J.-M. Frère

5.1k total citations
108 papers, 4.0k citations indexed

About

J.-M. Frère is a scholar working on Molecular Medicine, Molecular Biology and Nuclear and High Energy Physics. According to data from OpenAlex, J.-M. Frère has authored 108 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Molecular Medicine, 38 papers in Molecular Biology and 29 papers in Nuclear and High Energy Physics. Recurrent topics in J.-M. Frère's work include Antibiotic Resistance in Bacteria (52 papers), Particle physics theoretical and experimental studies (25 papers) and Peptidase Inhibition and Analysis (18 papers). J.-M. Frère is often cited by papers focused on Antibiotic Resistance in Bacteria (52 papers), Particle physics theoretical and experimental studies (25 papers) and Peptidase Inhibition and Analysis (18 papers). J.-M. Frère collaborates with scholars based in Belgium, United States and France. J.-M. Frère's co-authors include Bernard Joris, Moreno Galleni, S Normark, Christine Jacobs, André Matagne, Gianfranco Amicosante, M. Galleni, Rafel Escribano, Jean‐Marie Ghuysen and Jozef Van Beeumen and has published in prestigious journals such as Science, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

J.-M. Frère

106 papers receiving 3.9k citations

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
J.-M. Frère 2.2k 1.4k 875 656 584 108 4.0k
Satoshi Ohya 1.5k 0.7× 914 0.7× 706 0.8× 31 0.0× 352 0.6× 68 2.2k
Robert C. Goldman 362 0.2× 1.7k 1.2× 360 0.4× 19 0.0× 633 1.1× 101 3.6k
James R. Knox 2.5k 1.2× 2.1k 1.5× 1.1k 1.3× 6 0.0× 601 1.0× 83 4.5k
J.A. Brannigan 315 0.1× 3.4k 2.5× 193 0.2× 17 0.0× 807 1.4× 99 5.1k
Dean C. Crick 522 0.2× 3.6k 2.6× 556 0.6× 12 0.0× 1.9k 3.2× 138 6.0k
O. Dideberg 3.5k 1.6× 3.2k 2.3× 1.3k 1.4× 6 0.0× 1.5k 2.6× 156 7.3k
Paola Fucini 211 0.1× 2.9k 2.1× 225 0.3× 32 0.0× 155 0.3× 54 3.7k
Paul C. Moews 1.0k 0.5× 1.2k 0.9× 432 0.5× 6 0.0× 266 0.5× 36 2.5k
R P Ambler 1.5k 0.7× 2.5k 1.8× 533 0.6× 5 0.0× 228 0.4× 59 4.2k
Jean‐Pierre Samama 1.4k 0.7× 2.5k 1.8× 716 0.8× 4 0.0× 314 0.5× 81 4.4k

Countries citing papers authored by J.-M. Frère

Since Specialization
Citations

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

Fields of papers citing papers by J.-M. Frère

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of J.-M. Frère

This figure shows the co-authorship network connecting the top 25 collaborators of J.-M. Frère. A scholar is included among the top collaborators of J.-M. Frère 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 J.-M. Frère. J.-M. Frère 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.
Frère, J.-M., et al.. (2016). Neutrino hierarchy and fermion spectrum from a single family in six dimensions: realistic predictions.
2.
Vandevenne, Marylène, et al.. (2008). Rapid and easy development of versatile tools to study protein/ligand interactions. Protein Engineering Design and Selection. 21(7). 443–451. 9 indexed citations
3.
Schofield, Christopher J., et al.. (2004). The inhibition of metallo-β-lactamase by thioxo-cephalosporin derivatives. Bioorganic & Medicinal Chemistry Letters. 14(7). 1737–1739. 17 indexed citations
4.
Docquier, Jean‐Denis, et al.. (2003). Functional heterogeneity of VIM-type metallo-beta-lactamases Identification of residues critical to substrate binding. 43. 74. 1 indexed citations
5.
Moali, Catherine, Christine Anne, Josette Lamotte‐Brasseur, et al.. (2003). Analysis of the Importance of the Metallo-β-Lactamase Active Site Loop in Substrate Binding and Catalysis. Chemistry & Biology. 10(4). 319–329. 109 indexed citations
6.
Mercuri, Paola Sandra, Yoshikazu Ishii, Ling Ma, et al.. (2002). Clonal Diversity and Metallo- β -Lactamase Production in Clinical Isolates of Stenotrophomonas maltophilia. Microbial Drug Resistance. 8(3). 193–200. 20 indexed citations
7.
Seny, Dominique de, Carine Bebrone, Gian María Rossolini, et al.. (2002). Mutational analysis of the two zinc-binding sites of the Bacillus cereus 569/H/9 metallo-β-lactamase. Biochemical Journal. 363(3). 687–687. 40 indexed citations
8.
Lejeune, Annabelle, Marc Vanhove, Josette Lamotte‐Brasseur, et al.. (2001). Quantitative analysis of the stabilization by substrate of Staphylococcus aureus PC1 β-lactamase. Chemistry & Biology. 8(8). 831–842. 27 indexed citations
9.
Lee, Hwei‐Jen, Matthew D. Lloyd, I.J. Clifton, et al.. (2001). Alteration of the Co-substrate Selectivity of Deacetoxycephalosporin C Synthase. Journal of Biological Chemistry. 276(21). 18290–18295. 26 indexed citations
10.
Dubus, Alain, et al.. (2001). Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase. Cellular and Molecular Life Sciences. 58(5). 835–843. 24 indexed citations
11.
Bompard-Gilles, Coralie, Han Remaut, Vincent Villeret, et al.. (2000). Crystal structure of a d-aminopeptidase from Ochrobactrum anthropi, a new member of the ‘penicillin-recognizing enzyme’ family. Structure. 8(9). 971–980. 38 indexed citations
12.
Carfı́, Andrea, et al.. (1998). X-ray Structure of the ZnII β-Lactamase from Bacteroides fragilis in an Orthorhombic Crystal Form. Acta Crystallographica Section D Biological Crystallography. 54(1). 47–57. 54 indexed citations
13.
Carfı́, Andrea, et al.. (1997). Purification, crystallization and preliminary X-ray analysis ofBacteroides fragilisZn2+β-lactamase. Acta Crystallographica Section D Biological Crystallography. 53(4). 485–487. 9 indexed citations
14.
Lamotte‐Brasseur, Josette, James R. Knox, Judith A. Kelly, et al.. (1994). The Structures and Catalytic Mechanisms of Active-Site Serine β-Lactamases. Biotechnology and Genetic Engineering Reviews. 12(1). 189–230. 37 indexed citations
15.
Matagne, André, Josette Lamotte‐Brasseur, & J.-M. Frère. (1993). Interactions between active‐site serine β‐lactamases and so‐called β‐lactamase‐stable antibiotics. European Journal of Biochemistry. 217(1). 61–67. 16 indexed citations
16.
Monnaie, Didier & J.-M. Frère. (1993). Interaction of clavulanate with class C β‐lactamases. FEBS Letters. 334(3). 269–271. 21 indexed citations
17.
Amicosante, Gianfranco, J.-M. Frère, Nicola Franceschini, A Oratore, & Roberto Ström. (1991). Some Molecular Properties ofCitrobacter diversusBeta-Lactamases. Journal of Chemotherapy. 3(2). 83–85. 2 indexed citations
18.
Frère, J.-M., et al.. (1989). How to elucidate the mechanism ofCPviolation. Physical review. D. Particles, fields, gravitation, and cosmology/Physical review. D. Particles and fields. 39(9). 2633–2638. 14 indexed citations
19.
Knox, James R., et al.. (1989). Crystallographic mapping of β-lactams bound to a d-alanyl-d-alanine peptidase target enzyme. Journal of Molecular Biology. 209(2). 281–295. 93 indexed citations
20.

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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