Benjamin E. Turk

15.0k total citations · 2 hit papers
124 papers, 10.3k citations indexed

About

Benjamin E. Turk is a scholar working on Molecular Biology, Oncology and Cell Biology. According to data from OpenAlex, Benjamin E. Turk has authored 124 papers receiving a total of 10.3k indexed citations (citations by other indexed papers that have themselves been cited), including 94 papers in Molecular Biology, 28 papers in Oncology and 24 papers in Cell Biology. Recurrent topics in Benjamin E. Turk's work include Protein Kinase Regulation and GTPase Signaling (28 papers), Melanoma and MAPK Pathways (15 papers) and Peptidase Inhibition and Analysis (13 papers). Benjamin E. Turk is often cited by papers focused on Protein Kinase Regulation and GTPase Signaling (28 papers), Melanoma and MAPK Pathways (15 papers) and Peptidase Inhibition and Analysis (13 papers). Benjamin E. Turk collaborates with scholars based in United States, United Kingdom and Canada. Benjamin E. Turk's co-authors include Reuben J. Shaw, Maria M. Mihaylova, Dana M. Gwinn, David B. Shackelford, Debbie S. Vasquez, Annabelle Méry, Lewis C. Cantley, Hua Jane Lou, Chad J. Miller and Lisa Huang and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Benjamin E. Turk

123 papers receiving 10.2k citations

Hit Papers

AMPK Phosphorylation of Raptor Mediates a Metabolic Check... 2008 2026 2014 2020 2008 2015 1000 2.0k 3.0k

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Benjamin E. Turk United States 45 6.9k 2.0k 1.6k 1.3k 1.2k 124 10.3k
Eric Spooner United States 43 5.6k 0.8× 1.6k 0.8× 886 0.5× 1.1k 0.8× 492 0.4× 58 8.4k
Gérard Pierron France 43 6.4k 0.9× 3.8k 1.9× 1.3k 0.8× 1.3k 1.0× 1.4k 1.2× 100 10.9k
Michael J. Clague United Kingdom 51 8.8k 1.3× 2.6k 1.3× 2.0k 1.2× 3.6k 2.8× 738 0.6× 131 11.5k
Mathew E. Sowa United States 40 9.7k 1.4× 2.3k 1.2× 1.7k 1.1× 2.4k 1.8× 903 0.8× 50 12.0k
María A. Juliano Brazil 47 4.8k 0.7× 1.4k 0.7× 1.5k 0.9× 543 0.4× 872 0.7× 376 9.1k
Toshiaki Isobe Japan 62 10.1k 1.5× 1.3k 0.7× 957 0.6× 1.6k 1.3× 1.1k 0.9× 247 13.4k
Tohru Natsume Japan 58 11.3k 1.6× 5.1k 2.6× 1.5k 0.9× 3.9k 3.0× 1.2k 1.0× 198 16.3k
Chunaram Choudhary Denmark 52 12.7k 1.8× 2.0k 1.0× 3.2k 2.0× 1.6k 1.3× 1.2k 1.0× 86 16.0k
Blagoy Blagoev Denmark 42 10.6k 1.5× 986 0.5× 1.6k 1.0× 1.8k 1.4× 1.1k 0.9× 108 14.1k
David K. Ann United States 52 5.0k 0.7× 1.1k 0.6× 1.9k 1.2× 641 0.5× 2.0k 1.7× 171 8.3k

Countries citing papers authored by Benjamin E. Turk

Since Specialization
Citations

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

Fields of papers citing papers by Benjamin E. Turk

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Benjamin E. Turk

This figure shows the co-authorship network connecting the top 25 collaborators of Benjamin E. Turk. A scholar is included among the top collaborators of Benjamin E. Turk 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 Benjamin E. Turk. Benjamin E. Turk 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.
Stiegler, Amy L., et al.. (2025). Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions. Journal of Biological Chemistry. 301(4). 108348–108348. 1 indexed citations
2.
McGeary, Meaghan K., William Damsky, Sabine M. Lang, et al.. (2024). Setdb1 Loss Induces Type I Interferons and Immune Clearance of Melanoma. Cancer Immunology Research. 13(2). 245–257. 4 indexed citations
3.
Bibeau, Jeffrey P., Wenxiang Cao, Hua Jane Lou, et al.. (2024). Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications. 15(1). 1426–1426. 2 indexed citations
4.
Cataisson, Christophe, Howard H. Yang, Wei‐Chun Lee, et al.. (2024). Protein phosphatase 6 activates NF-κB to confer sensitivity to MAPK pathway inhibitors in KRAS - and BRAF -mutant cancer cells. Science Signaling. 17(836). eadd5073–eadd5073.
5.
Lou, Hua Jane, et al.. (2024). Aurora B controls anaphase onset and error-free chromosome segregation in trypanosomes. The Journal of Cell Biology. 223(11). 2 indexed citations
6.
Liao, Xiaofeng, Barani Kumar Rajendran, Ao Li, et al.. (2024). The CUL5 E3 ligase complex negatively regulates central signaling pathways in CD8+ T cells. Nature Communications. 15(1). 603–603. 8 indexed citations
7.
Li, Wenxue, Shisheng Wang, Barbora Šalovská, et al.. (2023). An optogenetic-phosphoproteomic study reveals dynamic Akt1 signaling profiles in endothelial cells. Nature Communications. 14(1). 3803–3803. 14 indexed citations
8.
Torres‐Ayuso, Pedro, Katherine M. Nyswaner, Daniel A. Ritt, et al.. (2021). TNIK Is a Therapeutic Target in Lung Squamous Cell Carcinoma and Regulates FAK Activation through Merlin. Cancer Discovery. 11(6). 1411–1423. 38 indexed citations
9.
Hammond, Charlotte I., et al.. (2021). Phosphorylation of Pal2 by the protein kinases Kin1 and Kin2 modulates HAC1 mRNA splicing in the unfolded protein response in yeast. Science Signaling. 14(684). 6 indexed citations
10.
Terekhov, Stanislav S., Yuliana A. Mokrushina, Arthur O. Zalevsky, et al.. (2020). A kinase bioscavenger provides antibiotic resistance by extremely tight substrate binding. Science Advances. 6(26). eaaz9861–eaaz9861. 19 indexed citations
11.
Zhou, Mo, Leena Kuruvilla, Xiarong Shi, et al.. (2020). Scaffold association factor B (SAFB) is required for expression of prenyltransferases and RAS membrane association. Proceedings of the National Academy of Sciences. 117(50). 31914–31922. 9 indexed citations
12.
Sang, Dajun, Sudarshan Pinglay, Rafal Wiewiora, et al.. (2019). Ancestral reconstruction reveals mechanisms of ERK regulatory evolution. eLife. 8. 18 indexed citations
13.
Lou, Hua Jane, et al.. (2018). In Silico Design and in Vitro Characterization of Universal Tyrosine Kinase Peptide Substrates. Biochemistry. 57(12). 1847–1851. 5 indexed citations
14.
Hara, Masatoshi, Sebastian Lourido, Boryana Petrova, et al.. (2018). Identification of PNG kinase substrates uncovers interactions with the translational repressor TRAL in the oocyte-to-embryo transition. eLife. 7. 21 indexed citations
15.
Lim, Ya Chee, Bruno Catimel, Daisy Lio, et al.. (2017). Csk-homologous kinase (Chk) is an efficient inhibitor of Src-family kinases but a poor catalyst of phosphorylation of their C-terminal regulatory tyrosine. Cell Communication and Signaling. 15(1). 29–29. 12 indexed citations
16.
Kang, Seong A., Michael E. Pacold, Christopher Cervantes, et al.. (2013). mTORC1 Phosphorylation Sites Encode Their Sensitivity to Starvation and Rapamycin. Science. 341(6144). 1236566–1236566. 3 indexed citations
17.
Ha, Byung Hak, Matthew J. Davis, Catherine Chen, et al.. (2012). Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Proceedings of the National Academy of Sciences. 109(40). 16107–16112. 66 indexed citations
18.
Lam, Hugo Y. K., Philip M. Kim, Janine Mok, et al.. (2010). MOTIPS: Automated Motif Analysis for Predicting Targets of Modular Protein Domains. BMC Bioinformatics. 11(1). 243–243. 26 indexed citations
19.
Bullock, Alex N., J.E. Debreczeni, P. Rellos, et al.. (2009). Kinase Domain Insertions Define Distinct Roles of CLK Kinases in SR Protein Phosphorylation. Structure. 17(3). 352–362. 92 indexed citations
20.
Park, Hyun I., et al.. (2002). Peptide Substrate Specificities and Protein Cleavage Sites of Human Endometase/Matrilysin-2/Matrix Metalloproteinase-26. Journal of Biological Chemistry. 277(38). 35168–35175. 53 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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