Nathalie Evrard‐Todeschi

943 total citations · 1 hit paper
23 papers, 808 citations indexed

About

Nathalie Evrard‐Todeschi is a scholar working on Molecular Biology, Infectious Diseases and Virology. According to data from OpenAlex, Nathalie Evrard‐Todeschi has authored 23 papers receiving a total of 808 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 4 papers in Infectious Diseases and 4 papers in Virology. Recurrent topics in Nathalie Evrard‐Todeschi's work include Protein Structure and Dynamics (7 papers), HIV Research and Treatment (4 papers) and Ubiquitin and proteasome pathways (4 papers). Nathalie Evrard‐Todeschi is often cited by papers focused on Protein Structure and Dynamics (7 papers), HIV Research and Treatment (4 papers) and Ubiquitin and proteasome pathways (4 papers). Nathalie Evrard‐Todeschi collaborates with scholars based in France, Russia and Thailand. Nathalie Evrard‐Todeschi's co-authors include Gildas Bertho, Jean‐Pierre Girault, María Flor García‐Mayoral, Herman Devijver, Fred Van Leuven, Tomasz Jaworski, Antonio Cuadrado, Ana I. Rojo, John D. Hayes and Patricia Rada and has published in prestigious journals such as Journal of Biological Chemistry, Bioinformatics and Molecular and Cellular Biology.

In The Last Decade

Nathalie Evrard‐Todeschi

23 papers receiving 798 citations

Hit Papers

Structural and Functional Characterization of Nrf2 Degrad... 2012 2026 2016 2021 2012 100 200 300 400

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Nathalie Evrard‐Todeschi France 14 587 83 63 61 53 23 808
Nagarajan Raju India 15 573 1.0× 36 0.4× 131 2.1× 36 0.6× 56 1.1× 38 886
Ram Chawda United States 15 402 0.7× 88 1.1× 172 2.7× 98 1.6× 91 1.7× 21 898
Kenneth S. Santone United States 17 274 0.5× 134 1.6× 33 0.5× 37 0.6× 57 1.1× 29 893
Roberta Ferraresi Italy 17 521 0.9× 75 0.9× 229 3.6× 49 0.8× 132 2.5× 22 1.1k
Françoise Heymans France 19 467 0.8× 219 2.6× 108 1.7× 25 0.4× 43 0.8× 54 1.0k
Xin Qi China 13 540 0.9× 40 0.5× 70 1.1× 80 1.3× 43 0.8× 41 839
F.J. Sorrell United Kingdom 13 672 1.1× 122 1.5× 58 0.9× 51 0.8× 48 0.9× 17 936
Masashi Hyuga Japan 17 519 0.9× 124 1.5× 99 1.6× 49 0.8× 41 0.8× 48 950
Paula M. Brito Portugal 11 257 0.4× 35 0.4× 60 1.0× 22 0.4× 53 1.0× 15 571
Hammou Oubrahim United States 14 562 1.0× 36 0.4× 98 1.6× 43 0.7× 66 1.2× 19 1.0k

Countries citing papers authored by Nathalie Evrard‐Todeschi

Since Specialization
Citations

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

Fields of papers citing papers by Nathalie Evrard‐Todeschi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Nathalie Evrard‐Todeschi. 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 Nathalie Evrard‐Todeschi. The network helps show where Nathalie Evrard‐Todeschi may publish in the future.

Co-authorship network of co-authors of Nathalie Evrard‐Todeschi

This figure shows the co-authorship network connecting the top 25 collaborators of Nathalie Evrard‐Todeschi. A scholar is included among the top collaborators of Nathalie Evrard‐Todeschi 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 Nathalie Evrard‐Todeschi. Nathalie Evrard‐Todeschi 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.
Corre, Laurent Le, Nicolas Pietrancosta, Nathalie Evrard‐Todeschi, et al.. (2018). Bacterial Transferase MraY, a Source of Inspiration towards New Antibiotics. Current Medicinal Chemistry. 25(42). 6013–6029. 13 indexed citations
2.
Rada, Patricia, Ana I. Rojo, Nathalie Evrard‐Todeschi, et al.. (2012). Structural and Functional Characterization of Nrf2 Degradation by the Glycogen Synthase Kinase 3/β-TrCP Axis. Molecular and Cellular Biology. 32(17). 3486–3499. 424 indexed citations breakdown →
3.
Pons, Josefina, et al.. (2011). NMR Applications for Identifying β-TrCP Protein-Ligand Interactions. Mini-Reviews in Medicinal Chemistry. 11(4). 283–297. 4 indexed citations
4.
Maria, Annick, et al.. (2010). Ecdysteroids from Chenopodium quinoa Willd., an ancient Andean crop of high nutritional value. Food Chemistry. 125(4). 1226–1234. 61 indexed citations
5.
Bouvier, Guillaume, Nathalie Evrard‐Todeschi, Jean‐Pierre Girault, & Gildas Bertho. (2009). Automatic clustering of docking poses in virtual screening process using self-organizing map. Bioinformatics. 26(1). 53–60. 56 indexed citations
6.
Evrard‐Todeschi, Nathalie, et al.. (2008). Structure of the Complex between Phosphorylated Substrates and the SCF β-TrCP Ubiquitin Ligase Receptor: A Combined NMR, Molecular Modeling, and Docking Approach. Journal of Chemical Information and Modeling. 48(12). 2350–2361. 9 indexed citations
7.
Evrard‐Todeschi, Nathalie, Gildas Bertho, Josyane Gharbi‐Benarous, et al.. (2007). Transfer-NMR and Docking Studies Identify the Binding of the Peptide Derived from Activating Transcription Factor 4 to Protein Ubiquitin Ligase β-TrCP. Competition STD-NMR with β-Catenin. Biochemistry. 47(1). 14–29. 23 indexed citations
8.
Evrard‐Todeschi, Nathalie, et al.. (2007). Phosphorylation-dependent structure of ATF4 peptides derived from a human ATF4 protein, a member of the family of transcription factors. Peptides. 28(12). 2253–2267. 15 indexed citations
9.
Evrard‐Todeschi, Nathalie, Josyane Gharbi‐Benarous, Gildas Bertho, et al.. (2005). NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein β-TrCP. Peptides. 27(1). 194–210. 14 indexed citations
10.
Mégy, Simon, Gildas Bertho, Josyane Gharbi‐Benarous, et al.. (2005). STD and TRNOESY NMR Studies on the Conformation of the Oncogenic Protein β-Catenin Containing the Phosphorylated Motif DpSGXXpS Bound to the β-TrCP Protein. Journal of Biological Chemistry. 280(32). 29107–29116. 22 indexed citations
11.
Одиноков, В. Н., Nathalie Evrard‐Todeschi, Л. М. Халилов, et al.. (2005). Low-Polarity Phytoecdysteroids from the Juice of Serratula coronata L. (Asteraceae). Collection of Czechoslovak Chemical Communications. 70(12). 2038–2052. 11 indexed citations
12.
Gharbi‐Benarous, Josyane, Gildas Bertho, Nathalie Evrard‐Todeschi, et al.. (2004). Epitope Mapping of the Phosphorylation Motif of the HIV-1 Protein Vpu Bound to the Selective Monoclonal Antibody Using TRNOESY and STD NMR Spectroscopy. Biochemistry. 43(46). 14555–14565. 7 indexed citations
13.
Coadou, Gaël, Josyane Gharbi‐Benarous, Simon Mégy, et al.. (2003). NMR Studies of the Phosphorylation Motif of the HIV-1 Protein Vpu Bound to the F-Box Protein β-TrCP. Biochemistry. 42(50). 14741–14751. 37 indexed citations
14.
Coadou, Gaël, et al.. (2002). HIV-1 encoded virus protein U (Vpu) solution structure of the 41–62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56. International Journal of Biological Macromolecules. 30(1). 23–40. 24 indexed citations
15.
Coadou, Gaël, Nathalie Evrard‐Todeschi, Josyane Gharbi‐Benarous, Richard Bénarous, & Jean‐Pierre Girault. (2001). Conformational analysis by NMR and molecular modelling of the 41–62 hydrophilic region of HIV-1 encoded virus protein U (Vpu). Effect of the phosphorylation on sites 52 and 56. Comptes Rendus de l Académie des Sciences - Series IIC - Chemistry. 4(10). 751–758. 7 indexed citations
16.
Evrard‐Todeschi, Nathalie, Josyane Gharbi‐Benarous, Christine Gaillet, et al.. (2000). Conformations in solution and bound to bacterial ribosomes of ketolides, HMR 3647 (telithromycin) and RU 72366: A new class of highly potent antibacterials. Bioorganic & Medicinal Chemistry. 8(7). 1579–1597. 16 indexed citations
17.
Verdier, Laurent, Josyane Gharbi‐Benarous, Gildas Bertho, et al.. (2000). Dissociation–equilibrium constant and bound conformation for weak antibiotic binding interaction with different bacterial ribosomes †. Journal of the Chemical Society Perkin Transactions 2. 2363–2371. 15 indexed citations
18.
Gharbi‐Benarous, Josyane, et al.. (1999). Conformational analysis of josamycin, a 16-membered macrolide free in solution and bound to bacterial ribosomes. Journal of the Chemical Society Perkin Transactions 2. 529–544. 8 indexed citations
19.
Evrard‐Todeschi, Nathalie, Josyane Gharbi‐Benarous, Valéry Larue, & Jean‐Pierre Girault. (1998). Predictive Study by Molecular Modeling To Promote Specific Probes of Glutamate Receptors, Using Methylated Cyclic Glutamic Acid Derivatives (trans- and cis-ACPD). Comparison with Specific Agonists. Journal of Chemical Information and Computer Sciences. 38(4). 742–760. 1 indexed citations
20.
Evrard‐Todeschi, Nathalie, et al.. (1997). Conformational analysis of 2-(carboxycyclopropyl)glycine agonists of glutamate receptors in aqueous solution using a combination of NMR and molecular modelling experiments and charge calculations. Journal of the Chemical Society Perkin Transactions 2. 2677–2690. 4 indexed citations

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