Yuk-Ching Tse-Dinh

1.4k total citations
34 papers, 1.1k citations indexed

About

Yuk-Ching Tse-Dinh is a scholar working on Molecular Biology, Oncology and Molecular Medicine. According to data from OpenAlex, Yuk-Ching Tse-Dinh has authored 34 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 29 papers in Molecular Biology, 15 papers in Oncology and 11 papers in Molecular Medicine. Recurrent topics in Yuk-Ching Tse-Dinh's work include Cancer therapeutics and mechanisms (29 papers), Antibiotic Resistance in Bacteria (11 papers) and Neutropenia and Cancer Infections (8 papers). Yuk-Ching Tse-Dinh is often cited by papers focused on Cancer therapeutics and mechanisms (29 papers), Antibiotic Resistance in Bacteria (11 papers) and Neutropenia and Cancer Infections (8 papers). Yuk-Ching Tse-Dinh collaborates with scholars based in United States, India and Canada. Yuk-Ching Tse-Dinh's co-authors include Bokun Cheng, Zhongtao Zhang, Nadrian C. Seeman, Camille J. Roche, Elena P. Sorokin, Thirunavukkarasu Annamalai, Gagandeep Narula, Mamta Gupta, Chen Zhu and Hui Wang and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

Yuk-Ching Tse-Dinh

34 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Yuk-Ching Tse-Dinh United States 20 894 251 213 197 175 34 1.1k
Alison J. Howells United Kingdom 13 628 0.7× 126 0.5× 195 0.9× 139 0.7× 132 0.8× 14 784
Clare V. Smith United States 10 931 1.0× 136 0.5× 224 1.1× 193 1.0× 159 0.9× 10 1.2k
Shantanu Karkare United Kingdom 7 725 0.8× 52 0.2× 141 0.7× 176 0.9× 126 0.7× 8 979
Ravishankar Ramachandran India 21 877 1.0× 81 0.3× 96 0.5× 222 1.1× 49 0.3× 71 1.3k
Martina Hrast Slovenia 20 566 0.6× 71 0.3× 136 0.6× 367 1.9× 37 0.2× 55 892
Folkert Reck United States 22 1.0k 1.1× 57 0.2× 245 1.2× 723 3.7× 51 0.3× 50 1.5k
Simon A. Weston United Kingdom 7 601 0.7× 60 0.2× 55 0.3× 87 0.4× 78 0.4× 8 761
W E Kohlbrenner United States 16 587 0.7× 85 0.3× 59 0.3× 250 1.3× 36 0.2× 19 891
Masatoshi Inukai Germany 23 969 1.1× 90 0.4× 124 0.6× 371 1.9× 35 0.2× 46 1.4k
Rupesh Kumar United States 15 838 0.9× 43 0.2× 52 0.2× 109 0.6× 39 0.2× 21 1.0k

Countries citing papers authored by Yuk-Ching Tse-Dinh

Since Specialization
Citations

This map shows the geographic impact of Yuk-Ching Tse-Dinh'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 Yuk-Ching Tse-Dinh with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Yuk-Ching Tse-Dinh more than expected).

Fields of papers citing papers by Yuk-Ching Tse-Dinh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Yuk-Ching Tse-Dinh. 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 Yuk-Ching Tse-Dinh. The network helps show where Yuk-Ching Tse-Dinh may publish in the future.

Co-authorship network of co-authors of Yuk-Ching Tse-Dinh

This figure shows the co-authorship network connecting the top 25 collaborators of Yuk-Ching Tse-Dinh. A scholar is included among the top collaborators of Yuk-Ching Tse-Dinh 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 Yuk-Ching Tse-Dinh. Yuk-Ching Tse-Dinh 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.
Tse-Dinh, Yuk-Ching, et al.. (2025). Search for Specific Inhibitors Targeting Type IA Topoisomerases. Journal of Molecular Biology. 438(5). 169349–169349. 1 indexed citations
2.
Beebe, Stephen J., Donald M. Cropek, Floyd A. Beckford, et al.. (2019). Synthesis, characterization, DNA binding, topoisomerase inhibition, and apoptosis induction studies of a novel cobalt(III) complex with a thiosemicarbazone ligand. Journal of Inorganic Biochemistry. 203. 110907–110907. 29 indexed citations
3.
Annamalai, Thirunavukkarasu, et al.. (2017). A Fluorescence-Based Assay for Identification of Bacterial Topoisomerase I Poisons. Methods in molecular biology. 1703. 259–268. 3 indexed citations
4.
5.
Li, Feng, Marcus M. Maddox, Gagandeep Narula, et al.. (2014). Synthesis, Structure–Activity Relationship Studies, and Antibacterial Evaluation of 4-Chromanones and Chalcones, as Well as Olympicin A and Derivatives. Journal of Medicinal Chemistry. 57(20). 8398–8420. 94 indexed citations
6.
Zhang, Zhongtao, Bokun Cheng, & Yuk-Ching Tse-Dinh. (2011). Crystal structure of a covalent intermediate in DNA cleavage and rejoining by Escherichia coli DNA topoisomerase I. Proceedings of the National Academy of Sciences. 108(17). 6939–6944. 62 indexed citations
7.
Narula, Gagandeep, et al.. (2011). The Strictly Conserved Arg-321 Residue in the Active Site of Escherichia coli Topoisomerase I Plays a Critical Role in DNA Rejoining. Journal of Biological Chemistry. 286(21). 18673–18680. 33 indexed citations
8.
Cheng, Bokun, et al.. (2008). Asp-to-Asn Substitution at the First Position of the DxD TOPRIM Motif of Recombinant Bacterial Topoisomerase I Is Extremely Lethal to E. coli. Journal of Molecular Biology. 385(2). 558–567. 30 indexed citations
9.
Cheng, Bokun, Elena P. Sorokin, & Yuk-Ching Tse-Dinh. (2007). Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I. Nucleic Acids Research. 36(3). 1017–1025. 19 indexed citations
10.
Cheng, Bokun, et al.. (2005). Bacterial Cell Killing Mediated by Topoisomerase I DNA Cleavage Activity. Journal of Biological Chemistry. 280(46). 38489–38495. 47 indexed citations
11.
Cheng, Bokun, et al.. (2004). Site-directed Mutagenesis of Residues Involved in G Strand DNA Binding by Escherichia coli DNA Topoisomerase I. Journal of Biological Chemistry. 279(38). 39207–39213. 13 indexed citations
12.
Tse-Dinh, Yuk-Ching. (2003). Topoisomerase function during bacterial responses to environmental challenge. Frontiers in bioscience. 8(4). d256–263. 42 indexed citations
13.
Cheng, Bokun, et al.. (2003). RNase H overproduction allows the expression of stress-induced genes in the absence of topoisomerase I. FEMS Microbiology Letters. 221(2). 237–242. 15 indexed citations
14.
Roche, Camille J. & Yuk-Ching Tse-Dinh. (2001). Effect of phosphorothioate substitutions on DNA cleavage by Escherichia coli DNA topoisomerase I. International Journal of Biological Macromolecules. 29(3). 175–180. 3 indexed citations
15.
Darżynkiewicz, Zbigniew, et al.. (2000). Differential Expression of Human Topoisomerase IIIα during the Cell Cycle Progression in HL-60 Leukemia Cells and Human Peripheral Blood Lymphocytes. Experimental Cell Research. 256(1). 225–236. 5 indexed citations
16.
Tse-Dinh, Yuk-Ching, et al.. (1996). Vaccinia virus DNA topoisomerase I preferentially removes positive supercoils from DNA. FEBS Letters. 384(3). 265–268. 7 indexed citations
17.
Du, Shou Ming, Hui Wang, Yuk-Ching Tse-Dinh, & Nadrian C. Seeman. (1995). Topological Transformations of Synthetic DNA Knots. Biochemistry. 34(2). 673–682. 38 indexed citations
18.
Gupta, Mamta, Chen Zhu, & Yuk-Ching Tse-Dinh. (1994). Mutations of vaccinia virus DNA topoisomerase I that stabilize the cleavage complex.. Journal of Biological Chemistry. 269(1). 573–578. 12 indexed citations
19.
Tse-Dinh, Yuk-Ching, et al.. (1994). Holliday Junction Crossover Topology. Journal of Molecular Biology. 236(1). 91–105. 56 indexed citations
20.
Gupta, Mamta, Chen Zhu, & Yuk-Ching Tse-Dinh. (1992). An engineered mutant of vaccinia virus DNA topoisomerase I is sensitive to the anti-cancer drug camptothecin.. Journal of Biological Chemistry. 267(34). 24177–24180. 17 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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