Robert E. Cohen

8.3k total citations · 3 hit papers
72 papers, 6.8k citations indexed

About

Robert E. Cohen is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Robert E. Cohen has authored 72 papers receiving a total of 6.8k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 17 papers in Oncology and 17 papers in Cell Biology. Recurrent topics in Robert E. Cohen's work include Ubiquitin and proteasome pathways (40 papers), Glycosylation and Glycoproteins Research (21 papers) and Peptidase Inhibition and Analysis (13 papers). Robert E. Cohen is often cited by papers focused on Ubiquitin and proteasome pathways (40 papers), Glycosylation and Glycoproteins Research (21 papers) and Peptidase Inhibition and Analysis (13 papers). Robert E. Cohen collaborates with scholars based in United States, Germany and China. Robert E. Cohen's co-authors include Tingting Yao, Cecile M. Pickart, Clinton E. Ballou, George Demartino, Joshua J. Sims, Wei Xu, Y. Amy Lam, Ling Song, Min Hu and Yigong Shi and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Robert E. Cohen

71 papers receiving 6.6k citations

Hit Papers

A cryptic protease couples deubiquitination and degradati... 2002 2026 2010 2018 2002 2004 2002 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert E. Cohen United States 38 5.7k 1.7k 1.4k 1.2k 668 72 6.8k
Jonathan M. Goldberg United States 39 4.6k 0.8× 883 0.5× 3.0k 2.1× 455 0.4× 451 0.7× 55 7.3k
Jens Schneider‐Mergener Germany 47 5.2k 0.9× 1.1k 0.6× 666 0.5× 593 0.5× 557 0.8× 124 7.5k
Eric Spooner United States 43 5.6k 1.0× 886 0.5× 1.1k 0.8× 1.6k 1.3× 501 0.8× 58 8.4k
Rudolf Volkmer Germany 47 6.1k 1.1× 753 0.4× 762 0.5× 697 0.6× 471 0.7× 155 8.1k
Sung Key Jang South Korea 49 5.4k 1.0× 802 0.5× 399 0.3× 1.0k 0.9× 755 1.1× 127 8.8k
Marco Rusnati Italy 55 5.8k 1.0× 996 0.6× 2.0k 1.5× 534 0.4× 660 1.0× 174 9.0k
Frank R. Masiarz United States 39 5.5k 1.0× 792 0.5× 638 0.5× 994 0.8× 1000 1.5× 52 8.2k
Ger J. Strous Netherlands 48 5.8k 1.0× 880 0.5× 3.1k 2.2× 491 0.4× 556 0.8× 126 8.5k
Marcelo Ehrlich Israel 35 3.9k 0.7× 705 0.4× 1.7k 1.2× 454 0.4× 565 0.8× 102 6.1k
Kirill Alexandrov Australia 47 5.5k 1.0× 540 0.3× 2.7k 1.9× 417 0.3× 376 0.6× 178 7.4k

Countries citing papers authored by Robert E. Cohen

Since Specialization
Citations

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

Fields of papers citing papers by Robert E. Cohen

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert E. Cohen

This figure shows the co-authorship network connecting the top 25 collaborators of Robert E. Cohen. A scholar is included among the top collaborators of Robert E. Cohen 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 Robert E. Cohen. Robert E. Cohen 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.
Eskelinen, Eeva‐Liisa, et al.. (2025). Trafficking of K63-polyubiquitin–modified membrane proteins in a macroautophagy-independent pathway is linked to ATG9A. Molecular Biology of the Cell. 36(4). ar42–ar42. 1 indexed citations
2.
Fischer, Tara D., Eric Bunker, Peng-Peng Zhu, et al.. (2024). STING induces HOIP-mediated synthesis of M1 ubiquitin chains to stimulate NF-κB signaling. The EMBO Journal. 44(1). 141–165. 6 indexed citations
3.
Choi, Yun‐Seok, et al.. (2023). Avidity-based biosensors for ubiquitylated PCNA reveal choreography of DNA damage bypass. Science Advances. 9(36). eadf3041–eadf3041. 4 indexed citations
4.
Passos, Carolina dos Santos, Yun‐Seok Choi, Christopher D. Snow, Tingting Yao, & Robert E. Cohen. (2021). Design of genetically encoded sensors to detect nucleosome ubiquitination in live cells. The Journal of Cell Biology. 220(4). 7 indexed citations
5.
Choi, Yun‐Seok, et al.. (2019). High-affinity free ubiquitin sensors for quantifying ubiquitin homeostasis and deubiquitination. Nature Methods. 16(8). 771–777. 21 indexed citations
6.
Choi, Yun‐Seok, Seo‐Yeon Lee, Lei Shi, et al.. (2014). Differential Ubiquitin Binding by the Acidic Loops of Ube2g1 and Ube2r1 Enzymes Distinguishes Their Lys-48-ubiquitylation Activities. Journal of Biological Chemistry. 290(4). 2251–2263. 23 indexed citations
7.
Nakasone, Mark A., Nurit Livnat‐Levanon, Michael H. Glickman, Robert E. Cohen, & David Fushman. (2013). Mixed-Linkage Ubiquitin Chains Send Mixed Messages. Structure. 21(5). 727–740. 85 indexed citations
8.
Samara, N.L., Ajit B. Datta, Christopher Berndsen, et al.. (2010). Structural Insights into the Assembly and Function of the SAGA Deubiquitinating Module. Science. 328(5981). 1025–1029. 178 indexed citations
9.
Winborn, Brett J, Sue M. Travis, Sokol V. Todi, et al.. (2008). The Deubiquitinating Enzyme Ataxin-3, a Polyglutamine Disease Protein, Edits Lys63 Linkages in Mixed Linkage Ubiquitin Chains. Journal of Biological Chemistry. 283(39). 26436–26443. 213 indexed citations
10.
Yao, Tingting, Ling Song, Jingji Jin, et al.. (2008). Distinct Modes of Regulation of the Uch37 Deubiquitinating Enzyme in the Proteasome and in the Ino80 Chromatin-Remodeling Complex. Molecular Cell. 31(6). 909–917. 124 indexed citations
11.
Lee, Daeyeon, et al.. (2007). pH-Dependent Structure and Properties of TiO2/SiO2Nanoparticle Multilayer Thin Films. Chemistry of Materials. 19(6). 1427–1433. 108 indexed citations
12.
Yao, Tingting, Ling Song, Wei Xu, et al.. (2006). Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1. Nature Cell Biology. 8(9). 994–1002. 275 indexed citations
13.
Hu, Min, Pingwei Li, Ling Song, et al.. (2005). Structure and mechanisms of the proteasome‐associated deubiquitinating enzyme USP14. The EMBO Journal. 24(21). 3747–3756. 339 indexed citations
14.
Wicks, Stephen J., et al.. (2005). The deubiquitinating enzyme UCH37 interacts with Smads and regulates TGF-β signalling. Oncogene. 24(54). 8080–8084. 150 indexed citations
15.
Pickart, Cecile M. & Robert E. Cohen. (2004). Proteasomes and their kin: proteases in the machine age. Nature Reviews Molecular Cell Biology. 5(3). 177–187. 567 indexed citations breakdown →
16.
Yao, Tingting & Robert E. Cohen. (2000). Cyclization of Polyubiquitin by the E2-25K Ubiquitin Conjugating Enzyme. Journal of Biological Chemistry. 275(47). 36862–36868. 25 indexed citations
17.
Lam, Y. Amy, George Demartino, Cecile M. Pickart, & Robert E. Cohen. (1997). Specificity of the Ubiquitin Isopeptidase in the PA700 Regulatory Complex of 26 S Proteasomes. Journal of Biological Chemistry. 272(45). 28438–28446. 80 indexed citations
18.
Shaeffer, Joseph R. & Robert E. Cohen. (1997). Ubiquitin Aldehyde Increases Adenosine Triphosphate–Dependent Proteolysis of Hemoglobin α-Subunits in β-Thalassemic Hemolysates. Blood. 90(3). 1300–1308. 15 indexed citations
19.
Cohen, Robert E., et al.. (1990). Gingival Manifestations of Wegener's Granulomatosis. Journal of Periodontology. 61(11). 705–709. 23 indexed citations
20.
Lehle, Ludwig, Robert E. Cohen, & Clinton E. Ballou. (1979). Carbohydrate structure of yeast invertase. Demonstration of a form with only core oligosaccharides and a form with completed polysaccharide chains.. Journal of Biological Chemistry. 254(23). 12209–12218. 78 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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