William K. Hagmann

7.2k total citations · 1 hit paper
78 papers, 5.4k citations indexed

About

William K. Hagmann is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, William K. Hagmann has authored 78 papers receiving a total of 5.4k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 27 papers in Oncology and 24 papers in Organic Chemistry. Recurrent topics in William K. Hagmann's work include Peptidase Inhibition and Analysis (25 papers), Cell Adhesion Molecules Research (18 papers) and Protease and Inhibitor Mechanisms (14 papers). William K. Hagmann is often cited by papers focused on Peptidase Inhibition and Analysis (25 papers), Cell Adhesion Molecules Research (18 papers) and Protease and Inhibitor Mechanisms (14 papers). William K. Hagmann collaborates with scholars based in United States. William K. Hagmann's co-authors include Alice I. Marcy, Jeffrey D. Hermes, Malcolm MacCoss, Craig K. Esser, James P. Springer, Ginger X. Yang, Richard A. Mumford, Thomas J. Lanza, Arthur G. Schultz and Linus S. Lin and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

William K. Hagmann

78 papers receiving 5.2k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

The Many Roles for Fluorine in Medicinal Chemistry

2008 3.2k citations William K. Hagmann Journal of Medicinal Chemistry profile →

Peers

William K. Hagmann

ONCOL

Matteo Zanda Italy

Günter Haufe Germany

Hiroaki Ohno Japan

Nicholas J. Lawrence United States

Alastair D. G. Lawson United Kingdom

Cesare Gennari Italy

S. Chandrasekhar India

David Hesk United States

William R. Ewing United States

Floris L. van Delft Netherlands

Matteo Zanda Italy

William K. Hagmann

2.7k ×0.9

1.6k ×0.7

1.8k ×1.3

437 ×0.5

410 ×0.6

ONCOL

Citations per year, relative to William K. Hagmann William K. Hagmann (= 1×) peers Matteo Zanda

Countries citing papers authored by William K. Hagmann

Since Specialization

Citations

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

Fields of papers citing papers by William K. Hagmann

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by William K. Hagmann. 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 William K. Hagmann. The network helps show where William K. Hagmann may publish in the future.

Co-authorship network of co-authors of William K. Hagmann

This figure shows the co-authorship network connecting the top 25 collaborators of William K. Hagmann. A scholar is included among the top collaborators of William K. Hagmann 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 William K. Hagmann. William K. Hagmann 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

Miller, Corin O., Jin Cao, Brande Thomas-Fowlkes, et al.. (2017). GPR40 partial agonist MK-2305 lower fasting glucose in the Goto Kakizaki rat via suppression of endogenous glucose production. PLoS ONE. 12(5). e0176182–e0176182. 10 indexed citations

Lai, Zhong, Shuwen He, Edward C. Sherer, et al.. (2015). Discovery of substituted (4-phenyl-1H-imidazol-2-yl)methanamine as potent somatostatin receptor 3 agonists. Bioorganic & Medicinal Chemistry Letters. 25(17). 3520–3525. 2 indexed citations

Kopka, Ihor E., Linus S. Lin, James P. Jewell, et al.. (2010). Synthesis and cannabinoid-1 receptor binding affinity of conformationally constrained analogs of taranabant. Bioorganic & Medicinal Chemistry Letters. 20(16). 4757–4761. 6 indexed citations

Du, Wu, James P. Jewell, Linus S. Lin, et al.. (2009). Synthesis and evaluation of N-[(1S,2S)-3-(4-chlorophenyl)-2-(3-cyanophenyl)-1-methylpropyl]-2-methyl-2-aminopropanamide as human cannabinoid-1 receptor (CB1R) inverse agonists. Bioorganic & Medicinal Chemistry Letters. 19(17). 5195–5199. 7 indexed citations

Xiao, Jing Chen, James P. Jewell, Linus S. Lin, et al.. (2008). Similar in vitro pharmacology of human cannabinoid CB1 receptor variants expressed in CHO cells. Brain Research. 1238. 36–43. 15 indexed citations

Chang, Linda, Ginger X. Yang, Ermengilda McCauley, et al.. (2008). Constraining the amide bond in N-Sulfonylated dipeptide VLA-4 antagonists. Bioorganic & Medicinal Chemistry Letters. 18(5). 1688–1691. 8 indexed citations

Hagmann, William K.. (2008). The Discovery of Taranabant, a Selective Cannabinoid‐1 Receptor Inverse Agonist for the Treatment of Obesity. Archiv der Pharmazie. 341(7). 405–411. 27 indexed citations

Shankaran, K., Shrenik K. Shah, Charles G. Caldwell, et al.. (2004). Synthesis of analogs of (1,4)-3- and 5-imino oxazepane, thiazepane, and diazepane as inhibitors of nitric oxide synthases. Bioorganic & Medicinal Chemistry Letters. 14(23). 5907–5911. 17 indexed citations

Hagmann, William K.. (2004). The Discovery and Potential of N-Sulfonylated Dipeptide VLA-4 Antagonists. Current Topics in Medicinal Chemistry. 4(14). 1461–1471. 11 indexed citations

10.

Kamenecka, Theodore M., Linus S. Lin, Ermengilda McCauley, et al.. (2004). Amidines as amide bond replacements in VLA-4 antagonists. Bioorganic & Medicinal Chemistry Letters. 14(9). 2323–2326. 15 indexed citations

11.

Lin, Linus S., Thomas J. Lanza, Laurie A. Castonguay, et al.. (2004). Bioisosteric replacement of anilide with benzoxazole: potent and orally bioavailable antagonists of VLA-4. Bioorganic & Medicinal Chemistry Letters. 14(9). 2331–2334. 14 indexed citations

12.

Koo, Gloria C., Kashmira Shah, G J Ding, et al.. (2003). A Small Molecule Very Late Antigen–4 Antagonist Can Inhibit Ovalbumin-induced Lung Inflammation. American Journal of Respiratory and Critical Care Medicine. 167(10). 1400–1409. 36 indexed citations

13.

Samuel, Koppara, Ralph A. Stearns, Yui S. Tang, et al.. (2003). Addressing the metabolic activation potential of new leads in drug discovery: a case study using ion trap mass spectrometry and tritium labeling techniques. Journal of Mass Spectrometry. 38(2). 211–221. 53 indexed citations

14.

Yang, Ginger X. & William K. Hagmann. (2003). VLA‐4 antagonists: Potent inhibitors of lymphocyte migration. Medicinal Research Reviews. 23(3). 369–392. 64 indexed citations

15.

Doherty, George, Theodore M. Kamenecka, Gail Van Riper, et al.. (2002). N-Aryl 2,6-Dimethoxybiphenylalanine Analogues as VLA-4 Antagonists. Bioorganic & Medicinal Chemistry Letters. 12(5). 729–731. 44 indexed citations

16.

Laszlo, Stephen E. de, Bing Li, Dooseop Kim, et al.. (1999). Potent, orally absorbed glucagon receptor antagonists. Bioorganic & Medicinal Chemistry Letters. 9(5). 641–646. 150 indexed citations

17.

Cascieri, Margaret A., Gregory Koch, Elżbieta Ber, et al.. (1999). Characterization of a Novel, Non-peptidyl Antagonist of the Human Glucagon Receptor. Journal of Biological Chemistry. 274(13). 8694–8697. 71 indexed citations

18.

Bayne, E K, Karen L. MacNaul, Susan Donatelli, et al.. (1995). Use of an antibody against the matrix metalloproteinase–generated aggrecan neoepitope fvdipen‐cooh to assess the effects of stromelysin in a rabbit model of cartilage degradation. Arthritis & Rheumatism. 38(10). 1400–1409. 15 indexed citations

19.

Gooley, Paul R., Bruce A. Johnson, Alice I. Marcy, et al.. (1993). Secondary structure and zinc ligation of human recombinant short-form stromelysin by multidimensional heteronuclear NMR. Biochemistry. 32(48). 13098–13108. 43 indexed citations

20.

Lanza, Thomas J., Philippe L. Durette, Thomas E. Rollins, et al.. (1992). Substituted 4,6-diaminoquinolines as inhibitors of C5a receptor binding. Journal of Medicinal Chemistry. 35(2). 252–258. 72 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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