Dr. Leonardo Astolfi Rosado

Research Scientist
Massachusetts Institute of Technology, USA


Highest Degree
Ph.D. in Molecular and Cellular Biology from Pontificia Universidade Catolica do Rio Grande do Sul, Brazil

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Biography

Dr. Leonardo Astolfi Rosado is currently working as Postdoctoral in Chemistry Department, Federal University of Santa Catarina. He has completed his Ph.D. in Molecular and Cellular Biology from Pontificia Universidade Catolica do Rio Grande do Sul, Brazil. He also worked as Postdoctoral Research Associate in Chemistry Department, Massachusetts Institute of Technology - Cambridge, USA, and Visiting Researcher at Pontifical Catholic University of Rio Grande do Sul, PUCRS. He has published 16 research articles in journals as author/co-author.

Area of Interest:

Biomedical Sciences
Gene Cloning
Cell Biology
Protein Purification
Spectroscopic Studies

Selected Publications

  1. Wei, Y., M.A. Funk, L.A. Rosado, J. Baek, C.L. Drennan and J. Stubbe, 2014. The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant. Proc. Natl. Acad. Sci., 111: E3756-E3765.
    CrossRef  |  PubMed  |  

  2. Wink, P.L., Z.A. Sanchez Quitian, L.A. Rosado, V. da Silva Rodrigues Jr. and G.O. Petersen et al., 2013. Biochemical characterization of recombinant nucleoside hydrolase from Mycobacterium tuberculosis H37Rv. Arch. Biochem. Biophys., 538: 80-94.
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  3. Villela, A.D., R.G. Ducati, L.A. Rosado, C.J. Bloch and M.V. Prates et al., 2013. Biochemical characterization of uracil phosphoribosyltransferase from Mycobacterium tuberculosis. PLoS ONE, Vol. 8. 10.1371/journal.pone.0056445.
    CrossRef  |  Direct Link  |  

  4. Roth, G., J.E.S. Nunes, L.A. Rosado, C.V. Bizarro and G. Volpato et al., 2013. Recombinant Erwinia carotovora L-asparaginase II production in Escherichia coli fed-batch cultures. Braz. J. Chem. Eng., 30: 245-256.
    CrossRef  |  Direct Link  |  

  5. Rosado, L.A., I.B. Vasconcelos, M.S. Palma, V. Frappier, R.J. Najmanovich, D.S. Santos and L.A. Basso, 2013. The mode of action of recombinant Mycobacterium tuberculosis Shikimate Kinase: Kinetics and thermodynamics analyses. PLoS One. 10.1371/journal.pone.0061918.
    CrossRef  |  PubMed  |  Direct Link  |  

  6. Renck, D., P. Machado, A.A. Souto, L.A. Rosado and T. Erig et al., 2013. Design of novel potent inhibitors of human uridine phosphorylase-1: Synthesis, inhibition studies, thermodynamics and in vitro influence on 5-fluorouracil cytotoxicity. J. Med. Chem., Vol. 1. 10.1021/jm401389u.
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  7. Jaskulski, L., L.A. Rosado, D.C. Rostirolla, L.F. Timmers, O.N. de Souza, D.S. Santos and L.A. Basso, 2013. Kinetic mechanism and energetics of binding of phosphoryl group acceptors to Mycobacterium tuberculosis cytidine monophosphate kinase. Arch. Biochem. Biophys., 536: 53-63.
    CrossRef  |  Direct Link  |  

  8. Rosado, L.A., R.A. Caceres, W.F. Azevedo, L.A. Basso and D.S. Santos, 2012. Role of Serine140 in the mode of action of Mycobacterium tuberculosis β-2 ketoacyl-ACP reductase (MabA). BMC Res. Notes. 10.1186/1756-0500-5-526.
    CrossRef  |  Direct Link  |  

  9. Breda, A., P. Machado, L.A. Rosado, A.A. Souto, D.S. Santos and L.A. Basso, 2012. Pyrimidin-2 (1H)-ones based inhibitors of Mycobacterium tuberculosis orotate phosphoribosyltransferase. Eur. J. Med. Chem., 54: 113-122.
    CrossRef  |  Direct Link  |  

  10. Breda, A., L.K.B. Martinelli, C.V. Bizarro, L.A. Rosado, C. Brancher, D.S. Santos and L.A. Basso, 2012. Wild-type Phosphoribosylpyrophosphate Synthase (PRS) from Mycobacterium tuberculosis: A bacterial class II PRS? Plos One. 10.1371/journal.pone.0039245.
    CrossRef  |  Direct Link  |  

  11. Breda, A., L.A. Rosado, D.M. Lorenzini, L.A. Basso and D.S. Santos, 2012. Molecular, kinetic and thermodynamic characterization of Mycobacterium tuberculosis orotate phosphoribosyltransferase. Mol. BioSyst., 8: 572-586.
    CrossRef  |  Direct Link  |  

  12. Rostirolla, D.C., A. Breda, L.A. Rosado, M.S. Palma, L.A. Basso and D.S. Santos, 2011. UMP kinase from Mycobacterium tuberculosis: Mode of action and allosteric interactions and their likely role in pyrimidine metabolism regulation. Arch. Biochem. Biophys., 505: 202-212.
    PubMed  |  

  13. Nunes, J.E.S., R.G. Ducati, A. Breda, L.A. Rosado and B.M. Souza et al., 2011. Mycobacterium tuberculosis histidinol dehydrogenase (EC 1.1.1.23): Molecular cloning, expression, purification, characterization and homology modeling. Arch. Biochem. Biophys. .

  14. Nunes, J.E., R.G. Ducati, A. Breda, L.A. Rosado and B.M. De Souza et al., 2011. Molecular, kinetic, thermodynamic and structural analyses of Mycobacterium tuberculosishis D-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1. 1.23). Arch. Biochem. Biophys., 512: 143-153.
    CrossRef  |  Direct Link  |  

  15. Martinelli, L.K., R.G. Ducati, L.A. Rosado, A. Breda, B.P. Selbach, D.S. Santos and L.A. Basso, 2011. Recombinant Escherichia coli GMP reductase: Kinetic, catalytic and chemical mechanisms and thermodynamics of enzyme-ligand binary complex formation. Mol. Biosyst., 7: 1289-1305.
    PubMed  |  

  16. De Mendonca, J.D., O. Adachi, L.A. Rosado, R.G. Ducati, D.S. Santos and L.A. Basso, 2011. 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. Mol. BioSyst., 7: 119-128.
    CrossRef  |  Direct Link  |  

  17. Silva, R., L. Rosado, D. Santos and L. Basso, 2008. Mycobacterium tuberculosis β-ketoacyl-ACP reductase: α-Secondary kinetic isotope effects and kinetic and equilibrium mechanisms of substrate binding. Arch. Biochem. Biophys., 471: 1-10.
    PubMed  |