Tamar Unger

6.6k total citations · 2 hit papers
67 papers, 4.6k citations indexed

About

Tamar Unger is a scholar working on Molecular Biology, Biotechnology and Oncology. According to data from OpenAlex, Tamar Unger has authored 67 papers receiving a total of 4.6k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Biology, 12 papers in Biotechnology and 11 papers in Oncology. Recurrent topics in Tamar Unger's work include Protein Structure and Dynamics (9 papers), Cancer-related Molecular Pathways (9 papers) and Monoclonal and Polyclonal Antibodies Research (9 papers). Tamar Unger is often cited by papers focused on Protein Structure and Dynamics (9 papers), Cancer-related Molecular Pathways (9 papers) and Monoclonal and Polyclonal Antibodies Research (9 papers). Tamar Unger collaborates with scholars based in Israel, United States and Germany. Tamar Unger's co-authors include Peter M. Howley, Yoav Peleg, Shira Albeck, Judy A. Mietz, Jon M. Huibregtse, Orly Dym, John D. Minna, Shoshana Segal, Marion M. Nau and Carole Yee and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Tamar Unger

65 papers receiving 4.5k citations

Hit Papers

Biosynthesis of Antinutritional Alkaloids in Solanaceous ... 2013 2026 2017 2021 2013 2016 100 200 300 400

Peers

Tamar Unger
Ido Goldstein United States
Ivo Tews Germany
Jac A. Nickoloff United States
Jeremy Minshull United States
Lanette Fee United States
Tamar Unger
Citations per year, relative to Tamar Unger Tamar Unger (= 1×) peers Jacek Otlewski

Countries citing papers authored by Tamar Unger

Since Specialization
Citations

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

Fields of papers citing papers by Tamar Unger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Tamar Unger. 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 Tamar Unger. The network helps show where Tamar Unger may publish in the future.

Co-authorship network of co-authors of Tamar Unger

This figure shows the co-authorship network connecting the top 25 collaborators of Tamar Unger. A scholar is included among the top collaborators of Tamar Unger 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 Tamar Unger. Tamar Unger 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.
McBride, J. Michael, Marta Siek, Jacques Rougemont, et al.. (2025). Enzymes as viscoelastic catalytic machines. Nature Physics. 21(5). 787–798. 4 indexed citations
2.
Avram, Liat, et al.. (2024). Unnatural enzyme activation by a metal-responsive regulatory protein. Chemical Science. 15(35). 14209–14217.
3.
Unger, Tamar, Shira Albeck, Gary Weisinger, et al.. (2024). Treating late-onset Tay Sachs disease: Brain delivery with a dual trojan horse protein. Molecular Therapy — Methods & Clinical Development. 32(3). 101300–101300. 2 indexed citations
4.
Franz, Florian, Rafael Tapia‐Rojo, Sabina Winograd‐Katz, et al.. (2023). Allosteric activation of vinculin by talin. Nature Communications. 14(1). 4311–4311. 20 indexed citations
5.
Giannoulis, Angeliki, Anna Vanyushkina, Tamar Unger, et al.. (2023). C-terminal domain dimerization in yeast Hsp90 is moderately modulated by the other domains. Biophysical Journal. 123(2). 172–183. 4 indexed citations
6.
Schütz, Anja, Frank Bernhard, Nicholas S. Berrow, et al.. (2023). A concise guide to choosing suitable gene expression systems for recombinant protein production. STAR Protocols. 4(4). 102572–102572. 36 indexed citations
7.
Sonawane, Prashant D., Adam Jóźwiak, Ranjit S. Barbole, et al.. (2022). 2‐oxoglutarate‐dependent dioxygenases drive expansion of steroidal alkaloid structural diversity in the genus Solanum. New Phytologist. 234(4). 1394–1410. 21 indexed citations
8.
Hatai, Joydev, Pragati K. Prasad, Tamar Unger, et al.. (2020). Assessing changes in the expression levels of cell surface proteins with a turn-on fluorescent molecular probe. Chemical Communications. 57(15). 1875–1878. 9 indexed citations
9.
Prasad, Pragati K., Tali Dadosh, Tamar Unger, et al.. (2020). Decorating bacteria with self-assembled synthetic receptors. Nature Communications. 11(1). 1299–1299. 37 indexed citations
10.
Georgeson, Joseph M., Tal Ilani, Vladimir Kiss, et al.. (2017). Protein recognition by a pattern-generating fluorescent molecular probe. Nature Nanotechnology. 12(12). 1161–1168. 110 indexed citations
11.
Sun, Liping, Anat Bashan, Ella Zimmerman, et al.. (2015). A Recombinant Collagen–mRNA Platform for Controllable Protein Synthesis. ChemBioChem. 16(10). 1415–1419. 2 indexed citations
12.
Itkin, Maxim, Uwe Heinig, Oren Tzfadia, et al.. (2013). Biosynthesis of Antinutritional Alkaloids in Solanaceous Crops Is Mediated by Clustered Genes. Science. 341(6142). 175–179. 428 indexed citations breakdown →
13.
Vazana, Yael, Yoav Barak, Tamar Unger, et al.. (2013). A synthetic biology approach for evaluating the functional contribution of designer cellulosome components to deconstruction of cellulosic substrates. Biotechnology for Biofuels. 6(1). 182–182. 72 indexed citations
14.
Sobolev, V. M., Marvin Edelman, Orly Dym, et al.. (2013). Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(2). 84–89. 8 indexed citations
15.
Peleg, Yoav & Tamar Unger. (2011). Resolving Bottlenecks for Recombinant Protein Expression in E. coli. Methods in molecular biology. 800. 173–186. 19 indexed citations
16.
Unger, Tamar & Yoav Peleg. (2011). Recombinant Protein Expression in the Baculovirus-Infected Insect Cell System. Methods in molecular biology. 800. 187–199. 20 indexed citations
17.
Karanicolas, John, Jacob E. Corn, Irwin Chen, et al.. (2011). A De Novo Protein Binding Pair By Computational Design and Directed Evolution. Molecular Cell. 42(2). 250–260. 136 indexed citations
18.
Dym, Orly, Shira Albeck, Tamar Unger, et al.. (2008). Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. Proceedings of the National Academy of Sciences. 105(32). 11170–11175. 37 indexed citations
19.
Liberman, Noa, Orly Dym, Tamar Unger, et al.. (2008). The Crystal Structure of the C-Terminal DAP5/p97 Domain Sheds Light on the Molecular Basis for Its Processing by Caspase Cleavage. Journal of Molecular Biology. 383(3). 539–548. 13 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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