Tomi K. Sawyer

10.2k total citations · 1 hit paper
154 papers, 5.8k citations indexed

About

Tomi K. Sawyer is a scholar working on Molecular Biology, Oncology and Organic Chemistry. According to data from OpenAlex, Tomi K. Sawyer has authored 154 papers receiving a total of 5.8k indexed citations (citations by other indexed papers that have themselves been cited), including 107 papers in Molecular Biology, 26 papers in Oncology and 20 papers in Organic Chemistry. Recurrent topics in Tomi K. Sawyer's work include Chemical Synthesis and Analysis (46 papers), Protein Kinase Regulation and GTPase Signaling (26 papers) and Receptor Mechanisms and Signaling (22 papers). Tomi K. Sawyer is often cited by papers focused on Chemical Synthesis and Analysis (46 papers), Protein Kinase Regulation and GTPase Signaling (26 papers) and Receptor Mechanisms and Signaling (22 papers). Tomi K. Sawyer collaborates with scholars based in United States, Brazil and Singapore. Tomi K. Sawyer's co-authors include Mac E. Hadley, Victor J. Hruby, Chester A. Metcalf, Christopher B. Heward, Michael H. Engel, William C. Shakespeare, David C. Dalgarno, Douglas J. Staples, Jean B. Burnett and Pauline J. Sanfilippo and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Tomi K. Sawyer

150 papers receiving 5.6k citations

Hit Papers

4-Norleucine, 7-D-phenylalanine-alpha-melanocyte-stimulat... 1980 2026 1995 2010 1980 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Tomi K. Sawyer United States 40 3.4k 1.1k 996 942 922 154 5.8k
Oded Livnah Israel 35 2.2k 0.6× 157 0.1× 936 0.9× 549 0.6× 520 0.6× 84 4.2k
Jenny Bain United Kingdom 25 5.5k 1.6× 129 0.1× 702 0.7× 683 0.7× 1.0k 1.1× 29 7.4k
Wim J. van Blitterswijk Netherlands 51 5.7k 1.7× 343 0.3× 1.1k 1.1× 415 0.4× 609 0.7× 111 7.4k
Chaim Gilon Israel 45 5.7k 1.7× 178 0.2× 414 0.4× 1.7k 1.8× 1.3k 1.5× 228 8.7k
John A. Hanover United States 68 10.6k 3.1× 399 0.4× 1.7k 1.7× 4.1k 4.4× 1.3k 1.4× 209 13.5k
Peter H. Fishman United States 49 6.1k 1.8× 300 0.3× 1.4k 1.4× 683 0.7× 370 0.4× 173 8.5k
Marilyn D. Resh United States 62 9.0k 2.6× 281 0.3× 2.9k 3.0× 327 0.3× 1.3k 1.4× 122 12.7k
Stephen R. Sprang United States 53 9.1k 2.7× 242 0.2× 2.2k 2.2× 615 0.7× 861 0.9× 126 11.7k
Sharon L. Campbell United States 50 6.4k 1.9× 324 0.3× 2.2k 2.2× 269 0.3× 1.6k 1.7× 149 9.0k
Weontae Lee South Korea 34 2.6k 0.8× 196 0.2× 550 0.6× 172 0.2× 638 0.7× 156 4.1k

Countries citing papers authored by Tomi K. Sawyer

Since Specialization
Citations

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

Fields of papers citing papers by Tomi K. Sawyer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Tomi K. Sawyer

This figure shows the co-authorship network connecting the top 25 collaborators of Tomi K. Sawyer. A scholar is included among the top collaborators of Tomi K. Sawyer 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 Tomi K. Sawyer. Tomi K. Sawyer 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.
Sweeney, Patrick, et al.. (2024). Subthreshold activation of the melanocortin system causes generalized sensitization to anorectic agents in mice. Journal of Clinical Investigation. 134(14). 2 indexed citations
2.
Li, Mingyue, Jianguo Li, Xingyu Lu, et al.. (2024). Molecular Mechanism of P53 Peptide Permeation through Lipid Membranes from Solid-State NMR Spectroscopy and Molecular Dynamics Simulations. Journal of the American Chemical Society. 146(33). 23075–23091. 3 indexed citations
3.
Olsen, Karl, et al.. (2023). Aqueous remote loading of setmelanotide in poly(lactic-co-glycolic acid) microspheres for long-term obesity treatment. Journal of Controlled Release. 364. 589–600. 10 indexed citations
5.
Lee, Hyelee, N. Boyer, Qiaolin Deng, et al.. (2019). Photoredox Ni-catalyzed peptide C(sp2)–O cross-coupling: from intermolecular reactions to side chain-to-tail macrocyclization. Chemical Science. 10(19). 5073–5078. 44 indexed citations
6.
Han, Liz Y., Charles N. Landen, José G. Treviño, et al.. (2006). Antiangiogenic and Antitumor Effects of Src Inhibition in Ovarian Carcinoma. Cancer Research. 66(17). 8633–8639. 68 indexed citations
7.
Azam, Mohammad, William C. Shakespeare, Tomi K. Sawyer, & George Q. Daley. (2006). Targeted inhibition of Gatekeeper variant “T315I” of BCR-ABL by a purine based ATP-competitive inhibitor. Cancer Research. 66. 1139–1139. 1 indexed citations
8.
Brunton, Valerie G., Egle Avizienyte, Valerie J. Fincham, et al.. (2005). Identification of Src-Specific Phosphorylation Site on Focal Adhesion Kinase: Dissection of the Role of Src SH2 and Catalytic Functions and Their Consequences for Tumor Cell Behavior. Cancer Research. 65(4). 1335–1342. 180 indexed citations
9.
Dalgarno, David C., Thilo Stehle, Surinder S. Narula, et al.. (2005). Structural Basis of Src Tyrosine Kinase Inhibition with a New Class of Potent and Selective Trisubstituted Purine‐based Compounds. Chemical Biology & Drug Design. 67(1). 46–57. 65 indexed citations
10.
Shahripour, Aurash, Mark S. Plummer, Elizabeth A. Lunney, et al.. (2002). Structure-Based design of nonpeptide inhibitors of interleukin-1β converting enzyme (ICE, Caspase-1). Bioorganic & Medicinal Chemistry. 10(1). 31–40. 21 indexed citations
11.
Sawyer, Tomi K., Brendan F. Boyce, David C. Dalgarno, & John D. Iuliucci. (2001). Src inhibitors: genomics to therapeutics. Expert Opinion on Investigational Drugs. 10(7). 1327–1344. 30 indexed citations
12.
Violette, Shelia M., William C. Shakespeare, Catherine Bartlett, et al.. (2000). A Src SH2 selective binding compound inhibits osteoclast-mediated resorption. Chemistry & Biology. 7(3). 225–235. 47 indexed citations
13.
Metcalf, Chester A., Charles J. Eyermann, Regine S. Bohacek, et al.. (2000). Structure-Based Design and Solid-Phase Parallel Synthesis of Phosphorylated Nonpeptides to Explore Hydrophobic Binding at the Src SH2 Domain. Journal of Combinatorial Chemistry. 2(4). 305–313. 8 indexed citations
14.
Sawyer, Tomi K.. (1998). Src homology-2 domains: Structure, mechanisms, and drug discovery. Biopolymers. 47(3). 243–261. 105 indexed citations
15.
Saltiel, Alan R. & Tomi K. Sawyer. (1996). Targeting signal transduction in the discovery of antiproliferative drugs. Chemistry & Biology. 3(11). 887–893. 22 indexed citations
16.
Castrucci, Ana Maria de Lauro, Wade C. Sherbrooke, Tomi K. Sawyer, et al.. (1994). Discovery of an α-melanotropin antagonist effective in vivo. Peptides. 15(4). 627–632. 7 indexed citations
17.
Decker, Stuart J., Derek Maclean, Dennis J. McNamara, et al.. (1994). Sequence specificity in the recognition of the epidermal growth factor receptor by the abl Src homology 2 domain.. PubMed. 9(5). 1379–85. 8 indexed citations
18.
Epps, D E Van, Tomi K. Sawyer, Douglas J. Staples, et al.. (1991). Spectroscopic analysis of [Trp3]‐β‐casomorphin analogs Comparative structure conformation‐activity studies. International journal of peptide & protein research. 37(4). 257–267. 1 indexed citations
19.
Tomasselli, Alfredo G., W. Jeffrey Howe, John O. Hui, et al.. (1991). Calcium‐free calmodulin is a substrate of proteases from human immunodeficiency viruses 1 and 2. Proteins Structure Function and Bioinformatics. 10(1). 1–9. 34 indexed citations
20.
Hadley, Mac E., et al.. (1981). Biological Actions of Melanocyte‐Stimulating Hormone. Novartis Foundation symposium. 81. 244–262. 8 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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