Seth M. Rubin

5.9k total citations · 1 hit paper
70 papers, 4.3k citations indexed

About

Seth M. Rubin is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Seth M. Rubin has authored 70 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 41 papers in Molecular Biology, 34 papers in Oncology and 25 papers in Cell Biology. Recurrent topics in Seth M. Rubin's work include Cancer-related Molecular Pathways (34 papers), Microtubule and mitosis dynamics (18 papers) and Ubiquitin and proteasome pathways (16 papers). Seth M. Rubin is often cited by papers focused on Cancer-related Molecular Pathways (34 papers), Microtubule and mitosis dynamics (18 papers) and Ubiquitin and proteasome pathways (16 papers). Seth M. Rubin collaborates with scholars based in United States, Canada and Estonia. Seth M. Rubin's co-authors include Frederick A. Dick, David E. Wemmer, Julien Sage, Alexander Pines, Eliseo Ruíz, Megan M. Spence, Jan M. Skotheim, Jason R. Burke, Mardo Kõivomägi and Nikola P. Pavletich and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Seth M. Rubin

68 papers receiving 4.3k citations

Hit Papers

Molecular mechanisms underlying RB protein function 2013 2026 2017 2021 2013 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Seth M. Rubin United States 35 2.5k 1.4k 707 603 580 70 4.3k
Masaki Matsumoto Japan 42 5.2k 2.1× 1.1k 0.8× 864 1.2× 470 0.8× 258 0.4× 166 7.4k
Sharon L. Campbell United States 50 6.4k 2.5× 1.6k 1.1× 2.2k 3.1× 271 0.4× 225 0.4× 149 9.0k
Stanley W. Botchway United Kingdom 39 2.1k 0.8× 459 0.3× 448 0.6× 625 1.0× 240 0.4× 152 5.5k
Sushmita Mukherjee United States 34 3.5k 1.4× 321 0.2× 1.1k 1.6× 205 0.3× 338 0.6× 74 5.6k
György Vereb Hungary 36 2.3k 0.9× 1.0k 0.7× 594 0.8× 81 0.1× 161 0.3× 158 4.5k
Jianming Zhang China 39 5.7k 2.3× 1.8k 1.2× 668 0.9× 189 0.3× 66 0.1× 165 8.6k
David C. Turner United States 42 3.0k 1.2× 616 0.4× 1.1k 1.6× 204 0.3× 340 0.6× 123 5.5k
Toshiki Tanaka Japan 42 3.4k 1.3× 767 0.5× 374 0.5× 180 0.3× 156 0.3× 239 6.2k
Wolfgang Hartmann Germany 44 3.3k 1.3× 1.8k 1.2× 307 0.4× 131 0.2× 200 0.3× 270 6.8k
John C. Williams United States 33 2.7k 1.1× 369 0.3× 799 1.1× 423 0.7× 48 0.1× 113 4.4k

Countries citing papers authored by Seth M. Rubin

Since Specialization
Citations

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

Fields of papers citing papers by Seth M. Rubin

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Seth M. Rubin. 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 Seth M. Rubin. The network helps show where Seth M. Rubin may publish in the future.

Co-authorship network of co-authors of Seth M. Rubin

This figure shows the co-authorship network connecting the top 25 collaborators of Seth M. Rubin. A scholar is included among the top collaborators of Seth M. Rubin 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 Seth M. Rubin. Seth M. Rubin 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.
Rubin, Seth M., et al.. (2026). Emerging Strategies to Inhibit the G1/S Transition for Cancer Therapy. Cancer Research.
2.
Castro, Anthony E., et al.. (2025). Structural and functional analysis of cancer-associated missense variants in the retinoblastoma protein pocket domain. Journal of Biological Chemistry. 301(3). 108284–108284. 1 indexed citations
3.
Wang, Xianxi, et al.. (2025). Structural mechanism for the recognition of E2F1 by the ubiquitin ligase adaptor Cyclin F. Proceedings of the National Academy of Sciences. 122(26). e2501057122–e2501057122.
4.
Arkile, Manisha, et al.. (2024). HDAC activity is dispensable for repression of cell-cycle genes by DREAM and E2F:RB complexes. Nature Communications. 15(1). 4450–4450. 11 indexed citations
5.
Silvestri, Anthony P., Qi Zhang, Jingsi Zhao, et al.. (2023). DNA-Encoded Macrocyclic Peptide Libraries Enable the Discovery of a Neutral MDM2–p53 Inhibitor. ACS Medicinal Chemistry Letters. 14(6). 820–826. 16 indexed citations
6.
Tripathi, Sarvind, B. Gayani K. Perera, Dustin J. Maly, et al.. (2023). Biolayer Interferometry Assay for Cyclin-Dependent Kinase-Cyclin Association Reveals Diverse Effects of Cdk2 Inhibitors on Cyclin Binding Kinetics. ACS Chemical Biology. 18(2). 431–440. 8 indexed citations
7.
Guiley, Keelan Z., et al.. (2022). Cyclin-dependent kinase-mediated phosphorylation and the negative regulatory domain of transcription factor B-Myb modulate its DNA binding. Journal of Biological Chemistry. 298(9). 102319–102319. 4 indexed citations
8.
Álvarez, Lucı́a, Peter Sehr, Gerd A. Müller, et al.. (2022). Structural basis for tunable affinity and specificity of LxCxE-dependent protein interactions with the retinoblastoma protein family. Structure. 30(9). 1340–1353.e3. 9 indexed citations
9.
Müller, Gerd A., et al.. (2022). Structure and function of MuvB complexes. Oncogene. 41(21). 2909–2919. 11 indexed citations
10.
Hazan, Ronen, Munemasa Mori, Paul S. Danielian, et al.. (2021). E2F4’s cytoplasmic role in multiciliogenesis is mediated via an N-terminal domain that binds two components of the centriole replication machinery, Deup1 and SAS6. Molecular Biology of the Cell. 32(20). ar1–ar1. 7 indexed citations
11.
Vorster, Paul J., Paul D. Goetsch, Keelan Z. Guiley, et al.. (2020). A long lost key opens an ancient lock: Drosophila Myb causes a synthetic multivulval phenotype in nematodes. Biology Open. 9(5). 6 indexed citations
12.
Guiley, Keelan Z., Kevin Lou, Krister J. Barkovich, et al.. (2019). p27 allosterically activates cyclin-dependent kinase 4 and antagonizes palbociclib inhibition. Science. 366(6471). 154 indexed citations
13.
Liban, Tyler, et al.. (2016). Structural Conservation and E2F Binding Specificity within the Retinoblastoma Pocket Protein Family. Journal of Molecular Biology. 428(20). 3960–3971. 31 indexed citations
14.
Kõivomägi, Mardo, Mihkel Örd, Ervin Valk, et al.. (2013). Multisite phosphorylation networks as signal processors for Cdk1. Nature Structural & Molecular Biology. 20(12). 1415–1424. 97 indexed citations
15.
Burke, Jason R., et al.. (2013). Multiple Mechanisms for E2F Binding Inhibition by Phosphorylation of the Retinoblastoma Protein C-Terminal Domain. Journal of Molecular Biology. 426(1). 245–255. 34 indexed citations
16.
Balog, Eva Rose M., Mardo Kõivomägi, Rafael Lucena, et al.. (2013). Cks confers specificity to phosphorylation-dependent CDK signaling pathways. Nature Structural & Molecular Biology. 20(12). 1407–1414. 72 indexed citations
17.
Saddic, Louis, Lisandra West, Aaron Aslanian, et al.. (2010). Methylation of the Retinoblastoma Tumor Suppressor by SMYD2. Journal of Biological Chemistry. 285(48). 37733–37740. 179 indexed citations
18.
Lima-de-Faria, A., et al.. (2009). Development of human male meiosis in vitro. Hereditas. 78(2). 265–271. 8 indexed citations
19.
Rubin, Seth M., et al.. (2005). Structure of the Rb C-Terminal Domain Bound to E2F1-DP1: A Mechanism for Phosphorylation-Induced E2F Release. Cell. 123(6). 1093–1106. 198 indexed citations
20.
Lowery, Thomas J., Seth M. Rubin, Eliseo Ruíz, et al.. (2003). Applications of laser-polarized 129xe to biomolecular assays. Magnetic Resonance Imaging. 21(10). 1235–1239. 24 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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