Brian Fuglestad

667 total citations
28 papers, 546 citations indexed

About

Brian Fuglestad is a scholar working on Molecular Biology, Cell Biology and Spectroscopy. According to data from OpenAlex, Brian Fuglestad has authored 28 papers receiving a total of 546 indexed citations (citations by other indexed papers that have themselves been cited), including 22 papers in Molecular Biology, 6 papers in Cell Biology and 6 papers in Spectroscopy. Recurrent topics in Brian Fuglestad's work include Protein Structure and Dynamics (11 papers), Lipid Membrane Structure and Behavior (8 papers) and Surfactants and Colloidal Systems (5 papers). Brian Fuglestad is often cited by papers focused on Protein Structure and Dynamics (11 papers), Lipid Membrane Structure and Behavior (8 papers) and Surfactants and Colloidal Systems (5 papers). Brian Fuglestad collaborates with scholars based in United States, Poland and Canada. Brian Fuglestad's co-authors include A. Joshua Wand, Phineus R. L. Markwick, Elizabeth A. Komives, J. Andrew McCammon, Paul M. Gasper, Nathaniel V. Nucci, Evan S. O’Brien, Cecilia Tommos, Kushol Gupta and Marco Tonelli and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

Brian Fuglestad

25 papers receiving 542 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Brian Fuglestad United States 12 394 90 85 72 57 28 546
Roman V. Agafonov United States 13 658 1.7× 68 0.8× 187 2.2× 57 0.8× 45 0.8× 22 839
Austin Vogt United States 11 517 1.3× 50 0.6× 118 1.4× 164 2.3× 34 0.6× 19 768
Edgar Specker Germany 16 405 1.0× 129 1.4× 105 1.2× 26 0.4× 90 1.6× 36 781
Jeff Peng United States 6 597 1.5× 79 0.9× 76 0.9× 65 0.9× 31 0.5× 7 774
Navratna Vajpai Switzerland 9 378 1.0× 92 1.0× 115 1.4× 111 1.5× 67 1.2× 16 520
Jens Sydor United States 14 553 1.4× 61 0.7× 45 0.5× 59 0.8× 47 0.8× 25 803
Raphaël Geney United States 12 403 1.0× 65 0.7× 79 0.9× 27 0.4× 146 2.6× 14 695
Emily B. Dunkelberger United States 11 392 1.0× 97 1.1× 54 0.6× 114 1.6× 18 0.3× 20 709
Lizhe Zhu China 18 615 1.6× 124 1.4× 252 3.0× 15 0.2× 83 1.5× 48 967
Anna Berteotti Italy 11 556 1.4× 40 0.4× 100 1.2× 13 0.2× 113 2.0× 13 808

Countries citing papers authored by Brian Fuglestad

Since Specialization
Citations

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

Fields of papers citing papers by Brian Fuglestad

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Brian Fuglestad

This figure shows the co-authorship network connecting the top 25 collaborators of Brian Fuglestad. A scholar is included among the top collaborators of Brian Fuglestad 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 Brian Fuglestad. Brian Fuglestad 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.
2.
Fuglestad, Brian, et al.. (2024). An NMR Approach for Investigating Membrane Protein–Lipid Interactions Using Native Reverse Micelles. BIO-PROTOCOL. 14(1349). e5039–e5039. 2 indexed citations
3.
Fuglestad, Brian, et al.. (2024). Characterization of 10MAG/LDAO reverse micelles: Understanding versatility for protein encapsulation. Biophysical Chemistry. 311. 107269–107269. 5 indexed citations
4.
Fuglestad, Brian, et al.. (2023). Aptabinding of tumor necrosis factor‐α (TNFα) inhibits its proinflammatory effects and alleviates islet inflammation. Biotechnology Journal. 19(1). e2300374–e2300374.
5.
Qu, Yun, et al.. (2023). Investigating protein‐membrane interactions using native reverse micelles constructed from naturally sourced lipids. Protein Science. 32(11). e4786–e4786. 6 indexed citations
6.
Artikis, Efrosini, Aron Broom, Brian Fuglestad, et al.. (2022). A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein. Proceedings of the National Academy of Sciences. 119(26). e2119686119–e2119686119. 5 indexed citations
7.
Offenbacher, Adam R., et al.. (2022). Membrane-Mimicking Reverse Micelles for High-Resolution Interfacial Study of Proteins and Membranes. Langmuir. 38(12). 3676–3686. 8 indexed citations
8.
O’Brien, Evan S., et al.. (2020). Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy. Angewandte Chemie International Edition. 59(27). 11108–11114. 20 indexed citations
9.
O’Brien, Evan S., et al.. (2020). Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy. Angewandte Chemie. 132(27). 11201–11207. 3 indexed citations
10.
Fuglestad, Brian, Kushol Gupta, A. Joshua Wand, & Kim A. Sharp. (2019). Water loading driven size, shape, and composition of cetyltrimethylammonium/hexanol/pentane reverse micelles. Journal of Colloid and Interface Science. 540. 207–217. 15 indexed citations
11.
Fuglestad, Brian, et al.. (2019). Site-Resolved and Quantitative Characterization of Very Weak Protein–Ligand Interactions. ACS Chemical Biology. 14(7). 1398–1402. 9 indexed citations
12.
Fuglestad, Brian, et al.. (2018). Reverse Micelle Encapsulation of Proteins for NMR Spectroscopy. Methods in enzymology on CD-ROM/Methods in enzymology. 615. 43–75. 16 indexed citations
13.
O’Brien, Evan S., et al.. (2018). Improving yields of deuterated, methyl labeled protein by growing in H2O. Journal of Biomolecular NMR. 71(4). 263–273. 19 indexed citations
14.
Fuglestad, Brian, et al.. (2017). NMR reveals a dynamic allosteric pathway in thrombin. Scientific Reports. 7(1). 39575–39575. 25 indexed citations
15.
Fuglestad, Brian, et al.. (2017). Solution NMR investigation of the response of the lactose repressor core domain dimer to hydrostatic pressure. Biophysical Chemistry. 231. 39–44. 8 indexed citations
16.
O’Brien, Evan S., Nathaniel V. Nucci, Brian Fuglestad, Cecilia Tommos, & A. Joshua Wand. (2015). Defining the Apoptotic Trigger. Journal of Biological Chemistry. 290(52). 30879–30887. 58 indexed citations
17.
Nucci, Nathaniel V., et al.. (2014). Role of cavities and hydration in the pressure unfolding of T4lysozyme. Proceedings of the National Academy of Sciences. 111(38). 13846–13851. 69 indexed citations
18.
Fuglestad, Brian, Paul M. Gasper, J. Andrew McCammon, Phineus R. L. Markwick, & Elizabeth A. Komives. (2013). Correlated Motions and Residual Frustration in Thrombin. The Journal of Physical Chemistry B. 117(42). 12857–12863. 37 indexed citations
19.
Fuglestad, Brian. (2013). Exploring the Dynamics of Thrombin by NMR. eScholarship (California Digital Library). 1 indexed citations
20.
Fuglestad, Brian, Paul M. Gasper, Marco Tonelli, et al.. (2012). The Dynamic Structure of Thrombin in Solution. Biophysical Journal. 103(1). 79–88. 47 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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