Gabby Rudenko

2.0k total citations
35 papers, 1.4k citations indexed

About

Gabby Rudenko is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Cell Biology. According to data from OpenAlex, Gabby Rudenko has authored 35 papers receiving a total of 1.4k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 15 papers in Cellular and Molecular Neuroscience and 14 papers in Cell Biology. Recurrent topics in Gabby Rudenko's work include Neuroscience and Neuropharmacology Research (15 papers), Cellular transport and secretion (10 papers) and RNA Research and Splicing (6 papers). Gabby Rudenko is often cited by papers focused on Neuroscience and Neuropharmacology Research (15 papers), Cellular transport and secretion (10 papers) and RNA Research and Splicing (6 papers). Gabby Rudenko collaborates with scholars based in United States, Canada and United Kingdom. Gabby Rudenko's co-authors include J. Deisenhofer, Eric J. Nestler, Els Wagenaar, Stephan Kemp, Alfred H. Schinkel, Martijn E.T. Dollé, Thomas C. Südhof, Mischa Machius, Paula G. Ulery and Alessandra d’Azzo and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

Gabby Rudenko

35 papers receiving 1.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Gabby Rudenko United States 22 771 449 271 208 149 35 1.4k
Catalina Ribas Spain 22 1.6k 2.1× 530 1.2× 217 0.8× 173 0.8× 182 1.2× 38 2.0k
Mark G. H. Scott France 26 1.3k 1.7× 558 1.2× 255 0.9× 235 1.1× 170 1.1× 42 1.8k
Dario Diviani Switzerland 26 1.9k 2.5× 471 1.0× 340 1.3× 147 0.7× 132 0.9× 49 2.3k
Wenjuan Su China 17 814 1.1× 299 0.7× 278 1.0× 135 0.6× 150 1.0× 33 1.4k
Shinichiro Toki Japan 13 1.3k 1.7× 362 0.8× 182 0.7× 129 0.6× 145 1.0× 28 1.9k
Junya Mitoma Japan 20 1.2k 1.6× 313 0.7× 213 0.8× 109 0.5× 156 1.0× 37 1.8k
Christian Le Gouill Canada 29 1.6k 2.1× 836 1.9× 181 0.7× 171 0.8× 258 1.7× 57 2.2k
Emma Williams United Kingdom 22 1.3k 1.7× 888 2.0× 460 1.7× 160 0.8× 79 0.5× 40 2.3k
Antonio García‐España Spain 27 1.1k 1.4× 447 1.0× 118 0.4× 217 1.0× 189 1.3× 61 1.7k
Roman Urfer United States 22 1.1k 1.5× 726 1.6× 201 0.7× 188 0.9× 187 1.3× 28 1.8k

Countries citing papers authored by Gabby Rudenko

Since Specialization
Citations

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

Fields of papers citing papers by Gabby Rudenko

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Gabby Rudenko

This figure shows the co-authorship network connecting the top 25 collaborators of Gabby Rudenko. A scholar is included among the top collaborators of Gabby Rudenko 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 Gabby Rudenko. Gabby Rudenko 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.
Liu, Jianfang, Aaron O. Bailey, William K. Russell, et al.. (2024). Molecular mechanism of contactin 2 homophilic interaction. Structure. 32(10). 1652–1666.e8. 3 indexed citations
2.
Nguyen, Phuong, Christian Poitras, Benoit Coulombe, et al.. (2024). Structural and functional characterization of the IgSF21-neurexin2α complex and its related signaling pathways in the regulation of inhibitory synapse organization. Frontiers in Molecular Neuroscience. 17. 1371145–1371145. 2 indexed citations
3.
Liu, Jianfang, Aaron O. Bailey, William K. Russell, et al.. (2023). Designer molecules of the synaptic organizer MDGA1 reveal 3D conformational control of biological function. Journal of Biological Chemistry. 299(4). 104586–104586. 4 indexed citations
4.
Venkannagari, Harikanth, James M. Kasper, Anurag Misra, et al.. (2020). Highly Conserved Molecular Features in IgLONs Contrast Their Distinct Structural and Biological Outcomes. Journal of Molecular Biology. 432(19). 5287–5303. 14 indexed citations
5.
Rudenko, Gabby. (2019). Neurexins — versatile molecular platforms in the synaptic cleft. Current Opinion in Structural Biology. 54. 112–121. 19 indexed citations
6.
Zhou, Yin, Harikanth Venkannagari, Galina V. Aglyamova, et al.. (2019). Self-assembly of the bZIP transcription factor ΔFosB. SHILAP Revista de lepidopterología. 2. 1–13. 7 indexed citations
7.
Liu, Jianfang, et al.. (2018). Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. Journal of Molecular Biology. 430(21). 4325–4343. 12 indexed citations
8.
Zhou, Yin, Mischa Machius, Eric J. Nestler, & Gabby Rudenko. (2017). Activator Protein-1: redox switch controlling structure and DNA-binding. Nucleic Acids Research. 45(19). 11425–11436. 45 indexed citations
9.
Gangwar, Shanti Pal, et al.. (2017). Molecular Mechanism of MDGA1: Regulation of Neuroligin 2:Neurexin Trans-synaptic Bridges. Neuron. 94(6). 1132–1141.e4. 55 indexed citations
10.
Wang, Yun, Fang Chen, Huimin Tong, et al.. (2014). Calsyntenin-3 Molecular Architecture and Interaction with Neurexin 1α. Journal of Biological Chemistry. 289(50). 34530–34542. 40 indexed citations
11.
Cates, Hannah M., Madeline L. Pfau, Elizabeth A. Heller, et al.. (2014). Threonine 149 Phosphorylation Enhances ΔFosB Transcriptional Activity to Control Psychomotor Responses to Cocaine. Journal of Neuroscience. 34(34). 11461–11469. 21 indexed citations
12.
Wang, Yun, Yoko Ohnishi, Vivian Lam, et al.. (2012). Small Molecule Screening Identifies Regulators of the Transcription Factor ΔFosB. ACS Chemical Neuroscience. 3(7). 546–556. 22 indexed citations
13.
Chen, Fang, et al.. (2011). The Structure of Neurexin 1α Reveals Features Promoting a Role as Synaptic Organizer. Structure. 19(6). 779–789. 54 indexed citations
14.
Huang, Sha, Lisa Henry, Y K Ho, Henry J. Pownall, & Gabby Rudenko. (2009). Mechanism of LDL binding and release probed by structure-based mutagenesis of the LDL receptor. Journal of Lipid Research. 51(2). 297–308. 43 indexed citations
15.
Rudenko, Gabby, et al.. (2008). Regulation of Neurexin 1β Tertiary Structure and Ligand Binding through Alternative Splicing. Structure. 16(3). 422–431. 37 indexed citations
16.
Ulery, Paula G., Gabby Rudenko, & Eric J. Nestler. (2006). Regulation of ΔFosB Stability by Phosphorylation. Journal of Neuroscience. 26(19). 5131–5142. 75 indexed citations
17.
Rudenko, Gabby & J. Deisenhofer. (2003). The low-density lipoprotein receptor: ligands, debates and lore. Current Opinion in Structural Biology. 13(6). 683–689. 51 indexed citations
18.
Rudenko, Gabby, et al.. (2003). 'MAD'ly phasing the extracellular domain of the LDL receptor: a medium-sized protein, large tungsten clusters and multiple non-isomorphous crystals. Acta Crystallographica Section D Biological Crystallography. 59(11). 1978–1986. 16 indexed citations
19.
Rudenko, Gabby, Erhard Hohenester, & Yves A. Muller. (2001). LG/LNS domains: multiple functions – one business end?. Trends in Biochemical Sciences. 26(6). 363–368. 75 indexed citations
20.
Rudenko, Gabby, Thai Nguyen, Yogarany Chelliah, Thomas C. Südhof, & J. Deisenhofer. (1999). Regulation of LNS Domain Function by Alternative Splicing: The Structure of the Ligand-Binding Domain of Neurexin Iβ. Cell. 99(1). 93–101. 107 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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