Bruce E. Bowler

3.0k total citations
95 papers, 2.4k citations indexed

About

Bruce E. Bowler is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Bruce E. Bowler has authored 95 papers receiving a total of 2.4k indexed citations (citations by other indexed papers that have themselves been cited), including 83 papers in Molecular Biology, 29 papers in Materials Chemistry and 20 papers in Cell Biology. Recurrent topics in Bruce E. Bowler's work include Photosynthetic Processes and Mechanisms (54 papers), Protein Structure and Dynamics (50 papers) and Enzyme Structure and Function (20 papers). Bruce E. Bowler is often cited by papers focused on Photosynthetic Processes and Mechanisms (54 papers), Protein Structure and Dynamics (50 papers) and Enzyme Structure and Function (20 papers). Bruce E. Bowler collaborates with scholars based in United States, Russia and India. Bruce E. Bowler's co-authors include Barbara Hammack, Stephen J. Lippard, Harry B. Gray, Swati Bandi, Aichun Dong, David A. Williamson, José N. Onuchic, David N. Beratan, Tung‐Chung Mou and Gareth R. Eaton and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Molecular Biology.

In The Last Decade

Bruce E. Bowler

93 papers receiving 2.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Bruce E. Bowler United States 30 1.9k 612 465 340 246 95 2.4k
T. Takano Japan 7 1.9k 1.0× 375 0.6× 691 1.5× 296 0.9× 309 1.3× 12 2.5k
Kathleen G. Valentine United States 29 1.8k 1.0× 619 1.0× 237 0.5× 265 0.8× 249 1.0× 57 2.5k
Marvin W. Makinen United States 27 1.1k 0.6× 532 0.9× 518 1.1× 163 0.5× 153 0.6× 80 2.2k
M. R. Ondrias United States 26 1.4k 0.7× 686 1.1× 1.3k 2.7× 396 1.2× 107 0.4× 104 2.4k
Paul D. Barker United Kingdom 28 1.7k 0.9× 427 0.7× 566 1.2× 183 0.5× 137 0.6× 74 2.4k
Thomas C. Strekas United States 21 1.1k 0.6× 625 1.0× 594 1.3× 289 0.8× 573 2.3× 45 2.6k
Peter B. Crowley Ireland 30 2.2k 1.2× 971 1.6× 246 0.5× 206 0.6× 635 2.6× 84 3.1k
Victor Pui‐Yan United States 26 1.1k 0.6× 378 0.6× 477 1.0× 384 1.1× 264 1.1× 39 2.4k
Joël Mispelter France 27 625 0.3× 527 0.9× 243 0.5× 246 0.7× 207 0.8× 101 2.1k
Esther Nachliel Israel 27 1.2k 0.6× 253 0.4× 205 0.4× 618 1.8× 210 0.9× 69 1.9k

Countries citing papers authored by Bruce E. Bowler

Since Specialization
Citations

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

Fields of papers citing papers by Bruce E. Bowler

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Bruce E. Bowler

This figure shows the co-authorship network connecting the top 25 collaborators of Bruce E. Bowler. A scholar is included among the top collaborators of Bruce E. Bowler 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 Bruce E. Bowler. Bruce E. Bowler 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.
Bowler, Bruce E., et al.. (2025). Physical and functional effects of substituting coevolved residues from Ω-loop C of yeast Iso-1-cytochrome c into human cytochrome c. Journal of Inorganic Biochemistry. 274. 113053–113053.
2.
Bowler, Bruce E., et al.. (2024). Binding of yeast and human cytochrome c to cardiolipin nanodiscs at physiological ionic strength. Journal of Inorganic Biochemistry. 260. 112699–112699. 2 indexed citations
3.
Martin, William J., et al.. (2023). Effect of proline content and histidine ligation on the dynamics of Ω-loop D and the peroxidase activity of iso-1-cytochrome c. Journal of Inorganic Biochemistry. 252. 112474–112474.
4.
Bowler, Bruce E., Christopher Davies, Dan Drecktrah, et al.. (2023). c‐di‐GMP regulates activity of the PlzA RNA chaperone from the Lyme disease spirochete. Molecular Microbiology. 119(6). 711–727. 4 indexed citations
5.
Bowler, Bruce E., et al.. (2018). Rapid quantification of vesicle concentration for DOPG/DOPC and Cardiolipin/DOPC mixed lipid systems of variable composition. Analytical Biochemistry. 553. 12–14. 7 indexed citations
6.
Bowler, Bruce E., et al.. (2018). Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c′. Biophysical Journal. 114(2). 311–322. 1 indexed citations
7.
Bowler, Bruce E., et al.. (2016). Rapid quantification of cardiolipin and DOPC lipid and vesicle concentration. Analytical Biochemistry. 520. 58–61. 8 indexed citations
8.
Mou, Tung‐Chung, et al.. (2015). Disruption of a hydrogen bond network in human versus spider monkey cytochrome c affects heme crevice stability. Journal of Inorganic Biochemistry. 158. 62–69. 24 indexed citations
9.
Khan, Md. Khurshid Alam & Bruce E. Bowler. (2012). Conformational Properties of Polyglutamine Sequences in Guanidine Hydrochloride Solutions. Biophysical Journal. 103(9). 1989–1999. 2 indexed citations
10.
Bowler, Bruce E., et al.. (2009). Thermodynamics of Loop Formation in the Denatured State of Rhodopseudomonas palustris Cytochrome c′: Scaling Exponents and the Reconciliation Problem. Journal of Molecular Biology. 392(5). 1315–1325. 12 indexed citations
11.
Bowler, Bruce E., et al.. (2009). Importance of Contact Persistence in Denatured State Loop Formation: Kinetic Insights into Sequence Effects on Nucleation Early in Folding. Journal of Molecular Biology. 390(1). 124–134. 7 indexed citations
12.
Bowler, Bruce E., et al.. (2008). Electron-Electron Distances in Spin-Labeled Low-Spin Metmyoglobin Variants by Relaxation Enhancement. Biophysical Journal. 95(11). 5306–5316. 15 indexed citations
13.
Bowler, Bruce E., et al.. (2007). Sequence Composition Effects on Denatured State Loop Formation in Iso-1-cytochrome c Variants: Polyalanine versus Polyglycine Inserts. Journal of Molecular Biology. 371(3). 577–584. 13 indexed citations
14.
Bowler, Bruce E., et al.. (2004). Proton-Mediated Dynamics of the Alkaline Conformational Transition of Yeast Iso-1-Cytochrome c. Journal of the American Chemical Society. 126(21). 6751–6758. 29 indexed citations
15.
Zhang, Miaomiao, et al.. (2004). Estimation of the Compaction of the Denatured State by a Protein Variant Involved in a Reverse Hydrophobic Effect. The Protein Journal. 23(2). 119–126. 1 indexed citations
16.
Bowler, Bruce E., et al.. (2004). Conformational Properties of the Iso-1-Cytochrome c Denatured State: Dependence on Guanidine Hydrochloride Concentration. Journal of Molecular Biology. 339(1). 185–197. 26 indexed citations
17.
Hammack, Barbara, et al.. (2000). Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c 1 1Edited by P. E. Wright. Journal of Molecular Biology. 296(1). 217–228. 51 indexed citations
18.
19.
Bowler, Bruce E., Aichun Dong, & Winslow S. Caughey. (1994). Characterization of the guanidine-hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy. Biochemistry. 33(9). 2402–2408. 31 indexed citations
20.
Bowler, Bruce E., et al.. (1993). Destabilizing effects of replacing a surface lysine of cytochrome c with aromatic amino acids: implications for the denatured state. Biochemistry. 32(1). 183–190. 83 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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