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Volumn 4, Issue 9, 2007, Pages 2031-2122

The biochemistry of drug metabolism - An introduction part 3. Reactions of hydrolysis and their enzymes

Author keywords

[No Author keywords available]

Indexed keywords

7 ETHYL 10 HYDROXYCAMPTOTHECIN; ACETYLSALICYLIC ACID; ACICLOVIR; CAMPTOTHECIN; DIAMORPHINE; DILTIAZEM; FELBAMATE; FLUAZIFOP BUTYL; FLUOROURACIL; IRINOTECAN; KETOPROFEN; LANDIOLOL; METHYLPHENIDATE; METHYLPREDNISOLONE SODIUM SUCCINATE; METRONIDAZOLE; MYCOPHENOLIC ACID 2 MORPHOLINOETHYL ESTER; NAFAMSTAT; NALTREXONE; NAPROXEN; PETHIDINE; PRODRUG; PROPANIDID; PROPRANOLOL; REPIRINAST; SALICYLIC ACID; SALICYLURIC ACID; SUXAMETHONIUM; UNINDEXED DRUG; VALACICLOVIR; XENOBIOTIC AGENT;

EID: 34948885743     PISSN: 16121872     EISSN: 16121880     Source Type: Journal    
DOI: 10.1002/cbdv.200790169     Document Type: Editorial
Times cited : (59)

References (300)
  • 1
    • 33750632169 scopus 로고    scopus 로고
    • The Biochemistry of Drug Metabolism - An Introduction. Part 1. Principles and Overview
    • B. Testa, S. D. Krämer,'The Biochemistry of Drug Metabolism - An Introduction. Part 1. Principles and Overview', Chem. Biodiv. 2006, 3, 1053-1101.
    • (2006) Chem. Biodiv , vol.3 , pp. 1053-1101
    • Testa, B.1    Krämer, S.D.2
  • 2
    • 33847092271 scopus 로고    scopus 로고
    • The Biochemistry of Drug Metabolism - An Introduction. Part 2: Redox Reactions and Their Enzymes
    • B. Testa, S. D. Krämer, 'The Biochemistry of Drug Metabolism - An Introduction. Part 2: Redox Reactions and Their Enzymes', Chem. Biodiv. 2007, 4, 257-405.
    • (2007) Chem. Biodiv , vol.4 , pp. 257-405
    • Testa, B.1    Krämer, S.D.2
  • 4
    • 2442601735 scopus 로고    scopus 로고
    • Principles of drug metabolism
    • 6th edn, Ed. D. J. Abraham, Wiley-Interscience, Hoboken
    • B. Testa, W. Soine, 'Principles of drug metabolism', in 'Burger's Medicinal Chemistry and Drug Discovery', 6th edn., Ed. D. J. Abraham, Wiley-Interscience, Hoboken, 2003, Vol. 2, p. 431-498.
    • (2003) Burger's Medicinal Chemistry and Drug Discovery , vol.2 , pp. 431-498
    • Testa, B.1    Soine, W.2
  • 5
    • 77957557296 scopus 로고    scopus 로고
    • B. Testa, 'Principles of drug metabolism 2: Hydrolysis and conjugation reactions', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 133-166.
    • B. Testa, 'Principles of drug metabolism 2: Hydrolysis and conjugation reactions', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, Vol. 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 133-166.
  • 6
    • 0020313118 scopus 로고
    • Nonenzymatic contributions to xenobiotic metabolism
    • B. Testa, 'Nonenzymatic contributions to xenobiotic metabolism', Drug Metab. Rev. 1982, 13, 25-50
    • (1982) Drug Metab. Rev , vol.13 , pp. 25-50
    • Testa, B.1
  • 7
    • 0023006986 scopus 로고
    • Detoxication reactions of glutathione and glutathione transferases
    • B. Ketterer, 'Detoxication reactions of glutathione and glutathione transferases', Xenobiotica 1986, 16, 957-973
    • (1986) Xenobiotica , vol.16 , pp. 957-973
    • Ketterer, B.1
  • 8
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • R. N. Armstrong, 'Structure, catalytic mechanism, and evolution of the glutathione transferases', Chem. Res. Toxicol. 1997, 10, 2-18.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 9
    • 0003450992 scopus 로고    scopus 로고
    • Nomenclature Committee of the International Union of Biochemistry and Molecular Biology IUBMB
    • Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), 'Enzyme Nomenclature', www.chem.qmul.ac.uk/ iubmb/enzyme.
    • Enzyme Nomenclature
  • 13
    • 34948820213 scopus 로고    scopus 로고
    • The ESTHER Database, http://bioweb.ensam.inra.fr/ESTHER/definition.
    • The ESTHER Database
  • 14
    • 84906428688 scopus 로고    scopus 로고
    • R. A. Totah, A. E. Rettie, 'Principles of drug metabolism 3: Enzymes and tissues', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, 5 in'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 167-191.
    • R. A. Totah, A. E. Rettie, 'Principles of drug metabolism 3: Enzymes and tissues', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, Vol. 5 in'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 167-191.
  • 15
    • 0027376703 scopus 로고    scopus 로고
    • N. W. McCracken, P. G. Blain, F. M. Williams, 'Human xenobiotic metabolizing esterases in liver and blood', Biochem. Pharmacol. 1993, 46, 1125-1129
    • N. W. McCracken, P. G. Blain, F. M. Williams, 'Human xenobiotic metabolizing esterases in liver and blood', Biochem. Pharmacol. 1993, 46, 1125-1129
  • 16
    • 0027279552 scopus 로고
    • The esterases: Perspectives and problems
    • W. N. Aldridge,'The esterases: perspectives and problems', Chem. Biol. Interact. 1993, 87, 5-13
    • (1993) Chem. Biol. Interact , vol.87 , pp. 5-13
    • Aldridge, W.N.1
  • 18
    • 0023614883 scopus 로고
    • Possible physiological roles of carboxylic ester hydrolases
    • F. J. Leinweber, 'Possible physiological roles of carboxylic ester hydrolases', Drug Metab. Rev. 1987, 18, 379-439.
    • (1987) Drug Metab. Rev , vol.18 , pp. 379-439
    • Leinweber, F.J.1
  • 19
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: From molecules to functions
    • T. Satoh, M. Hosokawa, 'The mammalian carboxylesterases: from molecules to functions', Annu. Rev. Pharmacol. Toxicol. 1998, 38, 257-288.
    • (1998) Annu. Rev. Pharmacol. Toxicol , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 20
    • 22944464763 scopus 로고    scopus 로고
    • Identification of esterases expressed in Caco-2 cells and effects of their hydrolyzing activity in predicting human intestinal absorption
    • T. Imai, M. Imoto, H. Sakamoto, M. Hashimoto, 'Identification of esterases expressed in Caco-2 cells and effects of their hydrolyzing activity in predicting human intestinal absorption', Drug Metab. Dispos. 2005, 33, 1185-1190.
    • (2005) Drug Metab. Dispos , vol.33 , pp. 1185-1190
    • Imai, T.1    Imoto, M.2    Sakamoto, H.3    Hashimoto, M.4
  • 21
    • 33749030999 scopus 로고    scopus 로고
    • Human carboxylesterase isozymes: Catalytic properties and rational drug design
    • T. Imai, 'Human carboxylesterase isozymes: catalytic properties and rational drug design', Drug Metab. Pharmacokinet. 2006, 21, 173-185
    • (2006) Drug Metab. Pharmacokinet , vol.21 , pp. 173-185
    • Imai, T.1
  • 23
    • 0023375904 scopus 로고
    • Distinction between 'A'-esterases and arylesterases. Implications for esterase classification
    • M. I. Mackness, H. M. Thompson, A. R. Hardy, C. H. Walker, 'Distinction between 'A'-esterases and arylesterases. Implications for esterase classification', Biochem. J 1987, 245, 293-296
    • (1987) Biochem. J , vol.245 , pp. 293-296
    • Mackness, M.I.1    Thompson, H.M.2    Hardy, A.R.3    Walker, C.H.4
  • 26
    • 0029937118 scopus 로고    scopus 로고
    • The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family
    • S. L. Primo-Parmo, R. C. Sorenson, J. Teiber, B. N. La Du, 'The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family', Genomics 1996, 33, 498-507
    • (1996) Genomics , vol.33 , pp. 498-507
    • Primo-Parmo, S.L.1    Sorenson, R.C.2    Teiber, J.3    La Du, B.N.4
  • 27
    • 0031915397 scopus 로고    scopus 로고
    • DNA polymorphism in two paraoxonase genes (PON1 and PON2) are associated with the risk of coronary heart disease
    • D. K. Sanghera, C. E. Aston, N. Saha, M. I. Kamboh, 'DNA polymorphism in two paraoxonase genes (PON1 and PON2) are associated with the risk of coronary heart disease', Am. J Hum. Genet. 1998, 62, 20-24
    • (1998) Am. J Hum. Genet , vol.62 , pp. 20-24
    • Sanghera, D.K.1    Aston, C.E.2    Saha, N.3    Kamboh, M.I.4
  • 29
    • 0028609492 scopus 로고    scopus 로고
    • M. M. Benning, J. M. Kuo, F. M. Kaushel, H. M. Holden, 'Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents', Biochemistry 1994, 33, 15001-15007
    • M. M. Benning, J. M. Kuo, F. M. Kaushel, H. M. Holden, 'Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents', Biochemistry 1994, 33, 15001-15007
  • 30
    • 0029993512 scopus 로고    scopus 로고
    • J. L. Vanhooke, M. M. Benning, F. M. Raushel, H. M. Holden, 'Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate', Biochemistry 1996, 35, 6020-6025.
    • J. L. Vanhooke, M. M. Benning, F. M. Raushel, H. M. Holden, 'Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate', Biochemistry 1996, 35, 6020-6025.
  • 31
    • 0344699371 scopus 로고    scopus 로고
    • EDTA-resistant and sensitive phosphotriesterase activities associated with albumin and lipoproteins in rabbit serum
    • M. A. Sogorb, I. Sanchez, M. Lopez-Rivadulla, V. Cespedes, E. Vilanova, 'EDTA-resistant and sensitive phosphotriesterase activities associated with albumin and lipoproteins in rabbit serum', Drug Metab. Dispos. 1999, 27, 53-59.
    • (1999) Drug Metab. Dispos , vol.27 , pp. 53-59
    • Sogorb, M.A.1    Sanchez, I.2    Lopez-Rivadulla, M.3    Cespedes, V.4    Vilanova, E.5
  • 32
    • 0033461179 scopus 로고    scopus 로고
    • Determination of paraoxonase (PON1) status requires more than genotyping
    • R. J. Richter, C. E. Furlong, 'Determination of paraoxonase (PON1) status requires more than genotyping', Pharmacogenetics 1999, 9, 745-753
    • (1999) Pharmacogenetics , vol.9 , pp. 745-753
    • Richter, R.J.1    Furlong, C.E.2
  • 33
    • 0030827926 scopus 로고    scopus 로고
    • Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon
    • B. Mackness, M. I. Mackness, S. Arrol, W Turkie, R N. Durrington, 'Effect of the molecular polymorphisms of human paraoxonase (PON1) on the rate of hydrolysis of paraoxon', Br J Pharmacol. 1997, 122, 265-168.
    • (1997) Br J Pharmacol , vol.122 , pp. 265-168
    • Mackness, B.1    Mackness, M.I.2    Arrol, S.3    Turkie, W.4    Durrington, R.N.5
  • 35
    • 0035028835 scopus 로고    scopus 로고
    • Human plasma paraoxonase (HuPON1): An anti-atherogenic enzyme with organophosphate hydrolase activity
    • D. Josse, P. Masson, 'Human plasma paraoxonase (HuPON1): an anti-atherogenic enzyme with organophosphate hydrolase activity', Ann. Pharm. Fr. 2001, 59, 108-118.
    • (2001) Ann. Pharm. Fr , vol.59 , pp. 108-118
    • Josse, D.1    Masson, P.2
  • 36
    • 0035056687 scopus 로고    scopus 로고
    • Serum paraoxonase (PON1) isozymes: The quantitative analysis of isozymes affecting individual sensitivity to environmental chemicals
    • B. N. La Du, S. Billecke, C. Hsu, R. W Haley, C. A. Broomfield, 'Serum paraoxonase (PON1) isozymes: the quantitative analysis of isozymes affecting individual sensitivity to environmental chemicals', Drug Metab. Dispos. 2001, 29, 566-569.
    • (2001) Drug Metab. Dispos , vol.29 , pp. 566-569
    • La Du, B.N.1    Billecke, S.2    Hsu, C.3    Haley, R.W.4    Broomfield, C.A.5
  • 37
    • 24344477569 scopus 로고    scopus 로고
    • Cloning, high level expression of paraoxonase-3 in Sf9 cells and pharmacological characterization of its product
    • H. Lu, J. Zhu, Y Zang, Y. Ze, J. Qin, 'Cloning, high level expression of paraoxonase-3 in Sf9 cells and pharmacological characterization of its product', Biochem. Pharmacol. 2005, 70, 1019-1025.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 1019-1025
    • Lu, H.1    Zhu, J.2    Zang, Y.3    Ze, Y.4    Qin, J.5
  • 39
    • 0342618613 scopus 로고    scopus 로고
    • Divergent effects of classical inducers on rat plasma and microsomal fraction paraoxonase and arylesterase
    • A. R Hernández, M. C. Gonzalvo, F. Gil, E. Villanueva, A. Pla, 'Divergent effects of classical inducers on rat plasma and microsomal fraction paraoxonase and arylesterase', Environ. Toxicol. Pharmacol. 1997, 3, 83-86.
    • (1997) Environ. Toxicol. Pharmacol , vol.3 , pp. 83-86
    • Hernández, A.R.1    Gonzalvo, M.C.2    Gil, F.3    Villanueva, E.4    Pla, A.5
  • 41
    • 33645382172 scopus 로고    scopus 로고
    • Enantiomer discrimination illustrated by the high-resolution crystal structures of type 4 phosphodiesterase
    • Q. Huai, Y Sun, H. Wang, D. Macdonald, R. Aspiotis, H. Robinson, Z. Huang, H. Ke, 'Enantiomer discrimination illustrated by the high-resolution crystal structures of type 4 phosphodiesterase', J Med Chem. 2006, 49, 1867-1873.
    • (2006) J Med Chem , vol.49 , pp. 1867-1873
    • Huai, Q.1    Sun, Y.2    Wang, H.3    Macdonald, D.4    Aspiotis, R.5    Robinson, H.6    Huang, Z.7    Ke, H.8
  • 42
    • 34948896007 scopus 로고    scopus 로고
    • 'Enzymes of the Cholinesterase Family', Eds. D. M. Quinn, A. S. Balasubramanian, B. P. Doctor, P.Taylor, Plenum Press, New York, 1995.
    • 'Enzymes of the Cholinesterase Family', Eds. D. M. Quinn, A. S. Balasubramanian, B. P. Doctor, P.Taylor, Plenum Press, New York, 1995.
  • 43
    • 0028174977 scopus 로고
    • The cholinesterases: From genes to proteins
    • R Taylor, Z. Radic, 'The cholinesterases: from genes to proteins', Annu. Rev. Pharmacol.. Toxicol. 1994, 34, 281-320
    • (1994) Annu. Rev. Pharmacol.. Toxicol , vol.34 , pp. 281-320
    • Taylor, R.1    Radic, Z.2
  • 44
    • 0025764041 scopus 로고
    • The cholinesterases
    • P. Taylor, 'The cholinesterases', J Biol. Chem. 1991, 266, 4025-4028
    • (1991) J Biol. Chem , vol.266 , pp. 4025-4028
    • Taylor, P.1
  • 45
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • A. Chatonnet, O. Lockridge, 'Comparison of butyrylcholinesterase and acetylcholinesterase', Biochem. J. 1989, 260, 625-634.
    • (1989) Biochem. J , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 46
    • 0034664228 scopus 로고    scopus 로고
    • Determination of the DNA sequences of acetylcholinesterase and butyry1cholinesterase from cat and demonstration of the existence of both in cat plasma
    • C. E Bartels, W. Xie, A. K. Miller-Lindholm, L. M. Schopfer, O. Lockridge, 'Determination of the DNA sequences of acetylcholinesterase and butyry1cholinesterase from cat and demonstration of the existence of both in cat plasma', Biochem. Pharmacol. 2000, 60, 479-487.
    • (2000) Biochem. Pharmacol , vol.60 , pp. 479-487
    • Bartels, C.E.1    Xie, W.2    Miller-Lindholm, A.K.3    Schopfer, L.M.4    Lockridge, O.5
  • 47
    • 0029142579 scopus 로고
    • Specificity and orientation of trigonal carboxylesters and tetrahedral alkylphosphonyl esters in cholinesterases
    • N. A. Hosea, H. A. Berman, P. Taylor, 'Specificity and orientation of trigonal carboxylesters and tetrahedral alkylphosphonyl esters in cholinesterases', Biochemistry 1995, 34, 11528-11536;
    • (1995) Biochemistry , vol.34 , pp. 11528-11536
    • Hosea, N.A.1    Berman, H.A.2    Taylor, P.3
  • 48
    • 0033942802 scopus 로고    scopus 로고
    • Phosphobutyrylcholinesterase: Phosphorylation of the esteratic site of butyrylcholinesterase by ethephon [(2-chloroethyl)phosphoric acid] dianion
    • J. E. Haux, G. B. Quistad, J. E. Casida, 'Phosphobutyrylcholinesterase: phosphorylation of the esteratic site of butyrylcholinesterase by ethephon [(2-chloroethyl)phosphoric acid] dianion', Chem. Res. Toxicol. 2000, 13, 646-651
    • (2000) Chem. Res. Toxicol , vol.13 , pp. 646-651
    • Haux, J.E.1    Quistad, G.B.2    Casida, J.E.3
  • 49
    • 33645687131 scopus 로고    scopus 로고
    • Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine
    • W Luo, Q. Yu, S. S. Kulkarni, D. A. Parrish, H. W Holloway, D. Tweedie, A. Shafferman, D. K. Lahiri, A. Brossi, N. H. Greig, 'Inhibition of human acetyl- and butyrylcholinesterase by novel carbamates of (-)- and (+)-tetrahydrofurobenzofuran and methanobenzodioxepine', J. Med. Chem. 2006, 49, 2174-2185
    • (2006) J. Med. Chem , vol.49 , pp. 2174-2185
    • Luo, W.1    Yu, Q.2    Kulkarni, S.S.3    Parrish, D.A.4    Holloway, H.W.5    Tweedie, D.6    Shafferman, A.7    Lahiri, D.K.8    Brossi, A.9    Greig, N.H.10
  • 50
    • 33746765583 scopus 로고    scopus 로고
    • Crystal structures of acetylcholinesterase in complex with HI-6, ortho-7 and obidoxime: Structural basis for differences in the ability to reactivate tabun conjugates
    • F. Ekström, Y.-P. Pang, M. Boman, E. Artursson, C. Akfur, S. Börjegren, 'Crystal structures of acetylcholinesterase in complex with HI-6, ortho-7 and obidoxime: structural basis for differences in the ability to reactivate tabun conjugates', Biochem. Pharmacol. 2006, 72, 597-607.
    • (2006) Biochem. Pharmacol , vol.72 , pp. 597-607
    • Ekström, F.1    Pang, Y.-P.2    Boman, M.3    Artursson, E.4    Akfur, C.5    Börjegren, S.6
  • 51
    • 27544478172 scopus 로고    scopus 로고
    • Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
    • B. Li, M. Sedlacek, I. Manoharan, R. Boopathy, E. G. Duysen, P. Masson, O. Lockridge, 'Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma', Biochem. Pharmacol. 2005, 70, 1673-1684.
    • (2005) Biochem. Pharmacol , vol.70 , pp. 1673-1684
    • Li, B.1    Sedlacek, M.2    Manoharan, I.3    Boopathy, R.4    Duysen, E.G.5    Masson, P.6    Lockridge, O.7
  • 52
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase', J Am. Chem. Soc. 1996, 118, 2340-2346.
    • (1996) J Am. Chem. Soc , vol.118 , pp. 2340-2346
    • Harel, M.1    Quinn, D.M.2    Nair, H.K.3    Silman, I.4    Sussman, J.L.5
  • 53
    • 0031012947 scopus 로고    scopus 로고
    • Molecular modeling of the structures of human and rat pancreatic cholesterol esterases
    • S. R. Feaster, D. M. Quinn, B. L. Barnett, 'Molecular modeling of the structures of human and rat pancreatic cholesterol esterases', Protein Sci. 1997, 6, 73-79.
    • (1997) Protein Sci , vol.6 , pp. 73-79
    • Feaster, S.R.1    Quinn, D.M.2    Barnett, B.L.3
  • 54
    • 0031716759 scopus 로고    scopus 로고
    • On the role of the peroxisome in the metabolism of drugs and xenobiotics
    • C. J. Masters, 'On the role of the peroxisome in the metabolism of drugs and xenobiotics', Biochem. Pharmacol. 1998, 56, 667-673
    • (1998) Biochem. Pharmacol , vol.56 , pp. 667-673
    • Masters, C.J.1
  • 55
    • 24344476275 scopus 로고    scopus 로고
    • M. C. Hunt, J. Yamada, L. J. Maltais, M. W. Wright, E. J. Podesta, S. E. H. Alexson, 'A revised nomenclature for mammalian acyl-CoA thioesterases/ hydrolases', J Lipid Res. 2005, 46, 2029-2032.
    • M. C. Hunt, J. Yamada, L. J. Maltais, M. W. Wright, E. J. Podesta, S. E. H. Alexson, 'A revised nomenclature for mammalian acyl-CoA thioesterases/ hydrolases', J Lipid Res. 2005, 46, 2029-2032.
  • 57
    • 0030939766 scopus 로고    scopus 로고
    • Esterase-like activity of human serum albumin toward prodrug esters of nicotinic acid
    • A. Salvi, P. A. Carrupt, J. M. Mayer, B. Testa, 'Esterase-like activity of human serum albumin toward prodrug esters of nicotinic acid', Drug Metab. Dispos. 1997, 25, 395-398
    • (1997) Drug Metab. Dispos , vol.25 , pp. 395-398
    • Salvi, A.1    Carrupt, P.A.2    Mayer, J.M.3    Testa, B.4
  • 58
    • 1242337279 scopus 로고    scopus 로고
    • Esterase-like activity of serum albumin: Characterization of its structural chemistry using p-nitrophenyl esters as substrates
    • Y. Sakurai, S. F. Ma, H. Watanabe, N. Yamaotsu, S. Hirono, Y. Kurono, U. Kragh-Hansen, M. Otagiri, 'Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates', Pharm. Res. 2004, 21, 285-292.
    • (2004) Pharm. Res , vol.21 , pp. 285-292
    • Sakurai, Y.1    Ma, S.F.2    Watanabe, H.3    Yamaotsu, N.4    Hirono, S.5    Kurono, Y.6    Kragh-Hansen, U.7    Otagiri, M.8
  • 59
    • 84944052122 scopus 로고    scopus 로고
    • 'Handbook of Proteolytic Enzymes', 2nd edn., Eds. A. J. Barrett, N. D. Rawlings, J. F. Woessner, Elsevier, Oxford, 2004
    • a) 'Handbook of Proteolytic Enzymes', 2nd edn., Eds. A. J. Barrett, N. D. Rawlings, J. F. Woessner, Elsevier, Oxford, 2004
  • 62
    • 0024559146 scopus 로고
    • A unique signature identifies a family of zinc-dependent metallopeptidases
    • C. V. Jongeneel, J. Bouvier, A. Bairoch, 'A unique signature identifies a family of zinc-dependent metallopeptidases', FEBS Lett. 1989, 242, 211-214.
    • (1989) FEBS Lett , vol.242 , pp. 211-214
    • Jongeneel, C.V.1    Bouvier, J.2    Bairoch, A.3
  • 63
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • G. Dodson, A. Wlodawer, 'Catalytic triads and their relatives', Trends Biochem. Sci. 1998, 23, 347-352.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 64
    • 14644422580 scopus 로고    scopus 로고
    • Mammalian carboxylesterases: From drug targets to protein therapeutics
    • M. R. Redinbo, P. M. Potter, 'Mammalian carboxylesterases: from drug targets to protein therapeutics', Drug Discov. Today 2005, 10, 313-325.
    • (2005) Drug Discov. Today , vol.10 , pp. 313-325
    • Redinbo, M.R.1    Potter, P.M.2
  • 67
    • 0026409452 scopus 로고
    • Structural biol.ogy of zinc
    • D. W. Christianson, 'Structural biol.ogy of zinc', Adv. Protein Chem. 1991, 42, 281-355.
    • (1991) Adv. Protein Chem , vol.42 , pp. 281-355
    • Christianson, D.W.1
  • 70
    • 0025874929 scopus 로고
    • In vitro hydrolysis of threo-methylphenidate by blood esterases. Differential and enantioselective interspecies variability
    • N. R. Srinavas, J. W. Hubbard, G. McKay, E. M. Hawes, K. K. Midha, 'In vitro hydrolysis of threo-methylphenidate by blood esterases. Differential and enantioselective interspecies variability', Chirality 1991, 3, 99-103.
    • (1991) Chirality , vol.3 , pp. 99-103
    • Srinavas, N.R.1    Hubbard, J.W.2    McKay, G.3    Hawes, E.M.4    Midha, K.K.5
  • 71
    • 0033042706 scopus 로고    scopus 로고
    • Binding and hydrolysis of meperidine by human liver carboxylesterase hCE-1
    • J. Zhang, J. C. Burnell, N. Dumaual, W. F. Bosron,'Binding and hydrolysis of meperidine by human liver carboxylesterase hCE-1', J. Pharmacol. Exp. Ther. 1999, 290, 314-318.
    • (1999) J. Pharmacol. Exp. Ther , vol.290 , pp. 314-318
    • Zhang, J.1    Burnell, J.C.2    Dumaual, N.3    Bosron, W.F.4
  • 74
    • 33845283189 scopus 로고
    • Enzymes in organic synthesis. 39. Preparations of chiral cyclic acid-esters and bicyclic lactones via stereoselective pig liver esterase catalyzed hydrolyses of cyclic meso diesters
    • G. Sabbioni, J. B. Jones, 'Enzymes in organic synthesis. 39. Preparations of chiral cyclic acid-esters and bicyclic lactones via stereoselective pig liver esterase catalyzed hydrolyses of cyclic meso diesters', J. Org. Chem. 1987, 52, 4565-457O.
    • (1987) J. Org. Chem , vol.52
    • Sabbioni, G.1    Jones, J.B.2
  • 75
    • 0029795257 scopus 로고    scopus 로고
    • Hydrolysis of aspirin studie by spectrophotometric and fluorometric variable-temperature kinetics
    • a) G. Alibrandi, N. Micali, S. Trusso, A. Villari, 'Hydrolysis of aspirin studie by spectrophotometric and fluorometric variable-temperature kinetics', J. Pharm. Sci. 1996, 85, 1105-1108
    • (1996) J. Pharm. Sci , vol.85 , pp. 1105-1108
    • Alibrandi, G.1    Micali, N.2    Trusso, S.3    Villari, A.4
  • 76
    • 0025179702 scopus 로고
    • Comparative metabolism of high doses of aspirin in man and rat
    • b) D. K. Patel, L. J. Notarianni, P. N. Bennett, 'Comparative metabolism of high doses of aspirin in man and rat' Xenobiotica 1990, 20, 847-854.
    • (1990) Xenobiotica , vol.20 , pp. 847-854
    • Patel, D.K.1    Notarianni, L.J.2    Bennett, P.N.3
  • 78
    • 0030694223 scopus 로고    scopus 로고
    • Species differences for stereoselective hydrolysis of propranolol prodrugs in plasma and liver
    • Y Yoshigae, T. Imai, A. Horita, M. Otagiri, 'Species differences for stereoselective hydrolysis of propranolol prodrugs in plasma and liver', Chirality 1997, 9, 661-666
    • (1997) Chirality , vol.9 , pp. 661-666
    • Yoshigae, Y.1    Imai, T.2    Horita, A.3    Otagiri, M.4
  • 79
    • 0032904639 scopus 로고    scopus 로고
    • Characterization of esterases invoved in the stereoselective hydrolysis of ester-type prodrugs of propranolol in rat liver and plasma
    • Y. Yoshigae, T. Imai, M. Taketani, M. Otagiri, 'Characterization of esterases invoved in the stereoselective hydrolysis of ester-type prodrugs of propranolol in rat liver and plasma', Chirality 1999, 11, 10-13.
    • (1999) Chirality , vol.11 , pp. 10-13
    • Yoshigae, Y.1    Imai, T.2    Taketani, M.3    Otagiri, M.4
  • 80
    • 0017234552 scopus 로고
    • Urinary excretion of heroin and its metabolites in man
    • S. Y. Yeb, C. W, Gorodetzky, R. L. McQuinn, 'Urinary excretion of heroin and its metabolites in man', J Pharmacol. Exp. Ther. 1976, 196, 249-256
    • (1976) J Pharmacol. Exp. Ther , vol.196 , pp. 249-256
    • Yeb, S.Y.1    Gorodetzky, C.W.2    McQuinn, R.L.3
  • 81
    • 0017351415 scopus 로고
    • Identification of diacetylmorphine metabolites in humans
    • S. Y. Yeh, R. L. McQuinn, C. W. Gorodetzky, 'Identification of diacetylmorphine metabolites in humans', J. Pharm. Sci. 1977, 66, 201-204
    • (1977) J. Pharm. Sci , vol.66 , pp. 201-204
    • Yeh, S.Y.1    McQuinn, R.L.2    Gorodetzky, C.W.3
  • 82
    • 0026769379 scopus 로고
    • The effect of temperature and pH on the deacetylation of diamorphine in aqueous solution and in human plasma
    • D. A. Barrett, A. L. P, Dyssegaard, P. N. Shaw, 'The effect of temperature and pH on the deacetylation of diamorphine in aqueous solution and in human plasma', J. Pharm. Pharmacol. 1992, 44, 606-608.
    • (1992) J. Pharm. Pharmacol , vol.44 , pp. 606-608
    • Barrett, D.A.1    Dyssegaard, A.L.P.2    Shaw, P.N.3
  • 83
    • 0030809784 scopus 로고    scopus 로고
    • Human liver carboxylesterase hCE-1: Binding specificity for cocaine, heroin, and their metabolites and analogs
    • M. R. Brzezinski, B. J. Spink, R. A. Dean, C. E. Berkman, J. R. Cashman, W. F. Bosron, 'Human liver carboxylesterase hCE-1: binding specificity for cocaine, heroin, and their metabolites and analogs', Drug Metab. Dispos. 1997, 25, 1089-1096.
    • (1997) Drug Metab. Dispos , vol.25 , pp. 1089-1096
    • Brzezinski, M.R.1    Spink, B.J.2    Dean, R.A.3    Berkman, C.E.4    Cashman, J.R.5    Bosron, W.F.6
  • 84
    • 0028348689 scopus 로고
    • The heroin metabolite, 6-monoacetyhnorphine, activates delta opiod receptors to produce antinociception in Swiss-Webster mice
    • J. J. Rady, E Aksu, J. M. Fujimoto, 'The heroin metabolite, 6-monoacetyhnorphine, activates delta opiod receptors to produce antinociception in Swiss-Webster mice', J. Pharmacol. Exp. Ther. 1994, 268, 1222-1231.
    • (1994) J. Pharmacol. Exp. Ther , vol.268 , pp. 1222-1231
    • Rady, J.J.1    Aksu, E.2    Fujimoto, J.M.3
  • 85
    • 2642655272 scopus 로고    scopus 로고
    • Synthesis and enzymatic hydrolysis of esters, constituting simple models of soft drugs
    • M. Graffner-Nordberg, K. Sjödin, A. Tunek, A. Hallberg, 'Synthesis and enzymatic hydrolysis of esters, constituting simple models of soft drugs', Chem. Pharm. Bull. 1998, 46, 591-601.
    • (1998) Chem. Pharm. Bull , vol.46 , pp. 591-601
    • Graffner-Nordberg, M.1    Sjödin, K.2    Tunek, A.3    Hallberg, A.4
  • 88
    • 0023910667 scopus 로고
    • Glycolamide esters as novel biolabile prodrug type for non-steroidal anti-inflammatory carboxylic acid drugs
    • H. Bundgaard, N. M. Nielsen, 'Glycolamide esters as novel biolabile prodrug type for non-steroidal anti-inflammatory carboxylic acid drugs', Int. J Pharmaceut. 1988, 43, 101-110
    • (1988) Int. J Pharmaceut , vol.43 , pp. 101-110
    • Bundgaard, H.1    Nielsen, N.M.2
  • 89
    • 0028912168 scopus 로고
    • Glycolamide esters of 6-methoxy-2-naphthylacetic acid as potential prodrugs - physicochemical properties, chemical stability and enzymatic hydrolysis
    • L. K. Wadhwa, P. D. Sharma, 'Glycolamide esters of 6-methoxy-2-naphthylacetic acid as potential prodrugs - physicochemical properties, chemical stability and enzymatic hydrolysis', Int. J. Pharmaceut. 1995, 118, 31-39.
    • (1995) Int. J. Pharmaceut , vol.118 , pp. 31-39
    • Wadhwa, L.K.1    Sharma, P.D.2
  • 91
    • 0031662109 scopus 로고    scopus 로고
    • 5′-Amino acid esters of antiviral nucleosides, acyclovir, and AZT are absorbed by the intestinal PEPT1 peptide transporter
    • H. Han, R. L. A. de Vrueh, J. K. Rhie, K. M. Y. Covitz, R L. Smith, C. P. Lee, D. M. Oh, W. Sadée, G. L. Amidon, '5′-Amino acid esters of antiviral nucleosides, acyclovir, and AZT are absorbed by the intestinal PEPT1 peptide transporter', Pharm. Res. 1998, 15, 1154-1159
    • (1998) Pharm. Res , vol.15 , pp. 1154-1159
    • Han, H.1    de Vrueh, R.L.A.2    Rhie, J.K.3    Covitz, K.M.Y.4    Smith, R.L.5    Lee, C.P.6    Oh, D.M.7    Sadée, W.8    Amidon, G.L.9
  • 92
    • 0029076466 scopus 로고
    • Purification and characterization of a rat liver enzyme that hydrolyzes valaciclovir, the L-valyl ester prodrug of acyclovir
    • T. C. Burnette, J. A. Harrington, J. E. Reardon, B. M. Merrill, P. de Miranda, 'Purification and characterization of a rat liver enzyme that hydrolyzes valaciclovir, the L-valyl ester prodrug of acyclovir', J Biol. Chem. 1995, 270, 15827-15831
    • (1995) J Biol. Chem , vol.270 , pp. 15827-15831
    • Burnette, T.C.1    Harrington, J.A.2    Reardon, J.E.3    Merrill, B.M.4    de Miranda, P.5
  • 93
    • 0035042563 scopus 로고    scopus 로고
    • Chemical stability, enzymatic hydrolysis, and nasal uptake of amino acid ester prodrugs of acyclovir
    • C. Yang, H. Gao, A. K. Mitra, 'Chemical stability, enzymatic hydrolysis, and nasal uptake of amino acid ester prodrugs of acyclovir', J. Pharm. Sci. 2001, 90, 617-624.
    • (2001) J. Pharm. Sci , vol.90 , pp. 617-624
    • Yang, C.1    Gao, H.2    Mitra, A.K.3
  • 94
    • 0021804622 scopus 로고
    • Serum-catalyzed hydrolysis of metronidazole amino acid esters
    • M. J. Cho, L. C. Haynes, 'Serum-catalyzed hydrolysis of metronidazole amino acid esters', J Pharm. Sci. 1985, 74, 883-885
    • (1985) J Pharm. Sci , vol.74 , pp. 883-885
    • Cho, M.J.1    Haynes, L.C.2
  • 95
    • 0034993669 scopus 로고    scopus 로고
    • Synthesis, chemical and enzymatic hydrolysis, and bioavailability evaluation in rabbits of metronidazole amino acid ester prodrugs with enhanced water solubility
    • N. M. Mahfouz, M. A. Hassan, 'Synthesis, chemical and enzymatic hydrolysis, and bioavailability evaluation in rabbits of metronidazole amino acid ester prodrugs with enhanced water solubility', J Pharm. Pharmacol. 2001, 53, 841-848.
    • (2001) J Pharm. Pharmacol , vol.53 , pp. 841-848
    • Mahfouz, N.M.1    Hassan, M.A.2
  • 96
    • 33745855129 scopus 로고    scopus 로고
    • Kinetics and mechanism of activation of a-amino acid ester prodrugs of camptothecins
    • L. Song, R. Bevins, B. D. Anderson, 'Kinetics and mechanism of activation of a-amino acid ester prodrugs of camptothecins', J Med. Chem. 2006, 49, 4344-4355.
    • (2006) J Med. Chem , vol.49 , pp. 4344-4355
    • Song, L.1    Bevins, R.2    Anderson, B.D.3
  • 98
    • 0031743198 scopus 로고    scopus 로고
    • In vitro evaluation of acyloxyalkyl esters as dermal prodrugs of ketoprofen and naproxen
    • J. Rautio, H. Taipale, J. Gynther, J. Vepsalainen, T. Nevalainen, T. Jarvinen, 'In vitro evaluation of acyloxyalkyl esters as dermal prodrugs of ketoprofen and naproxen', J. Pharm. Sci. 1998, 87, 1622-1628.
    • (1998) J. Pharm. Sci , vol.87 , pp. 1622-1628
    • Rautio, J.1    Taipale, H.2    Gynther, J.3    Vepsalainen, J.4    Nevalainen, T.5    Jarvinen, T.6
  • 99
    • 0023852518 scopus 로고
    • Kinetics of regeneration of metronidazole from hemiesters of maleic acid, succinic acid and glutaric acid in aqueous buffer, human plasma and pig liver homogenate
    • C. Larsen, P. Kurtzhals, M. Johansen, 'Kinetics of regeneration of metronidazole from hemiesters of maleic acid, succinic acid and glutaric acid in aqueous buffer, human plasma and pig liver homogenate', Int. J. Pharm. 1988, 41, 121-129.
    • (1988) Int. J. Pharm , vol.41 , pp. 121-129
    • Larsen, C.1    Kurtzhals, P.2    Johansen, M.3
  • 100
    • 15744400969 scopus 로고    scopus 로고
    • Dexamethasone-induced methylprednisolone hemisuccinate hydrolase: Its identification as a member of the rat carboxylesterase 2 family and its unique existence in plasma
    • T. Furihata, M. Hosokawa, A. Fujii, M. Derbel, T. Satoh, K. Chiba, 'Dexamethasone-induced methylprednisolone hemisuccinate hydrolase: its identification as a member of the rat carboxylesterase 2 family and its unique existence in plasma', Biochem. Pharmacol. 2005, 69, 1287-1297
    • (2005) Biochem. Pharmacol , vol.69 , pp. 1287-1297
    • Furihata, T.1    Hosokawa, M.2    Fujii, A.3    Derbel, M.4    Satoh, T.5    Chiba, K.6
  • 101
    • 4444360142 scopus 로고    scopus 로고
    • Anti-inflammatory steroids
    • 6th edn, Ed. D. J. Abraham, John Wiley & Sons, Hoboken
    • M. A. Avery, J. R. Woolfrey, 'Anti-inflammatory steroids ',in 'Burger's Medicinal Chemistry and Drug Discovery', 6th edn., Ed. D. J. Abraham, John Wiley & Sons, Hoboken, 2003, Vol. 3, p. 747-853.
    • (2003) Burger's Medicinal Chemistry and Drug Discovery , vol.3 , pp. 747-853
    • Avery, M.A.1    Woolfrey, J.R.2
  • 102
    • 0027318905 scopus 로고
    • Hydrolysis of carbonates, thiocarbonates, carbamates, and carboxylic esters of α-naphthol, β-naphthol, and p-nitrophenol by human, rat, and mouse liver carboxylesterases
    • T L. Huang, A. Székács, T. Uematsu, E. Kuwano, A. Parkinson, B. D. Hammock, 'Hydrolysis of carbonates, thiocarbonates, carbamates, and carboxylic esters of α-naphthol, β-naphthol, and p-nitrophenol by human, rat, and mouse liver carboxylesterases', Pharm. Res. 1993, 10, 639-648
    • (1993) Pharm. Res , vol.10 , pp. 639-648
    • Huang, T.L.1    Székács, A.2    Uematsu, T.3    Kuwano, E.4    Parkinson, A.5    Hammock, B.D.6
  • 103
    • 0031916675 scopus 로고    scopus 로고
    • Isozyme-selective metabolism of ethyl carbamate by cytochrome P450 (CYP2El) and carboxylesterase (hydrolase A) enzymes in murine liver microsomes
    • R. P. Lee, A. Parkinson, R G. Forkert, 'Isozyme-selective metabolism of ethyl carbamate by cytochrome P450 (CYP2El) and carboxylesterase (hydrolase A) enzymes in murine liver microsomes', Drug Metab. Dispos. 1998, 26, 60-65.
    • (1998) Drug Metab. Dispos , vol.26 , pp. 60-65
    • Lee, R.P.1    Parkinson, A.2    Forkert, R.G.3
  • 105
    • 0034860456 scopus 로고    scopus 로고
    • The chemistry, toxicology, and identification in rat and human urine of 4-hydroxy-5-phenyl-1,3-oxazaperhydroin-2-one: A reactive metabolite in felbamate bioactivation
    • C. M. Dieckhaus, W. L. Santos, R. D. Sofia, T. L. Macdonald, 'The chemistry, toxicology, and identification in rat and human urine of 4-hydroxy-5-phenyl-1,3-oxazaperhydroin-2-one: a reactive metabolite in felbamate bioactivation', Chem. Res. Toxicol. 2001, 14, 958-964.
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 958-964
    • Dieckhaus, C.M.1    Santos, W.L.2    Sofia, R.D.3    Macdonald, T.L.4
  • 106
    • 0038347273 scopus 로고    scopus 로고
    • Mouse liver and kidney carboxylesterase (M-LK) rapidly hydrolyzes antitumor prodrug irinotecan and the N-terminal three quarter sequence determines substrate selectivity
    • M. Xie, D. Yang, M. Wu, B. Xue, B. Yan, 'Mouse liver and kidney carboxylesterase (M-LK) rapidly hydrolyzes antitumor prodrug irinotecan and the N-terminal three quarter sequence determines substrate selectivity', Drug Metab. Dispos. 2003, 31, 21-27
    • (2003) Drug Metab. Dispos , vol.31 , pp. 21-27
    • Xie, M.1    Yang, D.2    Wu, M.3    Xue, B.4    Yan, B.5
  • 107
    • 26444594410 scopus 로고    scopus 로고
    • Clinical pharmacogentics of irinotecan (CPT-11)
    • Y. Ando, Y. Hasegawa, 'Clinical pharmacogentics of irinotecan (CPT-11)', Drug Metab. Rev. 2005, 37, 565-574.
    • (2005) Drug Metab. Rev , vol.37 , pp. 565-574
    • Ando, Y.1    Hasegawa, Y.2
  • 108
    • 0023153175 scopus 로고
    • Prodrugs of 5-fluorouracil. VIII. Improved rectal and oral delivery of 5-fluorouracil via various prodrugs. Structure-rectal absorption relationships
    • A. Buur, H. Bundgaard, 'Prodrugs of 5-fluorouracil. VIII. Improved rectal and oral delivery of 5-fluorouracil via various prodrugs. Structure-rectal absorption relationships', Int. J. Pharm. 1987, 36, 41-49.
    • (1987) Int. J. Pharm , vol.36 , pp. 41-49
    • Buur, A.1    Bundgaard, H.2
  • 110
    • 20044383036 scopus 로고    scopus 로고
    • Human skin permeation of branched-chain 3-O-alkyl ester and carbonate prodrugs of naltrexone
    • H. K. Vaddi, M. O. Hamad, J. Chen, S. L. Banks, P. A. Cooks, A. L. Stinchcomb, 'Human skin permeation of branched-chain 3-O-alkyl ester and carbonate prodrugs of naltrexone', Pharm. Res. 2005, 22, 758-765.
    • (2005) Pharm. Res , vol.22 , pp. 758-765
    • Vaddi, H.K.1    Hamad, M.O.2    Chen, J.3    Banks, S.L.4    Cooks, P.A.5    Stinchcomb, A.L.6
  • 111
    • 15144355782 scopus 로고    scopus 로고
    • D. K. Kim, N. Lee, Y. W, Kim, K. Chang, J. S. Kim, G. J. Im, W. S. Choi, 1. Jung, T. S. Kim, Y. Y. Hwang, D. S. Min, K. A. Um, Y. B. Cho, K. H. Kim, 'Synthesis and evaluaiton of 2-amino-9-(3-hydroxymethyl-4-alkoxycarbonyloxybut-1-yl) purines as potential prodrugs of penciclovir', J Med. Chem. 1998, 41, 3435-3441.
    • D. K. Kim, N. Lee, Y. W, Kim, K. Chang, J. S. Kim, G. J. Im, W. S. Choi, 1. Jung, T. S. Kim, Y. Y. Hwang, D. S. Min, K. A. Um, Y. B. Cho, K. H. Kim, 'Synthesis and evaluaiton of 2-amino-9-(3-hydroxymethyl-4-alkoxycarbonyloxybut-1-yl) purines as potential prodrugs of penciclovir', J Med. Chem. 1998, 41, 3435-3441.
  • 113
    • 33748702872 scopus 로고    scopus 로고
    • Transesterification of p-hydroxybenzoate esters (parabens) by human intestinal (Caco-2) cells
    • M. Lakeram, A. J. Paine, D. J. Lockley, D. J. Sanders, R. Pendlington, B. Forbes, 'Transesterification of p-hydroxybenzoate esters (parabens) by human intestinal (Caco-2) cells', Xenobiotica 2006, 36, 739-749.
    • (2006) Xenobiotica , vol.36 , pp. 739-749
    • Lakeram, M.1    Paine, A.J.2    Lockley, D.J.3    Sanders, D.J.4    Pendlington, R.5    Forbes, B.6
  • 114
    • 0034090152 scopus 로고    scopus 로고
    • Ethylphenidate formation in human subjects after the administration of a single dose of methylphenidate and ethanol
    • J. S. Markowitz, C. L. Devane, D. W. Boulton, Z. Nahas, S. C. Risch, F Diamond, K. S. Patrick, 'Ethylphenidate formation in human subjects after the administration of a single dose of methylphenidate and ethanol', Drug Metab. Dispos. 2000, 28, 620-624
    • (2000) Drug Metab. Dispos , vol.28 , pp. 620-624
    • Markowitz, J.S.1    Devane, C.L.2    Boulton, D.W.3    Nahas, Z.4    Risch, S.C.5    Diamond, F.6    Patrick, K.S.7
  • 116
    • 17444395255 scopus 로고    scopus 로고
    • Synthesis and pharmacology of ethylphenidate enantiomers: The human transesterification metabolite of methylphenidate and ethanol
    • K. S. Patrick, R. L. Williard, A. L. VanWert, J. J. Dowd, J. E. Oatis Jr., L. D. Middaugh, 'Synthesis and pharmacology of ethylphenidate enantiomers: the human transesterification metabolite of methylphenidate and ethanol', J. Med. Chem. 2005, 48, 2876-2881.
    • (2005) J. Med. Chem , vol.48 , pp. 2876-2881
    • Patrick, K.S.1    Williard, R.L.2    VanWert, A.L.3    Dowd, J.J.4    Oatis Jr., J.E.5    Middaugh, L.D.6
  • 117
    • 0031461193 scopus 로고    scopus 로고
    • 6]ethanol: Preliminary in vitro findings using a rat liver preparation
    • 6]ethanol: preliminary in vitro findings using a rat liver preparation', J. Pharm. Sci. 1997, 86, 1494-1496.
    • (1997) J. Pharm. Sci , vol.86 , pp. 1494-1496
    • Bourland, J.A.1    Martin, D.K.2    Mayersohn, M.3
  • 118
    • 0024912569 scopus 로고
    • Mass spectrometric studies of cocaine disposition in animals and humans using stable isotope-labeled analogues
    • S. P. Jindal, T. Lutz, 'Mass spectrometric studies of cocaine disposition in animals and humans using stable isotope-labeled analogues', J. Pharm. Sci. 1989, 78, 1009-1014.
    • (1989) J. Pharm. Sci , vol.78 , pp. 1009-1014
    • Jindal, S.P.1    Lutz, T.2
  • 119
    • 0026034719 scopus 로고
    • Activities of the enantiomers of cocaine and some related compounds as substrates and inhibitors of plasma butyrylcholinesterase
    • S. J. Gatley, 'Activities of the enantiomers of cocaine and some related compounds as substrates and inhibitors of plasma butyrylcholinesterase', Biochem. Pharmacol. 1991, 41, 1249-1254
    • (1991) Biochem. Pharmacol , vol.41 , pp. 1249-1254
    • Gatley, S.J.1
  • 120
    • 0026455201 scopus 로고    scopus 로고
    • R. B. Melchert, C. Göldlin, U. Zweifel, A. A. Welder, U. A. Boelsterli, 'Differential toxicity of cocaine and its enantiomers, (+)-cocaine and (-)-ψ-cocaine, is associated with stereoselective hydrolysis by hepatic carboxylesterases in cultured rat hepatocytes', Chem.-Biol. Interact. 1992, 84, 243-258.
    • R. B. Melchert, C. Göldlin, U. Zweifel, A. A. Welder, U. A. Boelsterli, 'Differential toxicity of cocaine and its enantiomers, (+)-cocaine and (-)-ψ-cocaine, is associated with stereoselective hydrolysis by hepatic carboxylesterases in cultured rat hepatocytes', Chem.-Biol. Interact. 1992, 84, 243-258.
  • 121
    • 0032944436 scopus 로고    scopus 로고
    • An improved cocaine hydrolase: The A328Y mutant of human butyry1cholinesterase is 4-fold more efficient
    • W. Xie, C. V. Altamirano, C. F. Bartels, R. J. Speirs, J. R. Cashman, O. Lockridge, 'An improved cocaine hydrolase: The A328Y mutant of human butyry1cholinesterase is 4-fold more efficient', Mol. Pharmacol. 1999, 55, 83-91
    • (1999) Mol. Pharmacol , vol.55 , pp. 83-91
    • Xie, W.1    Altamirano, C.V.2    Bartels, C.F.3    Speirs, R.J.4    Cashman, J.R.5    Lockridge, O.6
  • 122
    • 0036073873 scopus 로고    scopus 로고
    • Cocaine metabolism accelerated by a re-engineered human butyrylcholinesterase
    • H. Sun, M. L. Shen, Y.-P. Pang, O. Lockridge, S. Brimijoin, 'Cocaine metabolism accelerated by a re-engineered human butyrylcholinesterase', J. Pharmacol. Exp. Ther. 2002, 302, 710-716.
    • (2002) J. Pharmacol. Exp. Ther , vol.302 , pp. 710-716
    • Sun, H.1    Shen, M.L.2    Pang, Y.-P.3    Lockridge, O.4    Brimijoin, S.5
  • 123
    • 0027948970 scopus 로고
    • Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine
    • M. R. Brzezinski, T. L. Abraham, C. L. Stone, R. A. Dean, W. F. Bosron, 'Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine', Biochem. Pharmacol. 1994, 48, 1747-1755
    • (1994) Biochem. Pharmacol , vol.48 , pp. 1747-1755
    • Brzezinski, M.R.1    Abraham, T.L.2    Stone, C.L.3    Dean, R.A.4    Bosron, W.F.5
  • 125
    • 0038347311 scopus 로고    scopus 로고
    • Cocaethylene metabolism and interaction with cocaine and ethanol: Role of carboxylesterases
    • S. C. Laizure, T. Mandrell, N. M. Gades, R. B. Parker, 'Cocaethylene metabolism and interaction with cocaine and ethanol: role of carboxylesterases', Drug Metab. Dispos. 2003, 31, 16-20
    • (2003) Drug Metab. Dispos , vol.31 , pp. 16-20
    • Laizure, S.C.1    Mandrell, T.2    Gades, N.M.3    Parker, R.B.4
  • 126
    • 0029590085 scopus 로고
    • Tissue distribution of cocaine methyl esterase and ethyl transferase activities: Correlation with carboxylesterase protein
    • R. A. Dean, J. Zhang, M. R. Brzezinski, W. F. Bosron, 'Tissue distribution of cocaine methyl esterase and ethyl transferase activities: Correlation with carboxylesterase protein', J. Pharmacol. Exp. Ther. 1995, 275, 965-971
    • (1995) J. Pharmacol. Exp. Ther , vol.275 , pp. 965-971
    • Dean, R.A.1    Zhang, J.2    Brzezinski, M.R.3    Bosron, W.F.4
  • 127
    • 0031895399 scopus 로고    scopus 로고
    • In vitro transesterification of cocaethylene (ethylcocaine) in the presence of ethanol
    • J. A. Bourland, D. K. Martin, M. Mayersohn, 'In vitro transesterification of cocaethylene (ethylcocaine) in the presence of ethanol', Drug Metab. Dispos. 1998, 26, 203-206.
    • (1998) Drug Metab. Dispos , vol.26 , pp. 203-206
    • Bourland, J.A.1    Martin, D.K.2    Mayersohn, M.3
  • 128
    • 0029069876 scopus 로고
    • Increased blood and brain cocaine concentrations with ethanol cotreatment in mice
    • S. M. Roberts, D. L. Phillips, I. R. Tebbett, 'Increased blood and brain cocaine concentrations with ethanol cotreatment in mice', Drug Metab. Dispos. 1995, 23, 664-666.
    • (1995) Drug Metab. Dispos , vol.23 , pp. 664-666
    • Roberts, S.M.1    Phillips, D.L.2    Tebbett, I.R.3
  • 129
    • 0028865215 scopus 로고
    • Xenobiotic lipids: The inclusion of xenobiotic compounds in pathways of lipid synthesis
    • P. F. Dodds, 'Xenobiotic lipids: the inclusion of xenobiotic compounds in pathways of lipid synthesis', Prog. Lipid Res. 1995, 34, 219-247.
    • (1995) Prog. Lipid Res , vol.34 , pp. 219-247
    • Dodds, P.F.1
  • 130
    • 0033555691 scopus 로고    scopus 로고
    • M. A. Diczfalusy, I. Björkhem, C. Einarsson, S. E. H. Alexson, 'Formation of fatty acid ethyl esters in rat liver microsomes', Eur. J. Biochem. 1999, 259, 404-411
    • M. A. Diczfalusy, I. Björkhem, C. Einarsson, S. E. H. Alexson, 'Formation of fatty acid ethyl esters in rat liver microsomes', Eur. J. Biochem. 1999, 259, 404-411
  • 131
    • 0031041712 scopus 로고    scopus 로고
    • Purification and characterization of rat liver microsomal fatty acid ethyl and 2-chloroethyl ester synthase and their relationship with carboxylesterase (pl 6.1)
    • B. S. Kaphalia, R. R. Fritz, G. A. S. Ansari, 'Purification and characterization of rat liver microsomal fatty acid ethyl and 2-chloroethyl ester synthase and their relationship with carboxylesterase (pl 6.1)', Chem. Res. Toxicol. 1997, 10, 211-218
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 211-218
    • Kaphalia, B.S.1    Fritz, R.R.2    Ansari, G.A.S.3
  • 132
    • 0033376535 scopus 로고    scopus 로고
    • Fatty acid alcohol ester-synthetizing activity of lipoprotein lipase
    • T. Tsujita, M. Sumiyoshi, H. Okuda, 'Fatty acid alcohol ester-synthetizing activity of lipoprotein lipase', J. Biochem. 1999, 126, 1074-1079.
    • (1999) J. Biochem , vol.126 , pp. 1074-1079
    • Tsujita, T.1    Sumiyoshi, M.2    Okuda, H.3
  • 133
    • 0031706126 scopus 로고    scopus 로고
    • Fatty acid ethyl esters: Ethanol metabolites which mediate ethanol-induced organ damage and serve as markers of ethanol intake
    • M. Laposata, 'Fatty acid ethyl esters: ethanol metabolites which mediate ethanol-induced organ damage and serve as markers of ethanol intake', Prog. Lipid Res. 1998, 37, 307-316
    • (1998) Prog. Lipid Res , vol.37 , pp. 307-316
    • Laposata, M.1
  • 134
    • 0022634648 scopus 로고
    • Presence of nonoxidative ethanol metabolism in human organs commonly damaged by ethanol abuse
    • E. A. Laposata, L. L. Lange,'Presence of nonoxidative ethanol metabolism in human organs commonly damaged by ethanol abuse', Science 1986, 231, 497-499.
    • (1986) Science , vol.231 , pp. 497-499
    • Laposata, E.A.1    Lange, L.L.2
  • 135
    • 18844426012 scopus 로고    scopus 로고
    • Hydrolysis kinetics and QSAR investigation of soft antimicrobial agents
    • T. Loftsson, T. Thorsteinsson, M. Másson, 'Hydrolysis kinetics and QSAR investigation of soft antimicrobial agents', J. Pharm. Pharmacol. 2005, 57, 721-727.
    • (2005) J. Pharm. Pharmacol , vol.57 , pp. 721-727
    • Loftsson, T.1    Thorsteinsson, T.2    Másson, M.3
  • 137
    • 1842779114 scopus 로고    scopus 로고
    • Comparative pharmacokinetics and metabolism of levetiracetam, a new anti-epileptic agent, in mouse, rat, rabbit and dog
    • M. Strolin Benedetti, R. Coupez, R. Whomsley, J. M. Nicolas, P. Collart, E. Baltes, 'Comparative pharmacokinetics and metabolism of levetiracetam, a new anti-epileptic agent, in mouse, rat, rabbit and dog', Xenobiotica 2004, 34, 281-30O.
    • (2004) Xenobiotica , vol.34
    • Strolin Benedetti, M.1    Coupez, R.2    Whomsley, R.3    Nicolas, J.M.4    Collart, P.5    Baltes, E.6
  • 139
    • 0025380544 scopus 로고
    • 14C-oxaceprol in Beagle dogs after intramuscular and oral administration
    • 14C-oxaceprol in Beagle dogs after intramuscular and oral administration', Arzneim.-Forsch. 1990, 40, 200-206.
    • (1990) Arzneim.-Forsch , vol.40 , pp. 200-206
    • Lachmann, G.1    Siegemund, B.2    Kusche, W.3
  • 140
    • 0029989021 scopus 로고    scopus 로고
    • Reductive metabolism and its role in the disposition of the hydroxamic angiotensin-converting enzyme inhibitor idrapril calcium in rat
    • A. Lippi, M. Criscuoli, S. Canali, A. Subissi, 'Reductive metabolism and its role in the disposition of the hydroxamic angiotensin-converting enzyme inhibitor idrapril calcium in rat', Xenobiotica 1996, 26, 551-558.
    • (1996) Xenobiotica , vol.26 , pp. 551-558
    • Lippi, A.1    Criscuoli, M.2    Canali, S.3    Subissi, A.4
  • 143
    • 0029095550 scopus 로고
    • Testing the susceptibility of Mycobacterium tuberculosis to pyrazinamide: Comparison of Bactec method with pyrazinamidase assay
    • M. A. Miller, L. Thibert, F. Desjardins, H. Siddiqi, A. Dascal, 'Testing the susceptibility of Mycobacterium tuberculosis to pyrazinamide: comparison of Bactec method with pyrazinamidase assay', J. Clin. Microbiol. 1995, 33, 2468-247O.
    • (1995) J. Clin. Microbiol , vol.33
    • Miller, M.A.1    Thibert, L.2    Desjardins, F.3    Siddiqi, H.4    Dascal, A.5
  • 144
    • 0020568956 scopus 로고
    • Determination of salicylamide and five metabolites in biol.ogical fluids by HPLC
    • M. E. Morris, G. Levy, 'Determination of salicylamide and five metabolites in biol.ogical fluids by HPLC', J. Pharm. Sci. 1983, 72, 612-617.
    • (1983) J. Pharm. Sci , vol.72 , pp. 612-617
    • Morris, M.E.1    Levy, G.2
  • 145
    • 0023792429 scopus 로고
    • Metabolism of a new inotropic agent, 3,4-dihydro-6-[4-(3,4-dimethoxybenzoyl)-1-piperazinyl]-2-(l H)-quinolinone (OPC-8212), in the rat, mouse, dog, monkey, and human
    • G. Miyamoto, H. Sasabe, N. Tominaga, N. Uegaki, M. Tominaga, T. Shimizu, 'Metabolism of a new inotropic agent, 3,4-dihydro-6-[4-(3,4-dimethoxybenzoyl)-1-piperazinyl]-2-(l H)-quinolinone (OPC-8212), in the rat, mouse, dog, monkey, and human', Xenobiotica 1988, 18, 1143-1155.
    • (1988) Xenobiotica , vol.18 , pp. 1143-1155
    • Miyamoto, G.1    Sasabe, H.2    Tominaga, N.3    Uegaki, N.4    Tominaga, M.5    Shimizu, T.6
  • 146
    • 0033917858 scopus 로고    scopus 로고
    • Phenacetin deacetylase activity in human liver microsomes: Distribution, kinetics, and chemical inhibition and stimulation
    • S. Kudo, K. Umehara, M. Hosokawa, G. Miyamoto, K. Chiba, T. Satoh, 'Phenacetin deacetylase activity in human liver microsomes: distribution, kinetics, and chemical inhibition and stimulation', J. Pharmacol. Exp. Ther. 2000, 294, 80-88.
    • (2000) J. Pharmacol. Exp. Ther , vol.294 , pp. 80-88
    • Kudo, S.1    Umehara, K.2    Hosokawa, M.3    Miyamoto, G.4    Chiba, K.5    Satoh, T.6
  • 147
    • 0030697378 scopus 로고    scopus 로고
    • NMR spectroscopic studies on the metabolism and futile deacetylation of phenacetin in the rat
    • A. W. Nicholls, J. C. Lindon, S. Caddick, R. D. Farrant, I. D. Wilson, J. K. Nicholson, 'NMR spectroscopic studies on the metabolism and futile deacetylation of phenacetin in the rat', Xenobiotica 1997, 27, 1175-1186
    • (1997) Xenobiotica , vol.27 , pp. 1175-1186
    • Nicholls, A.W.1    Lindon, J.C.2    Caddick, S.3    Farrant, R.D.4    Wilson, I.D.5    Nicholson, J.K.6
  • 149
    • 0030459494 scopus 로고    scopus 로고
    • Identification of 2,6-xylidine as a major lidocaine metabolite in human liver slices
    • R. J. Parker, J. M. Collins, J. M. Strong, 'Identification of 2,6-xylidine as a major lidocaine metabolite in human liver slices', Drug Metab. Dispos. 1996, 24, 1167-1173
    • (1996) Drug Metab. Dispos , vol.24 , pp. 1167-1173
    • Parker, R.J.1    Collins, J.M.2    Strong, J.M.3
  • 150
    • 0036266122 scopus 로고    scopus 로고
    • Involvement of liver carboxylesterases in the in vitro metabolism of lidocaine
    • S. E. H. Axelson, M. Diczfalusy, M. Halldin, S. Swedmark, 'Involvement of liver carboxylesterases in the in vitro metabolism of lidocaine', Drug Metab. Dispos. 2002, 30, 643-647.
    • (2002) Drug Metab. Dispos , vol.30 , pp. 643-647
    • Axelson, S.E.H.1    Diczfalusy, M.2    Halldin, M.3    Swedmark, S.4
  • 151
    • 0024951492 scopus 로고
    • Oxicams: Metabolic disposition in man and animals
    • T. F. Woolf, L. L. Radulovic,'Oxicams: metabolic disposition in man and animals', Drug Metab. Rev. 1989, 21, 255-276
    • (1989) Drug Metab. Rev , vol.21 , pp. 255-276
    • Woolf, T.F.1    Radulovic, L.L.2
  • 153
    • 0023791164 scopus 로고
    • Metabolism of the prodrug DEGA (N-(2,6-dimethylphenyl)-4-[diethylamino)acetyl]amino]benzamide) to the potent anticonvulsant LY201116 in mice. Effect of bis-(p-nitrophenyl)phosphate
    • C. J. Parli, E. Evenson, B. D. Potts, E. Beedle, R. Lawson, D. W. Robertson, J. D. Leander, 'Metabolism of the prodrug DEGA (N-(2,6-dimethylphenyl)-4-[diethylamino)acetyl]amino]benzamide) to the potent anticonvulsant LY201116 in mice. Effect of bis-(p-nitrophenyl)phosphate', Drug Metab. Dispos. 1988, 16, 707-711
    • (1988) Drug Metab. Dispos , vol.16 , pp. 707-711
    • Parli, C.J.1    Evenson, E.2    Potts, B.D.3    Beedle, E.4    Lawson, R.5    Robertson, D.W.6    Leander, J.D.7
  • 154
    • 0024839968 scopus 로고
    • Metabolism, disposition, and pharmacokinetics of a potent anticonvulsant, 4-amino-N-(2,6-dimethylphenyl)benzamide (LY201116), in rats
    • B. D. Potts, S. Gabriel, C. J. Parli, 'Metabolism, disposition, and pharmacokinetics of a potent anticonvulsant, 4-amino-N-(2,6-dimethylphenyl)benzamide (LY201116), in rats', Drug Metab. Dispos. 1989, 17, 656-661.
    • (1989) Drug Metab. Dispos , vol.17 , pp. 656-661
    • Potts, B.D.1    Gabriel, S.2    Parli, C.J.3
  • 155
    • 0028326915 scopus 로고
    • Metabolism of aspartame by human and pig intestinal microvillar peptidases
    • N. M. Hooper, R. J. Hesp, S. Ticku, 'Metabolism of aspartame by human and pig intestinal microvillar peptidases', Biochem. J. 1994, 298, 635-639.
    • (1994) Biochem. J , vol.298 , pp. 635-639
    • Hooper, N.M.1    Hesp, R.J.2    Ticku, S.3
  • 157
    • 0029084078 scopus 로고
    • Metabolism of oxytocin in human decidua, chorion, and placenta
    • B. F. Mitchell, S. Wong, 'Metabolism of oxytocin in human decidua, chorion, and placenta', J. Clin. Endocrinol. Metab. 1995, 80, 2729-2733.
    • (1995) J. Clin. Endocrinol. Metab , vol.80 , pp. 2729-2733
    • Mitchell, B.F.1    Wong, S.2
  • 160
    • 0031422606 scopus 로고    scopus 로고
    • Rat jejunal permeability and metabolism of μ-selective tetrapeptides in gastrointestinal fluids from humans and rats
    • E. Krondahl, A. Orzechowski, G. Ekström, H. Lennernä ,'Rat jejunal permeability and metabolism of μ-selective tetrapeptides in gastrointestinal fluids from humans and rats', Pharm. Res. 1997, 14, 1780-1785
    • (1997) Pharm. Res , vol.14 , pp. 1780-1785
    • Krondahl, E.1    Orzechowski, A.2    Ekström, G.3    Lennernä, H.4
  • 161
    • 0033941442 scopus 로고    scopus 로고
    • Investigation of the in-vitro metabolism of three opioid tetrapeptides by pancreatic and intestinal enzymes
    • E. Krondahl, H. von Euler-Chelpin, A. Orzechowski, G. Ekström, H. Lennernäs, 'Investigation of the in-vitro metabolism of three opioid tetrapeptides by pancreatic and intestinal enzymes', J. Pharm. Pharmacol. 2000, 52, 785-795.
    • (2000) J. Pharm. Pharmacol , vol.52 , pp. 785-795
    • Krondahl, E.1    von Euler-Chelpin, H.2    Orzechowski, A.3    Ekström, G.4    Lennernäs, H.5
  • 162
    • 0141680887 scopus 로고    scopus 로고
    • Peptide science: Exploring the use of chemical principles and interdisciplinary collaboration for understanding life processes
    • V J. Hruby, 'Peptide science: exploring the use of chemical principles and interdisciplinary collaboration for understanding life processes', J. Med. Chem. 2003, 46, 4215-4231.
    • (2003) J. Med. Chem , vol.46 , pp. 4215-4231
    • Hruby, V.J.1
  • 163
    • 34948892665 scopus 로고    scopus 로고
    • 'Pseudo-peptides in Drug Discovery', Ed. P. E. Nielsen, Wiley-VCH, Weinheim, 2004.
    • 'Pseudo-peptides in Drug Discovery', Ed. P. E. Nielsen, Wiley-VCH, Weinheim, 2004.
  • 164
    • 18544399515 scopus 로고    scopus 로고
    • M. Schwalm, H. Schupke, A. Gasparic, a Krone, G. Peter, R. Hempel, T. Kronbach, M. Locher, W. Jahn, J. Engel, 'Disposition and metabolism of cetrorelix, a potent luteinizing hormone-releasing hormone antagonist, in rats and dogs', Drug Metab. Dispos. 2000, 28, 10-2O.
    • M. Schwalm, H. Schupke, A. Gasparic, a Krone, G. Peter, R. Hempel, T. Kronbach, M. Locher, W. Jahn, J. Engel, 'Disposition and metabolism of cetrorelix, a potent luteinizing hormone-releasing hormone antagonist, in rats and dogs', Drug Metab. Dispos. 2000, 28, 10-2O.
  • 166
    • 0031881755 scopus 로고    scopus 로고
    • Hydrophilicity/lipophilicity: Relevance for the pharmacology and clinical effects of HMG-CoA reductase inhibitors
    • a) B. A. Hamelin, J. Turgeon, 'Hydrophilicity/lipophilicity: relevance for the pharmacology and clinical effects of HMG-CoA reductase inhibitors', Trends Pharmacol. Sci. 1998, 19, 26-37
    • (1998) Trends Pharmacol. Sci , vol.19 , pp. 26-37
    • Hamelin, B.A.1    Turgeon, J.2
  • 167
    • 0035843962 scopus 로고    scopus 로고
    • Structural mechanism for statin inhibition of HMG-CoA reductase
    • b) E. S. Istvan, J. Deisenhofer, 'Structural mechanism for statin inhibition of HMG-CoA reductase', Science 2001 292, 1160-1164
    • (2001) Science , vol.292 , pp. 1160-1164
    • Istvan, E.S.1    Deisenhofer, J.2
  • 168
    • 33846245420 scopus 로고    scopus 로고
    • The origin of the statins
    • c) A. Endo, 'The origin of the statins', Int. Congr. Ser. 2004, 1262, 3-8.
    • (2004) Int. Congr. Ser , vol.1262 , pp. 3-8
    • Endo, A.1
  • 169
    • 0031736655 scopus 로고    scopus 로고
    • Metabolism and drug interactions of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors in transplant patients: Are the statins mechanistically similar?
    • a) U. Christians, W. Jacobsen, L. C. Floren, 'Metabolism and drug interactions of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors in transplant patients: are the statins mechanistically similar?', Pharmcol. Ther. 1998, 80, 1-34
    • (1998) Pharmcol. Ther , vol.80 , pp. 1-34
    • Christians, U.1    Jacobsen, W.2    Floren, L.C.3
  • 171
    • 11244283910 scopus 로고    scopus 로고
    • Metabolic properties of the acid and lactone forms of HMG-CoA reductase inhibitors
    • c) H. Fujino, T. Saito, Y. Tsunenari, J. Kojima, T. Sakaeda, 'Metabolic properties of the acid and lactone forms of HMG-CoA reductase inhibitors', Xenobiotica 2004, 34, 961-971
    • (2004) Xenobiotica , vol.34 , pp. 961-971
    • Fujino, H.1    Saito, T.2    Tsunenari, Y.3    Kojima, J.4    Sakaeda, T.5
  • 172
    • 33847099636 scopus 로고    scopus 로고
    • Predicting the oxidative metabolism of statins. An application of the MetaSite algorithm
    • d) G. Caron, G. Ermondi, B. Testa, 'Predicting the oxidative metabolism of statins. An application of the MetaSite algorithm', Pharm. Res. 2007, 24, 480-501.
    • (2007) Pharm. Res , vol.24 , pp. 480-501
    • Caron, G.1    Ermondi, G.2    Testa, B.3
  • 173
    • 0025667111 scopus 로고
    • Rate and equilibrium constants for acid-catalyzed lactone hydrolysis of HMG-CoA reductase inhibitors
    • M. J. Kaufman,'Rate and equilibrium constants for acid-catalyzed lactone hydrolysis of HMG-CoA reductase inhibitors', Int. J. Pharmaceut. 1990, 66, 97-106.
    • (1990) Int. J. Pharmaceut , vol.66 , pp. 97-106
    • Kaufman, M.J.1
  • 174
  • 175
    • 0042261695 scopus 로고    scopus 로고
    • Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3
    • J. F Teiber, D. I. Draganov, B. N. La Du, 'Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3', Biochem. Pharmacol. 2003, 66, 887-896.
    • (2003) Biochem. Pharmacol , vol.66 , pp. 887-896
    • Teiber, J.F.1    Draganov, D.I.2    La Du, B.N.3
  • 179
    • 0037235204 scopus 로고    scopus 로고
    • Metabolic fate of pitavastatin, a new inhibitor of HMG-CoA reductase: Human UDP-glucuronosyltransferase enzymes involved in lactonization
    • H. Fujino, I. Yamada, S. Shimada, M. Yoneda, J. Kojima, 'Metabolic fate of pitavastatin, a new inhibitor of HMG-CoA reductase: human UDP-glucuronosyltransferase enzymes involved in lactonization', Xenobiotica 2003, 33, 27-41.
    • (2003) Xenobiotica , vol.33 , pp. 27-41
    • Fujino, H.1    Yamada, I.2    Shimada, S.3    Yoneda, M.4    Kojima, J.5
  • 181
    • 0026791752 scopus 로고
    • Improved oral bioavailability of salicylamide in rabbits by a 1,3-benzoxazine-2,4-dione prodrug
    • A. H. Kahns, J. Moss, H. Bundgaard, 'Improved oral bioavailability of salicylamide in rabbits by a 1,3-benzoxazine-2,4-dione prodrug', Int. J Pharm. 1992, 78, 199-202.
    • (1992) Int. J Pharm , vol.78 , pp. 199-202
    • Kahns, A.H.1    Moss, J.2    Bundgaard, H.3
  • 182
    • 0036115697 scopus 로고    scopus 로고
    • Kinetics and mechnanism of hydrolysis of efavirenz
    • M. B. Maurin, S. M. Rowe, K. Blom, M. E. Pierce, 'Kinetics and mechnanism of hydrolysis of efavirenz', Pharm. Res. 2002, 19, 517-521.
    • (2002) Pharm. Res , vol.19 , pp. 517-521
    • Maurin, M.B.1    Rowe, S.M.2    Blom, K.3    Pierce, M.E.4
  • 183
    • 18144449536 scopus 로고    scopus 로고
    • Protection by L-2-oxothiazolidine-4-carboxylic acid of hydrogen peroxide-induced CDζ and CD3ζ chain downregulation in human peripheral blood lymphocytes and lymphokine-activated killer cells
    • M. M. Corsi, H. H. Maes, K. Wasserman, A. Fulgenzi, G. Gaja, M. E. Ferrero, 'Protection by L-2-oxothiazolidine-4-carboxylic acid of hydrogen peroxide-induced CDζ and CD3ζ chain downregulation in human peripheral blood lymphocytes and lymphokine-activated killer cells', Biochem. Pharmacol. 1998, 56, 657-662.
    • (1998) Biochem. Pharmacol , vol.56 , pp. 657-662
    • Corsi, M.M.1    Maes, H.H.2    Wasserman, K.3    Fulgenzi, A.4    Gaja, G.5    Ferrero, M.E.6
  • 184
    • 27844468083 scopus 로고    scopus 로고
    • Novel organic nitrate prodrug (4R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide (RS-7897) serves as a xenobiotic substrate for pyroglutamyl aminopeptidase I in dogs
    • K. Abe, M. Yamada, T. Terao, H. Mizuno, Y. Matsuoka, R. Yorikane, T. Tokui, T. Ikeda, 'Novel organic nitrate prodrug (4R)-N-(2-nitroxyethyl)-2-oxothiazolidine-4-carboxamide (RS-7897) serves as a xenobiotic substrate for pyroglutamyl aminopeptidase I in dogs', Drug Metab. Pharmacokinet. 2003, 18, 373-38O.
    • (2003) Drug Metab. Pharmacokinet , vol.18
    • Abe, K.1    Yamada, M.2    Terao, T.3    Mizuno, H.4    Matsuoka, Y.5    Yorikane, R.6    Tokui, T.7    Ikeda, T.8
  • 185
    • 0023850656 scopus 로고
    • Studies on prodrugs. VIII. Preparation and characterization of (5-methyl-2-oxo-1,3-dioxol-4-yl)methyl esters of sulbactam and its analogs
    • S. Ikeda, F. Sakamoto, R. Hirayama, Y. Takebe, M. Sotomura, G. Tsukamoto, 'Studies on prodrugs. VIII. Preparation and characterization of (5-methyl-2-oxo-1,3-dioxol-4-yl)methyl esters of sulbactam and its analogs', Chem. Pharm. Bull. 1988, 36, 218-226
    • (1988) Chem. Pharm. Bull , vol.36 , pp. 218-226
    • Ikeda, S.1    Sakamoto, F.2    Hirayama, R.3    Takebe, Y.4    Sotomura, M.5    Tsukamoto, G.6
  • 186
    • 0031920093 scopus 로고    scopus 로고
    • Paraoxonase has a major role in the hydrolysis of prulifloxacin (NM441), a prodrug of a new antibacterial agent
    • K. Tougou, A. Nakamura, S. Watanabe, Y. Okuyama, A. Morino, 'Paraoxonase has a major role in the hydrolysis of prulifloxacin (NM441), a prodrug of a new antibacterial agent', Drug Metab. Dispos. 1998, 26, 355-359.
    • (1998) Drug Metab. Dispos , vol.26 , pp. 355-359
    • Tougou, K.1    Nakamura, A.2    Watanabe, S.3    Okuyama, Y.4    Morino, A.5
  • 187
    • 0026049801 scopus 로고
    • Serine beta-lactamases and penicillin-binding proteins
    • J. M. Ghuysen,'Serine beta-lactamases and penicillin-binding proteins', Annu. Rev. Microbiol. 1991, 45, 37-67
    • (1991) Annu. Rev. Microbiol , vol.45 , pp. 37-67
    • Ghuysen, J.M.1
  • 188
    • 0029019031 scopus 로고
    • Beta-lactamases and bacterial resistance to antibiotics
    • J. M. Frère, 'Beta-lactamases and bacterial resistance to antibiotics', Mol. Microbiol. 1995, 16, 385-395
    • (1995) Mol. Microbiol , vol.16 , pp. 385-395
    • Frère, J.M.1
  • 189
    • 0033051211 scopus 로고    scopus 로고
    • The beta-lactam antibiotics: Past, present, and future
    • A. L. Demain, R. P. Elander, 'The beta-lactam antibiotics: past, present, and future', Antonie van Leeuwenhoek 1999, 75, 5-19.
    • (1999) Antonie van Leeuwenhoek , vol.75 , pp. 5-19
    • Demain, A.L.1    Elander, R.P.2
  • 191
    • 84879020577 scopus 로고    scopus 로고
    • C. Hubschwerlen, 'β-Lactam antibiotics', 'Therapeutic Areas II: Cancer, Infectious Diseases, Inflammation & Dermatology',Eds. J. J. Plattner, M. C. Desai, 7 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 479-518.
    • C. Hubschwerlen, 'β-Lactam antibiotics', 'Therapeutic Areas II: Cancer, Infectious Diseases, Inflammation & Dermatology',Eds. J. J. Plattner, M. C. Desai, Vol. 7 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 479-518.
  • 192
    • 0033857450 scopus 로고    scopus 로고
    • Correlation of penicillin structure with rate constant for basic hydrolysis
    • M. Grover, M. Gulati, B. Singh, S. Singh, 'Correlation of penicillin structure with rate constant for basic hydrolysis', Pharm. Pharmacol. Commun. 2000, 6, 355-363
    • (2000) Pharm. Pharmacol. Commun , vol.6 , pp. 355-363
    • Grover, M.1    Gulati, M.2    Singh, B.3    Singh, S.4
  • 193
    • 0034597574 scopus 로고    scopus 로고
    • Hydrolytic stability versus ring size in lactams: Implications for the development of lactam antibiotics and other serine protease inhibitors
    • P. Imming, B. Klar, D. Dix, 'Hydrolytic stability versus ring size in lactams: implications for the development of lactam antibiotics and other serine protease inhibitors', J. Med. Chem. 2000, 43, 4328-4331
    • (2000) J. Med. Chem , vol.43 , pp. 4328-4331
    • Imming, P.1    Klar, B.2    Dix, D.3
  • 194
    • 0034725847 scopus 로고    scopus 로고
    • The chemical reactivity of β-lactams, β-sultams and β-phospholactams
    • M. I. Page, A. P. Laws, 'The chemical reactivity of β-lactams, β-sultams and β-phospholactams', Tetrahedron Lett. 2000, 56, 5631-5638.
    • (2000) Tetrahedron Lett , vol.56 , pp. 5631-5638
    • Page, M.I.1    Laws, A.P.2
  • 196
    • 0027427697 scopus 로고
    • Biotransformation of the antidepressant D,L-rolipram. II. Metabolite patterns in man, rat, rabbit, rhesus and cynomolgus monkey
    • W. Krause, G. Kühne, 'Biotransformation of the antidepressant D,L-rolipram. II. Metabolite patterns in man, rat, rabbit, rhesus and cynomolgus monkey', Xenobiotica 1993, 23, 1277-1288.
    • (1993) Xenobiotica , vol.23 , pp. 1277-1288
    • Krause, W.1    Kühne, G.2
  • 198
    • 0026030527 scopus 로고
    • Comparative studies on the anticonvulsant activity of lipophilic derivatives of γ-aminobutyric acid and 2-pyrrolidinone in mice
    • J. Nakamura, T. Miwa, Y. Mori, H. Saski, 'Comparative studies on the anticonvulsant activity of lipophilic derivatives of γ-aminobutyric acid and 2-pyrrolidinone in mice', J Pharmacobiodyn. 1991, 14, 1-8.
    • (1991) J Pharmacobiodyn , vol.14 , pp. 1-8
    • Nakamura, J.1    Miwa, T.2    Mori, Y.3    Saski, H.4
  • 199
    • 0023205094 scopus 로고
    • Metabolic disposition of rolziracetam in laboratory animals
    • A. Black, T. Chang, 'Metabolic disposition of rolziracetam in laboratory animals', Eur. J. Drug Metab. Pharmacokinet. 1987, 12, 135-143
    • (1987) Eur. J. Drug Metab. Pharmacokinet , vol.12 , pp. 135-143
    • Black, A.1    Chang, T.2
  • 200
    • 0028224652 scopus 로고
    • Piracetam and other structurally related nootropics
    • A. H. Gouliaev, A. Senning, 'Piracetam and other structurally related nootropics', Brain Res. Rev. 1994, 19, 180-222.
    • (1994) Brain Res. Rev , vol.19 , pp. 180-222
    • Gouliaev, A.H.1    Senning, A.2
  • 201
    • 0032897603 scopus 로고    scopus 로고
    • Stereoselective metabolism of dexrazoxane (ICRF-187) and levrazoxane (ICRF-186)
    • B. B. Hasinoff, R. G. Aoyama, 'Stereoselective metabolism of dexrazoxane (ICRF-187) and levrazoxane (ICRF-186), Chirality 1999, 11, 286-290
    • (1999) Chirality , vol.11 , pp. 286-290
    • Hasinoff, B.B.1    Aoyama, R.G.2
  • 202
    • 0032942847 scopus 로고    scopus 로고
    • Relative plasma levels of the cardioprotective drug dexrazoxane and its two active ring-opened metabolites in the rat
    • B. B. Hasinoff, R. G. Aoyama, 'Relative plasma levels of the cardioprotective drug dexrazoxane and its two active ring-opened metabolites in the rat', Drug Metab. Dispos. 1999, 27, 265-268.
    • (1999) Drug Metab. Dispos , vol.27 , pp. 265-268
    • Hasinoff, B.B.1    Aoyama, R.G.2
  • 203
    • 0032411785 scopus 로고    scopus 로고
    • Chiral inversion and hydrolysis of thalidomide: Mechanisms and catalysis by bases and serum albumin, and chiral stability of teratogenic metabolites
    • a) M. Reist, P. A. Carrupt, E. Francotte, B. Testa, 'Chiral inversion and hydrolysis of thalidomide: mechanisms and catalysis by bases and serum albumin, and chiral stability of teratogenic metabolites', Chem. Res. Toxicol. 1998, 11, 1521-1528
    • (1998) Chem. Res. Toxicol , vol.11 , pp. 1521-1528
    • Reist, M.1    Carrupt, P.A.2    Francotte, E.3    Testa, B.4
  • 205
    • 0029147401 scopus 로고
    • Experimental studies on the pharmacokinetics and toxicity of 5-aminosalicylic acid-O-sulfate following local and systemic application
    • R. Herzog, J. Leuschner, 'Experimental studies on the pharmacokinetics and toxicity of 5-aminosalicylic acid-O-sulfate following local and systemic application', Arzneim.-Forsch. 1995, 45, 300-303.
    • (1995) Arzneim.-Forsch , vol.45 , pp. 300-303
    • Herzog, R.1    Leuschner, J.2
  • 206
    • 0026769059 scopus 로고
    • The metabolism of cyclamate to cyclohexylamine and its cardiovascular consequences in human volunteers
    • N. E. Buss, A. G. Renwick, K. M. Donaldson, C. F. George, 'The metabolism of cyclamate to cyclohexylamine and its cardiovascular consequences in human volunteers', Toxicol. Appl. Pharmacol. 1992, 115, 199-209.
    • (1992) Toxicol. Appl. Pharmacol , vol.115 , pp. 199-209
    • Buss, N.E.1    Renwick, A.G.2    Donaldson, K.M.3    George, C.F.4
  • 207
    • 0032989064 scopus 로고    scopus 로고
    • Organic nitrates
    • W. Sneader, 'Organic nitrates', Drug News Perspect. 1999, 12, 58-63
    • (1999) Drug News Perspect , vol.12 , pp. 58-63
    • Sneader, W.1
  • 208
    • 0028858786 scopus 로고    scopus 로고
    • A. R. Butler, F. W. Flitney, D. L. H. Williams, 'NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: a chemist's perspective', Trends Pharmacol. Sci. 1995, 16, 18-22
    • A. R. Butler, F. W. Flitney, D. L. H. Williams, 'NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: a chemist's perspective', Trends Pharmacol. Sci. 1995, 16, 18-22
  • 209
    • 0029835762 scopus 로고    scopus 로고
    • Bioactivation of organic nitrates and other nitrovasodilators
    • Eds. B. Testa, U. A. Meyer, Academic Press, London
    • H. Schröder, 'Bioactivation of organic nitrates and other nitrovasodilators', in 'Advances in Drug Research', Vol. 28, Eds. B. Testa, U. A. Meyer, Academic Press, London, 1996, p. 253-267.
    • (1996) Advances in Drug Research , vol.28 , pp. 253-267
    • Schröder, H.1
  • 213
    • 0242299572 scopus 로고    scopus 로고
    • Synthesis, in vitro evaluation, and intraocular pressure effects of water-soluble prodrugs of endocannabinoid noladin ether
    • J. Juntunen, J. Vepsäläinen, R. Niemi, K. Lame, T. Järvinen, 'Synthesis, in vitro evaluation, and intraocular pressure effects of water-soluble prodrugs of endocannabinoid noladin ether', J. Med. Chem. 2003, 46, 5083-5086
    • (2003) J. Med. Chem , vol.46 , pp. 5083-5086
    • Juntunen, J.1    Vepsäläinen, J.2    Niemi, R.3    Lame, K.4    Järvinen, T.5
  • 214
    • 25844481538 scopus 로고    scopus 로고
    • In-vitro corneal permeation of cannabinoids and their water-soluble phosphate ester prodrugs
    • J. Juntunen, T. Järvinen, R. Niemi, 'In-vitro corneal permeation of cannabinoids and their water-soluble phosphate ester prodrugs', J. Pharm. Pharmacol. 2005, 57, 1153-1157.
    • (2005) J. Pharm. Pharmacol , vol.57 , pp. 1153-1157
    • Juntunen, J.1    Järvinen, T.2    Niemi, R.3
  • 215
    • 0345669115 scopus 로고    scopus 로고
    • Bisphosphonate prodrugs: Synthesis and in vitro evaluation of novel acyloxyalkyl esters of clodronic acid
    • R. Niemi, J. Vepsäläinen, H. Taipale, T. Järvinen, 'Bisphosphonate prodrugs: synthesis and in vitro evaluation of novel acyloxyalkyl esters of clodronic acid', J. Med. Chem. 1999, 42, 5053-5058.
    • (1999) J. Med. Chem , vol.42 , pp. 5053-5058
    • Niemi, R.1    Vepsäläinen, J.2    Taipale, H.3    Järvinen, T.4
  • 216
    • 0033736202 scopus 로고    scopus 로고
    • Pronucleotides: Toward the in vivo delivery of antiviral and anticancer nucleotides
    • C. R. Wagner, V. V. Iyer, E. J. Mclntee, 'Pronucleotides: Toward the in vivo delivery of antiviral and anticancer nucleotides', Med. Res. Rev. 2000, 20, 417-451.
    • (2000) Med. Res. Rev , vol.20 , pp. 417-451
    • Wagner, C.R.1    Iyer, V.V.2    Mclntee, E.J.3
  • 217
    • 19444364011 scopus 로고    scopus 로고
    • Prodrug strategies in the design of nucleoside and nucleotide antiviral therapeutics
    • R. L. Mackman, T. Cihar, 'Prodrug strategies in the design of nucleoside and nucleotide antiviral therapeutics', Annu. Rep. Med. Chem. 2004, 39, 305-321.
    • (2004) Annu. Rep. Med. Chem , vol.39 , pp. 305-321
    • Mackman, R.L.1    Cihar, T.2
  • 218
    • 0033664988 scopus 로고    scopus 로고
    • J. Van Gelder, S. Deferme, P. Annaert, L. Naesens, E. de Clercq, G. Van den Mooter, R. Kinget, P, Augustijns, 'Increased absorption of the antiviral ester prodrug tenofovir disoproxil in rat ileum by inhibiting its intestinal metabolism', Drug Metab. Dispos. 2000, 28, 1394-1396
    • J. Van Gelder, S. Deferme, P. Annaert, L. Naesens, E. de Clercq, G. Van den Mooter, R. Kinget, P, Augustijns, 'Increased absorption of the antiviral ester prodrug tenofovir disoproxil in rat ileum by inhibiting its intestinal metabolism', Drug Metab. Dispos. 2000, 28, 1394-1396
  • 219
    • 30344432397 scopus 로고    scopus 로고
    • Multidrug resistance-associated protein 2 (MRP2) affects hepatobiliary elimination but not the intestinal disposition of tenofovir disoproxil fumarate and its metabolites
    • R. Mallants, K. Van Oosterwyck, L. Van Vaeck, R. Mols, E. de Clereq, P. Augustijns, 'Multidrug resistance-associated protein 2 (MRP2) affects hepatobiliary elimination but not the intestinal disposition of tenofovir disoproxil fumarate and its metabolites', Xenobiotica 2005, 35, 1055-1066.
    • (2005) Xenobiotica , vol.35 , pp. 1055-1066
    • Mallants, R.1    Van Oosterwyck, K.2    Van Vaeck, L.3    Mols, R.4    de Clereq, E.5    Augustijns, P.6
  • 220
    • 17644377247 scopus 로고    scopus 로고
    • Bis(carbamoyloxymethyl) esters of 2′,3′-dideoxyuridine 5′-monophosphate (ddUMP) as potential ddUMP prodrugs
    • S. R. Khan, S. K. Kumar, D. Farquhar, 'Bis(carbamoyloxymethyl) esters of 2′,3′-dideoxyuridine 5′-monophosphate (ddUMP) as potential ddUMP prodrugs', Pharm. Res. 2005, 22, 390-396.
    • (2005) Pharm. Res , vol.22 , pp. 390-396
    • Khan, S.R.1    Kumar, S.K.2    Farquhar, D.3
  • 222
    • 7444221716 scopus 로고    scopus 로고
    • Kinetic analysis of interactions between human acetyleholinesterase, structurally different organophosphorus compounds and oximes
    • F. Worek, H. Thiermann, L. Szinicz, P. Eyer, 'Kinetic analysis of interactions between human acetyleholinesterase, structurally different organophosphorus compounds and oximes', Biochem. Pharmacol. 2004, 68, 2237-2248.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 2237-2248
    • Worek, F.1    Thiermann, H.2    Szinicz, L.3    Eyer, P.4
  • 223
    • 0028240005 scopus 로고
    • Kinetic mechanism of the detoxification of the organophosphate paraoxon by human serum A-esterase
    • J. A. Vitarius, L. G. Sultatos, 'Kinetic mechanism of the detoxification of the organophosphate paraoxon by human serum A-esterase', Drug Metab. Dispos. 1994, 22, 472-478.
    • (1994) Drug Metab. Dispos , vol.22 , pp. 472-478
    • Vitarius, J.A.1    Sultatos, L.G.2
  • 224
    • 0030902962 scopus 로고    scopus 로고
    • In vitro metabolism of the new insecticide flupyrazofos by rat liver microsomes
    • H. S. Lee, S. Jeong, K. Kim, J. H. Kim, S. K. Lee, B. H. Kang, J. K. Roh, 'In vitro metabolism of the new insecticide flupyrazofos by rat liver microsomes', Xenobiotica 1997, 27, 423-429.
    • (1997) Xenobiotica , vol.27 , pp. 423-429
    • Lee, H.S.1    Jeong, S.2    Kim, K.3    Kim, J.H.4    Lee, S.K.5    Kang, B.H.6    Roh, J.K.7
  • 225
    • 0033943981 scopus 로고    scopus 로고
    • G. B. Quistad, N. Zhang, S. E. Sparks, J. E. Casida, 'Phosphoacetylcholinesterase: Toxicity of phosphorus oxychloride to mammals and insects that can be attributed to selective phosphorylation of acetylcholinesterase by phosphorodichloridic acid', Chem. Res. Toxicol. 2000, 13, 652-657.
    • G. B. Quistad, N. Zhang, S. E. Sparks, J. E. Casida, 'Phosphoacetylcholinesterase: Toxicity of phosphorus oxychloride to mammals and insects that can be attributed to selective phosphorylation of acetylcholinesterase by phosphorodichloridic acid', Chem. Res. Toxicol. 2000, 13, 652-657.
  • 226
    • 0029871481 scopus 로고    scopus 로고
    • Interaction of organophosphorus compounds with carboxylesterases in the rat
    • M. Jokanovic, M. Kosanovic, M. Maksimovic, 'Interaction of organophosphorus compounds with carboxylesterases in the rat', Arch. Toxicol. 1996, 70, 444-450.
    • (1996) Arch. Toxicol , vol.70 , pp. 444-450
    • Jokanovic, M.1    Kosanovic, M.2    Maksimovic, M.3
  • 227
    • 77957561475 scopus 로고    scopus 로고
    • W. F. Trager, 'Principles of drug metabolism 1: Redox reactions', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 87-132.
    • W. F. Trager, 'Principles of drug metabolism 1: Redox reactions', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, Vol. 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. J. B. Taylor, D. J. Triggle, Elsevier, Oxford, 2007, p. 87-132.
  • 230
    • 0032849109 scopus 로고    scopus 로고
    • Detoxification of environmental mutagens and carcinogens: Structure, mechanism, and evolution of liver epoxide hydrolase
    • M. A. Argiriadi, C. Morisseau, B. D. Hammock, D. W. Christianson, 'Detoxification of environmental mutagens and carcinogens: Structure, mechanism, and evolution of liver epoxide hydrolase', Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 10637-10642
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 10637-10642
    • Argiriadi, M.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 231
    • 0032934961 scopus 로고    scopus 로고
    • Genetic polymorphisms of human N-acetyl-transferase, cytochrome P450, glutathione S-transferase, and epoxide hydrolase enzymes: Relevance to xenobiotic metabolism and toxicity
    • L. W. Wormhoudt, J. N. Commandeur, N. P. Vermeulen, 'Genetic polymorphisms of human N-acetyl-transferase, cytochrome P450, glutathione S-transferase, and epoxide hydrolase enzymes: relevance to xenobiotic metabolism and toxicity', Crit. Rev. Toxicol. 1999, 29, 59-124
    • (1999) Crit. Rev. Toxicol , vol.29 , pp. 59-124
    • Wormhoudt, L.W.1    Commandeur, J.N.2    Vermeulen, N.P.3
  • 232
    • 0034534035 scopus 로고    scopus 로고
    • Epoxide hydrolases: Biochemistry and molecular biology
    • A. J. Fretland, C. J. Orniecinski, 'Epoxide hydrolases: biochemistry and molecular biology', Chem.-Biol. Interact. 2000, 129, 41-59.
    • (2000) Chem.-Biol. Interact , vol.129 , pp. 41-59
    • Fretland, A.J.1    Orniecinski, C.J.2
  • 233
    • 0028323534 scopus 로고
    • Developmental expression of human microsomal epoxide hydrolase
    • C. J. Omiecinski, L. Aicher, L. Swenson, 'Developmental expression of human microsomal epoxide hydrolase', J. Pharmacol. Exp. Ther. 1994, 269, 417-423
    • (1994) J. Pharmacol. Exp. Ther , vol.269 , pp. 417-423
    • Omiecinski, C.J.1    Aicher, L.2    Swenson, L.3
  • 234
    • 0031452319 scopus 로고    scopus 로고
    • Tissue-specific expression and alternative splicing of human microsomal epoxide hydrolase
    • A. Gaedigk, J. S. Leeder, D. M. Grant, 'Tissue-specific expression and alternative splicing of human microsomal epoxide hydrolase', DNA Cell Biol. 1997, 16, 1257-1266
    • (1997) DNA Cell Biol , vol.16 , pp. 1257-1266
    • Gaedigk, A.1    Leeder, J.S.2    Grant, D.M.3
  • 235
    • 0031981574 scopus 로고    scopus 로고
    • Post-transcriptionaI regulation of human microsomal epoxide hydrolase
    • E. M. Laurenzana, C. Hassett, C. J. Omiecinski, 'Post-transcriptionaI regulation of human microsomal epoxide hydrolase', Pharmacogenetics 1998, 8, 157-167
    • (1998) Pharmacogenetics , vol.8 , pp. 157-167
    • Laurenzana, E.M.1    Hassett, C.2    Omiecinski, C.J.3
  • 236
    • 33745227302 scopus 로고    scopus 로고
    • Induction of genes for metabolism and transport by trans-stilbene oxide in livers of Sprague-Dawley and Wistar-Kyoto rats
    • A. L. Slit, N. J. Cherrington, C. D. Fisher, M. Negishi, C. D. Klaassen, 'Induction of genes for metabolism and transport by trans-stilbene oxide in livers of Sprague-Dawley and Wistar-Kyoto rats', Drug Metab. Dispos. 2006, 34, 1190-1197.
    • (2006) Drug Metab. Dispos , vol.34 , pp. 1190-1197
    • Slit, A.L.1    Cherrington, N.J.2    Fisher, C.D.3    Negishi, M.4    Klaassen, C.D.5
  • 238
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases: Mechanism, inhibitor designs, and biological roles
    • C. Morisseau, B. D. Hammock, 'Epoxide hydrolases: mechanism, inhibitor designs, and biological roles', Annu. Rev. Pharmacol. Toxicol. 2005, 43, 311-333
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.43 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 239
    • 14644429730 scopus 로고    scopus 로고
    • Epoxide hydrolases: Their roles and interactions with lipid metabolism
    • J. W. Newman, C. Morisseau, B. D. Hammock, 'Epoxide hydrolases: their roles and interactions with lipid metabolism', Prog. Lipid Res. 2005, 44,1-51.
    • (2005) Prog. Lipid Res , vol.44 , pp. 1-51
    • Newman, J.W.1    Morisseau, C.2    Hammock, B.D.3
  • 240
    • 0342327333 scopus 로고    scopus 로고
    • The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics
    • J. Seidegard, G. Ekström, 'The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics', Environ. Health Perspect. 1997, 105, 791-799.
    • (1997) Environ. Health Perspect , vol.105 , pp. 791-799
    • Seidegard, J.1    Ekström, G.2
  • 241
    • 0028944334 scopus 로고
    • Molecular and biochemical evidence for the involvement of the Asp333-His523 pair in the catalytic mechanism of soluble epoxide hydrolase
    • F. Pinot, D. F Grant, J. K. Beetham, A. G. Parker, B. Borhan, S. Landt, A. D. Jones, B. D. Hammock, 'Molecular and biochemical evidence for the involvement of the Asp333-His523 pair in the catalytic mechanism of soluble epoxide hydrolase', J. Biol. Chem. 1995, 270, 7968-7974
    • (1995) J. Biol. Chem , vol.270 , pp. 7968-7974
    • Pinot, F.1    Grant, D.F.2    Beetham, J.K.3    Parker, A.G.4    Borhan, B.5    Landt, S.6    Jones, A.D.7    Hammock, B.D.8
  • 242
    • 0029664614 scopus 로고    scopus 로고
    • 523 form the catalytic triad of rat soluble epoxide hydrolase
    • 523 form the catalytic triad of rat soluble epoxide hydrolase', J. Biol. Chem. 1996, 271, 4223-4229
    • (1996) J. Biol. Chem , vol.271 , pp. 4223-4229
    • Arandt, M.1    Wagner, H.2    Oesch, E.3
  • 243
    • 0034538911 scopus 로고    scopus 로고
    • New structural and chemical insight into the catalytic mechanism of epoxide hydrolases
    • R. N. Armstrong, C. S. Cassidy, 'New structural and chemical insight into the catalytic mechanism of epoxide hydrolases', Drug Metab. Rev. 2000, 32, 327-338
    • (2000) Drug Metab. Rev , vol.32 , pp. 327-338
    • Armstrong, R.N.1    Cassidy, C.S.2
  • 244
    • 1942438591 scopus 로고    scopus 로고
    • Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis
    • G. A. Gomez, C. Morisseau, B. D. Hammock, D. W. Christianson, 'Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis', Biochemistry 2004, 43, 4716-4723
    • (2004) Biochemistry , vol.43 , pp. 4716-4723
    • Gomez, G.A.1    Morisseau, C.2    Hammock, B.D.3    Christianson, D.W.4
  • 245
    • 33847628757 scopus 로고    scopus 로고
    • Active site of epoxide hydrolases revisited: A noncannonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate
    • A. Thomaeus, J. Carlsson, J. Åqvist, M. Widersten, 'Active site of epoxide hydrolases revisited: a noncannonical residue in potato StEH1 promotes both formation and breakdown of the alkylenzyme intermediate', Biochemistry 2007, 46, 2466-1479.
    • (2007) Biochemistry , vol.46 , pp. 2466-1479
    • Thomaeus, A.1    Carlsson, J.2    Åqvist, J.3    Widersten, M.4
  • 246
    • 0028856676 scopus 로고
    • Mechanism of soluble epoxide hydrolase. Formation of an a-hydroxy ester-enzyme intermediate through Asp-333
    • B. Borhan, A. D. Jones, F. Pinot, D. E Grant, M. J. Kurth, B. D. Hammock, 'Mechanism of soluble epoxide hydrolase. Formation of an a-hydroxy ester-enzyme intermediate through Asp-333', J. Biol. Chem. 1995, 270, 26923-26930
    • (1995) J. Biol. Chem , vol.270 , pp. 26923-26930
    • Borhan, B.1    Jones, A.D.2    Pinot, F.3    Grant, D.E.4    Kurth, M.J.5    Hammock, B.D.6
  • 247
    • 0033011175 scopus 로고    scopus 로고
    • Kinetic and chemical mechanism of epoxide hydrolase
    • R. N. Armstrong, 'Kinetic and chemical mechanism of epoxide hydrolase', Drug Metab. Rev. 1999, 31, 71-86
    • (1999) Drug Metab. Rev , vol.31 , pp. 71-86
    • Armstrong, R.N.1
  • 248
    • 0034829750 scopus 로고    scopus 로고
    • A theoretical examination of the acid-catalyzed and noncatalyzed ring-opening reaction of an oxirane by nucleophilic addition of acetate. Implications to epoxide hydrolases
    • E. Y. Lau, Z. E. Newby, T. C. Bruice, 'A theoretical examination of the acid-catalyzed and noncatalyzed ring-opening reaction of an oxirane by nucleophilic addition of acetate. Implications to epoxide hydrolases', J. Am. Chem. Soc. 2001, 123, 3350-3357
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 3350-3357
    • Lau, E.Y.1    Newby, Z.E.2    Bruice, T.C.3
  • 249
    • 1942517067 scopus 로고    scopus 로고
    • Reaction mechanism of soluble epoxide hydrolase: Insights from molecular dynamics simulations
    • B. Schiøtt, T. C. Bruice, 'Reaction mechanism of soluble epoxide hydrolase: insights from molecular dynamics simulations', J. Am. Chem. Soc. 2002, 124, 14558-14570
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 14558-14570
    • Schiøtt, B.1    Bruice, T.C.2
  • 250
    • 33751280486 scopus 로고    scopus 로고
    • Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants
    • K. H. Hopmann, F. Himo, 'Insights into the reaction mechanism of soluble epoxide hydrolase from theoretical active site mutants', J. Phys. Chem., B 2006, 110, 21299-21310.
    • (2006) J. Phys. Chem., B , vol.110 , pp. 21299-21310
    • Hopmann, K.H.1    Himo, F.2
  • 251
    • 0035017926 scopus 로고    scopus 로고
    • R. A. Kemper, R. J. Krause, A. A. Elfarra, 'Metabolism of butadiene monoxide by freshly isolated hepatocytes from mice and rats: different partitioning between oxidative, hydrolytic, and conjugations pathways', Drug Metab. Dispos. 2001, 29, 830-836
    • R. A. Kemper, R. J. Krause, A. A. Elfarra, 'Metabolism of butadiene monoxide by freshly isolated hepatocytes from mice and rats: different partitioning between oxidative, hydrolytic, and conjugations pathways', Drug Metab. Dispos. 2001, 29, 830-836
  • 252
    • 0030992927 scopus 로고    scopus 로고
    • Stereoebemical aspects of 1,3-butadiene metabolism and toxicity in rat and mouse liver microsomes and feshly isolated rat hepatocytes
    • J. L. Nieusma, D. J. Claffey, C. Maniglier-Poulet, T. Imiolczyk, D. Ross, J. A. Ruth, 'Stereoebemical aspects of 1,3-butadiene metabolism and toxicity in rat and mouse liver microsomes and feshly isolated rat hepatocytes', Chem. Res. Toxicol. 1997, 10, 450-456.
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 450-456
    • Nieusma, J.L.1    Claffey, D.J.2    Maniglier-Poulet, C.3    Imiolczyk, T.4    Ross, D.5    Ruth, J.A.6
  • 253
    • 0035177945 scopus 로고    scopus 로고
    • In vitro metabolism of chloroprene: Species differences, epoxide stereochemistry and a de-chlorination pathway
    • L. Cottrell, B. T. Golding, I Munter, W. P. Watson, 'In vitro metabolism of chloroprene: species differences, epoxide stereochemistry and a de-chlorination pathway', Chem. Res. Toxicol. 2001, 14, 1552-1562
    • (2001) Chem. Res. Toxicol , vol.14 , pp. 1552-1562
    • Cottrell, L.1    Golding, B.T.2    Munter, I.3    Watson, W.P.4
  • 254
    • 0142232002 scopus 로고    scopus 로고
    • Detoxication pathways involving glutathione and epoxide hydrolase in the in vitro metabolism of chloroprene
    • T. Munter, L. Cottrell, T. Munter, W. P. Watson, 'Detoxication pathways involving glutathione and epoxide hydrolase in the in vitro metabolism of chloroprene', Chem. Res. Toxicol. 2003, 16, 1287-1297.
    • (2003) Chem. Res. Toxicol , vol.16 , pp. 1287-1297
    • Munter, T.1    Cottrell, L.2    Munter, T.3    Watson, W.P.4
  • 255
    • 0027939291 scopus 로고
    • Kinetics and stereochemistry of the microsomal epoxide hydrolase-catalyzed hydrolysis of cis-stilbene oxides
    • G. Bellucci, C. Chiappe, G. Ingrosso, 'Kinetics and stereochemistry of the microsomal epoxide hydrolase-catalyzed hydrolysis of cis-stilbene oxides', Chirality 1994, 6, 577-582.
    • (1994) Chirality , vol.6 , pp. 577-582
    • Bellucci, G.1    Chiappe, C.2    Ingrosso, G.3
  • 256
    • 0023243261 scopus 로고
    • The metabolism of carbamazepine in humans: Steric course of the enzymatic hydrolysis of the 10,11-epoxide
    • G. Bellucci, G. Berti, C. Chiappe, A. Lippi, E Marioni, 'The metabolism of carbamazepine in humans: steric course of the enzymatic hydrolysis of the 10,11-epoxide', J. Med. Chem. 1987 30, 768-773
    • (1987) J. Med. Chem , vol.30 , pp. 768-773
    • Bellucci, G.1    Berti, G.2    Chiappe, C.3    Lippi, A.4    Marioni, E.5
  • 257
  • 258
    • 0036841947 scopus 로고    scopus 로고
    • Pathways of carbamazepine bioactivation in vitro. I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites
    • R. E. Pearce, G. R. Vakkalagadda, J. S. Leeder, 'Pathways of carbamazepine bioactivation in vitro. I. Characterization of human cytochromes P450 responsible for the formation of 2- and 3-hydroxylated metabolites', Drug Metab. Dispos. 2002, 30, 1170-1179.
    • (2002) Drug Metab. Dispos , vol.30 , pp. 1170-1179
    • Pearce, R.E.1    Vakkalagadda, G.R.2    Leeder, J.S.3
  • 259
    • 33748844591 scopus 로고    scopus 로고
    • Stop cancer before it starts
    • J. Marchant, 'Stop cancer before it starts', New Sci. 2001, 170(2285), 4.
    • (2001) New Sci , vol.170 , Issue.2285 , pp. 4
    • Marchant, J.1
  • 260
    • 0029836346 scopus 로고    scopus 로고
    • Kinetics and mechanism of hydrolysis of aflatoxin B1 exo-8,9-epoxide and rearrangement of the dihydrodiol
    • W. W. Johnson, T. M. Harris, F. P. Guengerich, 'Kinetics and mechanism of hydrolysis of aflatoxin B1 exo-8,9-epoxide and rearrangement of the dihydrodiol', J. Am. Chem. Soc. 1996, 118, 8213-8220
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 8213-8220
    • Johnson, W.W.1    Harris, T.M.2    Guengerich, F.P.3
  • 261
    • 0030612534 scopus 로고    scopus 로고
    • Aflatoxin B1 8,9-epoxide hydrolysis in the presence of rat and human epoxide hydrolase
    • W. W. Johnson, H. Yamazaki, T. Shimada, Y. F. Ueng, F. P. Guengerich, 'Aflatoxin B1 8,9-epoxide hydrolysis in the presence of rat and human epoxide hydrolase', Chem. Res. Toxicol. 1997, 10, 672-676
    • (1997) Chem. Res. Toxicol , vol.10 , pp. 672-676
    • Johnson, W.W.1    Yamazaki, H.2    Shimada, T.3    Ueng, Y.F.4    Guengerich, F.P.5
  • 262
    • 0033010256 scopus 로고    scopus 로고
    • Kinetics of hydrolysis and reaction of aflatoxin B1 exo-8,9-epoxide and relevance to toxicity and detoxication
    • F. P. Guengerich, W. W. Johnson, 'Kinetics of hydrolysis and reaction of aflatoxin B1 exo-8,9-epoxide and relevance to toxicity and detoxication', Drug Metab. Rev. 1999, 31, 141-158
    • (1999) Drug Metab. Rev , vol.31 , pp. 141-158
    • Guengerich, F.P.1    Johnson, W.W.2
  • 264
    • 0022355540 scopus 로고
    • Differential stereoselectivity of cytochrome P450b and P450c in the formation of naphthalene and anthracene 1,2-oxides. The role of epoxide hydrolase in determining the enantiomer composition of the 1,2-dihydrodiols formed
    • P. J. van Bladeren, J. M. Sayer, D. E. Ryan, P. E. Thomas, W. Levin, D. M. Jerina, 'Differential stereoselectivity of cytochrome P450b and P450c in the formation of naphthalene and anthracene 1,2-oxides. The role of epoxide hydrolase in determining the enantiomer composition of the 1,2-dihydrodiols formed', J Biol. Chem. 1985, 260, 10226-10235.
    • (1985) J Biol. Chem , vol.260 , pp. 10226-10235
    • van Bladeren, P.J.1    Sayer, J.M.2    Ryan, D.E.3    Thomas, P.E.4    Levin, W.5    Jerina, D.M.6
  • 265
    • 34948897526 scopus 로고    scopus 로고
    • B. Oesch-Bartlomowicz, E Oesch, 'Mechanisms of toxification and detoxification that challenge drug candidates and drugs', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. I B. Taylor, D. I Triggle, Elsevier, Oxford, 2007, p. 193-214.
    • B. Oesch-Bartlomowicz, E Oesch, 'Mechanisms of toxification and detoxification that challenge drug candidates and drugs', in 'ADME-Tox Approaches', Eds. B. Testa, H. van de Waterbeemd, Vol. 5 in 'Comprehensive Medicinal Chemistry', 2nd edn., Eds. I B. Taylor, D. I Triggle, Elsevier, Oxford, 2007, p. 193-214.
  • 267
    • 0029758268 scopus 로고    scopus 로고
    • Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 lA1, 1A2, and epoxide hydrolase
    • M. Shou, F. J. Gonzalez, H. V. Gelboin, 'Stereoselective epoxidation and hydration at the K-region of polycyclic aromatic hydrocarbons by cDNA-expressed cytochromes P450 lA1, 1A2, and epoxide hydrolase', Biochemistry 1996, 35, 15807-15813.
    • (1996) Biochemistry , vol.35 , pp. 15807-15813
    • Shou, M.1    Gonzalez, F.J.2    Gelboin, H.V.3
  • 268
    • 0006229821 scopus 로고
    • Genetic regulation of the subcellular localization and expression of glucuronidase
    • Ed. F. C. Kauffman, Springer, Berlin
    • R. T. Swank, E. K. Novak, L. Zhen, 'Genetic regulation of the subcellular localization and expression of glucuronidase', in 'Conjugation-Deconjugation Reactions in Drug Metabolism and Toxicity', Ed. F. C. Kauffman, Springer, Berlin, 1994, p. 131-160.
    • (1994) Conjugation-Deconjugation Reactions in Drug Metabolism and Toxicity , pp. 131-160
    • Swank, R.T.1    Novak, E.K.2    Zhen, L.3
  • 269
    • 0026073226 scopus 로고
    • Hydrolysis of glycyrrhizin to 18β-glycyrrhetyl monoglucuronide by lysosomal β-D-glueuronidase of animal livers
    • T. Akao, T. Akao, M. Hattori, M. Kanaoka, K. Yamamoto, T. Namba, K. Kobashi, 'Hydrolysis of glycyrrhizin to 18β-glycyrrhetyl monoglucuronide by lysosomal β-D-glueuronidase of animal livers', Biochem. Pharmacol. 1991, 41, 1025-1029
    • (1991) Biochem. Pharmacol , vol.41 , pp. 1025-1029
    • Akao, T.1    Akao, T.2    Hattori, M.3    Kanaoka, M.4    Yamamoto, K.5    Namba, T.6    Kobashi, K.7
  • 270
    • 0031763499 scopus 로고    scopus 로고
    • Distribution of enzymes involved in the metabolism of glycyrrhizin in various organs of rat
    • T. Akao, 'Distribution of enzymes involved in the metabolism of glycyrrhizin in various organs of rat', Biol. Pharm. Bull. 1998, 21, 1036-1044.
    • (1998) Biol. Pharm. Bull , vol.21 , pp. 1036-1044
    • Akao, T.1
  • 271
    • 0031693008 scopus 로고    scopus 로고
    • Enterohepatic cycling and pharmacokinetics of oestradiol in postmeno-pausal women
    • T. B. Vree, C. J. Timmer, 'Enterohepatic cycling and pharmacokinetics of oestradiol in postmeno-pausal women', J. Pharm. Pharmacol. 1998, 50, 857-864.
    • (1998) J. Pharm. Pharmacol , vol.50 , pp. 857-864
    • Vree, T.B.1    Timmer, C.J.2
  • 272
    • 0026335157 scopus 로고
    • Carbohydrate prodrugs: Potential use for in situ activation and drug delivery
    • E. Palomino, E. H. Walker, S. L. Blumenthal, 'Carbohydrate prodrugs: Potential use for in situ activation and drug delivery', Drugs Future 1991, 16, 1029-1037
    • (1991) Drugs Future , vol.16 , pp. 1029-1037
    • Palomino, E.1    Walker, E.H.2    Blumenthal, S.L.3
  • 273
    • 0034956847 scopus 로고    scopus 로고
    • Colonic drug delivery: Prodrug approach
    • V. R. Sinha, R. Kumria,'Colonic drug delivery: prodrug approach', Pharm. Res. 2001, 18, 557-564.
    • (2001) Pharm. Res , vol.18 , pp. 557-564
    • Sinha, V.R.1    Kumria, R.2
  • 274
    • 0027972970 scopus 로고
    • Menthol-β-D-glucuronide: A potential prodrug for treatment of the irritable bowel syndrome
    • H. W. Nolen III, D. R. Friend, 'Menthol-β-D-glucuronide: a potential prodrug for treatment of the irritable bowel syndrome', Pharm. Res. 1994, 11, 1707-1711.
    • (1994) Pharm. Res , vol.11 , pp. 1707-1711
    • Nolen III, H.W.1    Friend, D.R.2
  • 276
    • 27644498400 scopus 로고    scopus 로고
    • P. Riley, P. C. Figary, J. R. Entwisle, A. L. Roe, G. A. 'Mompson, R. Ohashi, N. Ohashi, T. J. Moorehead, 'The metabolic profile of azimilide in man: in vivo and in vitro evaluations', J. Pharm. Sci. 2005, 94, 2084-2095.
    • P. Riley, P. C. Figary, J. R. Entwisle, A. L. Roe, G. A. 'Mompson, R. Ohashi, N. Ohashi, T. J. Moorehead, 'The metabolic profile of azimilide in man: in vivo and in vitro evaluations', J. Pharm. Sci. 2005, 94, 2084-2095.
  • 280
    • 0026045316 scopus 로고
    • Improved delivery through biological membranes. LVI. Pharmacological evaluation of alprenoxime - a new potential amiglaucoma agent
    • N. Bodor, A. Elkoussi, 'Improved delivery through biological membranes. LVI. Pharmacological evaluation of alprenoxime - a new potential amiglaucoma agent', Pharm. Res. 1991 8, 1389-1395
    • (1991) Pharm. Res , vol.8 , pp. 1389-1395
    • Bodor, N.1    Elkoussi, A.2
  • 281
    • 0029069037 scopus 로고
    • Ocular delivery of the β-adrenergic antagonist alprenolol by sequential bioactivation of its methoxime analogue
    • L. Prokai, W. M. Wu, G. Somogyi, N. Bodor, 'Ocular delivery of the β-adrenergic antagonist alprenolol by sequential bioactivation of its methoxime analogue', J. Med. Chem. 1995, 38, 2018-2020.
    • (1995) J. Med. Chem , vol.38 , pp. 2018-2020
    • Prokai, L.1    Wu, W.M.2    Somogyi, G.3    Bodor, N.4
  • 282
    • 0001231790 scopus 로고
    • Further advances in the chemistry of Mannich bases
    • M. Tramontini, L. Angiolini, 'Further advances in the chemistry of Mannich bases', Tetrahedron 1990, 46, 1791-1837
    • (1990) Tetrahedron , vol.46 , pp. 1791-1837
    • Tramontini, M.1    Angiolini, L.2
  • 283
    • 0019723346 scopus 로고
    • Pro-drugs of amides, imides, and amines
    • I. H. Pitman, 'Pro-drugs of amides, imides, and amines', Med. Res. Rev. 1981, 1, 189-214
    • (1981) Med. Res. Rev , vol.1 , pp. 189-214
    • Pitman, I.H.1
  • 284
    • 2842574633 scopus 로고
    • Mechanism of hydrolysis of benzamidomethyl derivatives of phenols and its implications for prodrug design
    • J. J. Getz, R. J. Prankerd, K. B. Sloan, 'Mechanism of hydrolysis of benzamidomethyl derivatives of phenols and its implications for prodrug design', J. Org. Chem. 1992, 57, 1702-1706.
    • (1992) J. Org. Chem , vol.57 , pp. 1702-1706
    • Getz, J.J.1    Prankerd, R.J.2    Sloan, K.B.3
  • 285
    • 0027965086 scopus 로고
    • Investigation of N-[(acyloxy)alkyl] ester as a prodrug model for drugs containing the phenyltetrazole moiety
    • J. Alexander, M. L. Renyer, G. S. Rork, 'Investigation of N-[(acyloxy)alkyl] ester as a prodrug model for drugs containing the phenyltetrazole moiety', J. Pharm. Sci. 1994, 83, 893-897.
    • (1994) J. Pharm. Sci , vol.83 , pp. 893-897
    • Alexander, J.1    Renyer, M.L.2    Rork, G.S.3
  • 286
    • 0141447807 scopus 로고    scopus 로고
    • Kinetics of degradation of 4-imidazolinone prodrug types obtained from reacting prilocaine with formaldehyde and acetaldehyde
    • S. W. Larsen, M. Sidenius, M. Ankersen, C. Larsen, 'Kinetics of degradation of 4-imidazolinone prodrug types obtained from reacting prilocaine with formaldehyde and acetaldehyde', Eur J. Pharm. Sci. 2003, 20, 233-240.
    • (2003) Eur J. Pharm. Sci , vol.20 , pp. 233-240
    • Larsen, S.W.1    Sidenius, M.2    Ankersen, M.3    Larsen, C.4
  • 288
    • 0031773510 scopus 로고    scopus 로고
    • Differential chemoprotection against acetaminophen-induced hepatotoxicity by latentiated L-cysteines
    • J. C. Roberts, H. L. Phaneuf, J. G. Szakacs, R. T. Zera, J. G. Lamb, M. R. Franklin, 'Differential chemoprotection against acetaminophen-induced hepatotoxicity by latentiated L-cysteines', Chem. Res. Toxicol. 1998, 11, 1274-1282
    • (1998) Chem. Res. Toxicol , vol.11 , pp. 1274-1282
    • Roberts, J.C.1    Phaneuf, H.L.2    Szakacs, J.G.3    Zera, R.T.4    Lamb, J.G.5    Franklin, M.R.6
  • 289
    • 0035797354 scopus 로고    scopus 로고
    • Thiazolidine prodrugs as protective agents against γ-radiation-induced toxicity and mutagenesis in V79 cells
    • B. H. Wilmore, P. B. Cassidy, R. L. Warters, J. C. Roberts, 'Thiazolidine prodrugs as protective agents against γ-radiation-induced toxicity and mutagenesis in V79 cells', J. Med. Chem. 2001, 44, 2661-2666.
    • (2001) J. Med. Chem , vol.44 , pp. 2661-2666
    • Wilmore, B.H.1    Cassidy, P.B.2    Warters, R.L.3    Roberts, J.C.4
  • 292
    • 0028051601 scopus 로고
    • Metabolism of chloramphenicol: A story of nearly 50 years
    • G. F Bories, J. P. Cravedi, 'Metabolism of chloramphenicol: a story of nearly 50 years', Drug Metab. Rev. 1994, 26, 767-783.
    • (1994) Drug Metab. Rev , vol.26 , pp. 767-783
    • Bories, G.F.1    Cravedi, J.P.2
  • 293
    • 34948907359 scopus 로고    scopus 로고
    • 'Cisplatin. Chemistry and Biochemistry of a Leading Anticancer Drug', Ed. B. Lippert, Verlag Helvetica Chimica Acta, Zurich, 1999.
    • 'Cisplatin. Chemistry and Biochemistry of a Leading Anticancer Drug', Ed. B. Lippert, Verlag Helvetica Chimica Acta, Zurich, 1999.
  • 294
    • 84990485077 scopus 로고
    • Cisplatin: Chemistry, distribution and biotransformation
    • D. F. Long, A. J. Repta, 'Cisplatin: Chemistry, distribution and biotransformation', Biopharm. Drug Dispos. 1981, 2, 1-16
    • (1981) Biopharm. Drug Dispos , vol.2 , pp. 1-16
    • Long, D.F.1    Repta, A.J.2
  • 295
    • 0029906642 scopus 로고    scopus 로고
    • Decomposition kinetics of cisplatin in human biological fluids
    • N. Nagai, R. Okuda, M. Kinoshita, H. Ogata, 'Decomposition kinetics of cisplatin in human biological fluids', J. Pharm. Pharmacol. 1996, 48, 918-924
    • (1996) J. Pharm. Pharmacol , vol.48 , pp. 918-924
    • Nagai, N.1    Okuda, R.2    Kinoshita, M.3    Ogata, H.4
  • 296
    • 0028814502 scopus 로고
    • Effect of intracellular chloride on the cellular pharmacodynamics of cis-diamminodi-chloroplatinum(II)
    • M. Jennerwein, P. A. Andrews, 'Effect of intracellular chloride on the cellular pharmacodynamics of cis-diamminodi-chloroplatinum(II)', Drug Metab. Dispos. 1995, 23, 178-184.
    • (1995) Drug Metab. Dispos , vol.23 , pp. 178-184
    • Jennerwein, M.1    Andrews, P.A.2
  • 297
    • 0025981764 scopus 로고
    • The degradation of carboplatin in aqueous solutions containing chloride or other selected nucleophiles
    • M. A. Allsopp, G. J. Sewell, C. G. Rowland, C. M. Rifley, R. L. Schowen, 'The degradation of carboplatin in aqueous solutions containing chloride or other selected nucleophiles', Int. J Pharm. 1991, 69, 197-210
    • (1991) Int. J Pharm , vol.69 , pp. 197-210
    • Allsopp, M.A.1    Sewell, G.J.2    Rowland, C.G.3    Rifley, C.M.4    Schowen, R.L.5
  • 298
    • 0030753473 scopus 로고    scopus 로고
    • Clinical pharmacokinctics and dose optimisation of carboplatin
    • S. B. Duffull, R A. Robinson, 'Clinical pharmacokinctics and dose optimisation of carboplatin', Clin. Pharmacokinet. 1997, 33, 161-183.
    • (1997) Clin. Pharmacokinet , vol.33 , pp. 161-183
    • Duffull, S.B.1    Robinson, R.A.2
  • 300
    • 3543021553 scopus 로고    scopus 로고
    • Oxaliplatin degradation in the presence of chloride: Identification and cytotoxicity of the monochloro monooxalato complex
    • E. Jerremalm, M. Hedeland, I. Wallin, U. Bondesson, H. Ehrsson, 'Oxaliplatin degradation in the presence of chloride: identification and cytotoxicity of the monochloro monooxalato complex', Pharm. Res. 2004, 21, 891-894.
    • (2004) Pharm. Res , vol.21 , pp. 891-894
    • Jerremalm, E.1    Hedeland, M.2    Wallin, I.3    Bondesson, U.4    Ehrsson, H.5


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