L. Salmon

2.2k total citations
66 papers, 1.7k citations indexed

About

L. Salmon is a scholar working on Materials Chemistry, Molecular Biology and Physiology. According to data from OpenAlex, L. Salmon has authored 66 papers receiving a total of 1.7k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Materials Chemistry, 21 papers in Molecular Biology and 20 papers in Physiology. Recurrent topics in L. Salmon's work include Erythrocyte Function and Pathophysiology (19 papers), Enzyme Structure and Function (16 papers) and Diet, Metabolism, and Disease (13 papers). L. Salmon is often cited by papers focused on Erythrocyte Function and Pathophysiology (19 papers), Enzyme Structure and Function (16 papers) and Diet, Metabolism, and Disease (13 papers). L. Salmon collaborates with scholars based in France, United States and Sweden. L. Salmon's co-authors include R. Gaertner, Nathalie Godin, Renaud Hardré, Constance J. Jeffery, Emmanuel S. Burgos, E. Vors, Jean‐Philip Piquemal, Nohad Gresh, Kenneth L. Brown and H. Daniel Wagner and has published in prestigious journals such as Proceedings of the National Academy of Sciences, The Lancet and Journal of Biological Chemistry.

In The Last Decade

L. Salmon

65 papers receiving 1.7k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
L. Salmon France 24 563 516 401 245 207 66 1.7k
Susumu Nakamura Japan 25 499 0.9× 322 0.6× 278 0.7× 154 0.6× 213 1.0× 184 2.3k
Takashi Satoh Japan 30 857 1.5× 330 0.6× 580 1.4× 113 0.5× 69 0.3× 137 3.8k
George Y. Chen China 32 808 1.4× 76 0.1× 270 0.7× 223 0.9× 80 0.4× 117 4.1k
Donald L. Hunston United States 27 568 1.0× 817 1.6× 285 0.7× 785 3.2× 517 2.5× 88 3.0k
Peili Chen United States 24 784 1.4× 84 0.2× 366 0.9× 78 0.3× 98 0.5× 73 1.9k
Kui Chen China 32 992 1.8× 68 0.1× 1.1k 2.9× 186 0.8× 114 0.6× 129 3.9k
Chao Tian China 25 629 1.1× 109 0.2× 326 0.8× 48 0.2× 108 0.5× 109 2.0k
Yoshikazu Takahashi Japan 29 457 0.8× 158 0.3× 454 1.1× 265 1.1× 514 2.5× 276 3.4k
Zirui Li China 28 432 0.8× 151 0.3× 323 0.8× 618 2.5× 88 0.4× 152 3.1k
Yihua Liu China 23 312 0.6× 214 0.4× 249 0.6× 301 1.2× 112 0.5× 157 2.0k

Countries citing papers authored by L. Salmon

Since Specialization
Citations

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

Fields of papers citing papers by L. Salmon

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of L. Salmon

This figure shows the co-authorship network connecting the top 25 collaborators of L. Salmon. A scholar is included among the top collaborators of L. Salmon 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 L. Salmon. L. Salmon 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.
Salmon, L., et al.. (2025). A thermo-mechanical cohesive zone model for damage and healing in brittle solids. Computational Mechanics. 77(2). 501–520.
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Islam, Zeyaul, et al.. (2015). Structural Basis for Competitive Inhibition of 3,4-Dihydroxy-2-butanone-4-phosphate Synthase from Vibrio cholerae. Journal of Biological Chemistry. 290(18). 11293–11308. 16 indexed citations
4.
Courcy, Benoît de, et al.. (2010). The reaction mechanism of type I phosphomannose isomerases: New information from inhibition and polarizable molecular mechanics studies. Proteins Structure Function and Bioinformatics. 79(1). 203–220. 22 indexed citations
5.
Kapetaniou, Evangelia G., Marja Lajunen, Marco G. Casteleijn, et al.. (2010). Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase. Acta Crystallographica Section D Biological Crystallography. 66(8). 934–944. 10 indexed citations
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Brouns, Stan J. J., T.R.M. Barends, Petra Worm, et al.. (2008). Structural Insight into Substrate Binding and Catalysis of a Novel 2-Keto-3-deoxy-d-arabinonate Dehydratase Illustrates Common Mechanistic Features of the FAH Superfamily. Journal of Molecular Biology. 379(2). 357–371. 36 indexed citations
9.
Brouns, Stan J. J., Ambrosius P. Snijders, Harmen J.G. van de Werken, et al.. (2006). Identification of the Missing Links in Prokaryotic Pentose Oxidation Pathways. Journal of Biological Chemistry. 281(37). 27378–27388. 92 indexed citations
10.
Salmon, L., et al.. (2006). Preliminary studies on the inhibition of D-sorbitol-6-phosphate 2–dehydrogenase fromEscherichia coliwith substrate analogues. Journal of Enzyme Inhibition and Medicinal Chemistry. 21(2). 187–192. 8 indexed citations
11.
Vors, E. & L. Salmon. (2006). Laser-induced breakdown spectroscopy (LIBS) for carbon single shot analysis of micrometer-sized particles. Analytical and Bioanalytical Chemistry. 385(2). 281–286. 29 indexed citations
12.
Cordeiro, Artur T., et al.. (2004). Leishmania mexicana mexicanaglucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition. Acta Crystallographica Section D Biological Crystallography. 60(5). 915–919. 8 indexed citations
13.
Berrisford, John M., Jasper Akerboom, Stan J. J. Brouns, et al.. (2004). The Structures of Inhibitor Complexes of Pyrococcus furiosus Phosphoglucose Isomerase Provide Insights into Substrate Binding and Catalysis. Journal of Molecular Biology. 343(3). 649–657. 18 indexed citations
14.
Roos, A.K., Emmanuel S. Burgos, Daniel J. Ericsson, L. Salmon, & Sherry L. Mowbray. (2004). Competitive Inhibitors of Mycobacterium tuberculosis Ribose-5-phosphate Isomerase B Reveal New Information about the Reaction Mechanism. Journal of Biological Chemistry. 280(8). 6416–6422. 35 indexed citations
15.
Cervellati, Carlo, et al.. (2003). Sugar derivatives as new 6-phosphogluconate dehydrogenase inhibitors selective for the parasite Trypanosoma brucei. Bioorganic & Medicinal Chemistry. 11(7). 1207–1214. 17 indexed citations
16.
Salmon, L., Élise Prost, C. Mérienne, Renaud Hardré, & Georges Morgant. (2001). A convenient preparation of aldonohydroxamic acids in water and crystal structure of l-erythronohydroxamic acid. Carbohydrate Research. 335(3). 195–204. 13 indexed citations
17.
Hardré, Renaud, L. Salmon, & Fred R. Opperdoes. (2000). Competitive Inhibition of Trypanosoma Brucei Phosphoglucose Isomerase by D-Arabinose-5-Phosphate Derivatives. Journal of enzyme inhibition. 15(5). 509–515. 15 indexed citations
18.
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Hardré, Renaud, et al.. (1998). Synthesis and evaluation of a new inhibitor of phosphoglucose isomerases: the enediolate analogue 5-phospho-D-arabinohydroxamate. Bioorganic & Medicinal Chemistry Letters. 8(23). 3435–3438. 29 indexed citations
20.
Brown, Kenneth L., Xiang Zou, & L. Salmon. (1991). Facile .alpha./.beta. diastereomerism in organocobalt corrins. Generality of the phenomenon and characterization of additional .alpha.-diastereomers. Inorganic Chemistry. 30(8). 1949–1953. 24 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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