Scott E. Boyken

5.6k total citations · 7 hit papers
28 papers, 3.0k citations indexed

About

Scott E. Boyken is a scholar working on Molecular Biology, Oncology and Ecology. According to data from OpenAlex, Scott E. Boyken has authored 28 papers receiving a total of 3.0k indexed citations (citations by other indexed papers that have themselves been cited), including 21 papers in Molecular Biology, 6 papers in Oncology and 5 papers in Ecology. Recurrent topics in Scott E. Boyken's work include RNA and protein synthesis mechanisms (12 papers), Protein Structure and Dynamics (10 papers) and Bacteriophages and microbial interactions (5 papers). Scott E. Boyken is often cited by papers focused on RNA and protein synthesis mechanisms (12 papers), Protein Structure and Dynamics (10 papers) and Bacteriophages and microbial interactions (5 papers). Scott E. Boyken collaborates with scholars based in United States, Norway and Austria. Scott E. Boyken's co-authors include David Baker, Po‐Ssu Huang, Zibo Chen, Robert A. Langan, Frank DiMaio, Robert L. Jernigan, Marc J. Lajoie, Vicki H. Wysocki, Mengxuan Jia and Galen Dods and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

Scott E. Boyken

28 papers receiving 2.9k citations

Hit Papers

The coming of age of de novo protein design 2016 2026 2019 2022 2016 2016 2019 2021 2020 250 500 750 1000

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Scott E. Boyken United States 20 2.3k 445 344 269 268 28 3.0k
Bjørn Dalhus Norway 34 2.2k 1.0× 400 0.9× 396 1.2× 313 1.2× 179 0.7× 94 3.4k
Feng Jiang China 32 2.1k 0.9× 619 1.4× 386 1.1× 271 1.0× 435 1.6× 78 3.6k
Vikram Khipple Mulligan United States 20 2.5k 1.1× 494 1.1× 112 0.3× 315 1.2× 183 0.7× 32 3.0k
John J. Correia United States 33 2.6k 1.2× 418 0.9× 183 0.5× 160 0.6× 649 2.4× 99 3.9k
Timothy A. Whitehead United States 24 1.9k 0.8× 350 0.8× 324 0.9× 481 1.8× 104 0.4× 69 2.4k
Gevorg Grigoryan United States 22 1.7k 0.7× 517 1.2× 118 0.3× 212 0.8× 98 0.4× 54 2.1k
Peer R. E. Mittl Switzerland 37 2.9k 1.3× 440 1.0× 201 0.6× 272 1.0× 411 1.5× 85 4.0k
Zibo Chen China 20 1.6k 0.7× 210 0.5× 348 1.0× 136 0.5× 206 0.8× 65 2.3k
Alexey V. Feofanov Russia 34 2.1k 0.9× 650 1.5× 483 1.4× 194 0.7× 262 1.0× 210 3.5k
Nobuyasu Koga Japan 17 2.0k 0.9× 856 1.9× 193 0.6× 188 0.7× 86 0.3× 28 2.5k

Countries citing papers authored by Scott E. Boyken

Since Specialization
Citations

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

Fields of papers citing papers by Scott E. Boyken

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Scott E. Boyken

This figure shows the co-authorship network connecting the top 25 collaborators of Scott E. Boyken. A scholar is included among the top collaborators of Scott E. Boyken 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 Scott E. Boyken. Scott E. Boyken 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.
Chang, Ya‐Ting, Andrew Norris, Scott E. Boyken, et al.. (2022). De novo design of obligate ABC-type heterotrimeric proteins. Nature Structural & Molecular Biology. 29(12). 1266–1276. 18 indexed citations
2.
Quijano‐Rubio, Alfredo, Hsien‐Wei Yeh, Hansol Lee, et al.. (2021). De novo design of modular and tunable protein biosensors. Nature. 591(7850). 482–487. 170 indexed citations breakdown →
3.
Chen, Zibo, Ryan D. Kibler, Andrew C. Hunt, et al.. (2020). De novo design of protein logic gates. Science. 368(6486). 78–84. 158 indexed citations breakdown →
4.
Wei, Kathy Y., Danai Moschidi, Matthew J. Bick, et al.. (2020). Computational design of closely related proteins that adopt two well-defined but structurally divergent folds. Proceedings of the National Academy of Sciences. 117(13). 7208–7215. 39 indexed citations
5.
Lajoie, Marc J., Scott E. Boyken, Alexander I. Salter, et al.. (2020). Designed protein logic to target cells with precise combinations of surface antigens. Science. 369(6511). 1637–1643. 144 indexed citations breakdown →
6.
VanAernum, Zachary L., Florian Büsch, Benjamin J. Jones, et al.. (2020). Rapid online buffer exchange for screening of proteins, protein complexes and cell lysates by native mass spectrometry. Nature Protocols. 15(3). 1132–1157. 125 indexed citations breakdown →
7.
McShan, Andrew C., Scott E. Boyken, Kathy Y. Wei, et al.. (2019). De novo design of a homo-trimeric amantadine-binding protein. eLife. 8. 19 indexed citations
8.
Langan, Robert A., Scott E. Boyken, Andrew H. Ng, et al.. (2019). De novo design of bioactive protein switches. Nature. 572(7768). 205–210. 185 indexed citations breakdown →
9.
Kristiansen, Per Eugen, Maria U. Johansson, Scott E. Boyken, et al.. (2019). The SH3 domains of the protein kinases ITK and LCK compete for adjacent sites on T cell–specific adapter protein. Journal of Biological Chemistry. 294(42). 15480–15494. 10 indexed citations
10.
Ng, Andrew H., Taylor H. Nguyen, Mariana Gómez-Schiavon, et al.. (2019). Modular and tunable biological feedback control using a de novo protein switch. Nature. 572(7768). 265–269. 87 indexed citations
11.
Lu, Peilong, Duyoung Min, Frank DiMaio, et al.. (2018). Accurate computational design of multipass transmembrane proteins. Science. 359(6379). 1042–1046. 137 indexed citations
12.
Chen, Zibo, Scott E. Boyken, Mengxuan Jia, et al.. (2018). Programmable design of orthogonal protein heterodimers. Nature. 565(7737). 106–111. 128 indexed citations
13.
Huang, Po‐Ssu, Scott E. Boyken, & David Baker. (2016). The coming of age of de novo protein design. Nature. 537(7620). 320–327. 1006 indexed citations breakdown →
14.
Boyken, Scott E., Zibo Chen, Benjamin Groves, et al.. (2016). De novo design of protein homo-oligomers with modular hydrogen-bond network–mediated specificity. Science. 352(6286). 680–687. 232 indexed citations breakdown →
15.
Wales, Thomas E., R Joseph, Scott E. Boyken, et al.. (2016). Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases. PLoS Computational Biology. 12(3). e1004826–e1004826. 41 indexed citations
16.
Marze, Nicholas, Jeliazko R. Jeliazkov, Shourya S. Roy Burman, et al.. (2016). Modeling oblong proteins and water‐mediated interfaces with RosettaDock in CAPRI rounds 28–35. Proteins Structure Function and Bioinformatics. 85(3). 479–486. 15 indexed citations
17.
Wang, Xinxin, Scott E. Boyken, Jiancheng Hu, et al.. (2014). Calmodulin and PI(3,4,5)P 3 cooperatively bind to the Itk pleckstrin homology domain to promote efficient calcium signaling and IL-17A production. Science Signaling. 7(337). ra74–ra74. 19 indexed citations
18.
Sparkman, Amanda M., Tonia S. Schwartz, Jill A. Madden, et al.. (2012). Rates of molecular evolution vary in vertebrates for insulin-like growth factor-1 (IGF-1), a pleiotropic locus that regulates life history traits. General and Comparative Endocrinology. 178(1). 164–173. 25 indexed citations
19.
Boyken, Scott E., D. Bruce Fulton, & Amy H. Andreotti. (2012). Rescue of the aggregation prone Itk Pleckstrin Homology domain by two mutations derived from the related kinases, Btk and Tec. Protein Science. 21(9). 1288–1297. 11 indexed citations
20.
Long, Feng, Chih‐Chia Su, Michael T. Zimmermann, et al.. (2010). Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport. Nature. 467(7314). 484–488. 195 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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