Registro:

Referencias:

• Bachurin, S.O., Bovina, E.V., Ustyugov, A.A., Drugs in clinical trials for Alzheimer's disease: the major trends (2017) Med. Res. Rev., 37, pp. 1186-1225
• Cummings, J., Lee, G., Mortsdorf, T., Ritter, A., Zhong, K., Alzheimer's disease drug development pipeline: 2017 (2017) Alzheimers Dement., 3, pp. 367-384
• Lanctôt, K.L., Amatniek, J., Ancoli-Israel, S., Arnold, S.E., Ballard, C., Cohen-Mansfield, J., Ismail, Z., Boot, B., Neuropsychiatric signs and symptoms of Alzheimer's disease: new treatment paradigms (2017) Alzheimers Dement., 3, pp. 440-449
• Huff, F.J., Reiter, C.T., Rand, J.B.J., The ratio of acetylcholinesterase to butyrylcholinesterase influences the specificity of assays for each enzyme in human brain (1989) J. Neural Transm., 75, pp. 129-134
• Dvir, H., Silman, I., Harel, M., Rosenberry, T.L., Sussman, J.L., Acetylcholinesterase: from 3D structure to function (2010) Chem. Biol. Interact., 187, pp. 10-22
• Nordberg, A., Ballard, C., Bullok, R., Darreh-Shori, T., Somogvi, M., A review of butyrylcholinesterase as a therapeutic target in the treatment of Alzheimer's disease, Prim. Care Companion J. Clin. Phys. 15 (2013) PCC.12r01412; Castro, M.J., Richmond, V., Romero, C., Maier, M.S., Estévez-Braun, A., Ravelo, A.G., Faraoni, M.B., Murray, A.P., Preparation, anticholinesterase activity and molecular docking of new lupane derivatives (2014) Bioorg. Med. Chem., 22, pp. 3341-3350
• Vela Gurovic, M.S., Castro, M.J., Richmond, V., Faraoni, M.B., Maier, M.S., Murray, A.P., Triterpenoids with acetylcholinesterase inhibition from Chuquiraga erinacea D. Don. subsp. erinacea (Asteraceae) (2010) Planta Med., 76, pp. 607-610
• Gutiérrez-Nicolás, F., Gordillo-Román, B., Oberti, J.C., Estévez-Braun, A., Ravelo, A.G., Joseph-Nathan, P., Synthesis and anti-HIV activity of lupane and olean-18-ene derivatives. Absolute configuration of 19,20-epoxylupanes by VCD (2012) J. Nat. Prod., 75, pp. 669-676
• Khan, M.F., Maurya, C.K., Dev, K., Arha, D., Rai, K., Tamrakar, A.K., Maurya, R., Design and synthesis of lupeol analogues and their in vitro PTP-1B inhibitory activity (2014) Bioorg. Med. Chem. Lett., 24, pp. 2674-2679
• Mutai, C., Abatis, D., Vagias, C., Moreauc, D., Roussakisc, C., Roussis, V., Lupane triterpenoids from Acacia mellifera with cytotoxic activity (2004) Phytochemistry, 65, pp. 1159-1164
• Prachayasittikul, S., Saraban, P., Cherdtrakulkiat, R., Ruchirawat, S., Prachayasittikul, V., New bioactive triterpenoids and antimalarial activity of Diospyros rubra lec (2010) Excli J., 9, pp. 1-10
• Bhandari, P., Patel, N.K., Bhutani, K.K., Synthesis of new heterocyclic lupeol derivatives as nitric oxide and pro-inflammatory cytokine inhibitors (2014) Bioorg. Med. Chem. Lett., 24, pp. 3596-3599
• Yasukawa, K., Yu, S.Y., Yamanouchi, S., Takido, M., Akihisa, T., Tamura, T., Some lupane-type triterpenes inhibit tumor promotion by 12-0-tetradecanoylphorbol-13-acetate in two-stage carcinogenesis in mouse skin (1995) Phytomedicine, 1, pp. 309-313
• Khan, M.F., Mishra, D.P., Ramakrishna, E., Rawat, A.K., Mishra, A., Srivastava, A.K., Maurya, R., Design and synthesis of lupeol analogues and their glucose uptake stimulatory effect in L6 skeletal muscle cells (2014) Med. Chem. Res., 23, pp. 4156-4166
• Burns, D., Reynolds, W.F., Buchanan, G., Reese, P.B., Enriquez, R.G., Assignment of 1 H and 13 C spectra and investigation of hindered side-chain rotation in lupeol derivatives (2000) Magn. Reson. Chem., 38, pp. 488-493
• Pech, G.G., Brito, W.F., Mena, G.J., Quijano, L., Constituents of Acacia cedilloi and Acacia gaumeri. Revised structure and complete NMR assignments of resinone (2002) Z. Naturforsch C., 57, pp. 773-776
• Wei, Y., Ma, C., Chen, D., Hattori, M., Anti-HIV-1 protease triterpenoids from Stauntonia obovatifoliola Hayata subsp. intermedia (2008) Phytochemistry, 69, pp. 1875-1879
• Ellman, G.L., Courtney, K.D., Andres, V., Featherstone, R.M., A new and rapid colorimetric determination of acetylcholinesterase activity (1961) Biochem. Pharmacol., 7, pp. 88-95
• Saxena, A., Redman, A.M., Jiang, X., Lockridge, O., Doctor, B.P., Differences in active-site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase (1999) Chem. Biol. Interact., 119-120, pp. 61-69
• Forli, S., Olson, A.J., Force field with discrete displaceable waters and desolvation entropy for hydrated ligand docking (2012) J. Med. Chem., 55, pp. 623-638
• Nicolet, Y., Lockridge, O., Masson, P., Fontecilla-Camps, J.C., Nachon, F., Crystal characterization of human butyrylcholinesterase and of its complexes with substrate and products (2003) J. Biol. Chem., 278, pp. 41141-41147
• Raves, M.L., Harel, M., Pang, Y.P., Silman, I., Kozikowski, A.P., Sussman, J.L., Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A (1997) Nat. Struct. Biol., 4, pp. 57-63
• Dewar, M.J.S., Zoebisch, E.G., Healy, E.F., Stewart, J.J.P., Development and use of quantum mechanical molecular models. 76. AM1: a new general purpose quantum mechanical molecular model (1985) J. Am. Chem. Soc., 107, pp. 3902-3909
• Roothaan, C.C.J., New developments in molecular orbital theory (1951) Rev. Mod. Phys., 23, pp. 69-89
• (2004), Gaussian 03, Revision C.01, M.J. Frisch, G.W. Trucks, H.B. Schlegel, G.E. Scuseria, M.A. Robb, J.R. Cheeseman, J.A. Montgomery, T. Vreven, K.N. Kudin, J.C. Burant, J.M. Millam, S.S. Iyengar, J. Tomasi, V. Barone, B. Mennucci, M. Cossi, G. Scalmani, N. Rega, G.A. Petersson, H. Nakatsuji, M. Hada, M. Ehara, K. Toyota, R. Fukuda, J. Hasegawa, M. Ishida, T. Nakajima, Y. Honda, O. Kitao, H. Nakai, M. Klene, X. Li, J.E. Knox, H.P. Hratchian, J.B. Cross, V. Bakken, C. Adamo, J. Jaramillo, R. Gomperts, R.E. Stratmann, O. Yazyev, A.J. Austin, R. Cammi, C. Pomelli, J.W. Ochterski, P.Y. Ayala, K. Morokuma, G.A. Voth, P. Salvador, J.J. Dannenberg, V.G. Zakrzewski, S. Dapprich, A.D. Daniels, M.C. Strain, O. Farkas, D.K. Malick, A.D. Rabuck, K. Raghavachari, J.B. Foresman, J.V. Ortiz, Q. Cui, A.G. Baboul, S. Clifford, J. Cioslowski, B.B. Stefanov, G. Liu, A. Liashenko, P. Piskorz, I. Komaromi, R.L. Martin, D.J. Fox, T. Keith, M.A. Al-Laham, C.Y. Peng, A. Nanayakkara, M. Challacombe, P.M.W. Gill, B. Johnson, W. Chen, M.W. Wong, C. Gonzalez, J.A. Pople, Gaussian Inc., Wallingford, CT; (2013), Auto-Dock 4.2, The Scripps Research Institute, Department of Molecular Biology, MB-5, La Jolla, CA

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------