Catherine D. Eichhorn

706 total citations
18 papers, 519 citations indexed

About

Catherine D. Eichhorn is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Catherine D. Eichhorn has authored 18 papers receiving a total of 519 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 3 papers in Genetics and 2 papers in Materials Chemistry. Recurrent topics in Catherine D. Eichhorn's work include RNA and protein synthesis mechanisms (15 papers), RNA modifications and cancer (14 papers) and RNA Research and Splicing (11 papers). Catherine D. Eichhorn is often cited by papers focused on RNA and protein synthesis mechanisms (15 papers), RNA modifications and cancer (14 papers) and RNA Research and Splicing (11 papers). Catherine D. Eichhorn collaborates with scholars based in United States, Taiwan and Canada. Catherine D. Eichhorn's co-authors include Juli Feigon, Hashim M. Al‐Hashimi, Mijeong Kang, Alexandar L. Hansen, Jameson R. Bothe, Evgenia N. Nikolova, Yuan Yang, Jeetender Chugh, Krishna C. Suddala and Jun Feng and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Molecular Cell.

In The Last Decade

Catherine D. Eichhorn

17 papers receiving 517 citations

Peers

Catherine D. Eichhorn

GENET

SPECT

Martin Hengesbach Germany

Isabelle Lebars France

Kristina Döring Germany

T. Tomizawa Japan

F. Voigts-Hoffmann Switzerland

Louis-Philippe Bergeron-Sandoval Canada

Lenka Skříšovská Switzerland

Petro Yakovchuk United States

Zainab Ahdash United Kingdom

Yusuke Sako Japan

Martin Hengesbach Germany

Catherine D. Eichhorn

686 ×1.4

48 ×0.7

GENET

30 ×0.9

SPECT

21 ×0.8

21 ×1.1

Citations per year, relative to Catherine D. Eichhorn Catherine D. Eichhorn (= 1×) peers Martin Hengesbach

Countries citing papers authored by Catherine D. Eichhorn

Since Specialization

Citations

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

Fields of papers citing papers by Catherine D. Eichhorn

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Catherine D. Eichhorn. 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 Catherine D. Eichhorn. The network helps show where Catherine D. Eichhorn may publish in the future.

Co-authorship network of co-authors of Catherine D. Eichhorn

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

All Works

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18 of 18 papers shown

Naldrett, Michael J., et al.. (2025). Rapid Microwave Fixation of the Brain Reveals Seasonal Changes in the Phosphoproteome of Hibernating Thirteen-Lined Ground Squirrels. ACS Chemical Neuroscience. 16(3). 428–438.

Eichhorn, Catherine D., et al.. (2025). An evolutionarily conserved tryptophan cage promotes folding of the extended RNA recognition motif in the hnRNPR ‐like protein family. Protein Science. 34(5). e70127–e70127. 1 indexed citations

Yesselman, Joseph D., et al.. (2023). Visualizing a two-state conformational ensemble in stem–loop 3 of the transcriptional regulator 7SK RNA. Nucleic Acids Research. 52(2). 940–952. 7 indexed citations

Wang, Yaqiang, Yao He, Yanjiao Wang, et al.. (2023). Structure of LARP7 Protein p65–telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR. Journal of Molecular Biology. 435(11). 168044–168044. 5 indexed citations

Eichhorn, Catherine D., et al.. (2023). Progress in 7SK ribonucleoprotein structural biology. Frontiers in Molecular Biosciences. 10. 1154622–1154622. 4 indexed citations

Miller, Amanda L., et al.. (2023). Identification and Biosynthetic Study of the Siderophore Lysochelin in the Biocontrol Agent Lysobacter enzymogenes. Journal of Agricultural and Food Chemistry. 71(19). 7418–7426. 9 indexed citations

Yang, Yuan, Shiheng Liu, Sylvain Egloff, et al.. (2022). Structural basis of RNA conformational switching in the transcriptional regulator 7SK RNP. Molecular Cell. 82(9). 1724–1736.e7. 28 indexed citations

Eichhorn, Catherine D., et al.. (2022). C-terminal determinants for RNA binding motif 7 protein stability and RNA recognition. Biophysical Chemistry. 292. 106928–106928. 1 indexed citations

Basu, Ritwika, Catherine D. Eichhorn, Ryan R. Cheng, Robert D. Peterson, & Juli Feigon. (2020). Structure of S. pombe telomerase protein Pof8 C-terminal domain is an xRRM conserved among LARP7 proteins. RNA Biology. 18(8). 1181–1192. 11 indexed citations

10.

Eichhorn, Catherine D., et al.. (2018). Structural basis for recognition of human 7SK long noncoding RNA by the La-related protein Larp7. Proceedings of the National Academy of Sciences. 115(28). E6457–E6466. 47 indexed citations

11.

Yang, Yuan, Catherine D. Eichhorn, Yaqiang Wang, Duilio Cascio, & Juli Feigon. (2018). Structural basis of 7SK RNA 5′-γ-phosphate methylation and retention by MePCE. Nature Chemical Biology. 15(2). 132–140. 26 indexed citations

12.

Eichhorn, Catherine D., et al.. (2016). hLARP7 C-terminal domain contains an xRRM that binds the 3′ hairpin of 7SK RNA. Nucleic Acids Research. 44(20). gkw833–gkw833. 32 indexed citations

13.

Eichhorn, Catherine D., Mijeong Kang, & Juli Feigon. (2014). Structure and function of preQ1 riboswitches. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. 1839(10). 939–950. 38 indexed citations

14.

Eichhorn, Catherine D. & Hashim M. Al‐Hashimi. (2014). Structural dynamics of a single-stranded RNA–helix junction using NMR. RNA. 20(6). 782–791. 15 indexed citations

15.

Kang, Mijeong, Catherine D. Eichhorn, & Juli Feigon. (2014). Structural determinants for ligand capture by a class II preQ ₁ riboswitch. Proceedings of the National Academy of Sciences. 111(6). E663–71. 48 indexed citations

16.

Suddala, Krishna C., Jun Feng, Anthony M. Mustoe, et al.. (2013). Single transcriptional and translational preQ1 riboswitches adopt similar pre-folded ensembles that follow distinct folding pathways into the same ligand-bound structure. Nucleic Acids Research. 41(22). 10462–10475. 72 indexed citations

17.

Eichhorn, Catherine D., Jun Feng, Krishna C. Suddala, et al.. (2011). Unraveling the structural complexity in a single-stranded RNA tail: implications for efficient ligand binding in the prequeuosine riboswitch. Nucleic Acids Research. 40(3). 1345–1355. 50 indexed citations

18.

Bothe, Jameson R., Evgenia N. Nikolova, Catherine D. Eichhorn, et al.. (2011). Characterizing RNA dynamics at atomic resolution using solution-state NMR spectroscopy. Nature Methods. 8(11). 919–931. 125 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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