M.D. Feese

2.0k total citations · 1 hit paper
18 papers, 1.6k citations indexed

About

M.D. Feese is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, M.D. Feese has authored 18 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 8 papers in Materials Chemistry and 3 papers in Oncology. Recurrent topics in M.D. Feese's work include Enzyme Structure and Function (8 papers), Protein Structure and Dynamics (4 papers) and Platelet Disorders and Treatments (3 papers). M.D. Feese is often cited by papers focused on Enzyme Structure and Function (8 papers), Protein Structure and Dynamics (4 papers) and Platelet Disorders and Treatments (3 papers). M.D. Feese collaborates with scholars based in United States and Japan. M.D. Feese's co-authors include Lance Stewart, Bart L. Staker, Alex B. Burgin, Craig A. Behnke, Kathryn A. Hjerrild, Mark Cushman, Yves Pommier, David E. Zembower, Donald W. Pettigrew and S. James Remington and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

M.D. Feese

18 papers receiving 1.6k citations

Hit Papers

The mechanism of topoisomerase I poisoning by a camptothe... 2002 2026 2010 2018 2002 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.D. Feese United States 15 1.3k 396 379 359 146 18 1.6k
Terry A. Beerman United States 27 2.0k 1.6× 160 0.4× 603 1.6× 546 1.5× 119 0.8× 93 2.5k
Marie‐Hélène David‐Cordonnier France 33 1.7k 1.3× 168 0.4× 321 0.8× 912 2.5× 57 0.4× 69 2.5k
Swee Y. Sharp United Kingdom 25 2.0k 1.6× 124 0.3× 750 2.0× 417 1.2× 269 1.8× 45 2.8k
Hoyun Lee Canada 28 1.5k 1.1× 120 0.3× 334 0.9× 881 2.5× 45 0.3× 64 2.5k
John E. Kerrigan United States 24 1.2k 0.9× 84 0.2× 416 1.1× 355 1.0× 60 0.4× 53 2.0k
Joseph Schoepfer Switzerland 24 1.5k 1.2× 82 0.2× 470 1.2× 532 1.5× 107 0.7× 43 2.0k
Rongshi Li United States 23 1.0k 0.8× 64 0.2× 339 0.9× 789 2.2× 139 1.0× 44 2.2k
Christine Jaxel France 24 1.8k 1.4× 395 1.0× 605 1.6× 193 0.5× 73 0.5× 44 2.0k
Yutaka Kanda Japan 24 2.1k 1.6× 116 0.3× 299 0.8× 674 1.9× 24 0.2× 51 3.0k
Jennifer L. Meagher United States 33 2.2k 1.7× 91 0.2× 708 1.9× 453 1.3× 79 0.5× 53 2.9k

Countries citing papers authored by M.D. Feese

Since Specialization
Citations

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

Fields of papers citing papers by M.D. Feese

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.D. Feese. 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 M.D. Feese. The network helps show where M.D. Feese may publish in the future.

Co-authorship network of co-authors of M.D. Feese

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

All Works

18 of 18 papers shown
1.
Jacobson, Ira M., M.D. Feese, Haixia Xiao, et al.. (2016). CC-31244, A Novel, Pan-Genotypic, Potent NS5B Non-Nucleoside Polymerase Inhibitor for the Treatment of Chronic Hepatitis C. Journal of Hepatology. 64(2). S421–S422. 1 indexed citations
2.
Tsai, Yingssu, S.E. McPhillips, Ana González, et al.. (2013). AutoDrug: fully automated macromolecular crystallography workflows for fragment-based drug discovery. Acta Crystallographica Section D Biological Crystallography. 69(5). 796–803. 19 indexed citations
3.
Okazaki, Nobuo, Taro Tamada, M.D. Feese, et al.. (2012). Substrate recognition mechanism of a glycosyltrehalose trehalohydrolase from Sulfolobus solfataricus KM1. Protein Science. 21(4). 539–552. 6 indexed citations
4.
Ahn, Yu Mi, Michael Clare, Carol L. Ensinger, et al.. (2010). Switch control pocket inhibitors of p38-MAP kinase. Durable type II inhibitors that do not require binding into the canonical ATP hinge region. Bioorganic & Medicinal Chemistry Letters. 20(19). 5793–5798. 26 indexed citations
5.
Dwyer, John J., Karen L. Wilson, Aisha Hasan, et al.. (2008). Design of an engineered N‐terminal HIV‐1 gp41 trimer with enhanced stability and potency. Protein Science. 17(4). 633–643. 26 indexed citations
6.
Staker, Bart L., M.D. Feese, Mark Cushman, et al.. (2005). Structures of Three Classes of Anticancer Agents Bound to the Human Topoisomerase I−DNA Covalent Complex. Journal of Medicinal Chemistry. 48(7). 2336–2345. 446 indexed citations
7.
Feese, M.D., Taro Tamada, Yoichi Kato, et al.. (2004). Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment. Proceedings of the National Academy of Sciences. 101(7). 1816–1821. 66 indexed citations
8.
Tamada, Taro, M.D. Feese, Stefano Ferri, et al.. (2003). Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) fromCucurbita moscataandSpinacea oleracea. Acta Crystallographica Section D Biological Crystallography. 60(1). 13–21. 46 indexed citations
9.
Kuroki, Ryota, Yoichi Kato, M.D. Feese, et al.. (2002). Crystallization of the functional domain of human thrombopoietin using an antigen-binding fragment derived from neutralizing monoclonal antibody. Acta Crystallographica Section D Biological Crystallography. 58(5). 856–858. 10 indexed citations
10.
Staker, Bart L., Kathryn A. Hjerrild, M.D. Feese, et al.. (2002). The mechanism of topoisomerase I poisoning by a camptothecin analog. Proceedings of the National Academy of Sciences. 99(24). 15387–15392. 659 indexed citations breakdown →
12.
Feese, M.D., Yoichi Kato, Taro Tamada, et al.. (2000). Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus 1 1Edited by D. Rees. Journal of Molecular Biology. 301(2). 451–464. 44 indexed citations
13.
Muto, Takanori, M.D. Feese, Yoshihiro Shimada, et al.. (2000). Functional Analysis of the C-terminal Region of Recombinant Human Thrombopoietin. Journal of Biological Chemistry. 275(16). 12090–12094. 26 indexed citations
14.
Feese, M.D., H.R. Faber, Cory Bystrom, Donald W. Pettigrew, & S. James Remington. (1998). Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Structure. 6(11). 1407–1418. 47 indexed citations
15.
Feese, M.D., Luis R. Comolli, Norman D. Meadow, Saul Roseman, & S. James Remington. (1997). Structural Studies of the Escherichia coli Signal Transducing Protein IIAGlc:  Implications for Target Recognition,. Biochemistry. 36(51). 16087–16096. 31 indexed citations
17.
Feese, M.D., et al.. (1994). Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation.. Proceedings of the National Academy of Sciences. 91(9). 3544–3548. 38 indexed citations
18.
Feese, M.D., Andrea Scaloni, Wanda M. Jones, James M. Manning, & S. James Remington. (1993). Crystallization and Preliminary X-ray Studies of Human Erythrocyte Acylpeptide Hydrolase. Journal of Molecular Biology. 233(3). 546–549. 19 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.

Explore authors with similar magnitude of impact

Rankless by CCL
2026