John C. Kath

4.7k total citations
30 papers, 2.4k citations indexed

About

John C. Kath is a scholar working on Molecular Biology, Organic Chemistry and Oncology. According to data from OpenAlex, John C. Kath has authored 30 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 14 papers in Organic Chemistry and 8 papers in Oncology. Recurrent topics in John C. Kath's work include Protein Degradation and Inhibitors (5 papers), HER2/EGFR in Cancer Research (5 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). John C. Kath is often cited by papers focused on Protein Degradation and Inhibitors (5 papers), HER2/EGFR in Cancer Research (5 papers) and Monoclonal and Polyclonal Antibodies Research (5 papers). John C. Kath collaborates with scholars based in United States, Poland and Germany. John C. Kath's co-authors include Clayton H. Heathcock, Roger B. Ruggeri, K.S. Gajiwala, Alma L. Burlingame, Jack Taunton, Xiaobo Wan, Lyn H. Jones, Michael J. Luzzio, Ethan Ung and W. Gregory Roberts and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

John C. Kath

29 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
John C. Kath United States 19 1.5k 905 555 280 249 30 2.4k
Patricia Pellicena United States 18 2.0k 1.3× 395 0.4× 579 1.0× 577 2.1× 98 0.4× 23 3.6k
Steven A. Middleton United States 30 1.8k 1.2× 798 0.9× 1.2k 2.2× 294 1.1× 81 0.3× 63 3.7k
Jennifer L. Stamos United States 14 2.2k 1.5× 566 0.6× 788 1.4× 260 0.9× 52 0.2× 17 3.3k
Morwenna Muir United Kingdom 20 753 0.5× 500 0.6× 940 1.7× 117 0.4× 152 0.6× 38 1.8k
Christopher J. Molloy United States 29 1.7k 1.1× 227 0.3× 733 1.3× 332 1.2× 199 0.8× 60 2.8k
Elena Ardini Italy 21 1.0k 0.7× 211 0.2× 537 1.0× 113 0.4× 264 1.1× 38 1.6k
Harald App United States 15 2.0k 1.4× 501 0.6× 574 1.0× 280 1.0× 99 0.4× 18 2.9k
Richard Kendall United States 24 1.8k 1.2× 315 0.3× 837 1.5× 236 0.8× 109 0.4× 43 3.0k
Gerhard Siemeister Germany 32 2.2k 1.5× 430 0.5× 959 1.7× 488 1.7× 130 0.5× 68 3.3k
Tyzoon Nomanbhoy United States 25 2.3k 1.6× 449 0.5× 582 1.0× 447 1.6× 40 0.2× 47 3.3k

Countries citing papers authored by John C. Kath

Since Specialization
Citations

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

Fields of papers citing papers by John C. Kath

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by John C. Kath. 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 John C. Kath. The network helps show where John C. Kath may publish in the future.

Co-authorship network of co-authors of John C. Kath

This figure shows the co-authorship network connecting the top 25 collaborators of John C. Kath. A scholar is included among the top collaborators of John C. Kath 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 John C. Kath. John C. Kath 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.
Kath, John C., John Golden, Allon G. Percus, & Daniel O’Malley. (2025). Predicting Flow in Fracture Networks With Quantum Algorithms. Water Resources Research. 61(12).
2.
Shi, Yingqi, John C. Kath, Allon G. Percus, et al.. (2024). Bayesian learning of gas transport in three-dimensional fracture networks. Computers & Geosciences. 192. 105700–105700. 1 indexed citations
4.
Yang, Tangpo, Adolfo Cuesta, Xiaobo Wan, et al.. (2022). Reversible lysine-targeted probes reveal residence time-based kinase selectivity. Nature Chemical Biology. 18(9). 934–941. 63 indexed citations
5.
Niessen, Sherry, Melissa M. Dix, Zachary E. Potter, et al.. (2017). Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors. Cell chemical biology. 24(11). 1388–1400.e7. 77 indexed citations
6.
Fadeyi, Olugbeminiyi, Mihir D. Parikh, Robert E. Kyne, et al.. (2016). Chemoselective Preparation of Clickable Aryl Sulfonyl Fluoride Monomers: A Toolbox of Highly Functionalized Intermediates for Chemical Biology Probe Synthesis. ChemBioChem. 17(20). 1925–1930. 46 indexed citations
7.
Lanning, Bryan, Landon R. Whitby, Melissa M. Dix, et al.. (2014). A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors. Nature Chemical Biology. 10(9). 760–767. 265 indexed citations
8.
Schwartz, Phillip A., Petr Kuzmič, James Solowiej, et al.. (2013). Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance. Proceedings of the National Academy of Sciences. 111(1). 173–178. 197 indexed citations
9.
Kath, John C., et al.. (2013). Selective addition of amines to 5-trifluoromethyl-2,4-dichloropyrimidine induced by Lewis acids. Tetrahedron Letters. 54(35). 4610–4612. 17 indexed citations
10.
Gajiwala, K.S., Junli Feng, Rose Ann Ferre, et al.. (2012). Insights into the Aberrant Activity of Mutant EGFR Kinase Domain and Drug Recognition. Structure. 21(2). 209–219. 140 indexed citations
11.
Johnson, M. Catherine, Qiyue Hu, Laura Lingardo, et al.. (2011). Novel isoquinolone PDK1 inhibitors discovered through fragment-based lead discovery. Journal of Computer-Aided Molecular Design. 25(7). 689–698. 15 indexed citations
12.
Jani, Jitesh P., Richard S. Finn, Mary E. Campbell, et al.. (2007). Discovery and Pharmacologic Characterization of CP-724,714, a Selective ErbB2 Tyrosine Kinase Inhibitor. Cancer Research. 67(20). 9887–9893. 62 indexed citations
13.
Slack‐Davis, Jill K., Karen H. Martin, Robert W. Tilghman, et al.. (2007). Cellular Characterization of a Novel Focal Adhesion Kinase Inhibitor. Journal of Biological Chemistry. 282(20). 14845–14852. 408 indexed citations
14.
Li, Bryan, Brian M. Andresen, Matthew F. Brown, et al.. (2005). Process Development of CP-481715, a Novel CCR1 Antagonist. Organic Process Research & Development. 9(4). 466–471. 9 indexed citations
15.
Kath, John C., William H. Brissette, Matthew F. Brown, et al.. (2004). Potent small molecule CCR1 antagonists. Bioorganic & Medicinal Chemistry Letters. 14(9). 2169–2173. 17 indexed citations
16.
Kath, John C., Ronald P. Gladue, William H. Martin, et al.. (2004). The discovery of structurally novel CCR1 antagonists derived from a hydroxyethylene peptide isostere template. Bioorganic & Medicinal Chemistry Letters. 14(9). 2163–2167. 17 indexed citations
17.
Barbacci, Elsa G., Leslie R. Pustilnik, Ann Marie Rossi, et al.. (2003). The biological and biochemical effects of CP-654577, a selective erbB2 kinase inhibitor, on human breast cancer cells.. PubMed. 63(15). 4450–9. 40 indexed citations
18.
Bhattacharya, Samit K., Eric Cox, John C. Kath, et al.. (2003). Achieving selectivity between highly homologous tyrosine kinases: a novel selective erbB2 inhibitor. Biochemical and Biophysical Research Communications. 307(2). 267–273. 16 indexed citations
19.
Gladue, Ronald P., Laurie Tylaska, William H. Brissette, et al.. (2003). CP-481,715, a Potent and Selective CCR1 Antagonist with Potential Therapeutic Implications for Inflammatory Diseases. Journal of Biological Chemistry. 278(42). 40473–40480. 59 indexed citations
20.
Hanson, Douglas C., Angela Nguyen, Robert J. Mather, et al.. (1999). UK‐78,282, a novel piperidine compound that potently blocks the Kv1.3 voltage‐gated potassium channel and inhibits human T cell activation. British Journal of Pharmacology. 126(8). 1707–1716. 62 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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