F.A. Saul

1.5k total citations
23 papers, 1.2k citations indexed

About

F.A. Saul is a scholar working on Molecular Biology, Radiology, Nuclear Medicine and Imaging and Epidemiology. According to data from OpenAlex, F.A. Saul has authored 23 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 16 papers in Molecular Biology, 9 papers in Radiology, Nuclear Medicine and Imaging and 6 papers in Epidemiology. Recurrent topics in F.A. Saul's work include Glycosylation and Glycoproteins Research (10 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and Protein purification and stability (5 papers). F.A. Saul is often cited by papers focused on Glycosylation and Glycoproteins Research (10 papers), Monoclonal and Polyclonal Antibodies Research (9 papers) and Protein purification and stability (5 papers). F.A. Saul collaborates with scholars based in France, United States and Poland. F.A. Saul's co-authors include Roberto J. Poljak, L. Mario Amzel, R. P. Phizackerley, H. P. AVEY, G.A. Bentley, Frank F. Richards, János Varga, B. Vulliez-Le Normand, J.M. Betton and Richard Kahn and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

F.A. Saul

23 papers receiving 1.0k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
F.A. Saul France 11 918 615 256 151 87 23 1.2k
Bradford C. Braden United States 21 1.1k 1.2× 654 1.1× 365 1.4× 307 2.0× 121 1.4× 34 1.7k
A.G. Amit France 8 1.0k 1.1× 901 1.5× 358 1.4× 159 1.1× 60 0.7× 10 1.5k
Klaas Decanniere Belgium 17 1.3k 1.4× 924 1.5× 304 1.2× 185 1.2× 51 0.6× 31 1.7k
Walter Palm Austria 12 1.2k 1.3× 797 1.3× 264 1.0× 320 2.1× 190 2.2× 20 1.5k
Maria Sakarellos‐Daitsiotis Greece 22 756 0.8× 492 0.8× 316 1.2× 78 0.5× 45 0.5× 103 1.6k
G. Boulot France 17 1.3k 1.4× 1.1k 1.9× 665 2.6× 236 1.6× 61 0.7× 30 1.9k
Rebecca To Canada 19 774 0.8× 461 0.7× 145 0.6× 59 0.4× 48 0.6× 24 1.0k
Edelmira Cabezas United States 12 1.1k 1.2× 271 0.4× 386 1.5× 66 0.4× 55 0.6× 13 1.7k
Milan Fábry Czechia 21 750 0.8× 309 0.5× 128 0.5× 139 0.9× 49 0.6× 82 1.3k
W.R. Tulip Australia 9 1.1k 1.2× 1.1k 1.8× 350 1.4× 136 0.9× 31 0.4× 11 1.6k

Countries citing papers authored by F.A. Saul

Since Specialization
Citations

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

Fields of papers citing papers by F.A. Saul

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by F.A. Saul. 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 F.A. Saul. The network helps show where F.A. Saul may publish in the future.

Co-authorship network of co-authors of F.A. Saul

This figure shows the co-authorship network connecting the top 25 collaborators of F.A. Saul. A scholar is included among the top collaborators of F.A. Saul 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 F.A. Saul. F.A. Saul 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.
Tardy, Florence, et al.. (2025). Detection of Mycoplasma spp. from snakes from five different families. BMC Veterinary Research. 21(1). 38–38. 1 indexed citations
2.
Saul, F.A., et al.. (2024). Western equine encephalitis, a report of two cases in pediatric patients. Archivos Argentinos de Pediatria. 123(1). e202410383–e202410383. 1 indexed citations
3.
Melo, Guilherme Dias de, Nicolas Gouault, Sophie Goyard, et al.. (2018). Designed mono- and di-covalent inhibitors trap modeled functional motions for Trypanosoma cruzi proline racemase in crystallography. PLoS neglected tropical diseases. 12(10). e0006853–e0006853. 5 indexed citations
4.
Normand, B. Vulliez-Le, F.A. Saul, Armelle Phalipon, et al.. (2008). Structures of synthetic O-antigen fragments from serotype 2aShigella flexneriin complex with a protective monoclonal antibody. Proceedings of the National Academy of Sciences. 105(29). 9976–9981. 70 indexed citations
5.
Saul, F.A., Jean‐Philippe Arié, B. Vulliez-Le Normand, et al.. (2003). Structural and Functional Studies of FkpA from Escherichia coli, a cis/trans Peptidyl-prolyl Isomerase with Chaperone Activity. Journal of Molecular Biology. 335(2). 595–608. 104 indexed citations
6.
Saul, F.A., et al.. (2000). Structure of the Fab fragment from F124, a monoclonal antibody specific for hepatitis B surface antigen. Acta Crystallographica Section D Biological Crystallography. 56(8). 945–951. 2 indexed citations
7.
8.
Saul, F.A., et al.. (1997). Crystal structure of a recombinant form of the maltodextrin-binding protein carrying an inserted sequence of a B-cell epitope from the preS2 region of hepatitis B virus. Proteins Structure Function and Bioinformatics. 27(1). 1–8. 11 indexed citations
9.
10.
Saul, F.A.. (1994). Structural implications of VH sequence patterns. Research in Immunology. 145(1). 61–66. 6 indexed citations
11.
Tello, Diana, S. Spinelli, H. Souchon, et al.. (1990). Three-dimensional structure and antigen binding specificity of antibodies. Biochimie. 72(8). 507–512. 16 indexed citations
12.
Saul, F.A. & Roberto J. Poljak. (1985). Three-dimensional structure and function of immunoglobulins. Annales de l Institut Pasteur Immunologie. 136(2). 259–259. 2 indexed citations
13.
Amit, A.G., G. Boulot, Roy A. Mariuzza, et al.. (1985). X-ray diffraction studiesof an anti-azophenylarsonate antibody and of an antigen-antibody complex. Annales de l Institut Pasteur Immunologie. 136(1). 121–129. 2 indexed citations
14.
Mariuzza, Roy A., A.G. Amit, G. Boulot, et al.. (1984). Crystallization of the fab fragments of monoclonal anti-p-azophenylarsonate antibodies and their complexes with haptens.. Journal of Biological Chemistry. 259(9). 5954–5958. 10 indexed citations
15.
Saul, F.A., L. Mario Amzel, & Roberto J. Poljak. (1978). Preliminary refinement and structural analysis of the Fab fragment from human immunoglobulin new at 2.0 A resolution.. Journal of Biological Chemistry. 253(2). 585–597. 262 indexed citations
16.
Poljak, Roberto J., et al.. (1975). Structure and specificity of antibody molecules. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 272(915). 43–51. 10 indexed citations
17.
18.
Poljak, Roberto J., et al.. (1974). The Three-Dimensional Structure of the Fab′ Fragment of a Human Myeloma Immunoglobulin at 2.0-Å Resolution. Proceedings of the National Academy of Sciences. 71(9). 3440–3444. 166 indexed citations
19.
Amzel, L. Mario, Roberto J. Poljak, F.A. Saul, János Varga, & Frank F. Richards. (1974). The Three Dimensional Structure of a Combining Region-Ligand Complex of Immunoglobulin NEW at 3.5-Å Resolution. Proceedings of the National Academy of Sciences. 71(4). 1427–1430. 169 indexed citations
20.
Poljak, Roberto J., et al.. (1973). Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution. Proceedings of the National Academy of Sciences. 70(12). 3305–3310. 285 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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