David F. Savage

7.0k total citations
66 papers, 4.4k citations indexed

About

David F. Savage is a scholar working on Molecular Biology, Ecology and Renewable Energy, Sustainability and the Environment. According to data from OpenAlex, David F. Savage has authored 66 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 13 papers in Ecology and 12 papers in Renewable Energy, Sustainability and the Environment. Recurrent topics in David F. Savage's work include Photosynthetic Processes and Mechanisms (18 papers), RNA and protein synthesis mechanisms (15 papers) and CRISPR and Genetic Engineering (14 papers). David F. Savage is often cited by papers focused on Photosynthetic Processes and Mechanisms (18 papers), RNA and protein synthesis mechanisms (15 papers) and CRISPR and Genetic Engineering (14 papers). David F. Savage collaborates with scholars based in United States, Australia and Israel. David F. Savage's co-authors include Pamela A. Silver, Avi I. Flamholz, Bruno Afonso, R. M. Stroud, Robert M. Stroud, Luke M. Oltrogge, Pascal F. Egea, Joseph D. O’Connell, Benjamin L. Oakes and Rachel D. Hood and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

David F. Savage

65 papers receiving 4.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David F. Savage United States 38 3.7k 688 582 549 433 66 4.4k
Jonathan J. Silberg United States 31 2.6k 0.7× 731 1.1× 281 0.5× 557 1.0× 272 0.6× 77 4.0k
Markus Sutter United States 31 2.7k 0.7× 686 1.0× 728 1.3× 385 0.7× 133 0.3× 61 3.1k
Leonid A. Sazanov United Kingdom 43 6.4k 1.7× 890 1.3× 319 0.5× 344 0.6× 190 0.4× 72 7.8k
Sabine Heinhorst United States 30 2.8k 0.8× 583 0.8× 797 1.4× 286 0.5× 240 0.6× 61 3.5k
Lu‐Ning Liu United Kingdom 40 2.7k 0.7× 1.2k 1.7× 448 0.8× 150 0.3× 149 0.3× 111 3.7k
Bernadette Byrne United Kingdom 35 3.6k 1.0× 443 0.6× 134 0.2× 320 0.6× 257 0.6× 134 5.3k
Frank T. Robb United States 44 3.6k 1.0× 324 0.5× 1.2k 2.0× 562 1.0× 460 1.1× 161 5.4k
Gordon C. Cannon United States 31 3.0k 0.8× 616 0.9× 901 1.5× 313 0.6× 232 0.5× 67 3.7k
Francis E. Jenney United States 34 1.9k 0.5× 808 1.2× 320 0.5× 156 0.3× 278 0.6× 70 3.4k
James W. Murray United Kingdom 30 1.9k 0.5× 432 0.6× 193 0.3× 274 0.5× 213 0.5× 71 3.0k

Countries citing papers authored by David F. Savage

Since Specialization
Citations

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

Fields of papers citing papers by David F. Savage

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David F. Savage. 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 David F. Savage. The network helps show where David F. Savage may publish in the future.

Co-authorship network of co-authors of David F. Savage

This figure shows the co-authorship network connecting the top 25 collaborators of David F. Savage. A scholar is included among the top collaborators of David F. Savage 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 David F. Savage. David F. Savage 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.
Ngo, Wayne, et al.. (2026). Targeted delivery of genome editors in vivo. Nature Biotechnology. 44(1). 49–59.
2.
Prywes, Noam, Luke M. Oltrogge, Benoit de Pins, et al.. (2024). Mapping the kinetic landscape of rubisco. Biophysical Journal. 123(3). 19a–19a. 1 indexed citations
3.
Oltrogge, Luke M., et al.. (2024). Conserved and repetitive motifs in an intrinsically disordered protein drive ⍺-carboxysome assembly. Journal of Biological Chemistry. 300(8). 107532–107532. 8 indexed citations
4.
Blikstad, Cecilia, Eli Dugan, Thomas G. Laughlin, et al.. (2023). Identification of a carbonic anhydrase–Rubisco complex within the alpha-carboxysome. Proceedings of the National Academy of Sciences. 120(43). e2308600120–e2308600120. 28 indexed citations
5.
Nichols, Robert J., Avi I. Flamholz, Juliana Artier, et al.. (2023). Carbon isotope fractionation by an ancestral rubisco suggests that biological proxies for CO 2 through geologic time should be reevaluated. Proceedings of the National Academy of Sciences. 120(20). e2300466120–e2300466120. 9 indexed citations
6.
Flamholz, Avi I., Eli Dugan, John J. Desmarais, et al.. (2022). Trajectories for the evolution of bacterial CO 2 -concentrating mechanisms. Proceedings of the National Academy of Sciences. 119(49). e2210539119–e2210539119. 23 indexed citations
7.
Metskas, Lauren Ann, Davi R. Ortega, Luke M. Oltrogge, et al.. (2022). Rubisco forms a lattice inside alpha-carboxysomes. Nature Communications. 13(1). 4863–4863. 43 indexed citations
8.
Carpenter, William Benjamin, et al.. (2022). Ratiometric Sensing of Redox Environments Inside Individual Carboxysomes Trapped in Solution. The Journal of Physical Chemistry Letters. 13(20). 4455–4462. 7 indexed citations
9.
Carpenter, William Benjamin, et al.. (2022). Exploring Masses and Internal Mass Distributions of Single Carboxysomes in Free Solution Using Fluorescence and Interferometric Scattering in an Anti-Brownian Trap. The Journal of Physical Chemistry B. 126(43). 8747–8759. 5 indexed citations
10.
Al-Shayeb, Basem, Petr Skopintsev, Katarzyna M. Soczek, et al.. (2022). Diverse virus-encoded CRISPR-Cas systems include streamlined genome editors. Cell. 185(24). 4574–4586.e16. 93 indexed citations
11.
Nichols, Robert J., Benjamin LaFrance, Devon Radford, et al.. (2021). Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism. eLife. 10. 55 indexed citations
12.
Desmarais, John J., Avi I. Flamholz, Cecilia Blikstad, et al.. (2019). DABs are inorganic carbon pumps found throughout prokaryotic phyla. Nature Microbiology. 4(12). 2204–2215. 48 indexed citations
13.
Lucas, James E., Kyle E. Watters, Christof Fellmann, et al.. (2019). Controlling CRISPR-Cas9 with ligand-activated and ligand-deactivated sgRNAs. Nature Communications. 10(1). 2127–2127. 147 indexed citations
14.
Nadler, Dana C., et al.. (2016). Rapid construction of metabolite biosensors using domain-insertion profiling. Nature Communications. 7(1). 12266–12266. 91 indexed citations
15.
Oakes, Benjamin L., Dana C. Nadler, Avi I. Flamholz, et al.. (2016). Profiling of engineering hotspots identifies an allosteric CRISPR-Cas9 switch. Nature Biotechnology. 34(6). 646–651. 160 indexed citations
16.
Oakes, Benjamin L., Dana C. Nadler, & David F. Savage. (2014). Protein Engineering of Cas9 for Enhanced Function. Methods in enzymology on CD-ROM/Methods in enzymology. 546. 491–511. 18 indexed citations
17.
Savage, David F., Joseph D. O’Connell, Larry J. W. Miercke, Janet Finer-Moore, & Robert M. Stroud. (2010). Structural context shapes the aquaporin selectivity filter. Proceedings of the National Academy of Sciences. 107(40). 17164–17169. 67 indexed citations
18.
Niederholtmeyer, Henrike, Bernd T. Wolfstädter, David F. Savage, Pamela A. Silver, & Jeffrey C. Way. (2010). Engineering Cyanobacteria To Synthesize and Export Hydrophilic Products. Applied and Environmental Microbiology. 76(11). 3462–3466. 177 indexed citations
19.
Savage, David F.. (2007). Towards Membrane Protein Structure Determination. eScholarship (California Digital Library). 1 indexed citations
20.
Keatinge‐Clay, Adrian T., Anang A. Shelat, David F. Savage, et al.. (2003). Catalysis, Specificity, and ACP Docking Site of Streptomyces coelicolor Malonyl-CoA:ACP Transacylase. Structure. 11(2). 147–154. 109 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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