Flavio Toma

1.8k total citations
47 papers, 1.5k citations indexed

About

Flavio Toma is a scholar working on Molecular Biology, Cell Biology and Organic Chemistry. According to data from OpenAlex, Flavio Toma has authored 47 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 34 papers in Molecular Biology, 10 papers in Cell Biology and 7 papers in Organic Chemistry. Recurrent topics in Flavio Toma's work include Microtubule and mitosis dynamics (8 papers), Protein Structure and Dynamics (7 papers) and Chemical Synthesis and Analysis (6 papers). Flavio Toma is often cited by papers focused on Microtubule and mitosis dynamics (8 papers), Protein Structure and Dynamics (7 papers) and Chemical Synthesis and Analysis (6 papers). Flavio Toma collaborates with scholars based in France, Greece and Norway. Flavio Toma's co-authors include Christian Roumestand, Bernard Gilquin, Andre Ménèz, François Bontems, Patrick A. Curmi, Sophie Zinn‐Justin, Marie‐Jeanne Clément, Serge Fermandjian, Vincent Dive and Philippe Savarin and has published in prestigious journals such as Science, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Flavio Toma

47 papers receiving 1.5k citations

Peers

Flavio Toma
Tai-he Xia Sweden
Flavio Toma
Citations per year, relative to Flavio Toma Flavio Toma (= 1×) peers Tai-he Xia

Countries citing papers authored by Flavio Toma

Since Specialization
Citations

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

Fields of papers citing papers by Flavio Toma

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Flavio Toma

This figure shows the co-authorship network connecting the top 25 collaborators of Flavio Toma. A scholar is included among the top collaborators of Flavio Toma 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 Flavio Toma. Flavio Toma 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.
Clément, Marie‐Jeanne, Guillaume Bollot, Flavio Toma, et al.. (2015). Cucurbitacin I elicits the formation of actin/phospho-myosin II co-aggregates by stimulation of the RhoA/ROCK pathway and inhibition of LIM-kinase. Biochemical Pharmacology. 102. 45–63. 18 indexed citations
2.
Clément, Marie‐Jeanne, Philippe Savarin, Élisabeth Adjadj, et al.. (2010). Probing Interactions of Tubulin with Small Molecules, Peptides, and Protein Fragments by Solution Nuclear Magnetic Resonance. Methods in cell biology. 95. 406–447. 4 indexed citations
3.
Lefèvre, Julien, Konstantin G. Chernov, Stéphanie Delga, et al.. (2010). The C Terminus of Tubulin, a Versatile Partner for Cationic Molecules. Journal of Biological Chemistry. 286(4). 3065–3078. 45 indexed citations
4.
Cormier, Anthony, Marie‐Jeanne Clément, M. Knossow, et al.. (2009). The PN2-3 Domain of Centrosomal P4.1-associated Protein Implements a Novel Mechanism for Tubulin Sequestration. Journal of Biological Chemistry. 284(11). 6909–6917. 41 indexed citations
5.
Clément, Marie‐Jeanne, Philippe Savarin, Jérôme Coûtant, Flavio Toma, & Patrick A. Curmi. (2008). NMR assignment of PN2-3, a tubulin interaction subdomain of the CPAP protein. Biomolecular NMR Assignments. 2(2). 115–117. 3 indexed citations
6.
Chernov, Konstantin G., N. V. Popova, David Pastré, et al.. (2008). YB-1 promotes microtubule assembly in vitro through interaction with tubulin and microtubules. BMC Biochemistry. 9(1). 23–23. 38 indexed citations
7.
Coûtant, Jérôme, Huifeng Yu, Marie‐Jeanne Clément, et al.. (2008). Both lipid environment and pH are critical for determining physiological solution structure of 3‐D‐conserved epitopes of the HIV‐1 gp41‐MPER peptide P1. The FASEB Journal. 22(12). 4338–4351. 27 indexed citations
8.
Clément, Marie‐Jeanne, Krishnan Rathinasamy, Élisabeth Adjadj, et al.. (2008). Benomyl and Colchicine Synergistically Inhibit Cell Proliferation and Mitosis: Evidence of Distinct Binding Sites for These Agents in Tubulin. Biochemistry. 47(49). 13016–13025. 40 indexed citations
9.
Gantier, René, Danièle Gilbert, Cécile Dumanchin, et al.. (2000). The pathogenic L392V mutation of presenilin 1 decreases the affinity to glycogen synthase kinase-3β. Neuroscience Letters. 283(3). 217–220. 29 indexed citations
10.
Gantier, René, Cécile Dumanchin, Corinne Loutelier‐Bourhis, et al.. (1999). The L392V mutation of presenilin 1 associated with autosomal dominant early-onset Alzheimerʼs disease alters the secondary structure of the hydrophilic loop. Neuroreport. 10(14). 3071–3074. 5 indexed citations
11.
Roumestand, Christian, Sophie Zinn‐Justin, Bernard Gilquin, et al.. (1995). Solution Structure of a Green Mamba Toxin That Activates Muscarinic Acetylcholine Receptors, As Studied by Nuclear Magnetic Resonance and Molecular Modeling. Biochemistry. 34(4). 1248–1260. 44 indexed citations
12.
Pertinhez, Thelma A., Clóvis R. Nakaie, Antonio C.M. Paiva, et al.. (1995). Conformational changes upon binding of a receptor loop to lipid structures: possible role in signal transduction. FEBS Letters. 375(3). 239–242. 17 indexed citations
14.
Jamin, Nadège, et al.. (1993). Secondary structure of the DNA‐binding domain of the c‐Myb oncoprotein in solution. European Journal of Biochemistry. 216(1). 147–154. 31 indexed citations
15.
Zinn‐Justin, Sophie, Christian Roumestand, Bernard Gilquin, et al.. (1992). Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study. Biochemistry. 31(46). 11335–11347. 71 indexed citations
16.
Dive, Vincent, Athanasios Yiotakis, Christian Roumestand, et al.. (1992). Peptide inhibitors of E. collagenolyticum bacterial collagenase ‐effect of N‐methylation. International journal of peptide & protein research. 39(6). 506–515. 8 indexed citations
17.
Dive, Vincent, Adolfo Lai, Gianni Valensin, et al.. (1991). Proton and tritium nmr relaxation studies of peptide inhibitor binding to bacterial collagenase: Conformation and dynamics. Biopolymers. 31(3). 305–317. 11 indexed citations
18.
Dufour, Éric, Vincent Dive, & Flavio Toma. (1988). Delineation of chicken cathepsin L secondary structure; relationship between pH dependence activity and helix content. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 955(1). 58–64. 20 indexed citations
19.
Prangé, T., et al.. (1983). Solid- and solvated-state conformation of the free tetrapeptide glycyl-L-prolyl-D-leucylglycine by x-ray and proton nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society. 105(20). 6306–6309. 9 indexed citations
20.
Lintner, Karl, et al.. (1977). Influence of hydrogen bonding on the rotamer distribution of the histidine side chain in peptides: 1H NMR and CD studies. Biochimica et Biophysica Acta (BBA) - Protein Structure. 492(2). 245–253. 12 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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