhibitor Design, Synthesis and NMR Spectroscopic Study by Transferred Nuclear Overhauser Spectroscopy of Novel Inhibitors of Cinnamyl Alcohol Dehydrogenase, a Critical Enzyme in Lignification. Journal of enzyme inhibition. 14(3). 217–237. 3 indexed citations

Chan, Cecil, Hong Yin, James H. McKie, et al.. (1998). Phenothiazine Inhibitors of Trypanothione Reductase as Potential Antitrypanosomal and Antileishmanial Drugs. Journal of Medicinal Chemistry. 41(24). 4910–4910. 11 indexed citations

Lüönd, Rainer M., et al.. (1998). Inhibitors of Glutathione Reductase as Potential Antimalarial Drugs Kinetic Cooperativity and Effect of Dimethyl Sulphoxide on Inhibition Kinetics. Journal of enzyme inhibition. 13(5). 327–345. 17 indexed citations

Yin, Hong, et al.. (1997). Rational design of selective ligands for trypanothione reductase fromtrypanosoma cruzStructural effects on the inhibition by dibenzazepines based on imipramine. Journal of enzyme inhibition. 12(3). 161–173. 35 indexed citations

Wibley, Jane, James H. McKie, Kevin J. Embrey, et al.. (1995). A homology model of the three-dimensional structure of human O6-alkylguanine-DNA alkyltransferase based on the crystal structure of the C-terminal domain of the Ada protein from Escherichia coli.. PubMed. 10(1). 75–95. 13 indexed citations

Parkinson, John A., et al.. (1995). Predictability of Designing Specific Binding Interactions for DNA Minor Groove Ligands from NMR Spectroscopy and Molecular Modeling: A Copper(II)-Activated DNA Cleaver Based on Hoechst 33258. Biochemistry. 34(50). 16240–16244. 4 indexed citations

10.

Jaouhari, Rabih, et al.. (1995). Synthesis of asymmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 2. Amino Acids. 9(4). 343–351. 2 indexed citations

11.

Lauvergeat, Virginie, Karen Kennedy, Catherine Feuillet, et al.. (1995). Site-Directed Mutagenesis of a Serine Residue in Cinnamyl Alcohol Dehydrogenase, a Plant NADPH-Dependent Dehydrogenase, Affects the Specificity for the Coenzyme. Biochemistry. 34(38). 12426–12434. 39 indexed citations

12.

Jaouhari, Rabih, et al.. (1995). Synthesis of symmetric disulfides as potential alternative substrates for trypanothione reductase and glutathione reductase: Part 1. Amino Acids. 9(4). 327–342. 8 indexed citations

13.

Parkinson, John A., et al.. (1994). Molecular Design of DNA-Directed Ligands with Specific Interactions: Solution NMR Studies of the Interaction of a m-Hydroxy Analog of Hoechst 33258 with d(CGCGAATTCGCG)2. Biochemistry. 33(28). 8442–8452. 46 indexed citations

14.

McKie, James H., et al.. (1994). Rational design of peptide-based inhibitors of trypanothione reductase as potential antitrypanosomal drugs. Amino Acids. 6(3). 295–299. 25 indexed citations

15.

Smith, Keith, et al.. (1993). The glutamyl binding site of trypanothione reductase from Crithidia fasciculata: enzyme kinetic properties of γ-glutamyl-modified substrate analogues. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1203(1). 93–98. 9 indexed citations

16.

Ebrahimi, Seyed Esmaeil Sadat, John A. Parkinson, Keith R. Fox, et al.. (1993). ChemInform Abstract: Studies on the Interaction of a meta‐Hydroxy Analogue (I) of Hoechst 33258 with DNA by Melting Temperature, Footprinting, and High‐ Resolution 1H NMR Spectroscopy.. ChemInform. 24(3). 1 indexed citations

17.

McKie, James H., Rabih Jaouhari, Kenneth T. Douglas, et al.. (1993). A molecular model for cinnamyl alcohol dehydrogenase, a plant aromatic alcohol dehydrogenase involved in lignification. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1202(1). 61–69. 42 indexed citations

18.

Lüönd, Rainer M., et al.. (1993). A direct link between LY83583, a selective repressor of cyclic GMP formation, and glutathione metabolism. Biochemical Pharmacology. 45(12). 2547–2549. 17 indexed citations

19.

Santibanez‐Koref, Mauro, Rhoderick H. Elder, Chun‐Yang Fan, et al.. (1992). Isolation and partial characterization of murine O⁶‐alkyiguanine‐DNA‐alkyltransferase: Comparative sequence and structural properties. Molecular Carcinogenesis. 5(2). 161–169. 18 indexed citations

20.

McKie, James H. & Kenneth T. Douglas. (1991). Evidence for gene duplication forming similar binding folds for NAD(P)H and FAD in pyridine nucleotide‐dependent flavoenzymes. FEBS Letters. 279(1). 5–8. 64 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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