Thomas C. Leeper

1.4k total citations
36 papers, 1.1k citations indexed

About

Thomas C. Leeper is a scholar working on Molecular Biology, Materials Chemistry and Oncology. According to data from OpenAlex, Thomas C. Leeper has authored 36 papers receiving a total of 1.1k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 7 papers in Materials Chemistry and 5 papers in Oncology. Recurrent topics in Thomas C. Leeper's work include RNA and protein synthesis mechanisms (15 papers), RNA Research and Splicing (8 papers) and Enzyme Structure and Function (5 papers). Thomas C. Leeper is often cited by papers focused on RNA and protein synthesis mechanisms (15 papers), RNA Research and Splicing (8 papers) and Enzyme Structure and Function (5 papers). Thomas C. Leeper collaborates with scholars based in United States, Switzerland and China. Thomas C. Leeper's co-authors include Gabriele Varani, Zafiria Athanassiou, John A. Robinson, Werner J. Geldenhuys, Richard T. Carroll, Mark J. Morris, Soumitra Basu, Krystyna Patora‐Komisarska, Amy Davidson and Jonathan Karn and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and SHILAP Revista de lepidopterología.

In The Last Decade

Thomas C. Leeper

36 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
Thomas C. Leeper United States 18 844 80 78 73 73 36 1.1k
Daniel B. Toso United States 19 847 1.0× 55 0.7× 51 0.7× 210 2.9× 21 0.3× 23 1.4k
Hilary Brooks Australia 11 1.3k 1.5× 126 1.6× 50 0.6× 57 0.8× 47 0.6× 19 1.7k
Lindsay G. Sparrow Australia 20 687 0.8× 71 0.9× 44 0.6× 48 0.7× 37 0.5× 44 1.1k
Deepak Sharma United States 20 1.2k 1.4× 174 2.2× 56 0.7× 149 2.0× 88 1.2× 44 1.7k
Nicole Boggetto France 25 861 1.0× 121 1.5× 259 3.3× 203 2.8× 123 1.7× 43 1.7k
Kanaka Pattabiraman United States 7 1.3k 1.6× 141 1.8× 173 2.2× 39 0.5× 28 0.4× 9 1.5k
S. V. Burov Russia 16 373 0.4× 119 1.5× 85 1.1× 57 0.8× 7 0.1× 54 702
Anni Zhao United States 8 542 0.6× 256 3.2× 79 1.0× 88 1.2× 19 0.3× 8 875
José A. Rodríguez‐Martínez Puerto Rico 15 643 0.8× 80 1.0× 66 0.8× 46 0.6× 6 0.1× 27 883
Xiaocui Zhu China 15 479 0.6× 46 0.6× 27 0.3× 61 0.8× 7 0.1× 25 816

Countries citing papers authored by Thomas C. Leeper

Since Specialization
Citations

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

Fields of papers citing papers by Thomas C. Leeper

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas C. Leeper. 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 Thomas C. Leeper. The network helps show where Thomas C. Leeper may publish in the future.

Co-authorship network of co-authors of Thomas C. Leeper

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas C. Leeper. A scholar is included among the top collaborators of Thomas C. Leeper 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 Thomas C. Leeper. Thomas C. Leeper 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.
2.
Leeper, Thomas C., et al.. (2019). The LARP1 La-Module recognizes both ends of TOP mRNAs. RNA Biology. 18(2). 248–258. 29 indexed citations
3.
Avila, Robin L., He Huang, Thomas C. Leeper, et al.. (2017). Cuprizone Intoxication Induces Cell Intrinsic Alterations in Oligodendrocyte Metabolism Independent of Copper Chelation. Biochemistry. 56(10). 1518–1528. 35 indexed citations
4.
Morris, Daniel L., et al.. (2017). Lysozyme-catalyzed formation of a conjugated polyacetylene. Polymer Chemistry. 8(41). 6344–6348. 4 indexed citations
5.
Khattri, Ram B., Daniel L. Morris, Caroline Davis, et al.. (2016). An NMR-Guided Screening Method for Selective Fragment Docking and Synthesis of a Warhead Inhibitor. Molecules. 21(7). 846–846. 6 indexed citations
6.
Geldenhuys, Werner J., Heather M. Yonutas, Daniel L. Morris, et al.. (2016). Identification of small molecules that bind to the mitochondrial protein mitoNEET. Bioorganic & Medicinal Chemistry Letters. 26(21). 5350–5353. 31 indexed citations
7.
Geldenhuys, Werner J., Thomas C. Leeper, & Richard T. Carroll. (2014). mitoNEET as a novel drug target for mitochondrial dysfunction. Drug Discovery Today. 19(10). 1601–1606. 83 indexed citations
8.
Bilinovich, Stephanie M., et al.. (2014). The C-Terminal Domain of SRA1p Has a Fold More Similar to PRP18 than to an RRM and Does Not Directly Bind to the SRA1 RNA STR7 Region. Journal of Molecular Biology. 426(8). 1753–1765. 7 indexed citations
9.
Panzner, Matthew J., et al.. (2014). Mercury metallation of the copper protein azurin and structural insight into possible heavy metal reactivity. Journal of Inorganic Biochemistry. 141. 152–160. 4 indexed citations
10.
Wu, Jiang, Chao Zhao, Rundong Hu, et al.. (2013). Probing the weak interaction of proteins with neutral and zwitterionic antifouling polymers. Acta Biomaterialia. 10(2). 751–760. 74 indexed citations
11.
Panzner, Matthew J., Stephanie M. Bilinovich, Jillian A. Parker, et al.. (2013). Isomorphic deactivation of a Pseudomonas aeruginosa oxidoreductase: The crystal structure of Ag(I) metallated azurin at 1.7Å. Journal of Inorganic Biochemistry. 128. 11–16. 11 indexed citations
12.
Leeper, Thomas C., et al.. (2011). Re(CO)3(H2O)3+ binding to lysozyme: structure and reactivity. Metallomics. 3(9). 909–909. 29 indexed citations
13.
Panzner, Matthew J., Stephanie M. Bilinovich, Wiley J. Youngs, & Thomas C. Leeper. (2011). Silver metallation of hen egg white lysozyme: X-ray crystal structure and NMR studies. Chemical Communications. 47(46). 12479–12479. 33 indexed citations
14.
Leeper, Thomas C., Suxin Zhang, Wesley C. Van Voorhis, Peter J. Myler, & Gabriele Varani. (2011). Comparative analysis of glutaredoxin domains from bacterial opportunistic pathogens. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(9). 1141–1147. 6 indexed citations
15.
Bilinovich, Stephanie M., Matthew J. Panzner, Wiley J. Youngs, & Thomas C. Leeper. (2011). Poly[[{μ3-2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonato}silver(I)] trihydrate]. Acta Crystallographica Section E Structure Reports Online. 67(9). m1178–m1179. 3 indexed citations
16.
Leeper, Thomas C., Xiangping Qu, Connie Lu, Claire Moore, & Gabriele Varani. (2010). Novel Protein–Protein Contacts Facilitate mRNA 3′-Processing Signal Recognition by Rna15 and Hrp1. Journal of Molecular Biology. 401(3). 334–349. 49 indexed citations
17.
Lunde, Bradley M., Steve Reichow, Minkyu Kim, et al.. (2010). Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain. Nature Structural & Molecular Biology. 17(10). 1195–1201. 124 indexed citations
18.
Leulliot, Nicolas, Sophie Quevillon‐Chéruel, Marc Graille, et al.. (2004). A new α‐helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III. The EMBO Journal. 23(13). 2468–2477. 50 indexed citations
19.
Leeper, Thomas C.. (2003). The solution structure of an essential stem-loop of human telomerase RNA. Nucleic Acids Research. 31(10). 2614–2621. 37 indexed citations
20.
Leeper, Thomas C., et al.. (2001). In vitro transactivation ofBacillus subtilisRNase P RNA. FEBS Letters. 506(3). 235–238. 4 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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