Leonardo Astolfi Rosado

645 total citations
27 papers, 482 citations indexed

About

Leonardo Astolfi Rosado is a scholar working on Molecular Biology, Materials Chemistry and Infectious Diseases. According to data from OpenAlex, Leonardo Astolfi Rosado has authored 27 papers receiving a total of 482 indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 9 papers in Materials Chemistry and 7 papers in Infectious Diseases. Recurrent topics in Leonardo Astolfi Rosado's work include Biochemical and Molecular Research (10 papers), Enzyme Structure and Function (9 papers) and Tuberculosis Research and Epidemiology (6 papers). Leonardo Astolfi Rosado is often cited by papers focused on Biochemical and Molecular Research (10 papers), Enzyme Structure and Function (9 papers) and Tuberculosis Research and Epidemiology (6 papers). Leonardo Astolfi Rosado collaborates with scholars based in Brazil, Belgium and United States. Leonardo Astolfi Rosado's co-authors include Luiz Augusto Basso, Diógenes Santiago Santos, Joris Messens, Khadija Wahni, Ardala Breda, David Young, Brandán Pedre, Frank Van Breusegem, Rodrigo G. Ducati and Didier Vertommen and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and PLoS ONE.

In The Last Decade

Leonardo Astolfi Rosado

25 papers receiving 479 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Leonardo Astolfi Rosado Brazil	16	366	93	68	68	57	27	482
Phimonphan Chuankhayan Taiwan	14	318 0.9×	49 0.5×	96 1.4×	69 1.0×	27 0.5×	32	611
Anthony S. Gizzi United States	8	349 1.0×	81 0.9×	29 0.4×	31 0.5×	46 0.8×	10	590
Esther M. M. Bulloch New Zealand	18	562 1.5×	175 1.9×	45 0.7×	125 1.8×	102 1.8×	36	764
Hui-Lin Shr Taiwan	7	367 1.0×	160 1.7×	108 1.6×	64 0.9×	17 0.3×	17	552
Martin Valachovič Slovakia	15	442 1.2×	89 1.0×	88 1.3×	22 0.3×	56 1.0×	30	633
Gautam Agnihotri United States	12	316 0.9×	119 1.3×	27 0.4×	97 1.4×	83 1.5×	14	537
Sook‐Kyung Kim South Korea	13	317 0.9×	43 0.5×	44 0.6×	45 0.7×	34 0.6×	32	513
Clarissa Melo Czekster United Kingdom	14	443 1.2×	38 0.4×	30 0.4×	80 1.2×	33 0.6×	31	544
María‐Natalia Lisa France	11	276 0.8×	162 1.7×	38 0.6×	51 0.8×	105 1.8×	25	556
Jean-Marie Frère Belgium	13	310 0.8×	85 0.9×	40 0.6×	84 1.2×	113 2.0×	17	699

Countries citing papers authored by Leonardo Astolfi Rosado

Since Specialization

Citations

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

Fields of papers citing papers by Leonardo Astolfi Rosado

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Leonardo Astolfi Rosado. 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 Leonardo Astolfi Rosado. The network helps show where Leonardo Astolfi Rosado may publish in the future.

Co-authorship network of co-authors of Leonardo Astolfi Rosado

This figure shows the co-authorship network connecting the top 25 collaborators of Leonardo Astolfi Rosado. A scholar is included among the top collaborators of Leonardo Astolfi Rosado 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 Leonardo Astolfi Rosado. Leonardo Astolfi Rosado 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

Pedre, Brandán, David Young, Daniël Charlier, et al.. (2018). Structural snapshots of OxyR reveal the peroxidatic mechanism of H ₂ O ₂ sensing. Proceedings of the National Academy of Sciences. 115(50). 48 indexed citations

Young, David, Brandán Pedre, Daria Ezeriņa, et al.. (2018). Protein Promiscuity in H ₂ O ₂ Signaling. Antioxidants and Redox Signaling. 30(10). 1285–1324. 25 indexed citations

Hillion, Mélanie, Brandán Pedre, Jörg Bernhardt, et al.. (2017). The glyceraldehyde-3-phosphate dehydrogenase GapDH of Corynebacterium diphtheriae is redox-controlled by protein S-mycothiolation under oxidative stress. Scientific Reports. 7(1). 5020–5020. 22 indexed citations

Tossounian, Maria‐Armineh, Inge Van Molle, Khadija Wahni, et al.. (2017). Disulfide bond formation protects Arabidopsis thaliana glutathione transferase tau 23 from oxidative damage. Biochimica et Biophysica Acta (BBA) - General Subjects. 1862(3). 775–789. 20 indexed citations

Bodra, Nandita, David Young, Leonardo Astolfi Rosado, et al.. (2017). Arabidopsis thaliana dehydroascorbate reductase 2: Conformational flexibility during catalysis. Scientific Reports. 7(1). 42494–42494. 14 indexed citations

Pedre, Brandán, Leonardo Astolfi Rosado, Inge Van Molle, et al.. (2016). The active site architecture in peroxiredoxins: a case study on Mycobacterium tuberculosis AhpE. Chemical Communications. 52(67). 10293–10296. 15 indexed citations

Wei, Yifeng, et al.. (2014). The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proceedings of the National Academy of Sciences. 111(36). E3756–65. 23 indexed citations

Rosado, Leonardo Astolfi, Diana Carolina Rostirolla, Luís Fernando Saraiva Macedo Timmers, et al.. (2013). Kinetic mechanism and energetics of binding of phosphoryl group acceptors to Mycobacterium tuberculosis cytidine monophosphate kinase. Archives of Biochemistry and Biophysics. 536(1). 53–63.

Villela, Anne Drumond, Rodrigo G. Ducati, Leonardo Astolfi Rosado, et al.. (2013). Biochemical Characterization of Uracil Phosphoribosyltransferase from Mycobacterium tuberculosis. PLoS ONE. 8(2). e56445–e56445. 19 indexed citations

10.

Rosado, Leonardo Astolfi, Mário Sérgio Palma, Vincent Frappier, et al.. (2013). The Mode of Action of Recombinant Mycobacterium tuberculosis Shikimate Kinase: Kinetics and Thermodynamics Analyses. PLoS ONE. 8(5). e61918–e61918. 15 indexed citations

11.

Wink, Priscila Lamb, Leonardo Astolfi Rosado, Valnês S. Rodrigues-Junior, et al.. (2013). Biochemical characterization of recombinant nucleoside hydrolase from Mycobacterium tuberculosis H37Rv. Archives of Biochemistry and Biophysics. 538(2). 80–94. 6 indexed citations

12.

Breda, Ardala, Leonardo Martinelli, Cristiano Valim Bizarro, et al.. (2012). Wild-Type Phosphoribosylpyrophosphate Synthase (PRS) from Mycobacterium tuberculosis: A Bacterial Class II PRS?. PLoS ONE. 7(6). e39245–e39245. 15 indexed citations

13.

Breda, Ardala, Pablo Machado, Leonardo Astolfi Rosado, et al.. (2012). Pyrimidin-2(1H)-ones based inhibitors of Mycobacterium tuberculosis orotate phosphoribosyltransferase. European Journal of Medicinal Chemistry. 54. 113–122. 15 indexed citations

14.

Rosado, Leonardo Astolfi, Rafael Andrade Caceres, Walter Filgueira de Azevedo, Luiz Augusto Basso, & Diógenes Santiago Santos. (2012). Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-ketoacyl-ACP Reductase (MabA). BMC Research Notes. 5(1). 526–526. 11 indexed citations

15.

Breda, Ardala, Leonardo Astolfi Rosado, Daniel M. Lorenzini, Luiz Augusto Basso, & Diógenes Santiago Santos. (2011). Molecular, kinetic and thermodynamic characterization of Mycobacterium tuberculosis orotate phosphoribosyltransferase. Molecular BioSystems. 8(2). 572–586. 17 indexed citations

16.

Martinelli, Leonardo, Rodrigo G. Ducati, Leonardo Astolfi Rosado, et al.. (2011). Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme–ligand binary complex formation. Molecular BioSystems. 7(4). 1289–1305. 21 indexed citations

17.

Ducati, Rodrigo G., Ardala Breda, Leonardo Astolfi Rosado, et al.. (2011). Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23). Archives of Biochemistry and Biophysics. 512(2). 143–153. 14 indexed citations

18.

Adachi, Osao, et al.. (2010). Kinetic mechanism determination and analysis of metal requirement of dehydroquinate synthase from Mycobacterium tuberculosis H37Rv: an essential step in the function-based rational design of anti-TB drugs. Molecular BioSystems. 7(1). 119–128. 12 indexed citations

19.

Rostirolla, Diana Carolina, Ardala Breda, Leonardo Astolfi Rosado, et al.. (2010). UMP kinase from Mycobacterium tuberculosis: Mode of action and allosteric interactions, and their likely role in pyrimidine metabolism regulation. Archives of Biochemistry and Biophysics. 505(2). 202–212. 11 indexed citations

20.

Silva, Rafael G. da, Leonardo Astolfi Rosado, Diógenes Santiago Santos, & Luiz Augusto Basso. (2007). Mycobacterium tuberculosis β-ketoacyl-ACP reductase: α-Secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding. Archives of Biochemistry and Biophysics. 471(1). 1–10. 12 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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