Wendy E. Lees

561 total citations
14 papers, 452 citations indexed

About

Wendy E. Lees is a scholar working on Molecular Biology, Nutrition and Dietetics and Health, Toxicology and Mutagenesis. According to data from OpenAlex, Wendy E. Lees has authored 14 papers receiving a total of 452 indexed citations (citations by other indexed papers that have themselves been cited), including 7 papers in Molecular Biology, 5 papers in Nutrition and Dietetics and 3 papers in Health, Toxicology and Mutagenesis. Recurrent topics in Wendy E. Lees's work include Trace Elements in Health (5 papers), Biochemical and Structural Characterization (3 papers) and Enzyme Production and Characterization (3 papers). Wendy E. Lees is often cited by papers focused on Trace Elements in Health (5 papers), Biochemical and Structural Characterization (3 papers) and Enzyme Production and Characterization (3 papers). Wendy E. Lees collaborates with scholars based in United Kingdom, United States and Denmark. Wendy E. Lees's co-authors include John Kay, John Kay, Lowri H. Phylip, Alexander Wlodawer, Alla Gustchina, Ben M. Dunn, Jakob R. Winther, Mi Li, Anthony Cryer and Peter Kille and has published in prestigious journals such as Journal of Biological Chemistry, Biochemical Journal and Biochemical and Biophysical Research Communications.

In The Last Decade

Wendy E. Lees

14 papers receiving 444 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Wendy E. Lees United Kingdom 12 230 137 83 66 57 14 452
Leena Penttilä Finland 14 532 2.3× 33 0.2× 36 0.4× 47 0.7× 49 0.9× 23 750
T Azuma Japan 10 196 0.9× 38 0.3× 24 0.3× 32 0.5× 52 0.9× 14 401
Ned M. Mozier United States 13 441 1.9× 48 0.4× 31 0.4× 43 0.7× 22 0.4× 15 646
Brian E. Eckenroth United States 15 445 1.9× 118 0.9× 7 0.1× 54 0.8× 17 0.3× 24 644
Thomas G. Warner United States 16 542 2.4× 52 0.4× 13 0.2× 16 0.2× 68 1.2× 29 749
Tomoko Hamma United States 11 917 4.0× 110 0.8× 34 0.4× 48 0.7× 5 0.1× 13 1.1k
Marie‐Thérèse Château France 11 366 1.6× 35 0.3× 6 0.1× 108 1.6× 12 0.2× 23 574
Diane Richter United States 8 138 0.6× 205 1.5× 7 0.1× 48 0.7× 11 0.2× 8 549
Dorothy E. Schumm United States 19 650 2.8× 50 0.4× 8 0.1× 65 1.0× 16 0.3× 47 813
Yasuyo Takemori Japan 7 572 2.5× 78 0.6× 5 0.1× 19 0.3× 32 0.6× 8 755

Countries citing papers authored by Wendy E. Lees

Since Specialization
Citations

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

Fields of papers citing papers by Wendy E. Lees

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Wendy E. Lees. 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 Wendy E. Lees. The network helps show where Wendy E. Lees may publish in the future.

Co-authorship network of co-authors of Wendy E. Lees

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

All Works

14 of 14 papers shown
1.
Lees, Wendy E., et al.. (2002). Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1596(1). 76–82. 24 indexed citations
2.
Gustchina, Alla, Mi Li, Lowri H. Phylip, et al.. (2002). An unusual orientation for Tyr75 in the active site of the aspartic proteinase from Saccharomyces cerevisiae. Biochemical and Biophysical Research Communications. 295(4). 1020–1026. 18 indexed citations
3.
Phylip, Lowri H., Wendy E. Lees, Brian G. Brownsey, et al.. (2001). The Potency and Specificity of the Interaction between the IA3 Inhibitor and Its Target Aspartic Proteinase fromSaccharomyces cerevisiae. Journal of Biological Chemistry. 276(3). 2023–2030. 31 indexed citations
4.
Kay, John, Alla Gustchina, Mi Li, et al.. (2000). The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.. Nature Structural Biology. 7(2). 113–117. 80 indexed citations
5.
Capasso, Clemente, Wendy E. Lees, Antonio Capasso, et al.. (1999). Cathepsin D from the liver of the Antarctic icefish Chionodraco hamatus exhibits unusual activity and stability at high temperatures. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1431(1). 64–73. 29 indexed citations
6.
Tatnell, Peter J., Wendy E. Lees, & John Kay. (1997). Cloning, expression and characterisation of murine procathepsin E. FEBS Letters. 408(1). 62–66. 18 indexed citations
7.
Schmid, Kurt Werner, Ian O. Ellis, Julia M.W. Gee, et al.. (1993). Presence and possible significance of immunocytochemically demonstrable metallothionein over-expression in primary invasive ductal carcinoma of the breast. Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin. 422(2). 153–159. 97 indexed citations
8.
Price-Jones, Molly, Peter Charlton, Claire Bessant, et al.. (1993). Analysis of Latent Forms of Renin Using Antibodies Raised Against the Propart Segment of Human Prorenin: Validation with Representative Samples of Ovarian Cyst and Follicular Fluids. Clinical and Experimental Hypertension. 15(4). 619–640. 2 indexed citations
9.
Robinson, Philip S., Wendy E. Lees, John Kay, & Neil D. Cook. (1992). Kinetic parameters for the generation of endothelins-1,-2 and -3 by human cathepsin E. Biochemical Journal. 284(2). 407–409. 4 indexed citations
10.
Kille, Peter, Wendy E. Lees, Dennis R. Winge, et al.. (1992). Sequestration of cadmium and copper by recombinant rainbow trout and human metallothioneins and by chimeric (mermaid and fishman) proteins with interchanged domains.. Journal of Biological Chemistry. 267(12). 8042–8049. 24 indexed citations
11.
Kay, John, Anthony Cryer, Peter Kille, et al.. (1991). Naturally occurring and recombinant metallothioneins: Structure, immunoreactivity and metal-binding functions. International Journal of Biochemistry. 23(1). 1–5. 28 indexed citations
12.
Lees, Wendy E., S. Kalinka, J.A. Meech, et al.. (1990). Generation of human endothelin by cathepsin E. FEBS Letters. 273(1-2). 99–102. 56 indexed citations
13.
Norey, Christopher G., Wendy E. Lees, J. M. Stark, et al.. (1990). Immunological distinction between piscine and mammalian metallothioneins. Comparative Biochemistry and Physiology Part B Comparative Biochemistry. 95(3). 597–601. 19 indexed citations
14.
Burnie, J., Michael J. Holland, Ruth Matthews, & Wendy E. Lees. (1987). Role of immunoblotting in the diagnosis of culture negative and enterococcal endocarditis.. Journal of Clinical Pathology. 40(10). 1149–1158. 22 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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