Christopher M. Bruns

3.4k total citations · 1 hit paper
16 papers, 2.2k citations indexed

About

Christopher M. Bruns is a scholar working on Molecular Biology, Physiology and Genetics. According to data from OpenAlex, Christopher M. Bruns has authored 16 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 2 papers in Physiology and 2 papers in Genetics. Recurrent topics in Christopher M. Bruns's work include Porphyrin Metabolism and Disorders (4 papers), Genomics, phytochemicals, and oxidative stress (3 papers) and Glutathione Transferases and Polymorphisms (3 papers). Christopher M. Bruns is often cited by papers focused on Porphyrin Metabolism and Disorders (4 papers), Genomics, phytochemicals, and oxidative stress (3 papers) and Glutathione Transferases and Polymorphisms (3 papers). Christopher M. Bruns collaborates with scholars based in United States, Sweden and Argentina. Christopher M. Bruns's co-authors include P. Andrew Karplus, Peter Eastman, Vijay S. Pande, Mike Houston, Mark S. Friedrichs, John A. Tainer, Daniel L. Ensign, Scott LeGrand, Michael R. Shirts and Lee‐Ping Wang and has published in prestigious journals such as Journal of Biological Chemistry, Journal of Molecular Biology and Biochemistry.

In The Last Decade

Christopher M. Bruns

16 papers receiving 2.2k citations

Hit Papers

OpenMM 4: A Reusable, Extensible, Hardware Independent Li... 2012 2026 2016 2021 2012 100 200 300 400 500

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Christopher M. Bruns United States 15 1.4k 453 225 221 201 16 2.2k
Nathalie Reuter Norway 34 2.1k 1.5× 558 1.2× 409 1.8× 230 1.0× 115 0.6× 94 3.3k
Hong Cheng United States 29 1.7k 1.2× 468 1.0× 116 0.5× 206 0.9× 102 0.5× 96 2.5k
Martin Held Switzerland 27 2.2k 1.5× 374 0.8× 223 1.0× 109 0.5× 92 0.5× 63 3.5k
Gerald H. Lushington United States 35 1.4k 1.0× 301 0.7× 329 1.5× 295 1.3× 76 0.4× 163 3.8k
Yasushi Kawata Japan 35 2.2k 1.5× 946 2.1× 327 1.5× 143 0.6× 521 2.6× 205 3.8k
Werner Kremer Germany 28 1.3k 0.9× 489 1.1× 126 0.6× 238 1.1× 112 0.6× 101 2.2k
Karel Berka Czechia 34 2.8k 2.0× 757 1.7× 356 1.6× 114 0.5× 109 0.5× 107 4.6k
Marco De Vivo Italy 35 2.7k 1.9× 710 1.6× 287 1.3× 110 0.5× 106 0.5× 116 4.2k
Felice C. Lightstone United States 32 2.2k 1.5× 500 1.1× 463 2.1× 115 0.5× 82 0.4× 105 3.9k
G.E. Wesenberg United States 19 2.6k 1.8× 648 1.4× 348 1.5× 147 0.7× 84 0.4× 43 3.5k

Countries citing papers authored by Christopher M. Bruns

Since Specialization
Citations

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

Fields of papers citing papers by Christopher M. Bruns

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Christopher M. Bruns. 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 Christopher M. Bruns. The network helps show where Christopher M. Bruns may publish in the future.

Co-authorship network of co-authors of Christopher M. Bruns

This figure shows the co-authorship network connecting the top 25 collaborators of Christopher M. Bruns. A scholar is included among the top collaborators of Christopher M. Bruns 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 Christopher M. Bruns. Christopher M. Bruns is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

16 of 16 papers shown
1.
Haberkern, Hannah, Biafra Ahanonu, David Schauder, et al.. (2019). Visually Guided Behavior and Optogenetically Induced Learning in Head-Fixed Flies Exploring a Virtual Landscape. Current Biology. 29(10). 1647–1659.e8. 39 indexed citations
2.
Weaver, Charlotte A., et al.. (2014). SharkViewer 1.1. Zenodo (CERN European Organization for Nuclear Research). 1 indexed citations
3.
Eastman, Peter, Mark S. Friedrichs, John D. Chodera, et al.. (2012). OpenMM 4: A Reusable, Extensible, Hardware Independent Library for High Performance Molecular Simulation. Journal of Chemical Theory and Computation. 9(1). 461–469. 540 indexed citations breakdown →
4.
Flores, Samuel Coulbourn, Michael Sherman, Christopher M. Bruns, Peter Eastman, & Russ B. Altman. (2010). Fast Flexible Modeling of RNA Structure Using Internal Coordinates. IEEE/ACM Transactions on Computational Biology and Bioinformatics. 8(5). 1247–1257. 51 indexed citations
5.
Friedrichs, Mark S., Peter Eastman, Mike Houston, et al.. (2009). Accelerating molecular dynamic simulation on graphics processing units. Journal of Computational Chemistry. 30(6). 864–872. 424 indexed citations
6.
Garcin, Elsa D., Christopher M. Bruns, S. J. Lloyd, et al.. (2004). Structural Basis for Isozyme-specific Regulation of Electron Transfer in Nitric-oxide Synthase. Journal of Biological Chemistry. 279(36). 37918–37927. 235 indexed citations
7.
Bruns, Christopher M. & Joseph W. Kemnitz. (2004). Sex Hormones, Insulin Sensitivity, and Diabetes Mellitus. ILAR Journal. 45(2). 160–169. 64 indexed citations
8.
Cardoso, Rosa M. F., Douglas S. Daniels, Christopher M. Bruns, & John A. Tainer. (2003). Characterization of the electrophile binding site and substrate binding mode of the 26‐kDa glutathione S‐transferase from Schistosoma japonicum. Proteins Structure Function and Bioinformatics. 51(1). 137–146. 41 indexed citations
9.
Bruns, Christopher M., et al.. (2002). Design of a monomeric human glutathione transferase GSTP1, a structurally stable but catalytically inactive protein. Protein Engineering Design and Selection. 15(10). 827–834. 28 indexed citations
10.
Bruns, Christopher M., Damon S. Anderson, Kevin G. Vaughan, et al.. (2001). Crystallographic and Biochemical Analyses of the Metal-Free Haemophilus influenzae Fe3+-Binding Protein. Biochemistry. 40(51). 15631–15637. 59 indexed citations
11.
Bruns, Christopher M., Ina Hubatsch, Marianne Ridderström, Bengt Mannervik, & John A. Tainer. (1999). Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. Journal of Molecular Biology. 288(3). 427–439. 154 indexed citations
12.
Bruns, Christopher M., Andrew Nowalk, A.S. Arvai, et al.. (1997). Structure of Haemophilus influenzae Fe+3-binding protein reveals convergent evolution within a superfamily. Nature Structural & Molecular Biology. 4(11). 919–924. 140 indexed citations
13.
Bruns, Christopher M. & P. Andrew Karplus. (1995). Refined Crystal Structure of Spinach Ferredoxin Reductase at 1.7 Å Resolution: Oxidized, Reduced and 2′-Phospho-5′-AMP Bound States. Journal of Molecular Biology. 247(1). 125–145. 164 indexed citations
14.
Aliverti, Alessandro, Christopher M. Bruns, V. Pandini, et al.. (1995). Involvement of Serine 96 in the Catalytic Mechanism of Ferredoxin-NADP+ Reductase: Structure-Function Relationship As Studied by Site-Directed Mutagenesis and X-ray Crystallography. Biochemistry. 34(26). 8371–8379. 57 indexed citations
15.
Karplus, P. Andrew & Christopher M. Bruns. (1994). Structure-function relations for ferredoxin reductase. Journal of Bioenergetics and Biomembranes. 26(1). 89–99. 88 indexed citations
16.
Correll, Carl C., Martha Ludwig, Christopher M. Bruns, & P. Andrew Karplus. (1993). Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science. 2(12). 2112–2133. 130 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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