Karen G. Fleming

5.8k total citations
92 papers, 4.4k citations indexed

About

Karen G. Fleming is a scholar working on Molecular Biology, Genetics and Cell Biology. According to data from OpenAlex, Karen G. Fleming has authored 92 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 84 papers in Molecular Biology, 24 papers in Genetics and 11 papers in Cell Biology. Recurrent topics in Karen G. Fleming's work include Lipid Membrane Structure and Behavior (51 papers), Protein Structure and Dynamics (49 papers) and RNA and protein synthesis mechanisms (26 papers). Karen G. Fleming is often cited by papers focused on Lipid Membrane Structure and Behavior (51 papers), Protein Structure and Dynamics (49 papers) and RNA and protein synthesis mechanisms (26 papers). Karen G. Fleming collaborates with scholars based in United States, Canada and South Korea. Karen G. Fleming's co-authors include C. Preston Moon, Donald M. Engelman, Patrick J. Fleming, Ann Marie Stanley, Ashlee M. Plummer, Emily J. Danoff, N. K. Burgess, Nathan R. Zaccai, Thuy P. Dao and Dennis Gessmann and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Karen G. Fleming

87 papers receiving 4.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Karen G. Fleming United States 40 3.7k 902 496 378 363 92 4.4k
Eugene Palovcak United States 10 4.1k 1.1× 675 0.7× 542 1.1× 496 1.3× 499 1.4× 13 5.9k
Alexis Rohou United States 18 3.8k 1.0× 658 0.7× 398 0.8× 453 1.2× 389 1.1× 27 5.4k
Jimin Wang United States 38 4.0k 1.1× 547 0.6× 267 0.5× 461 1.2× 465 1.3× 142 5.0k
Shirley A. Müller Switzerland 43 3.9k 1.0× 1.0k 1.1× 827 1.7× 569 1.5× 270 0.7× 84 5.7k
Kliment A. Verba United States 9 4.3k 1.1× 643 0.7× 593 1.2× 544 1.4× 415 1.1× 19 5.9k
Dari Kimanius United Kingdom 14 4.1k 1.1× 531 0.6× 507 1.0× 562 1.5× 338 0.9× 22 5.8k
Imre Berger United Kingdom 42 4.9k 1.3× 658 0.7× 368 0.7× 211 0.6× 146 0.4× 133 6.0k
Thorsten Mielke Germany 43 5.1k 1.4× 1.2k 1.3× 326 0.7× 301 0.8× 425 1.2× 90 5.7k
Michael C. Wiener United States 33 3.5k 0.9× 823 0.9× 223 0.4× 399 1.1× 197 0.5× 67 4.3k
F. Heitz France 46 6.5k 1.7× 1.1k 1.2× 297 0.6× 340 0.9× 337 0.9× 142 7.5k

Countries citing papers authored by Karen G. Fleming

Since Specialization
Citations

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

Fields of papers citing papers by Karen G. Fleming

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Karen G. Fleming. 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 Karen G. Fleming. The network helps show where Karen G. Fleming may publish in the future.

Co-authorship network of co-authors of Karen G. Fleming

This figure shows the co-authorship network connecting the top 25 collaborators of Karen G. Fleming. A scholar is included among the top collaborators of Karen G. Fleming 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 Karen G. Fleming. Karen G. Fleming 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.
Freindorf, Marek, Karen G. Fleming, & Elfi Kraka. (2025). Iron‐Histidine Coordination in Cytochrome b5: A Local Vibrational Mode Study. ChemPhysChem. 26(7). e202401098–e202401098. 2 indexed citations
2.
Yao, Jiaqi, Michael D. Bridges, Kelly H. Kim, et al.. (2025). The lipid bilayer strengthens the cooperative network of membrane proteins. Science Advances. 11(27). eadv9568–eadv9568.
3.
Fleming, Karen G., et al.. (2024). A team of chaperones play to win in the bacterial periplasm. Trends in Biochemical Sciences. 49(8). 667–680. 3 indexed citations
4.
Chan, Christina K., Sid Feldman, Andrew E. Simor, et al.. (2023). Integration of hospital with congregate care homes in response to the COVID-19 pandemic. Canada Communicable Disease Report. 49(2/3). 67–75. 4 indexed citations
5.
Marx, Dagan C., et al.. (2023). FkpA enhances membrane protein folding using an extensive interaction surface. Protein Science. 32(4). e4592–e4592. 6 indexed citations
6.
Vorobieva, Anastassia A., Paul White, Binyong Liang, et al.. (2021). De novo design of transmembrane β barrels. Science. 371(6531). 86 indexed citations
7.
Marx, Dagan C., Ashlee M. Plummer, Anneliese M. Faustino, et al.. (2020). SurA is a cryptically grooved chaperone that expands unfolded outer membrane proteins. Proceedings of the National Academy of Sciences. 117(45). 28026–28035. 29 indexed citations
8.
Mo, Gary, Brian Ross, Fabian Hertel, et al.. (2017). Genetically encoded biosensors for visualizing live-cell biochemical activity at super-resolution. Nature Methods. 14(4). 427–434. 139 indexed citations
9.
Marx, Dagan C. & Karen G. Fleming. (2017). Influence of Protein Scaffold on Side-Chain Transfer Free Energies. Biophysical Journal. 113(3). 597–604. 21 indexed citations
10.
Fleming, Patrick J., Dhilon S. Patel, Emilia L. Wu, et al.. (2016). BamA POTRA Domain Interacts with a Native Lipid Membrane Surface. Biophysical Journal. 110(12). 2698–2709. 57 indexed citations
11.
Zaccai, Nathan R., J. Todd Hoopes, Joseph E. Curtis, et al.. (2015). Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins. Methods in enzymology on CD-ROM/Methods in enzymology. 159–210. 39 indexed citations
12.
Gessmann, Dennis, Yong Hee Chung, Emily J. Danoff, et al.. (2014). Outer membrane β-barrel protein folding is physically controlled by periplasmic lipid head groups and BamA. Proceedings of the National Academy of Sciences. 111(16). 5878–5883. 155 indexed citations
13.
Moon, C. Preston, Nathan R. Zaccai, Patrick J. Fleming, Dennis Gessmann, & Karen G. Fleming. (2013). Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm. Proceedings of the National Academy of Sciences. 110(11). 4285–4290. 94 indexed citations
14.
O’Neill, Maura, et al.. (2012). Induced fit on heme binding to the Pseudomonas aeruginosa cytoplasmic protein (PhuS) drives interaction with heme oxygenase (HemO). Proceedings of the National Academy of Sciences. 109(15). 5639–5644. 43 indexed citations
15.
16.
Burgess, N. K. & Karen G. Fleming. (2009). Beta-barrel Proteins that Reside in the E. coli Outer Membrane In Vivo Demonstrate Varied Folding Behavior In Vitro. Biophysical Journal. 96(3). 79a–79a. 3 indexed citations
17.
Stanley, Ann Marie, Pitak Chuawong, Tamara L. Hendrickson, & Karen G. Fleming. (2006). Energetics of Outer Membrane Phospholipase A (OMPLA) Dimerization. Journal of Molecular Biology. 358(1). 120–131. 25 indexed citations
18.
Fleming, Karen G., et al.. (2006). Dimerization of the Erythropoietin Receptor Transmembrane Domain in Micelles. Journal of Molecular Biology. 366(2). 517–524. 40 indexed citations
19.
Fleming, Karen G., et al.. (2004). Thermodynamics of glycophorin A transmembrane helix dimerization in C14 betaine micelles. Biophysical Chemistry. 108(1-3). 43–49. 42 indexed citations
20.
Fleming, Karen G.. (2002). Standardizing the Free Energy Change of Transmembrane Helix–Helix Interactions. Journal of Molecular Biology. 323(3). 563–571. 114 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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