Joseph E. Deweese

1.6k total citations
35 papers, 1.2k citations indexed

About

Joseph E. Deweese is a scholar working on Molecular Biology, Oncology and Toxicology. According to data from OpenAlex, Joseph E. Deweese has authored 35 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 13 papers in Oncology and 11 papers in Toxicology. Recurrent topics in Joseph E. Deweese's work include Cancer therapeutics and mechanisms (31 papers), Bioactive Compounds and Antitumor Agents (11 papers) and Lung Cancer Research Studies (7 papers). Joseph E. Deweese is often cited by papers focused on Cancer therapeutics and mechanisms (31 papers), Bioactive Compounds and Antitumor Agents (11 papers) and Lung Cancer Research Studies (7 papers). Joseph E. Deweese collaborates with scholars based in United States, Australia and South Korea. Joseph E. Deweese's co-authors include Neil Osheroff, Alex B. Burgin, Susan L. Mercer, Bryan H. Thurtle-Schmidt, James M. Berger, Jo Ann W. Byl, David Jacob, Xiaohua Jiang, James T. Wilson and Sungchul Hohng and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Joseph E. Deweese

33 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Joseph E. Deweese United States 18 1.0k 412 274 251 151 35 1.2k
Jo Ann W. Byl United States 16 607 0.6× 268 0.7× 242 0.9× 115 0.5× 53 0.4× 24 807
Ewa Maj Poland 20 469 0.5× 256 0.6× 336 1.2× 122 0.5× 59 0.4× 43 999
Kyosuke Kitoh Japan 16 757 0.7× 267 0.6× 733 2.7× 55 0.2× 174 1.2× 25 1.5k
M Tomasz United States 15 890 0.9× 172 0.4× 294 1.1× 288 1.1× 70 0.5× 25 1.3k
Riham F. George Egypt 25 576 0.6× 166 0.4× 1.2k 4.4× 89 0.4× 189 1.3× 76 1.6k
Mary Jo Caranfa United States 10 1.5k 1.4× 748 1.8× 446 1.6× 393 1.6× 305 2.0× 12 1.9k
Rabah A.T. Serya Egypt 20 429 0.4× 178 0.4× 671 2.4× 66 0.3× 68 0.5× 38 1.0k
Dalia R. Jakas United States 12 876 0.8× 467 1.1× 394 1.4× 214 0.9× 182 1.2× 23 1.3k
Andreas Hilgeroth Germany 22 615 0.6× 364 0.9× 831 3.0× 67 0.3× 156 1.0× 110 1.5k
C. Yu United States 6 484 0.5× 148 0.4× 153 0.6× 130 0.5× 62 0.4× 7 654

Countries citing papers authored by Joseph E. Deweese

Since Specialization
Citations

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

Fields of papers citing papers by Joseph E. Deweese

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Joseph E. Deweese

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph E. Deweese. A scholar is included among the top collaborators of Joseph E. Deweese 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 Joseph E. Deweese. Joseph E. Deweese 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.
Deweese, Joseph E., et al.. (2025). Plasmid DNA Binding Electrophoretic Mobility Shift Assay with Eukaryotic Topoisomerase II. Methods in molecular biology. 2928. 109–114.
2.
Deweese, Joseph E., et al.. (2024). Bioinformatic Analysis of Topoisomerase IIα Reveals Interdomain Interdependencies and Critical C-Terminal Domain Residues. International Journal of Molecular Sciences. 25(11). 5674–5674. 2 indexed citations
3.
Jiang, Xiaohua, et al.. (2023). Inhibition of Topoisomerases by Metal Thiosemicarbazone Complexes. International Journal of Molecular Sciences. 24(15). 12010–12010. 12 indexed citations
4.
Deweese, Joseph E., et al.. (2021). Cannabidiol oxidation product HU-331 is a potential anticancer cannabinoid-quinone: a narrative review. SHILAP Revista de lepidopterología. 3(1). 11–11. 11 indexed citations
5.
Deweese, Joseph E., et al.. (2020). Reviewing the Modification, Interactions, and Regulation of the C-TerminalDomain of Topoisomerase IIα as a Prospect for Future Therapeutic Targeting. 8(6). 27–43. 1 indexed citations
6.
Murphy, Matthew B., et al.. (2020). Synthesis and evaluation of etoposide and podophyllotoxin analogs against topoisomerase IIα and HCT-116 cells. Bioorganic & Medicinal Chemistry. 28(22). 115773–115773. 4 indexed citations
7.
Wallace, J., et al.. (2019). Examining the Impact of Antimicrobial Fluoroquinolones on Human DNA Topoisomerase IIα and IIβ. ACS Omega. 4(2). 4049–4055. 36 indexed citations
8.
Morris, William, James T. Wilson, Anthony Brown, et al.. (2018). Structural and Metal Ion Effects on Human Topoisomerase IIα Inhibition by α-(N)-Heterocyclic Thiosemicarbazones. Chemical Research in Toxicology. 32(1). 90–99. 14 indexed citations
9.
Lindsey, R. Hunter, et al.. (2014). Catalytic Core of Human Topoisomerase IIα: Insights into Enzyme–DNA Interactions and Drug Mechanism. Biochemistry. 53(41). 6595–6602. 26 indexed citations
10.
Mercer, Susan L., et al.. (2014). HU-331 Is a Catalytic Inhibitor of Topoisomerase IIα. Chemical Research in Toxicology. 27(12). 2044–2051. 29 indexed citations
11.
Smith, Nicholas A., Jo Ann W. Byl, Susan L. Mercer, Joseph E. Deweese, & Neil Osheroff. (2014). Etoposide Quinone Is a Covalent Poison of Human Topoisomerase IIβ. Biochemistry. 53(19). 3229–3236. 38 indexed citations
12.
Jacob, David, et al.. (2013). Etoposide Catechol Is an Oxidizable Topoisomerase II Poison. Chemical Research in Toxicology. 26(8). 1156–1158. 18 indexed citations
13.
Lee, Sang-Hwa, Seung‐Ryoung Jung, Jo Ann W. Byl, et al.. (2012). DNA cleavage and opening reactions of human topoisomerase IIα are regulated via Mg 2+ -mediated dynamic bending of gate-DNA. Proceedings of the National Academy of Sciences. 109(8). 2925–2930. 63 indexed citations
14.
Thurtle-Schmidt, Bryan H., Alex B. Burgin, Joseph E. Deweese, Neil Osheroff, & James M. Berger. (2010). A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases. Nature. 465(7298). 641–644. 142 indexed citations
15.
Deweese, Joseph E. & Neil Osheroff. (2010). The use of divalent metal ions by type II topoisomerases. Metallomics. 2(7). 450–450. 57 indexed citations
16.
Deweese, Joseph E., et al.. (2009). DNA topology and topoisomerases. Biochemistry and Molecular Biology Education. 37(1). 2–10. 94 indexed citations
17.
Deweese, Joseph E., F. Peter Guengerich, Alex B. Burgin, & Neil Osheroff. (2009). Metal Ion Interactions in the DNA Cleavage/Ligation Active Site of Human Topoisomerase IIα. Biochemistry. 48(38). 8940–8947. 22 indexed citations
18.
Deweese, Joseph E., et al.. (2009). Use of Divalent Metal Ions in the DNA Cleavage Reaction of Human Type II Topoisomerases. Biochemistry. 48(9). 1862–1869. 13 indexed citations
19.
Deweese, Joseph E., Alex B. Burgin, & Neil Osheroff. (2008). Human topoisomerase II  uses a two-metal-ion mechanism for DNA cleavage. Nucleic Acids Research. 36(15). 4883–4893. 48 indexed citations
20.
Deweese, Joseph E. & Neil Osheroff. (2008). The DNA cleavage reaction of topoisomerase II: wolf in sheep's clothing. Nucleic Acids Research. 37(3). 738–748. 369 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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