Joseph E. Tropea

5.4k total citations
91 papers, 4.3k citations indexed

About

Joseph E. Tropea is a scholar working on Molecular Biology, Genetics and Oncology. According to data from OpenAlex, Joseph E. Tropea has authored 91 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 75 papers in Molecular Biology, 29 papers in Genetics and 12 papers in Oncology. Recurrent topics in Joseph E. Tropea's work include Bacterial Genetics and Biotechnology (14 papers), Yersinia bacterium, plague, ectoparasites research (14 papers) and RNA and protein synthesis mechanisms (12 papers). Joseph E. Tropea is often cited by papers focused on Bacterial Genetics and Biotechnology (14 papers), Yersinia bacterium, plague, ectoparasites research (14 papers) and RNA and protein synthesis mechanisms (12 papers). Joseph E. Tropea collaborates with scholars based in United States, Russia and Hungary. Joseph E. Tropea's co-authors include David S. Waugh, Scott Cherry, Alan D. Elbein, Xinhua Ji, Donald L. Court, Gagan Kaushal, Jianhua Gan, Alexander Wlodawer, Brian Austin and Karen M. Routzahn and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Joseph E. Tropea

90 papers receiving 4.2k 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. Tropea United States 38 3.1k 920 555 375 349 91 4.3k
Aldis Darzins United States 21 2.6k 0.8× 794 0.9× 507 0.9× 449 1.2× 139 0.4× 31 3.5k
S.A. McMahon United Kingdom 26 1.9k 0.6× 435 0.5× 362 0.7× 265 0.7× 152 0.4× 52 2.6k
Mark Paetzel Canada 32 2.2k 0.7× 960 1.0× 232 0.4× 354 0.9× 388 1.1× 59 3.3k
Bart Hazes Canada 27 2.1k 0.7× 394 0.4× 261 0.5× 270 0.7× 232 0.7× 53 3.6k
Walter F. Mangel United States 34 2.5k 0.8× 1.5k 1.6× 186 0.3× 546 1.5× 546 1.6× 104 4.3k
A.G. Evdokimov United States 30 1.5k 0.5× 539 0.6× 306 0.6× 162 0.4× 148 0.4× 51 2.4k
David S. Waugh United States 48 5.8k 1.9× 1.8k 2.0× 289 0.5× 834 2.2× 549 1.6× 140 7.7k
David E. Anderson United States 23 2.5k 0.8× 530 0.6× 131 0.2× 229 0.6× 221 0.6× 43 3.4k
Warren W. Wakarchuk Canada 53 5.2k 1.7× 655 0.7× 2.7k 4.9× 651 1.7× 216 0.6× 156 7.7k
Klaus Fütterer United Kingdom 27 1.5k 0.5× 377 0.4× 231 0.4× 147 0.4× 185 0.5× 55 2.6k

Countries citing papers authored by Joseph E. Tropea

Since Specialization
Citations

This map shows the geographic impact of Joseph E. Tropea'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. Tropea 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. Tropea more than expected).

Fields of papers citing papers by Joseph E. Tropea

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

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

This figure shows the co-authorship network connecting the top 25 collaborators of Joseph E. Tropea. A scholar is included among the top collaborators of Joseph E. Tropea 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. Tropea. Joseph E. Tropea 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.
Cherry, Scott, Joseph E. Tropea, G.T. Lountos, et al.. (2024). P1′ specificity of the S219V/R203G mutant tobacco etch virus protease. Proteins Structure Function and Bioinformatics. 92(9). 1085–1096.
2.
Zhao, Xue Zhi, Evgeny Kiselev, G.T. Lountos, et al.. (2021). Small molecule microarray identifies inhibitors of tyrosyl-DNA phosphodiesterase 1 that simultaneously access the catalytic pocket and two substrate binding sites. Chemical Science. 12(11). 3876–3884. 27 indexed citations
3.
Botos, Istvan, G.T. Lountos, Weimin Wu, et al.. (2019). Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery. SHILAP Revista de lepidopterología. 1. 13–20. 19 indexed citations
4.
Hewitt, William M., G.T. Lountos, Samuel D. Dahlhauser, et al.. (2016). Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9. Angewandte Chemie. 128(19). 5797–5801. 1 indexed citations
5.
Hewitt, William M., G.T. Lountos, Samuel D. Dahlhauser, et al.. (2016). Insights Into the Allosteric Inhibition of the SUMO E2 Enzyme Ubc9. Angewandte Chemie International Edition. 55(19). 5703–5707. 16 indexed citations
6.
Raran‐Kurussi, Sreejith, József Tőzsér, Scott Cherry, Joseph E. Tropea, & David S. Waugh. (2013). Differential temperature dependence of tobacco etch virus and rhinovirus 3C proteases. Analytical Biochemistry. 436(2). 142–144. 20 indexed citations
7.
Lountos, G.T., Joseph E. Tropea, & David S. Waugh. (2011). Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution. Acta Crystallographica Section D Biological Crystallography. 67(5). 471–479. 17 indexed citations
8.
Tu, Chao, Xiaomei Zhou, Sergey G. Tarasov, et al.. (2011). The Era GTPase recognizes the GAUCACCUCC sequence and binds helix 45 near the 3′ end of 16S rRNA. Proceedings of the National Academy of Sciences. 108(25). 10156–10161. 34 indexed citations
9.
Lountos, G.T., Joseph E. Tropea, Scott Cherry, & David S. Waugh. (2010). Overproduction, Purification and Structure Determination of Human Dual Specificity Phosphatase 14. Biophysical Journal. 98(3). 247a–247a. 8 indexed citations
10.
Tu, Chao, Joseph E. Tropea, Brian Austin, et al.. (2009). Structural Basis for Binding of RNA and Cofactor by a KsgA Methyltransferase. Structure. 17(3). 374–385. 26 indexed citations
11.
Jobson, Andrew G., G.T. Lountos, Philip L. Lorenzi, et al.. (2009). Cellular Inhibition of Checkpoint Kinase 2 (Chk2) and Potentiation of Camptothecins and Radiation by the Novel Chk2 Inhibitor PV1019 [7-Nitro-1H-indole-2-carboxylic acid {4-[1-(guanidinohydrazone)-ethyl]-phenyl}-amide]. Journal of Pharmacology and Experimental Therapeutics. 331(3). 816–826. 81 indexed citations
12.
Lountos, G.T., Joseph E. Tropea, Di Zhang, et al.. (2008). Crystal structure of checkpoint kinase 2 in complex with NSC 109555, a potent and selective inhibitor. Protein Science. 18(1). 92–100. 25 indexed citations
13.
Phan, Jason, Joseph E. Tropea, & David S. Waugh. (2007). Structure-assisted discovery ofVariola majorH1 phosphatase inhibitors. Acta Crystallographica Section D Biological Crystallography. 63(6). 698–704. 16 indexed citations
14.
Gan, Jianhua, Joseph E. Tropea, Brian Austin, et al.. (2006). Structural Insight into the Mechanism of Double-Stranded RNA Processing by Ribonuclease III. Cell. 124(2). 355–366. 185 indexed citations
15.
Tropea, Joseph E., Jason Phan, & David S. Waugh. (2006). Overproduction, purification, and biochemical characterization of the dual specificity H1 protein phosphatase encoded by variola major virus. Protein Expression and Purification. 50(1). 31–36. 11 indexed citations
16.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2005). Atomic-resolution Crystal Structure of the Proteolytic Domain of Archaeoglobus fulgidus Lon Reveals the Conformational Variability in the Active Sites of Lon Proteases. Journal of Molecular Biology. 351(1). 144–157. 43 indexed citations
17.
Błaszczyk, Jarosław, Jianhua Gan, Joseph E. Tropea, et al.. (2004). Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA. Structure. 12(3). 457–466. 106 indexed citations
18.
Botos, Istvan, Edward E. Melnikov, Scott Cherry, et al.. (2003). Crystal structure of the AAA+ α domain of E. coli Lon protease at 1.9Å resolution. Journal of Structural Biology. 146(1-2). 113–122. 69 indexed citations
19.
Błaszczyk, Jarosław, Joseph E. Tropea, Mikhail Bubunenko, et al.. (2001). Crystallographic and Modeling Studies of RNase III Suggest a Mechanism for Double-Stranded RNA Cleavage. Structure. 9(12). 1225–1236. 186 indexed citations
20.
Grossmann, Mathis, Mariusz W. Szkudlinski, Joseph E. Tropea, et al.. (1995). Expression of Human Thyrotropin in Cell Lines with Different Glycosylation Patterns Combined with Mutagenesis of Specific Glycosylation Sites. Journal of Biological Chemistry. 270(49). 29378–29385. 46 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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