S. Petrella

1.7k total citations
32 papers, 1.3k citations indexed

About

S. Petrella is a scholar working on Molecular Biology, Infectious Diseases and Molecular Medicine. According to data from OpenAlex, S. Petrella has authored 32 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 14 papers in Infectious Diseases and 14 papers in Molecular Medicine. Recurrent topics in S. Petrella's work include Tuberculosis Research and Epidemiology (14 papers), Antibiotic Resistance in Bacteria (14 papers) and Cancer therapeutics and mechanisms (13 papers). S. Petrella is often cited by papers focused on Tuberculosis Research and Epidemiology (14 papers), Antibiotic Resistance in Bacteria (14 papers) and Cancer therapeutics and mechanisms (13 papers). S. Petrella collaborates with scholars based in France, Belgium and United States. S. Petrella's co-authors include Vincent Jarlier, Wladimir Sougakoff, Claudine Mayer, Alexandra Aubry, Aurélie Chauffour, E. Sauvage, P. Charlier, R. Herman, Emmanuelle Cambau and Frédéric Kerff and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nucleic Acids Research and Journal of Biological Chemistry.

In The Last Decade

S. Petrella

32 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
S. Petrella France 20 687 544 393 377 148 32 1.3k
Silvia Buroni Italy 23 848 1.2× 446 0.8× 381 1.0× 361 1.0× 169 1.1× 54 1.6k
M. Inês Borges‐Walmsley United Kingdom 20 521 0.8× 316 0.6× 389 1.0× 316 0.8× 140 0.9× 28 1.3k
Anne Lemassu France 24 757 1.1× 951 1.7× 159 0.4× 997 2.6× 136 0.9× 41 1.9k
Jaiyanth Daniel United States 14 748 1.1× 1.1k 2.1× 309 0.8× 854 2.3× 49 0.3× 20 1.8k
Luke J. Alderwick United Kingdom 27 1.3k 1.9× 715 1.3× 174 0.4× 594 1.6× 129 0.9× 54 2.1k
Jamese J. Hilliard United States 19 675 1.0× 491 0.9× 250 0.6× 180 0.5× 36 0.2× 37 1.4k
Sarah Schmidt Grant United States 12 541 0.8× 415 0.8× 199 0.5× 243 0.6× 29 0.2× 19 1.1k
Vinod S. Dubey United States 17 788 1.1× 1.0k 1.9× 255 0.6× 834 2.2× 111 0.8× 21 1.7k
Ute Müh United States 16 691 1.0× 415 0.8× 175 0.4× 486 1.3× 32 0.2× 26 1.5k
Andrej Trauner Switzerland 17 749 1.1× 745 1.4× 183 0.5× 615 1.6× 54 0.4× 24 1.4k

Countries citing papers authored by S. Petrella

Since Specialization
Citations

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

Fields of papers citing papers by S. Petrella

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of S. Petrella

This figure shows the co-authorship network connecting the top 25 collaborators of S. Petrella. A scholar is included among the top collaborators of S. Petrella 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 S. Petrella. S. Petrella 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.
Piveteau, Catherine, Anne Marie Wehenkel, Francesca Gubellini, et al.. (2024). Molecular mechanism of a triazole-containing inhibitor of Mycobacterium tuberculosis DNA gyrase. iScience. 27(10). 110967–110967. 4 indexed citations
2.
Giacomelli, Giacomo, Ahmed Haouz, Peng Feng, et al.. (2023). The MksG nuclease is the executing part of the bacterial plasmid defense system MksBEFG. Nucleic Acids Research. 51(7). 3288–3306. 15 indexed citations
3.
Gadelle, Danièle, Keli Agama, Evgeny Kiselev, et al.. (2022). Topoisomerase I (TOP1) dynamics: conformational transition from open to closed states. Nature Communications. 13(1). 59–59. 20 indexed citations
4.
Chauffour, Aurélie, F. Morel, Florence Reibel, et al.. (2021). A systematic review of Mycobacterium leprae DNA gyrase mutations and their impact on fluoroquinolone resistance. Clinical Microbiology and Infection. 27(11). 1601–1612. 12 indexed citations
5.
Petrella, S., Bertrand Raynal, Aurélien Thureau, et al.. (2019). Overall Structures of Mycobacterium tuberculosis DNA Gyrase Reveal the Role of a Corynebacteriales GyrB-Specific Insert in ATPase Activity. Structure. 27(4). 579–589.e5. 32 indexed citations
6.
Bedini, Andrea, Elisa Garlassi, Chiara Stentarelli, et al.. (2016). Multidrug-resistant tuberculosis outbreak in an Italian prison: tolerance of pyrazinamide plus levofloxacin prophylaxis and serial interferon gamma release assays. New Microbes and New Infections. 12. 45–51. 5 indexed citations
7.
8.
Pantel, Alix, S. Petrella, Nicolas Véziris, et al.. (2016). Description of compensatorygyrAmutations restoring fluoroquinolone susceptibility inMycobacterium tuberculosis. Journal of Antimicrobial Chemotherapy. 71(9). 2428–2431. 9 indexed citations
9.
Agrawal, Alka, Mélanie Roué, Claus Spitzfaden, et al.. (2013). Mycobacterium tuberculosis DNA gyrase ATPase domain structures suggest a dissociative mechanism that explains how ATP hydrolysis is coupled to domain motion. Biochemical Journal. 456(2). 263–273. 40 indexed citations
10.
Piton, Jérémie, Mélanie Roué, S. Petrella, et al.. (2013). Mycobacterium tuberculosis DNA gyrase possesses two functional GyrA-boxes. Biochemical Journal. 455(3). 285–294. 28 indexed citations
11.
Bonnafous, Pascale, S. Petrella, Claire Deback, et al.. (2010). Conservation of HHV-6 DNA polymerase processivity factor sequence and predicted structure suggests it as a target for antiviral development. Antiviral Research. 86(3). 316–319. 2 indexed citations
12.
Piton, Jérémie, S. Petrella, Marc Delarue, et al.. (2010). Structural Insights into the Quinolone Resistance Mechanism of Mycobacterium tuberculosis DNA Gyrase. PLoS ONE. 5(8). e12245–e12245. 119 indexed citations
13.
Piton, Jérémie, Stéphanie Matrat, S. Petrella, et al.. (2009). Purification, crystallization and preliminary X-ray diffraction experiments on the breakage-reunion domain of the DNA gyrase fromMycobacterium tuberculosis. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(11). 1182–1186. 8 indexed citations
14.
Kerff, Frédéric, S. Petrella, F. Mercier, et al.. (2009). Specific Structural Features of the N-Acetylmuramoyl-l-Alanine Amidase AmiD from Escherichia coli and Mechanistic Implications for Enzymes of This Family. Journal of Molecular Biology. 397(1). 249–259. 42 indexed citations
15.
Kerff, Frédéric, Ana Amoroso, R. Herman, et al.. (2008). Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization. Proceedings of the National Academy of Sciences. 105(44). 16876–16881. 166 indexed citations
16.
Sauvage, E., Colette Duez, R. Herman, et al.. (2007). Crystal Structure of the Bacillus subtilis Penicillin-binding Protein 4a, and its Complex with a Peptidoglycan Mimetic Peptide. Journal of Molecular Biology. 371(2). 528–539. 45 indexed citations
17.
Sauvage, E., R. Herman, S. Petrella, et al.. (2005). Crystal Structure of the Actinomadura R39 DD-peptidase Reveals New Domains in Penicillin-binding Proteins. Journal of Biological Chemistry. 280(35). 31249–31256. 45 indexed citations
18.
Petrella, S., et al.. (2005). Characterization of the chromosomal class A β-lactamase CKO fromCitrobacter koseri. FEMS Microbiology Letters. 254(2). 285–292. 14 indexed citations
19.
Petrella, S., L. Pernot, & Wladimir Sougakoff. (2003). Crystallization and preliminary X-ray diffraction study of the class A β-lactamase SED-1 and its mutant SED-G238C fromCitrobacter sedlakii. Acta Crystallographica Section D Biological Crystallography. 60(1). 125–128. 1 indexed citations
20.
Pernot, L., Frédéric Frénois, Tania Rybkine, et al.. (2001). Crystal structures of the class D β-lactamase OXA-13 in the native form and in complex with meropenem. Journal of Molecular Biology. 310(4). 859–874. 57 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.

Explore authors with similar magnitude of impact

Breakdown of academic impact, for papers by Silvia Buroni Breakdown of academic impact, for papers by M. Inês Borges‐Walmsley Breakdown of academic impact, for papers by Anne Lemassu Breakdown of academic impact, for papers by Jaiyanth Daniel Breakdown of academic impact, for papers by Luke J. Alderwick Breakdown of academic impact, for papers by Jamese J. Hilliard Breakdown of academic impact, for papers by Sarah Schmidt Grant Breakdown of academic impact, for papers by Vinod S. Dubey Breakdown of academic impact, for papers by Ute Müh Breakdown of academic impact, for papers by Andrej Trauner
Rankless by CCL
2026