Judith Frydman

21.5k total citations · 5 hit papers
157 papers, 15.8k citations indexed

About

Judith Frydman is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, Judith Frydman has authored 157 papers receiving a total of 15.8k indexed citations (citations by other indexed papers that have themselves been cited), including 137 papers in Molecular Biology, 50 papers in Materials Chemistry and 27 papers in Cell Biology. Recurrent topics in Judith Frydman's work include Heat shock proteins research (85 papers), Enzyme Structure and Function (50 papers) and Protein Structure and Dynamics (48 papers). Judith Frydman is often cited by papers focused on Heat shock proteins research (85 papers), Enzyme Structure and Function (50 papers) and Protein Structure and Dynamics (48 papers). Judith Frydman collaborates with scholars based in United States, Germany and Switzerland. Judith Frydman's co-authors include Sebastian Pechmann, F. Ulrich Hartl, Daniel Kaganovich, Amie J. McClellan, Ron R. Kopito, Christoph Spiess, Raul Andino, Ron Geller, Elmar Nimmesgern and Véronique Albanèse and has published in prestigious journals such as Nature, Science and Cell.

In The Last Decade

Judith Frydman

155 papers receiving 15.6k citations

Hit Papers

Folding of Newly Translat... 1994 2026 2004 2015 2001 2008 1994 2017 2018 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Judith Frydman United States 68 12.9k 3.4k 2.5k 1.4k 1.3k 157 15.8k
Manajit Hayer‐Hartl Germany 53 15.6k 1.2× 3.5k 1.0× 3.6k 1.4× 1.6k 1.1× 1.6k 1.2× 98 18.1k
Jason E. Gestwicki United States 70 10.8k 0.8× 2.5k 0.8× 983 0.4× 1.1k 0.8× 1.1k 0.8× 226 14.8k
Matthias P. Mayer Germany 61 11.7k 0.9× 2.9k 0.8× 1.9k 0.7× 374 0.3× 1.6k 1.2× 137 13.8k
Len Neckers United States 85 19.4k 1.5× 3.0k 0.9× 1.5k 0.6× 931 0.7× 4.0k 3.0× 248 24.9k
Michael K. Rosen United States 70 18.4k 1.4× 5.6k 1.7× 1.4k 0.6× 1.1k 0.8× 1.9k 1.4× 142 23.6k
Laurence H. Pearl United Kingdom 76 18.0k 1.4× 2.2k 0.7× 2.7k 1.1× 396 0.3× 2.1k 1.6× 217 21.3k
Péter Tompa Hungary 64 19.9k 1.5× 3.4k 1.0× 4.9k 1.9× 1.0k 0.7× 769 0.6× 240 23.8k
A. Keith Dunker United States 75 22.6k 1.7× 2.8k 0.8× 6.2k 2.4× 884 0.6× 919 0.7× 163 26.8k
Harm H. Kampinga Netherlands 65 9.6k 0.7× 2.9k 0.9× 750 0.3× 1.4k 1.0× 796 0.6× 232 13.6k
Andreas Bracher Germany 47 8.2k 0.6× 2.3k 0.7× 1.4k 0.6× 505 0.4× 688 0.5× 100 10.1k

Countries citing papers authored by Judith Frydman

Since Specialization
Citations

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

Fields of papers citing papers by Judith Frydman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Judith Frydman. 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 Judith Frydman. The network helps show where Judith Frydman may publish in the future.

Co-authorship network of co-authors of Judith Frydman

This figure shows the co-authorship network connecting the top 25 collaborators of Judith Frydman. A scholar is included among the top collaborators of Judith Frydman 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 Judith Frydman. Judith Frydman 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.
Chou, Ching‐Chieh, Ryan T. Vest, Miguel A. Prado, et al.. (2025). Proteostasis and lysosomal repair deficits in transdifferentiated neurons of Alzheimer’s disease. Nature Cell Biology. 27(4). 619–632. 10 indexed citations
2.
Tilk, Susanne, Judith Frydman, Christina Curtis, & Dmitri A. Petrov. (2024). Cancers adapt to their mutational load by buffering protein misfolding stress. eLife. 12. 1 indexed citations
3.
Rodriguez-Aliaga, Piere, Tomáš Majtner, Stefanie Böhm, et al.. (2024). In situ analysis reveals the TRiC duty cycle and PDCD5 as an open-state cofactor. Nature. 637(8047). 983–990. 4 indexed citations
4.
Groh, Carina, Lena Krämer, Kevin C. Stein, et al.. (2023). The unfolded protein response of the endoplasmic reticulum supports mitochondrial biogenesis by buffering nonimported proteins. Molecular Biology of the Cell. 34(10). ar95–ar95. 8 indexed citations
5.
Collier, M, Kathy H. Li, Yuchan Chen, et al.. (2021). Native mass spectrometry analyses of chaperonin complex TRiC/CCT reveal subunit N-terminal processing and re-association patterns. Scientific Reports. 11(1). 13084–13084. 9 indexed citations
6.
Knowlton, Jonathan J., Daniel R. Gestaut, Boxue Ma, et al.. (2021). Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network. Proceedings of the National Academy of Sciences. 118(11). 28 indexed citations
7.
Wu, Gong‐Her, Jesús G. Galaz-Montoya, Corey W. Hecksel, et al.. (2020). Multi-scale 3D Cryo-Correlative Microscopy for Vitrified Cells. Structure. 28(11). 1231–1237.e3. 48 indexed citations
8.
Shen, Koning, Yulian Gavrilov, Pieter E. S. Smith, et al.. (2018). Huntingtin’s N-Terminus Rearrangements in the Presence of Membranes: A Joint Spectroscopic and Computational Perspective. ACS Chemical Neuroscience. 10(1). 472–481. 16 indexed citations
9.
Leeman, Dena S., Katja Hebestreit, Ashley E. Webb, et al.. (2018). Lysosome activation clears aggregates and enhances quiescent neural stem cell activation during aging. Science. 359(6381). 1277–1283. 382 indexed citations breakdown →
10.
Nayak, Arabinda, Dong Young Kim, Michael J. Trnka, et al.. (2018). A Viral Protein Restricts Drosophila RNAi Immunity by Regulating Argonaute Activity and Stability. Cell Host & Microbe. 24(4). 542–557.e9. 27 indexed citations
11.
Frydman, Judith, et al.. (2018). Post-extubation non-invasive ventilation in the pediatric intensive care unit: a multicenter study. Archivos Argentinos de Pediatria. 116(5). 333–339. 12 indexed citations
12.
Ogawa, N., Yohei Yamamoto, Keisuke Abé, et al.. (2018). Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking. International Journal of Molecular Sciences. 19(4). 950–950. 2 indexed citations
13.
Frydman, Judith. (2018). Proteostasis Function and Disfunction: The Folding Machines that Maintain Proteome Health. Biophysical Journal. 114(3). 544a–545a. 1 indexed citations
14.
Shen, Koning, Barbara Calamini, Jonathan A. Fauerbach, et al.. (2016). Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract. eLife. 5. 53 indexed citations
15.
Frydman, Judith. (2012). Mechanism and Function of the Eukaryotic Ring-Shaped Chaperonin TRiC/CCT. Biophysical Journal. 102(3). 428a–428a. 1 indexed citations
16.
Cong, Yao, Matthew L. Baker, Joanita Jakana, et al.. (2010). 4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proceedings of the National Academy of Sciences. 107(11). 4967–4972. 139 indexed citations
17.
Pan, Xuewen, Zhiwei Huang, Daniel Yuan, et al.. (2010). Trivalent Arsenic Inhibits the Functions of Chaperonin Complex. Genetics. 186(2). 725–734. 48 indexed citations
18.
McClellan, Amie J., Stephen J. Tam, Daniel Kaganovich, & Judith Frydman. (2005). Protein quality control: chaperones culling corrupt conformations. Nature Cell Biology. 7(8). 736–741. 226 indexed citations
19.
Meyer, Anne S., et al.. (2003). Closing the Folding Chamber of the Eukaryotic Chaperonin Requires the Transition State of ATP Hydrolysis. Cell. 113(3). 369–381. 166 indexed citations
20.
Frydman, Judith & F. Ulrich Hartl. (1994). 10 Molecular Chaperone Functions of hsp70 and hsp60 in Protein Folding. Cold Spring Harbor Monograph Archive. 26. 251–283. 34 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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