[1. F. K. Winkler, Structure of human pancreatic lipase, Nature343 (1990) 771–774; https://doi.org/10.1038/343771a010.1038/343771a0]Search in Google Scholar
[2. S. Ransac, Y. Gargouri, F. Marguet, G. Buono, C. Beglinger, P. Hildebrand, H. Lengsfeld, P. Hadváry and R. Verger, Covalent inactivation of lipases, Methods Enzymol.286 (1997) 190–231; https://doi.org/10.1016/S0076-6879(97)86012-010.1016/S0076-6879(97)86012-0]Search in Google Scholar
[3. G. Singh, S. Suresh, B. V. Krishna and K. R. Kumar, Lipase inhibitors from plants and their medical applications, Int. J. Pharm. Pharm. Sci.7 (2015) 1–5.]Search in Google Scholar
[4. E. Kato, M. Yama, R. Nakagomi, T. Shibata, K. Hosokawa and J. Kawabata, Substrate-like water soluble lipase inhibitors from Filipendula kamtschatica, Bioorg. Med. Chem. Lett.22 (2012) 6410–6412; https://doi.org/10.1016/j.bmcl.2012.08.05510.1016/j.bmcl.2012.08.05522995617]Search in Google Scholar
[5. Y. Narita, K. Iwai, T. Fukunaga and O. Nakagiri, Inhibitory activity of chlorogenic acids in decaffeinated green coffee beans against porcine pancreas lipase and effect of a decaffeinated green coffee bean extract on an emulsion of olive oil, Biosci. Biotechnol. Biochem. 76 (2012) 2329–2331; https://doi.org/10.1271/bbb.12051810.1271/bbb.12051823221697]Search in Google Scholar
[6. E. Mentese, F. Yιlmaz, N. Karaali, S. Ülker and B. Kahveci, Rapid synthesis and lipase inhibition activity of some new benzimidazole and perimidine derivatives, Bioorg. Khim.40 (2014) 363–369; https://doi.org/10.1134/S106816201403009110.1134/S1068162014030091]Search in Google Scholar
[7. Y. H. Jo, S. B. Kim, Q. Liu, J. W. Lee, B. Y. Hwang and M. K. Lee, Benzylated and prenylated flavonoids from the root barks of Cudrania tricuspidata with pancreatic lipase inhibitory activity, Bioorg. Med. Chem. Lett.25 (2015) 3455–3457; https://doi.org/10.1016/j.bmcl.2015.07.01710.1016/j.bmcl.2015.07.01726227773]Search in Google Scholar
[8. S. N. Sridhar, G. Ginson, P. O. Venkataramana Reddy, M. P. Tantak, D. Kumar and A. T. Paul, Synthesis, evaluation and molecular modeling studies of 2-(carbazol-3-yl)-2-oxoacetamide analogues as a new class of potential pancreatic lipase inhibitors, Bioorg. Med. Chem. 25 (2017) 609–620; https://doi.org/10.1016/j.bmc.2016.11.03110.1016/j.bmc.2016.11.03127908755]Search in Google Scholar
[9. A. M. Brzozowski, U. Derewenda, Z. S. Derewenda, G. G. Dodson, D. M. Lawson, J. P. Turkenburg, F. Bjorkling, B. Huge-Jensen, S. A. Patkar and L. Thim, A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex, Nature351 (1991) 491–494; https://doi.org/10.1038/351491a010.1038/351491a02046751]Search in Google Scholar
[10. M. P. Egloff, L. Sarda, R. Verger, C. Cambillau and H. van Tilbeurgh, Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase, Protein Sci.4 (1995) 44–57; https://doi.org/10.1002/pro.556004010710.1002/pro.556004010721429707773176]Search in Google Scholar
[11. A. Bourbon-Freie, R. E. Dub, X. Xiao and M. E. Lowe, Trp-107 and trp-253 account for the increased steady state fluorescence that accompanies the conformational change in human pancreatic triglyceride lipase induced by tetrahydrolipstatin and bile salt, J. Biol. Chem.284 (2009) 14157–14164; https://doi.org/10.1074/jbc.M90115420010.1074/jbc.M901154200268286419346257]Search in Google Scholar
[12. V. Delorme, R. Dhouib, S. Canaan, F. Fotiadu, F. Carrièreand and J. F. Cavalier, Effects of surfactants on lipase structure, activity, and inhibition, Pharm. Res.8 (2011) 1831–1842; https://doi.org/10.1007/s11095-010-0362-910.1007/s11095-010-0362-921234659]Search in Google Scholar
[13. P. Alam, G. Rabbani, G. Badr, B. M. Badr and R. H. Khan, The surfactant-induced conformational and activity alterations in Rhizopus niveus lipase, Cell Biochem. Biophys. 71 (2015) 1199–1206; https://doi.org/10.1007/s12013-014-0329-210.1007/s12013-014-0329-225424356]Search in Google Scholar
[14. E. Mateos-Diaz, S. Amara, A. Roussel, S. Longhi, C. Cambillau and F. Carrière, Probing conformational changes and interfacial recognition site of lipases with surfactants and inhibitors, Methods Enzymol.583 (2017) 279–307; https://doi.org/10.1016/bs.mie.2016.09.04010.1016/bs.mie.2016.09.04028063495]Search in Google Scholar
[15. I. I. Hamdan, F. Afifi and M. O. Taha, In vitro alpha amylase inhibitory effect of some clinically-used drugs, Pharmazie59 (2004) 799–801.]Search in Google Scholar
[16. Y. Bustanji, M. Mohammad Mohammad, M. Hudaib, K. Tawaha, I. M. Al-Masri, H. S. Al Khatib, A. Issa and F. Q. Alali, Screening of some medicinal plants for their pancreatic lipase inhibitory potential, Jordan J. Pharm. Sci.4 (2011) 81–88.]Search in Google Scholar
[17. FRED (version 2.2.5) 2009. OpenEye Scientific Software (www.eyesopen.com), Santa Fe, USA.]Search in Google Scholar
[18. S. Habtemariam, The anti-obesity potential of sigmoidin A, Pharm. Biol. 50 (2012) 1519–1522; https://doi.org/10.3109/13880209.2012.68883810.3109/13880209.2012.68883822978690]Search in Google Scholar
[19. M. Karamać and R. Amarowicz, Inhibition of pancreatic lipase by phenolic acids-examination in vitro, Z. Naturforsch. C.51 (1996) 903–905.10.1515/znc-1996-11-12229031529]Search in Google Scholar
[20. J. A. van Diepen, I. O. C. M. Vroegrijk, J. F. P. Berbée, S. E. Shoelson, J. A. Romijn, L. M. Havekes, P. C. N. Rensen and P. J. Voshol, Aspirin reduces hypertriglyceridemia by lowering VLDL-triglyceride production in mice fed a high-fat diet, Am. J. Physiol. Endocrinol. Metab.301 (2011) 1099–1107; https://doi.org/10.1152/ajpendo.00185.201110.1152/ajpendo.00185.2011411635321862721]Search in Google Scholar
[21. A. Kumarand and S. Chauhan, Monte Carlo method based QSAR modeling of natural lipase inhibitors using hybrid optimal descriptors, SAR QSAR Environ. Res.28 (2017) 179–197; https://doi.org/10.1080/1062936X.2017.129372910.1080/1062936X.2017.129372928271914]Search in Google Scholar
[22. R. Emral, O. Köseoğlulari, V. Tonyukuk, A. R. Uysal, N. Kamel and D. Corapcioğlu, The effect of short-term glycemic regulation with gliclazide and metformin on postprandial lipemia, Exp. Clin. Endocrinol. Diabetes113 (2005) 80–84; https://doi.org/10.1055/s-2004-83053610.1055/s-2004-83053615772898]Search in Google Scholar
[23. L. S. Chupak, X. Zheng, S. Hu, Y. Huang, M. Ding, M. A. Lewis, R. S. Westphal, Y. Blat, A. McClure and R. G. Gentles, Structure activity relationship studies on chemically non-reactive glycine sulfonamide inhibitors of diacylglycerol lipase, Bioorg. Med. Chem. 24 (2016) 1455–1468; https://doi.org/10.1016/j.bmc.2016.02.00610.1016/j.bmc.2016.02.00626917221]Search in Google Scholar
[24. F. J. Janssen, H. Deng, M. P. Baggelaar, M. Allarà, T. van der Wel, H. den Dulk, A. Ligresti, A. C. van Esbroeck, R. McGuire, V. Di Marzo, H. S. Overkleeft and M. van der Stelt, Discovery of glycine sulfonamides as dual inhibitors of sn-1-diacylglycerol lipase α and α/β-hydrolase domain 6, J. Med. Chem.57 (2014) 6610–6622; https://doi.org/10.1021/jm500681z10.1021/jm500681z24988361]Search in Google Scholar
[25. J. Kim, Y. S. Lee, C. S. Kim and J. S. Kim, Betulinic acid has an inhibitory effect on pancreatic lipase and induces adipocyte lipolysis, Phytother. Res. 26 (2012) 1103–1106; https://doi.org/10.1002/ptr.367210.1002/ptr.3672]Search in Google Scholar
[26. Y. Bustanji, I. M. Al-Masri, M. Mohammad, M. Hudaib, K. Tawaha, H. Tarazi and H. S. Alkhatib, Pancreatic lipase inhibition activity of trilactoneterpenes of Ginkgo biloba, J. Enzyme Inhib. Med. Chem.26 (2011) 453–459; https://doi.org/10.3109/14756366.2010.52550910.3109/14756366.2010.525509]Search in Google Scholar
[27. Y. M. Al-Hiari, V. N. Kasabri, A. K. Shakya, M. H. Alzweiri, F. U. Afifi, Y. K. Bustanji and I. M. Al-Masri, Fluoroquinolones: novel class of gastrointestinal dietary lipid digestion and absorption inhibitors, Med. Chem. Res. 23 (2014) 3336–3346; https://doi.org/10.1007/s00044-014-0913-410.1007/s00044-014-0913-4]Search in Google Scholar
[28. P. Hadváry, W. Sidler, W. Meister, W. Vetter and H. Wolfer, The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase, J. Biol. Chem.266 (1991) 2021–2027.10.1016/S0021-9258(18)52203-1]Search in Google Scholar
[29. C. Schouand and N. H. Heegaard, Recent applications of affinity interactions in capillary electrophoresis, Electrophoresis27 (2006) 44–59; https://doi.org/10.1002/elps.20050051610.1002/elps.200500516716365416315182]Search in Google Scholar
[30. A. Lookene, N. Skottova and G. Olivecrona, Interactions of lipoprotein lipase with the active-site inhibitor tetrahydrolipstatin (Orlistat), Eur. J. Biochem. 222 (1994) 395–403; https://doi.org/10.1111/j.1432-1033.1994.tb18878.x10.1111/j.1432-1033.1994.tb18878.x8020477]Search in Google Scholar
[31. H. Lee, S. Cao, K. E. Hevener, L. Truong, J. L. Gatuz, K. Patel, A. K. Ghosh and M. E. Johnson, Synergistic inhibitor binding to the papain-like protease of human SARS corona virus: mechanistic and inhibitor design implications, Chem. Med. Chem.8 (2013) 1361–1372; https://doi.org/10.1002/cmdc.20130013410.1002/cmdc.201300134395498623788528]Search in Google Scholar
[32. C. W. Murray and T. L. Blundell, Structural biology in fragment-based drug design, Curr. Opin. Struct. Biol.20 (2010) 497–507; https://doi.org/10.1016/j.sbi.2010.04.00310.1016/j.sbi.2010.04.00320471246]Search in Google Scholar