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Biomedical Chemistry: Current Trends and Developments
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Tetraoxanepyrimidine nitrile as dual stage antimalarials. Journal of Medicinal Chemistry, 57, 4916-4923. Olson, J. E., Lee, G. K., Semenov, A., & Rosenthal, P. J. (1999). Antimalarial effects in mice of orally administered peptidyl cysteine protease inhibitors. Bioorganic & Medicinal Chemistry, 7(4), 633-638. O’Neill, P. M., Stocks, P. A., Pugh, M. D., Araujo, N. C., Korshin, E. E., Bickley, J. F., Ward, S. A., Bray, P. G., Pasini, E., Davies, J., Verissimo, E., & Bachi, M. D. (2004). Design and Synthesis of Endoperoxide Antimalarial Prodrug Models. Angewandte Chemie International Edition, 43, 4193-4197. Potashman, M. H., & Duggan, D. E. (2009). Covalent modifiers: an orthogonal approach to drug design. Journal of Medicinal Chemistry, 52, 1231–1246. Powers, J. C., Asgian, J. L., Ekici, O. D., & James K. E. (2002). Irreversible inhibitors of serine, cysteine, and threonine proteases. Chemical Reviews, 102, 4639–4750. Pritchard, R. B., Lough, C. E., Currie, D. J., & Holmes, H. L. (1968). Equilibrium Reactions of N- Butanethiol with Some Conjugated Heteroenoid Compounds. Canadian Journal of Chemistry, 46, 775–781. Robertson, J.G. (2005). Mechanistic basis of enzyme-targeted drugs. Biochemistry, 44, 5561– 5571. Robertson, J.G. (2007). Enzymes as a special class of therapeutic target: clinical drugs and modes of action. Current Opinion in Structural Biology, 17, 674–679. Roush, W. R., Cheng, J. M., Knapp-Reed, B., Alvarez-Hernandez, A., McKerrow, J. H., Hansell, E., & Engel, J. C. (2001). Potent second generation vinyl sulfonamide inhibitors of the trypanosomal cysteine protease cruzain. Bioorg. ACS Medicinal Chemistry Letters, 11(20), 2759-2762. Santos, M. M. M., & Moreira, R. (2007). Michael acceptors as cysteine protease inhibitors. Mini- Reviews in Medicinal Chemistry, 7(10), 1040-1050. Serafimova, I. M., Pufall, M. A., Krishnan, S., Duda, K., Cohen, M. S., Maglathlin, R. L., McFarland, J. M., Miller, R. M., Frödin, M., Taunton, J. (2012). Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles. Nature Chemical Biology, 8, 471- 476. Shenai, B. R., Lee, B. J., Alvarez-Fernandes, A., Chong, P. Y., Emal, C. D., Neitz, R. J., Roush, W. R., & Rosenthal, P. J. (2003). Structure-activity Relationships for Inhibition of Cysteine Protease Activity and Development of Plasmodium falciparum by Peptidyl Vinyl Sulfones. Antimicrobial Agents and Chemotherapy, 47, 154-160. Singh, J., Petter, R.C., Baillie, T.A., & Whitty, A. (2011). The resurgence of covalent drugs. Nature Reviews Drug Discovery, 10, 307–317. Tan, J., George, S., Kusov, Y., Perbandt, M., Anemueller, S., Mesters, J. R., Norder, H., Coutard, B., Lacroix, C., Leyssen, P., Neyts, J., & Hilgenfeld, R. (2013). 3C Protease of Enterovirus 68: Structure-Based Design of Michael Acceptor Inhibitors and Their Broad-Spectrum Antiviral Effects against Picornaviruses. Journal of Virology, 87(8), 4339-4351. Thompson, S. A., Andrews, P. R., & Hanzlik, R. P. (1986). Carboxyl-modified Amino-acids and Peptides as Protease Inhibitors. Journal of Medicinal Chemistry, 29(1), 104-111. Wilkinson, S. R., & Kelly, J. M. (2009). Trypanocidal drugs: mechanisms, resistance and new targets. Expert Reviews in Molecular Medicine, 11, e31.
zurĂĽck zum  Buch Biomedical Chemistry: Current Trends and Developments"
Biomedical Chemistry: Current Trends and Developments
Titel
Biomedical Chemistry: Current Trends and Developments
Autor
Nuno Vale
Verlag
De Gruyter Open Ltd
Datum
2016
Sprache
englisch
Lizenz
CC BY-NC-ND 4.0
ISBN
978-3-11-046887-8
Abmessungen
21.0 x 29.7 cm
Seiten
427
Schlagwörter
Physical Sciences, Engineering and Technology, Chemistry, Organic Chemistry, Green Chemistry
Kategorien
Naturwissenschaften Chemie
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Biomedical Chemistry: Current Trends and Developments