Kendra K. Frederick

2.1k total citations · 1 hit paper
32 papers, 1.7k citations indexed

About

Kendra K. Frederick is a scholar working on Molecular Biology, Spectroscopy and Materials Chemistry. According to data from OpenAlex, Kendra K. Frederick has authored 32 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 14 papers in Spectroscopy and 12 papers in Materials Chemistry. Recurrent topics in Kendra K. Frederick's work include Advanced NMR Techniques and Applications (13 papers), Protein Structure and Dynamics (12 papers) and Enzyme Structure and Function (10 papers). Kendra K. Frederick is often cited by papers focused on Advanced NMR Techniques and Applications (13 papers), Protein Structure and Dynamics (12 papers) and Enzyme Structure and Function (10 papers). Kendra K. Frederick collaborates with scholars based in United States, Sweden and Australia. Kendra K. Frederick's co-authors include A. Joshua Wand, Michael S. Marlow, Kathleen G. Valentine, Tatyana I. Igumenova, Jakob Dogan, Susan Lindquist, Robert G. Griffin, Yiling Xiao, Vladimir K. Michaelis and Bruce A. Palfey and has published in prestigious journals such as Nature, Cell and Chemical Reviews.

In The Last Decade

Kendra K. Frederick

30 papers receiving 1.7k citations

Hit Papers

Conformational entropy in molecular recognition by proteins 2007 2026 2013 2019 2007 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
Kendra K. Frederick United States 16 1.2k 567 555 198 139 32 1.7k
Ashok Sekhar Canada 24 1.5k 1.2× 503 0.9× 518 0.9× 147 0.7× 124 0.9× 53 2.0k
Kathleen G. Valentine United States 29 1.8k 1.5× 619 1.1× 633 1.1× 265 1.3× 237 1.7× 57 2.5k
Beat Vögeli United States 26 1.7k 1.4× 665 1.2× 865 1.6× 175 0.9× 113 0.8× 100 2.1k
Paul Robustelli United States 17 2.3k 1.9× 1.0k 1.8× 634 1.1× 305 1.5× 143 1.0× 28 2.8k
Sang‐Choul Im United States 25 1.1k 0.9× 274 0.5× 562 1.0× 65 0.3× 117 0.8× 75 2.0k
Charalampos G. Kalodimos United States 17 2.1k 1.7× 588 1.0× 353 0.6× 123 0.6× 242 1.7× 28 2.4k
Vu Thai United States 7 2.0k 1.6× 866 1.5× 361 0.7× 275 1.4× 306 2.2× 8 2.2k
William E. Meador United States 14 1.9k 1.5× 821 1.4× 332 0.6× 150 0.8× 282 2.0× 29 2.6k
Alvar D. Gossert Switzerland 21 985 0.8× 330 0.6× 426 0.8× 83 0.4× 53 0.4× 50 1.5k
Tatyana I. Igumenova United States 17 761 0.6× 354 0.6× 539 1.0× 86 0.4× 131 0.9× 49 1.2k

Countries citing papers authored by Kendra K. Frederick

Since Specialization
Citations

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

Fields of papers citing papers by Kendra K. Frederick

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kendra K. Frederick. 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 Kendra K. Frederick. The network helps show where Kendra K. Frederick may publish in the future.

Co-authorship network of co-authors of Kendra K. Frederick

This figure shows the co-authorship network connecting the top 25 collaborators of Kendra K. Frederick. A scholar is included among the top collaborators of Kendra K. Frederick 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 Kendra K. Frederick. Kendra K. Frederick 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.
Kragelj, Jaka, et al.. (2025). Spatially resolved DNP-assisted NMR illuminates the conformational ensemble of α-synuclein in intact viable cells. Proceedings of the National Academy of Sciences. 122(23). e2500367122–e2500367122.
2.
Kragelj, Jaka, et al.. (2025). Structural Context Modulates the Conformational Ensemble of the Intrinsically Disordered Amino Terminus of α-Synuclein. Journal of the American Chemical Society. 147(14). 11800–11810.
3.
Xiao, Yiling, et al.. (2025). Stability of the polarization agent AsymPolPOK in intact and lysed mammalian cells. Journal of Magnetic Resonance. 374. 107864–107864. 1 indexed citations
4.
Xiao, Yiling, et al.. (2024). DNP-assisted solid-state NMR enables detection of proteins at nanomolar concentrations in fully protonated cellular milieu. Journal of Biomolecular NMR. 78(2). 95–108. 9 indexed citations
5.
Kragelj, Jaka, et al.. (2023). Conformational ensembles explain NMR spectra of frozen intrinsically disordered proteins. Protein Science. 32(5). e4628–e4628. 6 indexed citations
6.
Xiao, Yiling, et al.. (2022). Stability of the nitroxide biradical AMUPol in intact and lysed mammalian cells. Journal of Magnetic Resonance. 336. 107150–107150. 9 indexed citations
7.
Xiao, Yiling, et al.. (2022). In-Cell NMR of Intact Mammalian Cells Preserved with the Cryoprotectants DMSO and Glycerol Have Similar DNP Performance. Frontiers in Molecular Biosciences. 8. 789478–789478. 12 indexed citations
8.
Xiao, Yiling, et al.. (2021). In-Cell Sensitivity-Enhanced NMR of Intact Viable Mammalian Cells. Journal of the American Chemical Society. 143(44). 18454–18466. 46 indexed citations
9.
Kragelj, Jaka, et al.. (2020). Cryogenic Sample Loading into a Magic Angle Spinning Nuclear Magnetic Resonance Spectrometer that Preserves Cellular Viability. Journal of Visualized Experiments. 13 indexed citations
10.
Frederick, Kendra K.. (2019). Sensitivity-Enhanced Dnp NMR for In Situ Structural Biology. Biophysical Journal. 116(3). 203a–203a. 2 indexed citations
11.
Xiao, Yiling, et al.. (2018). DNP-Assisted NMR Investigation of Proteins at Endogenous Levels in Cellular Milieu. Methods in enzymology on CD-ROM/Methods in enzymology. 615. 373–406. 15 indexed citations
12.
Silvers, Robert, Michael T. Colvin, Kendra K. Frederick, et al.. (2017). Aggregation and Fibril Structure of AβM01–42 and Aβ1–42. Biochemistry. 56(36). 4850–4859. 22 indexed citations
13.
Frederick, Kendra K., Vladimir K. Michaelis, Marc A. Caporini, et al.. (2017). Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register. Proceedings of the National Academy of Sciences. 114(14). 3642–3647. 57 indexed citations
14.
Frederick, Kendra K., Vladimir K. Michaelis, Björn Corzilius, et al.. (2015). Sensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
15.
Frederick, Kendra K., Vladimir K. Michaelis, Björn Corzilius, et al.. (2015). Sensitivity-Enhanced NMR Reveals Alterations in Protein Structure by Cellular Milieus. Cell. 163(3). 620–628. 127 indexed citations
16.
Frederick, Kendra K., et al.. (2014). Distinct Prion Strains Are Defined by Amyloid Core Structure and Chaperone Binding Site Dynamics. Chemistry & Biology. 21(2). 295–305. 65 indexed citations
17.
Marlow, Michael S., Jakob Dogan, Kendra K. Frederick, Kathleen G. Valentine, & A. Joshua Wand. (2010). The role of conformational entropy in molecular recognition by calmodulin. Nature Chemical Biology. 6(5). 352–358. 216 indexed citations
18.
Frederick, Kendra K., Michael S. Marlow, Kathleen G. Valentine, & A. Joshua Wand. (2007). Conformational entropy in molecular recognition by proteins. Nature. 448(7151). 325–329. 550 indexed citations breakdown →
19.
Palfey, Bruce A., Rajit K. Basu, Kendra K. Frederick, Barrie Entsch, & David P. Ballou. (2002). Role of Protein Flexibility in the Catalytic Cycle of p-Hydroxybenzoate Hydroxylase Elucidated by the Pro293Ser Mutant. Biochemistry. 41(26). 8438–8446. 34 indexed citations
20.
Frederick, Kendra K., David P. Ballou, & Bruce A. Palfey. (2001). Protein Dynamics Control Proton Transfers to the Substrate on the His72Asn Mutant of p-Hydroxybenzoate Hydroxylase. Biochemistry. 40(13). 3891–3899. 20 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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