J. Rajan Prabu

1.8k total citations
25 papers, 1.2k citations indexed

About

J. Rajan Prabu is a scholar working on Molecular Biology, Oncology and Epidemiology. According to data from OpenAlex, J. Rajan Prabu has authored 25 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 7 papers in Oncology and 4 papers in Epidemiology. Recurrent topics in J. Rajan Prabu's work include Ubiquitin and proteasome pathways (12 papers), Biochemical and Molecular Research (5 papers) and Protein Degradation and Inhibitors (5 papers). J. Rajan Prabu is often cited by papers focused on Ubiquitin and proteasome pathways (12 papers), Biochemical and Molecular Research (5 papers) and Protein Degradation and Inhibitors (5 papers). J. Rajan Prabu collaborates with scholars based in Germany, United States and India. J. Rajan Prabu's co-authors include Brenda A. Schulman, Kheewoong Baek, Gary Kleiger, David T. Krist, Susanne von Gronau, Elena Conti, Daniel Horn‐Ghetko, Spencer Hill, Sebastian Falk and Monique P. C. Mulder and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

J. Rajan Prabu

25 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J. Rajan Prabu Germany 18 970 250 110 109 101 25 1.2k
Sung Hwan Kang South Korea 8 640 0.7× 189 0.8× 139 1.3× 176 1.6× 107 1.1× 12 840
Carine Froment France 23 1.2k 1.3× 217 0.9× 50 0.5× 221 2.0× 32 0.3× 51 1.5k
Y. John Shyu United States 8 635 0.7× 57 0.2× 45 0.4× 153 1.4× 27 0.3× 9 846
Pamela Riemer Germany 12 424 0.4× 203 0.8× 29 0.3× 33 0.3× 97 1.0× 15 722
Barbara A. Thorne United States 12 548 0.6× 184 0.7× 41 0.4× 331 3.0× 69 0.7× 16 901
Jennifer I. Semple Spain 14 962 1.0× 183 0.7× 63 0.6× 215 2.0× 11 0.1× 23 1.2k
Gian Marco De Donatis United States 14 409 0.4× 101 0.4× 23 0.2× 194 1.8× 49 0.5× 19 790
Ulrich Elling Austria 17 1.1k 1.2× 96 0.4× 55 0.5× 76 0.7× 11 0.1× 37 1.4k
Marcello Maresca Sweden 21 1.4k 1.5× 86 0.3× 78 0.7× 42 0.4× 16 0.2× 36 1.7k
Robert Townley United States 14 786 0.8× 52 0.2× 147 1.3× 196 1.8× 16 0.2× 17 1.0k

Countries citing papers authored by J. Rajan Prabu

Since Specialization
Citations

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

Fields of papers citing papers by J. Rajan Prabu

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J. Rajan Prabu. 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 J. Rajan Prabu. The network helps show where J. Rajan Prabu may publish in the future.

Co-authorship network of co-authors of J. Rajan Prabu

This figure shows the co-authorship network connecting the top 25 collaborators of J. Rajan Prabu. A scholar is included among the top collaborators of J. Rajan Prabu 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 J. Rajan Prabu. J. Rajan Prabu 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.
Scott, Daniel C., Barbara Steigenberger, Trent Hinkle, et al.. (2024). Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting. Molecular Cell. 84(7). 1304–1320.e16. 20 indexed citations
2.
Horn‐Ghetko, Daniel, Jiale Du, Viola Beier, et al.. (2024). Noncanonical assembly, neddylation and chimeric cullin–RING/RBR ubiquitylation by the 1.8 MDa CUL9 E3 ligase complex. Nature Structural & Molecular Biology. 31(7). 1083–1094. 3 indexed citations
3.
Krist, David T., Daniel C. Scott, Barbara Steigenberger, et al.. (2024). Mechanism of millisecond Lys48-linked poly-ubiquitin chain formation by cullin-RING ligases. Nature Structural & Molecular Biology. 31(2). 378–389. 26 indexed citations
4.
Chrustowicz, Jakub, Dawafuti Sherpa, Christine Langlois, et al.. (2023). Multisite phosphorylation dictates selective E2-E3 pairing as revealed by Ubc8/UBE2H-GID/CTLH assemblies. Molecular Cell. 84(2). 293–308.e14. 11 indexed citations
5.
Wallace, I. R., Kheewoong Baek, J. Rajan Prabu, et al.. (2023). Insights into the ISG15 transfer cascade by the UBE1L activating enzyme. Nature Communications. 14(1). 7970–7970. 10 indexed citations
6.
Prabu, J. Rajan, Kheewoong Baek, Daniel Horn‐Ghetko, et al.. (2021). CUL5-ARIH2 E3-E3 ubiquitin ligase structure reveals cullin-specific NEDD8 activation. Nature Chemical Biology. 17(10). 1075–1083. 41 indexed citations
7.
Horn‐Ghetko, Daniel, David T. Krist, J. Rajan Prabu, et al.. (2021). Ubiquitin ligation to F-box protein targets by SCF–RBR E3–E3 super-assembly. Nature. 590(7847). 671–676. 126 indexed citations
8.
Chrustowicz, Jakub, Dawafuti Sherpa, Joan Teyra, et al.. (2021). Multifaceted N-Degron Recognition and Ubiquitylation by GID/CTLH E3 Ligases. Journal of Molecular Biology. 434(2). 167347–167347. 22 indexed citations
9.
Sherpa, Dawafuti, Jakub Chrustowicz, Shuai Qiao, et al.. (2021). GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme. Molecular Cell. 81(11). 2445–2459.e13. 49 indexed citations
10.
Schuller, Sandra K., Jan M. Schuller, J. Rajan Prabu, et al.. (2020). Structural insights into the nucleic acid remodeling mechanisms of the yeast THO-Sub2 complex. eLife. 9. 34 indexed citations
11.
Miller-Vedam, Lakshmi E., Bastian Bräuning, Katerina D. Popova, et al.. (2020). Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients. eLife. 9. 68 indexed citations
12.
Oh, Eugene, Kevin G. Mark, Edmond R. Watson, et al.. (2020). Gene expression and cell identity controlled by anaphase-promoting complex. Nature. 579(7797). 136–140. 67 indexed citations
13.
Qiao, Shuai, Christine Langlois, Jakub Chrustowicz, et al.. (2019). Interconversion between Anticipatory and Active GID E3 Ubiquitin Ligase Conformations via Metabolically Driven Substrate Receptor Assembly. Molecular Cell. 77(1). 150–163.e9. 60 indexed citations
14.
Prabu, J. Rajan, et al.. (2015). Structural studies on Mycobacterium tuberculosis RecA: Molecular plasticity and interspecies variability. Journal of Biosciences. 40(1). 13–30. 11 indexed citations
15.
Prabu, J. Rajan, Marisa Müller, Andreas W. Thomae, et al.. (2015). Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling. Molecular Cell. 60(3). 487–499. 58 indexed citations
16.
Reischl, Silke, Thomas Wallach, Roman Klemz, et al.. (2014). Interaction of Circadian Clock Proteins CRY1 and PER2 Is Modulated by Zinc Binding and Disulfide Bond Formation. Cell. 157(5). 1203–1215. 144 indexed citations
17.
Prabu, J. Rajan, et al.. (2009). Crystallographic and modelling studies on Mycobacterium tuberculosis RuvA. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794(7). 1001–1009. 25 indexed citations
18.
Prabu, J. Rajan, G. Manjunath, Nagasuma Chandra, K. Muniyappa, & M. Vijayan. (2008). Functionally important movements in RecA molecules and filaments: studies involving mutation and environmental changes. Acta Crystallographica Section D Biological Crystallography. 64(11). 1146–1157. 10 indexed citations
19.
20.
Prabu, J. Rajan, Subbiah Thamotharan, Chang‐Yub Kim, et al.. (2006). Structure ofMycobacterium tuberculosisRuvA, a protein involved in recombination. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(8). 731–734. 10 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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