Clemente Capasso

12.6k total citations
314 papers, 10.3k citations indexed

About

Clemente Capasso is a scholar working on Molecular Biology, Organic Chemistry and Pharmacology. According to data from OpenAlex, Clemente Capasso has authored 314 papers receiving a total of 10.3k indexed citations (citations by other indexed papers that have themselves been cited), including 268 papers in Molecular Biology, 124 papers in Organic Chemistry and 112 papers in Pharmacology. Recurrent topics in Clemente Capasso's work include Enzyme function and inhibition (250 papers), Cholinesterase and Neurodegenerative Diseases (110 papers) and Phenothiazines and Benzothiazines Synthesis and Activities (107 papers). Clemente Capasso is often cited by papers focused on Enzyme function and inhibition (250 papers), Cholinesterase and Neurodegenerative Diseases (110 papers) and Phenothiazines and Benzothiazines Synthesis and Activities (107 papers). Clemente Capasso collaborates with scholars based in Italy, Saudi Arabia and Australia. Clemente Capasso's co-authors include Claudiu T. Supuran, Sonia Del Prete, Viviana De Luca, Daniela Vullo, Vincenzo Carginale, Andrea Scozzafava, Alessio Nocentini, Mosé Rossi, Zeid A. ALOthman and Sameh M. Osman and has published in prestigious journals such as Journal of the American Chemical Society, SHILAP Revista de lepidopterología and PLoS ONE.

In The Last Decade

Clemente Capasso

309 papers receiving 10.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Clemente Capasso Italy	54	8.5k	4.4k	3.3k	1.2k	634	314	10.3k
Michael D. Burkart United States	51	5.6k 0.7×	2.7k 0.6×	2.4k 0.7×	56 0.0×	125 0.2×	260	9.7k
Teruhiko Beppu Japan	54	7.3k 0.9×	938 0.2×	2.4k 0.7×	84 0.1×	194 0.3×	394	10.4k
Burt Zerner Australia	38	3.6k 0.4×	974 0.2×	424 0.1×	161 0.1×	305 0.5×	113	6.9k
Gerhard Schenk Australia	49	3.0k 0.4×	1.2k 0.3×	347 0.1×	65 0.1×	198 0.3×	234	7.2k
Timothy D. H. Bugg United Kingdom	53	5.5k 0.7×	1.6k 0.4×	882 0.3×	25 0.0×	164 0.3×	192	11.7k
Anna Laura Capriotti Italy	46	3.5k 0.4×	212 0.0×	533 0.2×	88 0.1×	132 0.2×	202	7.6k
Paweł Kafarski Poland	43	2.3k 0.3×	4.7k 1.1×	214 0.1×	64 0.1×	70 0.1×	301	8.3k
Isabelle J. Schalk France	47	2.9k 0.3×	596 0.1×	963 0.3×	33 0.0×	60 0.1×	114	5.9k
Ishtiaq Ahmed Germany	33	1.2k 0.1×	787 0.2×	483 0.1×	54 0.0×	313 0.5×	186	3.8k
Huan Wang China	39	2.3k 0.3×	1.8k 0.4×	513 0.2×	23 0.0×	231 0.4×	293	5.1k

Countries citing papers authored by Clemente Capasso

Since Specialization

Citations

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

Fields of papers citing papers by Clemente Capasso

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Clemente Capasso

This figure shows the co-authorship network connecting the top 25 collaborators of Clemente Capasso. A scholar is included among the top collaborators of Clemente Capasso 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 Clemente Capasso. Clemente Capasso is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Luca, Viviana De, et al.. (2025). Acetazolamide-Loaded Nanoparticle Based on Modified Hyaluronic Acid as Delivery System to Target Carbonic Anhydrases in Escherichia coli. International Journal of Molecular Sciences. 26(10). 4908–4908.

Bonardi, Alessandro, Simone Carradori, Andrea Angeli, et al.. (2025). Production, crystallographic studies, and functional profiling of γ-carbonic anhydrase from the probiotic Limosilactobacillus reuteri: In vitro and cell-based insights. European Journal of Medicinal Chemistry. 302(Pt 1). 118291–118291.

D’Agostino, Ilaria, Andrea Angeli, Simone Carradori, et al.. (2024). Inhibition of Pseudomonas aeruginosa Carbonic Anhydrases, Exploring Ciprofloxacin Functionalization Toward New Antibacterial Agents: An In-Depth Multidisciplinary Study. Journal of Medicinal Chemistry. 67(21). 19077–19102. 9 indexed citations

D’Agostino, Ilaria, Valentina Puca, Valentina Crocetta, et al.. (2024). Cyclization of acyl thiosemicarbazides led to new Helicobacter pylori α‐carbonic anhydrase inhibitors. Archiv der Pharmazie. 357(11). e2400548–e2400548. 9 indexed citations

Abdoli, Morteza, Viviana De Luca, Clemente Capasso, Claudiu T. Supuran, & Raivis Žalubovskis. (2023). Inhibition Studies on Carbonic Anhydrase Isoforms I, II, IX, and XII with a Series of Sulfaguanidines. ChemMedChem. 18(6). e202200658–e202200658. 9 indexed citations

Giovannuzzi, Simone, Viviana De Luca, Clemente Capasso, & Claudiu T. Supuran. (2023). Inhibition studies with simple and complex (in)organic anions of the γ-carbonic anhydrase from Mammaliicoccus (Staphylococcus) sciuri, MscCAγ. Journal of Enzyme Inhibition and Medicinal Chemistry. 38(1). 2173748–2173748. 5 indexed citations

Abdoli, Morteza, Viviana De Luca, Clemente Capasso, Claudiu T. Supuran, & Raivis Žalubovskis. (2023). Novel thiazolone-benzenesulphonamide inhibitors of human and bacterial carbonic anhydrases. Journal of Enzyme Inhibition and Medicinal Chemistry. 38(1). 2163243–2163243. 9 indexed citations

Fiore, Anna Di, Viviana De Luca, Emma Langella, et al.. (2022). Biochemical, structural, and computational studies of a γ-carbonic anhydrase from the pathogenic bacterium Burkholderia pseudomallei. Computational and Structural Biotechnology Journal. 20. 4185–4194. 18 indexed citations

Luca, Viviana De, Vincenzo Carginale, Claudiu T. Supuran, & Clemente Capasso. (2022). The gram-negative bacterium Escherichia coli as a model for testing the effect of carbonic anhydrase inhibition on bacterial growth. Journal of Enzyme Inhibition and Medicinal Chemistry. 37(1). 2092–2098. 25 indexed citations

10.

Grande, Rossella, Simone Carradori, Valentina Puca, et al.. (2021). Selective Inhibition of Helicobacter pylori Carbonic Anhydrases by Carvacrol and Thymol Could Impair Biofilm Production and the Release of Outer Membrane Vesicles. International Journal of Molecular Sciences. 22(21). 11583–11583. 48 indexed citations

11.

Petreni, Andrea, Viviana De Luca, Andrea Scaloni, et al.. (2021). Anion inhibition studies of the Zn(II)-bound ι-carbonic anhydrase from the Gram-negative bacterium Burkholderia territorii. Journal of Enzyme Inhibition and Medicinal Chemistry. 36(1). 372–376. 22 indexed citations

12.

Shaldam, Moataz A., Alessio Nocentini, Zainab M. Elsayed, et al.. (2021). Development of Novel Quinoline-Based Sulfonamides as Selective Cancer-Associated Carbonic Anhydrase Isoform IX Inhibitors. International Journal of Molecular Sciences. 22(20). 11119–11119. 27 indexed citations

13.

Prete, Sonia Del, Viviana De Luca, Alessio Nocentini, et al.. (2020). Anion Inhibition Studies of the Beta-Carbonic Anhydrase from Escherichia coli. Molecules. 25(11). 2564–2564. 22 indexed citations

14.

Capasso, Clemente, Alessio Nocentini, & Claudiu T. Supuran. (2020). Protease inhibitors targeting the main protease and papain-like protease of coronaviruses. Expert Opinion on Therapeutic Patents. 31(4). 309–324. 23 indexed citations

15.

Angeli, Andrea, Mariana Pinteală, Stelian S. Maier, et al.. (2020). Evaluation of Thio- and Seleno-Acetamides Bearing Benzenesulfonamide as Inhibitor of Carbonic Anhydrases from Different Pathogenic Bacteria. International Journal of Molecular Sciences. 21(2). 598–598. 17 indexed citations

16.

Angeli, Andrea, Marta Ferraroni, Mariana Pinteală, et al.. (2020). Crystal Structure of a Tetrameric Type II β-Carbonic Anhydrase from the Pathogenic Bacterium Burkholderia pseudomallei. Molecules. 25(10). 2269–2269. 12 indexed citations

17.

Angeli, Andrea, Stelian S. Maier, William A. Donald, et al.. (2019). The first activation study of the β-carbonic anhydrases from the pathogenic bacteria Brucella suis and Francisella tularensis with amines and amino acids. Journal of Enzyme Inhibition and Medicinal Chemistry. 34(1). 1178–1185. 9 indexed citations

18.

Bua, Silvia, Sameh M. Osman, Sonia Del Prete, et al.. (2019). Click-tailed benzenesulfonamides as potent bacterial carbonic anhydrase inhibitors for targeting Mycobacterium tuberculosis and Vibrio cholerae. Bioorganic Chemistry. 86. 183–186. 18 indexed citations

19.

Vita, Daniela De, Andrea Angeli, Fabiana Pandolfi, et al.. (2017). Inhibition of the α-carbonic anhydrase fromVibrio choleraewith amides and sulfonamides incorporating imidazole moieties. Journal of Enzyme Inhibition and Medicinal Chemistry. 32(1). 798–804. 37 indexed citations

20.

Brier, Sébastien, Vincenzo Carginale, Antonio Capasso, et al.. (2007). Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii. FEBS Journal. 274(23). 6152–6166. 39 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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