Ronald L. Koder

1.9k total citations
56 papers, 1.5k citations indexed

About

Ronald L. Koder is a scholar working on Molecular Biology, Materials Chemistry and Organic Chemistry. According to data from OpenAlex, Ronald L. Koder has authored 56 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 17 papers in Materials Chemistry and 10 papers in Organic Chemistry. Recurrent topics in Ronald L. Koder's work include Photosynthetic Processes and Mechanisms (15 papers), Protein Structure and Dynamics (14 papers) and Porphyrin and Phthalocyanine Chemistry (7 papers). Ronald L. Koder is often cited by papers focused on Photosynthetic Processes and Mechanisms (15 papers), Protein Structure and Dynamics (14 papers) and Porphyrin and Phthalocyanine Chemistry (7 papers). Ronald L. Koder collaborates with scholars based in United States, Romania and Israel. Ronald L. Koder's co-authors include Anne‐Frances Miller, Vikas Nanda, P. Leslie Dutton, Chad Haynes, David W. Rodgers, J. L. Ross Anderson, Christopher C. Moser, Konda S. Reddy, Lee A. Solomon and José F. Cerda and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Ronald L. Koder

55 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ronald L. Koder United States 19 907 368 202 189 166 56 1.5k
Marco Klähn Singapore 21 758 0.8× 290 0.8× 266 1.3× 167 0.9× 211 1.3× 30 1.7k
Scott A. White United Kingdom 29 1.5k 1.7× 606 1.6× 222 1.1× 86 0.5× 157 0.9× 81 2.5k
Jaroslava Mikšovská United States 21 729 0.8× 280 0.8× 141 0.7× 60 0.3× 187 1.1× 80 1.3k
Michael R. DeFelippis United States 23 811 0.9× 259 0.7× 208 1.0× 71 0.4× 102 0.6× 30 1.4k
Marián Antalı́k Slovakia 21 1.0k 1.1× 306 0.8× 167 0.8× 199 1.1× 153 0.9× 102 1.7k
Pierre Labbé France 31 1.4k 1.6× 345 0.9× 215 1.1× 573 3.0× 222 1.3× 89 2.5k
Serge Pin France 21 418 0.5× 300 0.8× 119 0.6× 91 0.5× 200 1.2× 55 1.3k
Kunihiko Tajima Japan 22 620 0.7× 518 1.4× 333 1.6× 157 0.8× 93 0.6× 112 1.6k
Lianzhi Li China 26 816 0.9× 479 1.3× 458 2.3× 199 1.1× 127 0.8× 140 1.9k
Antonio Donaire Spain 24 772 0.9× 398 1.1× 349 1.7× 110 0.6× 102 0.6× 62 1.6k

Countries citing papers authored by Ronald L. Koder

Since Specialization
Citations

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

Fields of papers citing papers by Ronald L. Koder

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald L. Koder. 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 Ronald L. Koder. The network helps show where Ronald L. Koder may publish in the future.

Co-authorship network of co-authors of Ronald L. Koder

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald L. Koder. A scholar is included among the top collaborators of Ronald L. Koder 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 Ronald L. Koder. Ronald L. Koder 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.
Koder, Ronald L., et al.. (2024). Elastin recoil is driven by the hydrophobic effect. Proceedings of the National Academy of Sciences. 121(11). e2304009121–e2304009121. 7 indexed citations
2.
Miller, Michelle, Joshua T. Atkinson, J. Dongun Kim, et al.. (2023). The energetics and evolution of oxidoreductases in deep time. Proteins Structure Function and Bioinformatics. 92(1). 52–59. 7 indexed citations
3.
Wang, Hsin, et al.. (2022). Oxidation-reduction and photophysical properties of isomeric forms of Safranin. PLoS ONE. 17(6). e0265105–e0265105. 2 indexed citations
4.
Sabo, T. Michael, et al.. (2021). Dynamics in natural and designed elastins and their relation to elastic fiber structure and recoil. Biophysical Journal. 120(20). 4623–4634. 4 indexed citations
5.
Dean, William L., et al.. (2018). Order, Disorder, and Temperature-Driven Compaction in a Designed Elastin Protein. The Journal of Physical Chemistry B. 122(10). 2725–2736. 13 indexed citations
6.
Gunner, M. R. & Ronald L. Koder. (2017). The design features cells use to build their transmembrane proton gradient. Physical Biology. 14(1). 13001–13001. 5 indexed citations
7.
Koder, Ronald L., et al.. (2015). Fast, cheap and out of control — Insights into thermodynamic and informatic constraints on natural protein sequences from de novo protein design. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857(5). 485–492. 8 indexed citations
8.
Nanda, Vikas, et al.. (2013). Hemoprotein Design using Minimal Sequence Information. Biophysical Journal. 104(2). 661a–661a. 1 indexed citations
9.
Koder, Ronald L., et al.. (2013). An Artificial Safranine Enzyme which Activates Chemotherapeutic Prodrugs. Biophysical Journal. 104(2). 205a–205a. 1 indexed citations
10.
Norman, Jessica, et al.. (2013). Rational design of a zinc phthalocyanine binding protein. Journal of Structural Biology. 185(2). 178–185. 11 indexed citations
11.
Punnoose, Alexander, et al.. (2012). Fundamental Limits on Wavelength, Efficiency and Yield of the Charge Separation Triad. PLoS ONE. 7(6). e36065–e36065. 19 indexed citations
12.
Koder, Ronald L., J. L. Ross Anderson, Lee A. Solomon, et al.. (2009). Design and engineering of an O2 transport protein. Nature. 458(7236). 305–309. 188 indexed citations
13.
Nanda, Vikas & Ronald L. Koder. (2009). Designing artificial enzymes by intuition and computation. Nature Chemistry. 2(1). 15–24. 223 indexed citations
14.
Negron, Christopher, Christian Fufezan, & Ronald L. Koder. (2008). Geometric constraints for porphyrin binding in helical protein binding sites. Proteins Structure Function and Bioinformatics. 74(2). 400–416. 18 indexed citations
15.
Koder, Ronald L., Bruce R. Lichtenstein, José F. Cerda, Anne‐Frances Miller, & P. Leslie Dutton. (2007). A flavin analogue with improved solubility in organic solvents. Tetrahedron Letters. 48(31). 5517–5520. 11 indexed citations
16.
Koder, Ronald L. & P. Leslie Dutton. (2006). Intelligent design: the de novo engineering of proteins with specified functions. Dalton Transactions. 3045–3045. 52 indexed citations
17.
Haynes, Chad, Ronald L. Koder, Anne‐Frances Miller, & David W. Rodgers. (2002). Structures of Nitroreductase in Three States. Journal of Biological Chemistry. 277(13). 11513–11520. 137 indexed citations
18.
Koder, Ronald L. & Anne‐Frances Miller. (1998). Steady-state kinetic mechanism, stereospecificity, substrate and inhibitor specificity of Enterobacter cloacae nitroreductase. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1387(1-2). 395–405. 125 indexed citations
19.
Koder, Ronald L. & Anne‐Frances Miller. (1998). Overexpression, Isotopic Labeling, and Spectral Characterization ofEnterobacter cloacaeNitroreductase. Protein Expression and Purification. 13(1). 53–60. 19 indexed citations
20.
Beecher, Brian S., Ronald L. Koder, & Peter A. Tipton. (1994). Tartrate Dehydrogenase-Oxalate Complexes: Formation of a Stable Analog of a Reaction Intermediate Complex. Archives of Biochemistry and Biophysics. 315(2). 255–261. 2 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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