David Cobessi

1.7k total citations
40 papers, 1.3k citations indexed

About

David Cobessi is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, David Cobessi has authored 40 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 32 papers in Molecular Biology, 13 papers in Materials Chemistry and 10 papers in Genetics. Recurrent topics in David Cobessi's work include Enzyme Structure and Function (12 papers), Bacterial Genetics and Biotechnology (10 papers) and Photosynthetic Processes and Mechanisms (9 papers). David Cobessi is often cited by papers focused on Enzyme Structure and Function (12 papers), Bacterial Genetics and Biotechnology (10 papers) and Photosynthetic Processes and Mechanisms (9 papers). David Cobessi collaborates with scholars based in France, United States and Germany. David Cobessi's co-authors include F. Pattus, Hervé Celia, Edward A. Berry, Li-Shar Huang, F. Favier, Isabelle J. Schalk, Stéphane Marchal, Saı̈d Azza, Karl Brillet and Nicolas Folschweiller and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and The EMBO Journal.

In The Last Decade

David Cobessi

39 papers receiving 1.3k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David Cobessi France 19 902 349 276 249 123 40 1.3k
Dirk-Jan Slotboom Netherlands 22 1.3k 1.5× 474 1.4× 95 0.3× 174 0.7× 93 0.8× 30 1.9k
Ingar Leiros Norway 21 1.3k 1.5× 229 0.7× 104 0.4× 241 1.0× 111 0.9× 49 1.7k
K.H. Kalk Netherlands 13 1.2k 1.3× 274 0.8× 135 0.5× 255 1.0× 103 0.8× 17 1.6k
Faik N. Musayev United States 25 853 0.9× 158 0.5× 73 0.3× 338 1.4× 188 1.5× 64 1.5k
Gareth Butland United States 18 1.7k 1.9× 589 1.7× 100 0.4× 236 0.9× 194 1.6× 25 2.2k
E. Bitto United States 21 946 1.0× 197 0.6× 148 0.5× 192 0.8× 141 1.1× 38 1.4k
Shan Wu China 19 1.4k 1.5× 177 0.5× 365 1.3× 135 0.5× 106 0.9× 45 2.0k
Anil K. Joshi United States 24 1.4k 1.5× 156 0.4× 118 0.4× 342 1.4× 76 0.6× 33 1.9k
Arjan Snijder Sweden 21 1.1k 1.2× 307 0.9× 120 0.4× 102 0.4× 86 0.7× 39 1.5k
Dindial Ramotar Canada 30 2.5k 2.8× 205 0.6× 391 1.4× 71 0.3× 125 1.0× 115 2.9k

Countries citing papers authored by David Cobessi

Since Specialization
Citations

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

Fields of papers citing papers by David Cobessi

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Cobessi

This figure shows the co-authorship network connecting the top 25 collaborators of David Cobessi. A scholar is included among the top collaborators of David Cobessi 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 David Cobessi. David Cobessi 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.
Job, Viviana, Maxime Bour, Mylène Robert‐Genthon, et al.. (2024). Pseudomonas aeruginosa MipA-MipB envelope proteins act as new sensors of polymyxins. mBio. 15(3). e0221123–e0221123. 6 indexed citations
2.
Kieffer‐Jaquinod, Sylvie, François‐Xavier Gillet, Daphna Fenel, et al.. (2022). Three-Dimensional Envelope and Subunit Interactions of the Plastid-Encoded RNA Polymerase from Sinapis alba. International Journal of Molecular Sciences. 23(17). 9922–9922. 11 indexed citations
3.
Liebers, Monique, François‐Xavier Gillet, Fabien Chevalier, et al.. (2020). Nucleo‐plastidic PAP 8/ pTAC 6 couples chloroplast formation with photomorphogenesis. The EMBO Journal. 39(22). e104941–e104941. 30 indexed citations
4.
Curien, Gilles, et al.. (2017). Crystal Structure of the Chloroplastic Oxoene Reductase ceQORH from Arabidopsis thaliana. Frontiers in Plant Science. 8. 329–329. 7 indexed citations
5.
Giustini, Cécile, et al.. (2015). Analytical ultracentrifugation and preliminary X-ray studies of the chloroplast envelope quinone oxidoreductase homologue fromArabidopsis thaliana. Acta Crystallographica Section F Structural Biology Communications. 71(4). 455–458. 2 indexed citations
6.
Curien, Gilles, Cécile Giustini, Jean‐Luc Montillet, et al.. (2015). The chloroplast membrane associated ceQORH putative quinone oxidoreductase reduces long-chain, stress-related oxidized lipids. Phytochemistry. 122. 45–55. 18 indexed citations
7.
Kieffer‐Jaquinod, Sylvie, Andrés Palencia, David Cobessi, et al.. (2014). Biochemical and Biophysical Characterization of the Selenium-binding and Reducing Site in Arabidopsis thaliana Homologue to Mammals Selenium-binding Protein 1. Journal of Biological Chemistry. 289(46). 31765–31776. 29 indexed citations
8.
Dumas, Renaud, et al.. (2011). The many faces of aspartate kinases. Archives of Biochemistry and Biophysics. 519(2). 186–193. 22 indexed citations
9.
Cobessi, David, et al.. (2009). Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: Heme binding by an induced fit mechanism. Proteins Structure Function and Bioinformatics. 78(2). 286–294. 43 indexed citations
10.
Brillet, Karl, et al.. (2009). Use of an in-house approach to study the three-dimensional structures of various outer membrane proteins: structure of the alcaligin outer membrane transporter FauA fromBordetella pertussis. Acta Crystallographica Section D Biological Crystallography. 65(4). 326–331. 7 indexed citations
11.
Wirth, Christophe, Wolfram Meyer‐Klaucke, F. Pattus, & David Cobessi. (2007). From the Periplasmic Signaling Domain to the Extracellular Face of an Outer Membrane Signal Transducer of Pseudomonas aeruginosa: Crystal Structure of the Ferric Pyoverdine Outer Membrane Receptor. Journal of Molecular Biology. 368(2). 398–406. 55 indexed citations
12.
Mislin, Gaëtan L. A., Françoise Hoegy, David Cobessi, et al.. (2006). Binding Properties of Pyochelin and Structurally Related Molecules to FptA of Pseudomonas aeruginosa. Journal of Molecular Biology. 357(5). 1437–1448. 53 indexed citations
13.
14.
Huang, Li-Shar, Gang Sun, David Cobessi, et al.. (2005). 3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme. Journal of Biological Chemistry. 281(9). 5965–5972. 9 indexed citations
15.
Cobessi, David, Hervé Celia, & F. Pattus. (2005). Crystal Structure at High Resolution of Ferric-pyochelin and its Membrane Receptor FptA from Pseudomonas aeruginosa. Journal of Molecular Biology. 352(4). 893–904. 125 indexed citations
16.
Cobessi, David, Hervé Celia, & F. Pattus. (2004). Crystallization and X-ray diffraction analyses of the outer membrane pyochelin receptor FptA fromPseudomonas aeruginosa. Acta Crystallographica Section D Biological Crystallography. 60(10). 1919–1921. 18 indexed citations
17.
Folschweiller, Nicolas, Hervé Celia, Noëlle Potier, et al.. (2004). In vivo incorporation of selenomethionine in proteins using Pseudomonas aeruginosa as expression host: case study—the outer membrane receptor FpvA. Protein Expression and Purification. 38(1). 79–83. 3 indexed citations
18.
Marchal, Stéphane, et al.. (2001). Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans. Chemico-Biological Interactions. 130-132(1-3). 15–28. 24 indexed citations
19.
Cobessi, David, et al.. (2001). The 2.6 Å resolution structure ofRhodobacter capsulatusbacterioferritin with metal-free dinuclear site and heme iron in a crystallographic `special position'. Acta Crystallographica Section D Biological Crystallography. 58(1). 29–38. 31 indexed citations
20.
Favier, F., et al.. (2000). Cellular detoxification: crystal structure of a repair enzyme fromEscherichia coliat 1.9 Å resolution. Acta Crystallographica Section A Foundations of Crystallography. 56(s1). s261–s261. 2 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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