M. Tegoni

5.8k total citations
89 papers, 4.8k citations indexed

About

M. Tegoni is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Materials Chemistry. According to data from OpenAlex, M. Tegoni has authored 89 papers receiving a total of 4.8k indexed citations (citations by other indexed papers that have themselves been cited), including 54 papers in Molecular Biology, 24 papers in Cellular and Molecular Neuroscience and 22 papers in Materials Chemistry. Recurrent topics in M. Tegoni's work include Neurobiology and Insect Physiology Research (20 papers), Photosynthetic Processes and Mechanisms (19 papers) and Enzyme Structure and Function (16 papers). M. Tegoni is often cited by papers focused on Neurobiology and Insect Physiology Research (20 papers), Photosynthetic Processes and Mechanisms (19 papers) and Enzyme Structure and Function (16 papers). M. Tegoni collaborates with scholars based in France, Italy and Canada. M. Tegoni's co-authors include Christian Cambillau, Silvia Spinelli, Valérie Campanacci, Roberto Ramoni, Audrey Lartigue, Paolo Pelosi, Stefano Grolli, Kieron Brown, Florence Vincent and Stéphanie Blangy and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Accounts of Chemical Research.

In The Last Decade

M. Tegoni

88 papers receiving 4.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M. Tegoni France 42 2.2k 1.6k 1.2k 1.0k 559 89 4.8k
David N. M. Jones United States 28 1.5k 0.7× 1.1k 0.7× 745 0.6× 634 0.6× 137 0.2× 56 2.8k
Roman G. Efremov Russia 39 3.4k 1.6× 464 0.3× 128 0.1× 727 0.7× 197 0.4× 218 4.6k
Elias Eliopoulos Greece 30 2.0k 0.9× 548 0.3× 305 0.3× 306 0.3× 80 0.1× 148 3.7k
Heinz Decker Germany 38 1.6k 0.8× 1.1k 0.7× 600 0.5× 217 0.2× 72 0.1× 162 5.6k
Donatella Barra Italy 52 5.6k 2.6× 1.3k 0.8× 258 0.2× 625 0.6× 48 0.1× 215 9.0k
ChulHee Kang United States 44 6.0k 2.7× 549 0.3× 123 0.1× 540 0.5× 111 0.2× 126 7.8k
Jiawei Wang China 48 5.8k 2.6× 411 0.3× 120 0.1× 664 0.7× 98 0.2× 132 8.6k
Marc le Maire France 47 5.1k 2.3× 450 0.3× 99 0.1× 428 0.4× 63 0.1× 143 6.6k
Masafumi Yohda Japan 40 3.8k 1.7× 252 0.2× 146 0.1× 263 0.3× 199 0.4× 257 5.5k
Norelle L. Daly Australia 66 10.5k 4.8× 500 0.3× 350 0.3× 606 0.6× 43 0.1× 223 12.1k

Countries citing papers authored by M. Tegoni

Since Specialization
Citations

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

Fields of papers citing papers by M. Tegoni

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of M. Tegoni

This figure shows the co-authorship network connecting the top 25 collaborators of M. Tegoni. A scholar is included among the top collaborators of M. Tegoni 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 M. Tegoni. M. Tegoni 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.
Spinelli, Silvia, M. Tegoni, Xiaoli He, et al.. (2011). The Crystal Structure of Odorant Binding Protein 7 from Anopheles gambiae Exhibits an Outstanding Adaptability of Its Binding Site. Journal of Molecular Biology. 414(3). 401–412. 81 indexed citations
2.
Douzi, Badreddine, Éric Durand, Cédric Bernard, et al.. (2009). The XcpV/GspI Pseudopilin Has a Central Role in the Assembly of a Quaternary Complex within the T2SS Pseudopilus. Journal of Biological Chemistry. 284(50). 34580–34589. 50 indexed citations
3.
Scaltriti, Erika, Sylvain Moineau, Hélène Launay, et al.. (2009). Deciphering the function of lactococcal phage ul36 Sak domains. Journal of Structural Biology. 170(3). 462–469. 17 indexed citations
4.
Campanacci, Valérie, Russell E. Bishop, Stéphanie Blangy, M. Tegoni, & Christian Cambillau. (2006). The membrane bound bacterial lipocalin Blc is a functional dimer with binding preference for lysophospholipids. FEBS Letters. 580(20). 4877–4883. 44 indexed citations
5.
Spinelli, Silvia, Valérie Campanacci, Stéphanie Blangy, et al.. (2006). Modular Structure of the Receptor Binding Proteins of Lactococcus lactis Phages. Journal of Biological Chemistry. 281(20). 14256–14262. 101 indexed citations
6.
Tegoni, M., Valérie Campanacci, & Christian Cambillau. (2004). Structural aspects of sexual attraction and chemical communication in insects. Trends in Biochemical Sciences. 29(5). 257–264. 217 indexed citations
7.
Gruez, Arnaud, V. Roig-Zamboni, Sacha Grisel, et al.. (2004). Crystal Structure and Kinetics Identify Escherichia coli YdcW Gene Product as a Medium-chain Aldehyde Dehydrogenase. Journal of Molecular Biology. 343(1). 29–41. 66 indexed citations
8.
Sulzenbacher, Gerlind, Karine Alvarez, Robert H. H. van den Heuvel, et al.. (2004). Crystal Structure of E.coli Alcohol Dehydrogenase YqhD: Evidence of a Covalently Modified NADP Coenzyme. Journal of Molecular Biology. 342(2). 489–502. 93 indexed citations
9.
Lartigue, Audrey, Arnaud Gruez, Loı̈c Briand, et al.. (2003). Optimization of crystals from nanodrops: crystallization and preliminary crystallographic study of a pheromone-binding protein from the honeybeeApis melliferaL.. Acta Crystallographica Section D Biological Crystallography. 59(5). 919–921. 13 indexed citations
10.
Cabrito, Inês, Alice S. Pereira, Pedro Tavares, et al.. (2001). Nitrous oxide reductase (N2OR) from Pseudomonas nautica 617. Journal of Inorganic Biochemistry. 86(1). 165–165. 1 indexed citations
11.
Ramoni, Roberto, Florence Vincent, Stefano Grolli, et al.. (2001). The Insect Attractant 1-Octen-3-ol Is the Natural Ligand of Bovine Odorant-binding Protein. Journal of Biological Chemistry. 276(10). 7150–7155. 74 indexed citations
12.
Tegoni, M., Paolo Pelosi, Florence Vincent, et al.. (2000). Mammalian odorant binding proteins. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1482(1-2). 229–240. 212 indexed citations
13.
Nurizzo, Didier, Francesca Cutruzzolà, Marzia Arese, et al.. (1999). Does the Reduction of c Heme Trigger the Conformational Change of Crystalline Nitrite Reductase?. Journal of Biological Chemistry. 274(21). 14997–15004. 23 indexed citations
14.
Brown, Kieron, Didier Nurizzo, S Besson, et al.. (1999). MAD Structure of Pseudomonas nautica Dimeric Cytochrome c552Mimicks thec4 Dihemic Cytochrome Domain Association. Journal of Molecular Biology. 289(4). 1017–1028. 28 indexed citations
15.
Campanacci, Valérie, Sonia Longhi, Patricia Nagnan‐Le Meillour, Christian Cambillau, & M. Tegoni. (1999). Recombinant pheromone binding protein 1 from Mamestra brassicae (MbraPBP1). European Journal of Biochemistry. 264(3). 707–716. 38 indexed citations
16.
Maı̈bèche-Coisné, Martine, Sonia Longhi, Emmanuelle Jacquin‐Joly, et al.. (1998). Molecular cloning and bacterial expression of a general odorant-binding protein from the cabbage armyworm Mamestra brassicae. HAL (Le Centre pour la Communication Scientifique Directe). 1 indexed citations
17.
Tegoni, M., Roberto Ramoni, Enrico Bignetti, Silvia Spinelli, & Christian Cambillau. (1996). Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Structural & Molecular Biology. 3(10). 863–867. 169 indexed citations
18.
Tegoni, M. & Christian Cambillau. (1994). The 2.6‐Å refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2‐sulfite complex. Protein Science. 3(2). 303–313. 26 indexed citations
19.
Chen, Longyin, F. Scott Mathews, Victor L. Davidson, et al.. (1993). Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c‐type cytochrome. Protein Science. 2(2). 147–154. 26 indexed citations
20.
Tegoni, M., Scott A. White, Alain Roussel, F. Scott Mathews, & Christian Cambillau. (1993). A hypothetical complex between crystalline flavocytochrome b2 and Cytochrome c. Proteins Structure Function and Bioinformatics. 16(4). 408–422. 18 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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