Frederick Stull

1.0k total citations
30 papers, 752 citations indexed

About

Frederick Stull is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Frederick Stull has authored 30 papers receiving a total of 752 indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 9 papers in Materials Chemistry and 5 papers in Cell Biology. Recurrent topics in Frederick Stull's work include Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (8 papers) and Photosynthetic Processes and Mechanisms (5 papers). Frederick Stull is often cited by papers focused on Enzyme Structure and Function (9 papers), Protein Structure and Dynamics (8 papers) and Photosynthetic Processes and Mechanisms (5 papers). Frederick Stull collaborates with scholars based in United States, Germany and United Kingdom. Frederick Stull's co-authors include James C.A. Bardwell, Robin Teufel, Philipp Koldewey, Bruce A. Palfey, Bradley S. Moore, Quentin Michaudel, Scott Horowitz, Raoul Martin, Akimasa Miyanaga and Phil S. Baran and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Frederick Stull

28 papers receiving 745 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Frederick Stull United States 15 491 135 114 100 85 30 752
Caroline Haupt Germany 12 365 0.7× 117 0.9× 104 0.9× 100 1.0× 64 0.8× 20 654
Per Greisen United States 15 989 2.0× 172 1.3× 103 0.9× 73 0.7× 129 1.5× 27 1.4k
Konstantin M. Boyko Russia 19 661 1.3× 281 2.1× 93 0.8× 44 0.4× 54 0.6× 105 988
Laura S. Busenlehner United States 16 555 1.1× 148 1.1× 34 0.3× 53 0.5× 52 0.6× 27 1.1k
Patrick C. Cirino United States 18 1.0k 2.1× 102 0.8× 119 1.0× 45 0.5× 36 0.4× 28 1.3k
Chitra Rajendran Germany 16 516 1.1× 192 1.4× 82 0.7× 53 0.5× 32 0.4× 32 717
Nanne M. Kamerbeek Netherlands 11 1.1k 2.2× 115 0.9× 177 1.6× 102 1.0× 319 3.8× 13 1.5k
H.J. Hecht Germany 12 422 0.9× 116 0.9× 90 0.8× 86 0.9× 95 1.1× 21 695
Patrick A. Frantom United States 16 537 1.1× 211 1.6× 181 1.6× 41 0.4× 13 0.2× 38 856
René M. de Jong Netherlands 15 706 1.4× 131 1.0× 79 0.7× 61 0.6× 123 1.4× 22 884

Countries citing papers authored by Frederick Stull

Since Specialization
Citations

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

Fields of papers citing papers by Frederick Stull

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Frederick Stull

This figure shows the co-authorship network connecting the top 25 collaborators of Frederick Stull. A scholar is included among the top collaborators of Frederick Stull 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 Frederick Stull. Frederick Stull 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.
Zhang, Zhiyao, et al.. (2025). Role of glutamate 292 and lysine 331 in catalysis for the flavoenzyme (S)-6-hydroxynicotine oxidase from Shinella sp. HZN7. Archives of Biochemistry and Biophysics. 771. 110492–110492. 1 indexed citations
2.
Ghosh, Kingshuk, et al.. (2025). G-quadruplexes catalyze protein folding by reshaping the energetic landscape. Proceedings of the National Academy of Sciences. 122(6). e2414045122–e2414045122. 1 indexed citations
3.
Shearer, Heather L., Michael Currie, Claudia Trappetti, et al.. (2024). Hypothiocyanous acid reductase is critical for host colonization and infection by Streptococcus pneumoniae. Journal of Biological Chemistry. 300(5). 107282–107282. 1 indexed citations
4.
Zhang, Zhiyao, et al.. (2024). Rapid reaction studies on the chemistry of flavin oxidation in urocanate reductase. Journal of Biological Chemistry. 300(3). 105689–105689. 1 indexed citations
5.
Pathak, Ekta, et al.. (2024). Breaking the habit: isolating nicotine-degrading bacteria in undergraduate microbiology teaching labs. Journal of Microbiology and Biology Education. 25(2). e0015223–e0015223.
6.
Taylor, Christopher J., et al.. (2023). Analysis of histidine‐tagged recombinant proteins from nickel and copper coated surfaces by direct electrospray ionization and desorption electrospray ionization mass spectrometry. Rapid Communications in Mass Spectrometry. 37(S1). e9516–e9516. 3 indexed citations
7.
Dulchavsky, Mark, Qiang Li, Xiaomeng Liu, et al.. (2023). Directed evolution unlocks oxygen reactivity for a nicotine-degrading flavoenzyme. Nature Chemical Biology. 19(11). 1406–1414. 9 indexed citations
8.
Ulrich, Kathrin, et al.. (2022). Escherichia coli RclA is a highly active hypothiocyanite reductase. Proceedings of the National Academy of Sciences. 119(30). e2119368119–e2119368119. 16 indexed citations
9.
Zhang, Zhiyao, et al.. (2022). The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase. Journal of Biological Chemistry. 298(8). 102251–102251. 6 indexed citations
10.
Bou‐Nader, Charles, Frederick Stull, Ludovic Pecqueur, et al.. (2021). An enzymatic activation of formaldehyde for nucleotide methylation. Nature Communications. 12(1). 4542–4542. 13 indexed citations
11.
Dulchavsky, Mark, et al.. (2021). A cytochrome c is the natural electron acceptor for nicotine oxidoreductase. Nature Chemical Biology. 17(3). 344–350. 21 indexed citations
12.
Saleem-Batcha, R., et al.. (2020). Aminoperoxide adducts expand the catalytic repertoire of flavin monooxygenases. Nature Chemical Biology. 16(5). 556–563. 52 indexed citations
13.
Stull, Frederick, et al.. (2019). Protein folding while chaperone bound is dependent on weak interactions. Nature Communications. 10(1). 4833–4833. 29 indexed citations
14.
Stull, Frederick, et al.. (2018). In vivo chloride concentrations surge to proteotoxic levels during acid stress. Nature Chemical Biology. 14(11). 1051–1058. 15 indexed citations
15.
Horowitz, Scott, Philipp Koldewey, Frederick Stull, & James C.A. Bardwell. (2017). Folding while bound to chaperones. Current Opinion in Structural Biology. 48. 1–5. 34 indexed citations
16.
Salmon, Loïc, Frederick Stull, Linda Foit, et al.. (2017). The Mechanism of HdeA Unfolding and Chaperone Activation. Journal of Molecular Biology. 430(1). 33–40. 13 indexed citations
17.
Koldewey, Philipp, Frederick Stull, Scott Horowitz, Raoul Martin, & James C.A. Bardwell. (2016). Forces Driving Chaperone Action. Cell. 166(2). 369–379. 83 indexed citations
18.
Stull, Frederick, et al.. (2015). Substrate protein folds while it is bound to the ATP-independent chaperone Spy. Nature Structural & Molecular Biology. 23(1). 53–58. 71 indexed citations
19.
Teufel, Robin, Akimasa Miyanaga, Quentin Michaudel, et al.. (2013). Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement. Nature. 503(7477). 552–556. 143 indexed citations
20.
Stull, Frederick & Dean F. Martin. (2009). Comparative ease of separation of mixtures of selected nuisance anions (nitrate, nitrite, sulfate, phosphate) using Octolig®. Journal of Environmental Science and Health Part A. 44(14). 1545–1550. 15 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Caroline Haupt Breakdown of academic impact, for papers by Per Greisen Breakdown of academic impact, for papers by Konstantin M. Boyko Breakdown of academic impact, for papers by Laura S. Busenlehner Breakdown of academic impact, for papers by Patrick C. Cirino Breakdown of academic impact, for papers by Chitra Rajendran Breakdown of academic impact, for papers by Nanne M. Kamerbeek Breakdown of academic impact, for papers by H.J. Hecht Breakdown of academic impact, for papers by Patrick A. Frantom Breakdown of academic impact, for papers by René M. de Jong
Rankless by CCL
2026