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Volumn , Issue , 2012, Pages 165-198

Hydrolytic Enzymes

Author keywords

Carboxylesterase; Catalysis; Classification nomenclature; Epoxide hydrolase; Hydrolytic enzyme; Paraoxonase; Structure

Indexed keywords


EID: 84872686993     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527630905.ch6     Document Type: Chapter
Times cited : (8)

References (125)
  • 2
    • 33748744628 scopus 로고    scopus 로고
    • Structure, function and regulation of carboxylesterases
    • Satoh, T. and Hosokawa, M. (2006) Structure, function and regulation of carboxylesterases. Chem. Biol. Interact., 162, 195-211.
    • (2006) Chem. Biol. Interact , vol.162 , pp. 195-211
    • Satoh, T.1    Hosokawa, M.2
  • 3
    • 33749030999 scopus 로고    scopus 로고
    • Human carboxylesterase isozymes:catalytic properties and rational drug design
    • Imai, T. (2006) Human carboxylesterase isozymes:catalytic properties and rational drug design. Drug Metab. Pharmacokinet., 21, 173-185.
    • (2006) Drug Metab. Pharmacokinet , vol.21 , pp. 173-185
    • Imai, T.1
  • 4
    • 33751171573 scopus 로고    scopus 로고
    • Antiplatelet agents aspirin and clopidogrel are hydrolyzed by distinct carboxylesterases, and clopidogrel is transesterificated in the presence of ethyl alcohol
    • Tang, M., Mukundan, M., Yang, J., Charpentier, N., LeCluyse, E.L., Black, C., Yang, D., Shi, D., and Yan, B. (2006) Antiplatelet agents aspirin and clopidogrel are hydrolyzed by distinct carboxylesterases, and clopidogrel is transesterificated in the presence of ethyl alcohol. J. Pharmacol. Exp. Ther., 319, 1467-1476.
    • (2006) J. Pharmacol. Exp. Ther , vol.319 , pp. 1467-1476
    • Tang, M.1    Mukundan, M.2    Yang, J.3    Charpentier, N.4    LeCluyse, E.L.5    Black, C.6    Yang, D.7    Shi, D.8    Yan, B.9
  • 5
    • 0344926367 scopus 로고    scopus 로고
    • Molecular characterization of human eye and heart fatty acid ethyl ester synthase/carboxylesterase by site-directed mutagenesis
    • Bora, P.S., Guruge, B.L., and Bora, N.S. (2003) Molecular characterization of human eye and heart fatty acid ethyl ester synthase/carboxylesterase by site-directed mutagenesis. Biochem. Biophys. Res. Commun., 312, 1094-1098.
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , pp. 1094-1098
    • Bora, P.S.1    Guruge, B.L.2    Bora, N.S.3
  • 6
    • 33744979992 scopus 로고    scopus 로고
    • Human liver cholesteryl ester hydrolase:cloning, molecular characterization, and role in cellular cholesterol homeostasis
    • Zhao, B., Natarajan, R., and Ghosh, S. (2005) Human liver cholesteryl ester hydrolase:cloning, molecular characterization, and role in cellular cholesterol homeostasis. Physiol. Genomics, 23, 304-310.
    • (2005) Physiol. Genomics , vol.23 , pp. 304-310
    • Zhao, B.1    Natarajan, R.2    Ghosh, S.3
  • 7
    • 37249076416 scopus 로고    scopus 로고
    • Apolipoprotein B and triacylglycerol secretion in human triacylglycerol hydrolase transgenic mice
    • Wei, E., Alam, M., Sun, F., Agellon, L.B., Vance, D.E., and Lehner, R. (2007) Apolipoprotein B and triacylglycerol secretion in human triacylglycerol hydrolase transgenic mice. J. Lipid Res., 48, 2597-2606.
    • (2007) J. Lipid Res , vol.48 , pp. 2597-2606
    • Wei, E.1    Alam, M.2    Sun, F.3    Agellon, L.B.4    Vance, D.E.5    Lehner, R.6
  • 8
    • 67349083616 scopus 로고    scopus 로고
    • Pyrethroid insecticides:isoform-dependent hydrolysis, induction of cytochrome P450 3A4 and evidence on the involvement of the pregnane X receptor
    • Yang, D., Wang, X., Yang, D., and Yan, B. (2009) Pyrethroid insecticides:isoform-dependent hydrolysis, induction of cytochrome P450 3A4 and evidence on the involvement of the pregnane X receptor. Toxicol. Appl. Pharmacol., 237, 49-58.
    • (2009) Toxicol. Appl. Pharmacol , vol.237 , pp. 49-58
    • Yang, D.1    Wang, X.2    Yang, D.3    Yan, B.4
  • 9
    • 0028355643 scopus 로고
    • Oxime-induced reactivation of carboxylesterase inhibited by organophosphorus compounds
    • Maxwell, D.M., Lieske, C.N., and Brecht, K.M. (1994) Oxime-induced reactivation of carboxylesterase inhibited by organophosphorus compounds. Chem. Res. Toxicol., 7, 428-433.
    • (1994) Chem. Res. Toxicol , vol.7 , pp. 428-433
    • Maxwell, D.M.1    Lieske, C.N.2    Brecht, K.M.3
  • 10
    • 0030030930 scopus 로고    scopus 로고
    • Metabolic deglucuronidation and demethylation of estrogen conjugates as a source of parent estrogens and catecholestrogen metabolites in Syrian hamster kidney, a target organ of estrogen-induced tumorigenesis
    • Zhu, B.T., Evaristus, E.N., Antoniak, S.K., Sarabia, S.F., Ricci, M.J., and Liehr, J.G. (1996) Metabolic deglucuronidation and demethylation of estrogen conjugates as a source of parent estrogens and catecholestrogen metabolites in Syrian hamster kidney, a target organ of estrogen-induced tumorigenesis. Toxicol. Appl. Pharmacol., 136, 186-193.
    • (1996) Toxicol. Appl. Pharmacol , vol.136 , pp. 186-193
    • Zhu, B.T.1    Evaristus, E.N.2    Antoniak, S.K.3    Sarabia, S.F.4    Ricci, M.J.5    Liehr, J.G.6
  • 11
    • 0015888882 scopus 로고
    • Current problems on the structure and classification of mammalian liver carboxylesterases (EC 3.1.1.1)
    • Junge, W. and Krisch, K. (1973) Current problems on the structure and classification of mammalian liver carboxylesterases (EC 3.1.1.1). Mol. Cell. Biochem., 1, 41-52.
    • (1973) Mol. Cell. Biochem , vol.1 , pp. 41-52
    • Junge, W.1    Krisch, K.2
  • 12
    • 48049114394 scopus 로고    scopus 로고
    • Mammalian carboxylesterase 5:comparative biochemistry and genomics
    • Holmes, R.S., Cox, L.A., and Vandeberg, J.L. (2008) Mammalian carboxylesterase 5:comparative biochemistry and genomics. Comp. Biochem. Physiol. D, 3, 195-204.
    • (2008) Comp. Biochem. Physiol. D , vol.3 , pp. 195-204
    • Holmes, R.S.1    Cox, L.A.2    Vandeberg, J.L.3
  • 15
    • 0032779726 scopus 로고    scopus 로고
    • Human placental carboxylesterases:enzymatic characterization, molecular cloning, and evidence for the existence of multiple forms
    • Yan, B., Matoney, L., and Yang, D. (1999) Human placental carboxylesterases:enzymatic characterization, molecular cloning, and evidence for the existence of multiple forms. Placenta, 20, 599-607.
    • (1999) Placenta , vol.20 , pp. 599-607
    • Yan, B.1    Matoney, L.2    Yang, D.3
  • 16
    • 0027427772 scopus 로고
    • Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases:cDNA cloning and characterization of two highly similar enzyme forms
    • Kroetz, D.L., McBride, O.W., and Gonzalez, F.J. (1993) Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases:cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry, 32, 11606-11617.
    • (1993) Biochemistry , vol.32 , pp. 11606-11617
    • Kroetz, D.L.1    McBride, O.W.2    Gonzalez, F.J.3
  • 17
    • 0042868357 scopus 로고    scopus 로고
    • Characterization of multiple promoters in the human carboxylesterase 2 gene
    • Wu, M.H., Chen, P., Remo, B.F., Cook, E.H., Jr, Das, S., and Dolan, M.E. (2003) Characterization of multiple promoters in the human carboxylesterase 2 gene. Pharmacogenetics, 13, 425-435.
    • (2003) Pharmacogenetics , vol.13 , pp. 425-435
    • Wu, M.H.1    Chen, P.2    Remo, B.F.3    Cook Jr., E.H.4    Das, S.5    Dolan, M.E.6
  • 18
    • 2042544103 scopus 로고    scopus 로고
    • Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3
    • Sanghani, S.P., Quinney, S.K., Fredenburg, T.B., Davis, W.I., Murry, D.J., and Bosron, W.F. (2004) Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3. Drug Metab. Dispos., 32, 505-511.
    • (2004) Drug Metab. Dispos , vol.32 , pp. 505-511
    • Sanghani, S.P.1    Quinney, S.K.2    Fredenburg, T.B.3    Davis, W.I.4    Murry, D.J.5    Bosron, W.F.6
  • 19
    • 0028034430 scopus 로고
    • Rat kidney carboxylesterase:cloning, sequencing, cellular localization and relationship to liver hydrolase B
    • Yan, B., Yang, D., Brady, M., and Parkinson, A. (1994) Rat kidney carboxylesterase:cloning, sequencing, cellular localization and relationship to liver hydrolase B. J. Biol. Chem., 269, 29688-29696.
    • (1994) J. Biol. Chem , vol.269 , pp. 29688-29696
    • Yan, B.1    Yang, D.2    Brady, M.3    Parkinson, A.4
  • 20
    • 0028954602 scopus 로고
    • Rat testicular carboxylesterase:cloning, sequencing, cellular localization and relationship to liver hydrolase A
    • Yan, B., Yang, D., Brady, M., and Parkinson, A. (1995) Rat testicular carboxylesterase:cloning, sequencing, cellular localization and relationship to liver hydrolase A. Arch. Biochem. Biophys., 316, 899-908.
    • (1995) Arch. Biochem. Biophys , vol.316 , pp. 899-908
    • Yan, B.1    Yang, D.2    Brady, M.3    Parkinson, A.4
  • 21
    • 0029146341 scopus 로고    scopus 로고
    • Rat serum carboxylesterase:cloning, expression, regulation and evidence of secretion from liver
    • Yan, B., Yang, D., Bolluck, P., and Parkinson, A. (1996) Rat serum carboxylesterase:cloning, expression, regulation and evidence of secretion from liver. J. Biol. Chem., 270, 19128-19134.
    • (1996) J. Biol. Chem , vol.270 , pp. 19128-19134
    • Yan, B.1    Yang, D.2    Bolluck, P.3    Parkinson, A.4
  • 22
    • 2942603512 scopus 로고    scopus 로고
    • Intramolecular disulfide bonds are required for folding hydrolase B into a catalytically active conformation but not for maintaining it during catalysis
    • Song, X., Gragen, S., Li, Y., Ma, Y., Liu, J., Yang, D., Matoney, L., and Yan, B. (2004) Intramolecular disulfide bonds are required for folding hydrolase B into a catalytically active conformation but not for maintaining it during catalysis. Biochem. Biophys. Res. Commun., 319, 1072-1080.
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 1072-1080
    • Song, X.1    Gragen, S.2    Li, Y.3    Ma, Y.4    Liu, J.5    Yang, D.6    Matoney, L.7    Yan, B.8
  • 24
    • 0242600811 scopus 로고    scopus 로고
    • Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme
    • Bencharit, S., Morton, C.L., Xue, Y., Potter, P.M., and Redinbo, M.R. (2003) Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. Nat. Struct. Biol., 10, 349-356.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 349-356
    • Bencharit, S.1    Morton, C.L.2    Xue, Y.3    Potter, P.M.4    Redinbo, M.R.5
  • 25
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica:a prototypic acetylcholine-binding protein
    • Sussman, J.L., Harel, M., Frolow, F., Oefner, C., Goldman, A., Toker, L., and Silman, I. (1991) Atomic structure of acetylcholinesterase from Torpedo californica:a prototypic acetylcholine-binding protein. Science, 253, 872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 27
    • 33751173450 scopus 로고    scopus 로고
    • Anti-influenza prodrug oseltamivir is activated by carboxylesterase HCE1 and the activation is inhibited by anti-platelet agent clopidogrel
    • Shi, D., Yang, J., Yang, D., LeCluyse, E.L., Black, C., You, L., Akhlaghi, F., and Yan, B. (2006) Anti-influenza prodrug oseltamivir is activated by carboxylesterase HCE1 and the activation is inhibited by anti-platelet agent clopidogrel. J. Pharmacol. Exp. Ther., 319, 1477-1484.
    • (2006) J. Pharmacol. Exp. Ther , vol.319 , pp. 1477-1484
    • Shi, D.1    Yang, J.2    Yang, D.3    LeCluyse, E.L.4    Black, C.5    You, L.6    Akhlaghi, F.7    Yan, B.8
  • 28
    • 0027375307 scopus 로고
    • Enhancement of hepatic microsomal esterase activity following soman pretreatment in guinea pigs
    • Luttrell, W.E. and Castle, M.C. (1993) Enhancement of hepatic microsomal esterase activity following soman pretreatment in guinea pigs. Biochem. Pharmacol., 46, 2083-2092.
    • (1993) Biochem. Pharmacol , vol.46 , pp. 2083-2092
    • Luttrell, W.E.1    Castle, M.C.2
  • 29
    • 38949194598 scopus 로고    scopus 로고
    • Influence of sulfur oxidation state and steric bulk upon trifluoromethyl ketone (TFK) binding kinetics to carboxylesterases and fatty acid amide hydrolase (FAAH)
    • Wheelock, C.E., Nishi, K., Ying, A., Jones, P.D., Colvin, M.E., Olmstead, M.M., and Hammock, B.D. (2008) Influence of sulfur oxidation state and steric bulk upon trifluoromethyl ketone (TFK) binding kinetics to carboxylesterases and fatty acid amide hydrolase (FAAH). Bioorg. Med. Chem., 16, 2114-2130.
    • (2008) Bioorg. Med. Chem , vol.16 , pp. 2114-2130
    • Wheelock, C.E.1    Nishi, K.2    Ying, A.3    Jones, P.D.4    Colvin, M.E.5    Olmstead, M.M.6    Hammock, B.D.7
  • 30
    • 67549128953 scopus 로고    scopus 로고
    • Improved, selective, human intestinal carboxylesterase inhibitors designed to modulate 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin (irinotecan; CPT-11) toxicity
    • Hicks, L.D., Hyatt, J.L., Stoddard, S., Tsurkan, L., Edwards, C.C., Wadkins, R.M., and Potter, P.M. (2009) Improved, selective, human intestinal carboxylesterase inhibitors designed to modulate 7-ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin (irinotecan; CPT-11) toxicity. J. Med. Chem., 52, 3742-3752.
    • (2009) J. Med. Chem , vol.52 , pp. 3742-3752
    • Hicks, L.D.1    Hyatt, J.L.2    Stoddard, S.3    Tsurkan, L.4    Edwards, C.C.5    Wadkins, R.M.6    Potter, P.M.7
  • 31
    • 57749208164 scopus 로고    scopus 로고
    • Comparison of benzil and trifluoromethyl ketone (TFK)-mediated carboxylesterase inhibition using classical and 3D-quantitative structure-activity relationship analysis
    • Harada, T., Nakagawa, Y., Wadkins, R.M., Potter, P.M., and Wheelock, C.E. (2009) Comparison of benzil and trifluoromethyl ketone (TFK)-mediated carboxylesterase inhibition using classical and 3D-quantitative structure-activity relationship analysis. Bioorg. Med. Chem., 17, 149-164.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 149-164
    • Harada, T.1    Nakagawa, Y.2    Wadkins, R.M.3    Potter, P.M.4    Wheelock, C.E.5
  • 32
    • 0028174977 scopus 로고
    • The cholinesterases:from genes to proteins
    • Taylor, P. and Radic, Z. (1994) The cholinesterases:from genes to proteins. Annu. Rev. Pharmacol. Toxicol., 34, 281-320.
    • (1994) Annu. Rev. Pharmacol. Toxicol , vol.34 , pp. 281-320
    • Taylor, P.1    Radic, Z.2
  • 33
    • 0001776175 scopus 로고
    • Pathways of drug metabolism
    • in, 2nd edn (eds W.B. Pratt and P. Taylor), Churchill Livingstone, London
    • Alvares, A.P. and Pratt, W.B. (1990) Pathways of drug metabolism, in Principle of Drug Action, 2nd edn (eds W.B. Pratt and P. Taylor), Churchill Livingstone, London, pp. 383-384.
    • (1990) Principle of Drug Action , pp. 383-384
    • Alvares, A.P.1    Pratt, W.B.2
  • 34
    • 45749116975 scopus 로고    scopus 로고
    • Rufinamide:clinical pharmacokinetics and concentration-response relationships in patients with epilepsy
    • Perucca, E., Cloyd, J., Critchley, D., and Fuseau, E. (2008) Rufinamide:clinical pharmacokinetics and concentration-response relationships in patients with epilepsy. Epilepsia, 49, 1123-1141.
    • (2008) Epilepsia , vol.49 , pp. 1123-1141
    • Perucca, E.1    Cloyd, J.2    Critchley, D.3    Fuseau, E.4
  • 35
    • 0030965160 scopus 로고    scopus 로고
    • Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin
    • Pindel, E.V., Kedishvili, N.Y., Abraham, T.L., Brzezinski, M.R., Zhang, J., Dean, R.A., and Bosron, W.F. (1997) Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J. Biol. Chem., 272, 14769-14775.
    • (1997) J. Biol. Chem , vol.272 , pp. 14769-14775
    • Pindel, E.V.1    Kedishvili, N.Y.2    Abraham, T.L.3    Brzezinski, M.R.4    Zhang, J.5    Dean, R.A.6    Bosron, W.F.7
  • 36
    • 34249028187 scopus 로고    scopus 로고
    • Similarity in pharmacokinetics of oseltamivir and oseltamivir carboxylate in Japanese and Caucasian subjects
    • Schentag, J.J., Hill, G., Chu, T., and Rayner, C.R. (2007) Similarity in pharmacokinetics of oseltamivir and oseltamivir carboxylate in Japanese and Caucasian subjects. J. Clin. Pharmacol., 47, 689-696.
    • (2007) J. Clin. Pharmacol , vol.47 , pp. 689-696
    • Schentag, J.J.1    Hill, G.2    Chu, T.3    Rayner, C.R.4
  • 38
    • 0028092140 scopus 로고
    • Purification and characterization of two rat liver microsomal carboxylesterases (hydrolase A and B)
    • Morgan, E.W., Yan, B., Petersen, D., Greenway, D., and Parkinson, A. (1994) Purification and characterization of two rat liver microsomal carboxylesterases (hydrolase A and B). Arch. Biochem. Biophys., 315, 494-513.
    • (1994) Arch. Biochem. Biophys , vol.315 , pp. 494-513
    • Morgan, E.W.1    Yan, B.2    Petersen, D.3    Greenway, D.4    Parkinson, A.5
  • 39
  • 41
  • 45
    • 28444456318 scopus 로고    scopus 로고
    • A single nucleotide polymorphism in the carboxylesterase gene is associated with the responsiveness to imidapril medication and the promoter activity
    • Geshi, E., Kimura, T., Yoshimura, M., Suzuki, H., Koba, S., Sakai, T., Saito, T., Koga, A., Muramatsu, M., and Katagiri, T. (2005) A single nucleotide polymorphism in the carboxylesterase gene is associated with the responsiveness to imidapril medication and the promoter activity. Hypertens. Res., 28, 719-725.
    • (2005) Hypertens. Res , vol.28 , pp. 719-725
    • Geshi, E.1    Kimura, T.2    Yoshimura, M.3    Suzuki, H.4    Koba, S.5    Sakai, T.6    Saito, T.7    Koga, A.8    Muramatsu, M.9    Katagiri, T.10
  • 47
    • 0037819284 scopus 로고    scopus 로고
    • Pharmacogenomics of human UDP-glucuronosyltransferase enzymes
    • Guillemette, C. (2003) Pharmacogenomics of human UDP-glucuronosyltransferase enzymes. Pharmacogenomics J., 3, 136-158.
    • (2003) Pharmacogenomics J , vol.3 , pp. 136-158
    • Guillemette, C.1
  • 48
    • 74249102458 scopus 로고    scopus 로고
    • Regulation of drug metabolism and transporters
    • Muntané, J. (2009) Regulation of drug metabolism and transporters. Curr. Drug Metab., 10, 932-945.
    • (2009) Curr. Drug Metab , vol.10 , pp. 932-945
    • Muntané, J.1
  • 49
    • 41349107158 scopus 로고    scopus 로고
    • Multidrug resistance protein 4 (MRP4/ABCC4):a versatile efflux transporter for drugs and signalling molecules
    • Russel, F.G., Koenderink, J.B., and Masereeuw, R. (2008) Multidrug resistance protein 4 (MRP4/ABCC4):a versatile efflux transporter for drugs and signalling molecules. Trends Pharmacol. Sci., 29, 200-207.
    • (2008) Trends Pharmacol. Sci , vol.29 , pp. 200-207
    • Russel, F.G.1    Koenderink, J.B.2    Masereeuw, R.3
  • 51
    • 56049098362 scopus 로고    scopus 로고
    • Dexamethasone suppresses the expression of multiple rat carboxylesterases through transcriptional repression:evidence for an involvement of the glucocorticoid receptor
    • Shi, D., Yang, J., Yang, D., You, L., and Yan, B. (2008) Dexamethasone suppresses the expression of multiple rat carboxylesterases through transcriptional repression:evidence for an involvement of the glucocorticoid receptor. Toxicology, 254, 97-105.
    • (2008) Toxicology , vol.254 , pp. 97-105
    • Shi, D.1    Yang, J.2    Yang, D.3    You, L.4    Yan, B.5
  • 54
    • 0038508970 scopus 로고    scopus 로고
    • The metabolism of clopidogrel is catalyzed by human cytochrome P450 3A and is inhibited by atorvastatin
    • Clarke, T.A. and Waskell, L.A. (2003) The metabolism of clopidogrel is catalyzed by human cytochrome P450 3A and is inhibited by atorvastatin. Drug Metab. Dispos., 31, 53-59.
    • (2003) Drug Metab. Dispos , vol.31 , pp. 53-59
    • Clarke, T.A.1    Waskell, L.A.2
  • 56
    • 0036263708 scopus 로고    scopus 로고
    • Determination of drug interactions occurring with the metabolic pathways of irinotecan
    • Charasson, V., Haaz, M.C., and Robert, J. (2002) Determination of drug interactions occurring with the metabolic pathways of irinotecan. Drug Metab. Dispos., 30, 731-733.
    • (2002) Drug Metab. Dispos , vol.30 , pp. 731-733
    • Charasson, V.1    Haaz, M.C.2    Robert, J.3
  • 57
    • 73349138231 scopus 로고    scopus 로고
    • UGT1A1 genotyping:a predictor of irinotecan-associated side effects and drug efficacy?
    • Schulz, C., Boeck, S., Heinemann, V., and Stemmler, H.J. (2009) UGT1A1 genotyping:a predictor of irinotecan-associated side effects and drug efficacy? Anticancer Drugs, 20, 867-879.
    • (2009) Anticancer Drugs , vol.20 , pp. 867-879
    • Schulz, C.1    Boeck, S.2    Heinemann, V.3    Stemmler, H.J.4
  • 59
    • 59649111761 scopus 로고    scopus 로고
    • Limited brain distribution of [3R,4R,5S]-4-acetamido-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1-carbox ylate phosphate (Ro 64-0802), a pharmacologically active form of oseltamivir, by active efflux across the blood-brain barrier mediated by organic anion transporter 3 (Oat3/Slc22a8) and multidrug resistance-associated protein 4 (Mrp4/Abcc4)
    • Ose, A., Ito, M., Kusuhara, H., Yamatsugu, K., Kanai, M., Shibasaki, M., Hosokawa, M., Schuetz, J.D., and Sugiyama, Y. (2009) Limited brain distribution of [3R,4R,5S]-4-acetamido-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1-carbox ylate phosphate (Ro 64-0802), a pharmacologically active form of oseltamivir, by active efflux across the blood-brain barrier mediated by organic anion transporter 3 (Oat3/Slc22a8) and multidrug resistance-associated protein 4 (Mrp4/Abcc4). Drug Metab. Dispos., 37, 315-321.
    • (2009) Drug Metab. Dispos , vol.37 , pp. 315-321
    • Ose, A.1    Ito, M.2    Kusuhara, H.3    Yamatsugu, K.4    Kanai, M.5    Shibasaki, M.6    Hosokawa, M.7    Schuetz, J.D.8    Sugiyama, Y.9
  • 63
    • 17644438510 scopus 로고    scopus 로고
    • Different role of carboxylesterases in toxicity and tolerance to paraoxon and DFP
    • Dettbarn, W.D., Yang, Z.P., and Milatovic, D. (1999) Different role of carboxylesterases in toxicity and tolerance to paraoxon and DFP. Chem. Biol. Interact., 119-120, 445-454.
    • (1999) Chem. Biol. Interact , vol.119-120 , pp. 445-454
    • Dettbarn, W.D.1    Yang, Z.P.2    Milatovic, D.3
  • 64
    • 0033969811 scopus 로고    scopus 로고
    • Dexamethasone differentially regulates the expression of carboxylesterase genes in humans and rats
    • Zhu, W., Song, L., Matoney, L., LeCluyse, E., and Yan, B. (2000) Dexamethasone differentially regulates the expression of carboxylesterase genes in humans and rats. Drug Metab. Dispos., 28, 186-191.
    • (2000) Drug Metab. Dispos , vol.28 , pp. 186-191
    • Zhu, W.1    Song, L.2    Matoney, L.3    LeCluyse, E.4    Yan, B.5
  • 65
    • 34547671307 scopus 로고    scopus 로고
    • Specificity of procaine and ester hydrolysis by human, minipig, and rat skin and liver
    • Jewell, C., Ackermann, C., Payne, N.A., Fate, G., Voorman, R., and Williams, F.M. (2007) Specificity of procaine and ester hydrolysis by human, minipig, and rat skin and liver. Drug Metab. Dispos., 35, 2015-2022.
    • (2007) Drug Metab. Dispos , vol.35 , pp. 2015-2022
    • Jewell, C.1    Ackermann, C.2    Payne, N.A.3    Fate, G.4    Voorman, R.5    Williams, F.M.6
  • 66
    • 26444610105 scopus 로고    scopus 로고
    • Carboxylesterase isoform 2 mRNA expression in peripheral blood mononuclear cells is a predictive marker of the irinotecan to SN38 activation step in colorectal cancer patients
    • Cecchin, E., Corona, G., Masier, S., Biason, P., Cattarossi, G., Frustaci, S., Buonadonna, A., Colussi, A., and Toffoli, G. (2005) Carboxylesterase isoform 2 mRNA expression in peripheral blood mononuclear cells is a predictive marker of the irinotecan to SN38 activation step in colorectal cancer patients. Clin. Cancer Res., 11, 6901-6907.
    • (2005) Clin. Cancer Res , vol.11 , pp. 6901-6907
    • Cecchin, E.1    Corona, G.2    Masier, S.3    Biason, P.4    Cattarossi, G.5    Frustaci, S.6    Buonadonna, A.7    Colussi, A.8    Toffoli, G.9
  • 68
    • 34250739888 scopus 로고    scopus 로고
    • Comments on "Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel"
    • Fowler, S., Lennon, S.M., Hoffmann, G., and Rayner, C.R. (2007) Comments on "Anti-influenza prodrug oseltamivir is activated by carboxylesterase human carboxylesterase 1, and the activation is inhibited by antiplatelet agent clopidogrel". J. Pharmacol. Exp. Ther., 322, 422-423.
    • (2007) J. Pharmacol. Exp. Ther , vol.322 , pp. 422-423
    • Fowler, S.1    Lennon, S.M.2    Hoffmann, G.3    Rayner, C.R.4
  • 69
    • 0028153358 scopus 로고
    • Regulation of two rat liver microsomal carboxylesterase isozymes:species differences, tissue distribution and the effects of age, sex and xenobiotic treatment of rats
    • Morgan, E.W., Yan, B., Greenway, D., and Parkinson, A. (1994) Regulation of two rat liver microsomal carboxylesterase isozymes:species differences, tissue distribution and the effects of age, sex and xenobiotic treatment of rats. Arch. Biochem. Biophys., 315, 514-526.
    • (1994) Arch. Biochem. Biophys , vol.315 , pp. 514-526
    • Morgan, E.W.1    Yan, B.2    Greenway, D.3    Parkinson, A.4
  • 70
    • 33748901822 scopus 로고    scopus 로고
    • Species differences in the in vitro metabolism of deltamethrin and esfenvalerate:differential oxidative and hydrolytic metabolism by humans and rats
    • Godin, S.J., Scollon, E.J., Hughes, M.F., Potter, P.M., DeVito, M.J., and Ross, M.K. (2006) Species differences in the in vitro metabolism of deltamethrin and esfenvalerate:differential oxidative and hydrolytic metabolism by humans and rats. DrugMetab. Dispos., 34, 1764-1771.
    • (2006) DrugMetab. Dispos , vol.34 , pp. 1764-1771
    • Godin, S.J.1    Scollon, E.J.2    Hughes, M.F.3    Potter, P.M.4    DeVito, M.J.5    Ross, M.K.6
  • 71
    • 0023708137 scopus 로고
    • Species differences in the hydrolysis of meperidine and its inhibition by organophosphate compounds
    • Luttrell, W.E. and Castle, M.C. (1988) Species differences in the hydrolysis of meperidine and its inhibition by organophosphate compounds. Fundam. Appl. Toxicol., 11, 323-332.
    • (1988) Fundam. Appl. Toxicol , vol.11 , pp. 323-332
    • Luttrell, W.E.1    Castle, M.C.2
  • 72
    • 0025877746 scopus 로고
    • Enantioselective hydrolysis of lorazepam 3-acetate by esterases in human and rat liver microsomes and rat brain S9 fraction
    • Liu, K., Guengerich, F.P., and Yang, S.K. (1991) Enantioselective hydrolysis of lorazepam 3-acetate by esterases in human and rat liver microsomes and rat brain S9 fraction. Drug Metab. Dispos., 19, 609-613.
    • (1991) Drug Metab. Dispos , vol.19 , pp. 609-613
    • Liu, K.1    Guengerich, F.P.2    Yang, S.K.3
  • 73
    • 57249113725 scopus 로고    scopus 로고
    • Human carboxylesterases HCE1 and HCE2:ontogenic expression, interindividual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin
    • Yang, D., Pearce, R., Wang, X., Gaedigk, R., Wan, Y.J.Y., and Yan, B. (2009) Human carboxylesterases HCE1 and HCE2:ontogenic expression, interindividual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin. Biochem. Pharmacol., 77, 238-247.
    • (2009) Biochem. Pharmacol , vol.77 , pp. 238-247
    • Yang, D.1    Pearce, R.2    Wang, X.3    Gaedigk, R.4    Wan, Y.J.Y.5    Yan, B.6
  • 74
    • 0035159958 scopus 로고    scopus 로고
    • Regulation of rat carboxylesterase expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) involves multiple signaling pathways
    • Yang, D., Li, Y., Yuan, X., Matoney, L., and Yan, B. (2001) Regulation of rat carboxylesterase expression by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) involves multiple signaling pathways. Toxicol. Sci., 64, 20-27.
    • (2001) Toxicol. Sci , vol.64 , pp. 20-27
    • Yang, D.1    Li, Y.2    Yuan, X.3    Matoney, L.4    Yan, B.5
  • 75
    • 34548320846 scopus 로고    scopus 로고
    • Interleukin-6 suppresses the expression of carboxylesterases HCE1 and HCE2 through transcriptional repression
    • Yang, J., Shi, D., Yang, D., Song, X., and Yan, B. (2007) Interleukin-6 suppresses the expression of carboxylesterases HCE1 and HCE2 through transcriptional repression. Mol. Pharmacol., 72, 686-694.
    • (2007) Mol. Pharmacol , vol.72 , pp. 686-694
    • Yang, J.1    Shi, D.2    Yang, D.3    Song, X.4    Yan, B.5
  • 76
    • 70349127799 scopus 로고    scopus 로고
    • Age-and sex-related expression and activity of carboxylesterase 1 and 2 in mouse and human liver
    • Zhu, H.J., Appel, D.I., Jiang, Y., and Markowitz, J.S. (2009) Age-and sex-related expression and activity of carboxylesterase 1 and 2 in mouse and human liver. Drug Metab. Dispos., 37, 1819-1825.
    • (2009) Drug Metab. Dispos , vol.37 , pp. 1819-1825
    • Zhu, H.J.1    Appel, D.I.2    Jiang, Y.3    Markowitz, J.S.4
  • 77
    • 0031794525 scopus 로고    scopus 로고
    • Comparison of the effects of some CYP3A and other enzyme inducers on replicative DNA synthesis and cytochrome P450 isoforms in rat liver
    • Lake, B.G., Renwick, A.B., Cunninghame, M.E., Price, R.J., Surry, D., and Evans, D.C. (1998) Comparison of the effects of some CYP3A and other enzyme inducers on replicative DNA synthesis and cytochrome P450 isoforms in rat liver. Toxicology, 131, 9-20.
    • (1998) Toxicology , vol.131 , pp. 9-20
    • Lake, B.G.1    Renwick, A.B.2    Cunninghame, M.E.3    Price, R.J.4    Surry, D.5    Evans, D.C.6
  • 78
    • 2542616771 scopus 로고    scopus 로고
    • Sequence and structure of epoxide hydrolases:a systematic analysis
    • Barth, S., Fischer, M., Schmid, R.D., and Pleiss, J. (2004) Sequence and structure of epoxide hydrolases:a systematic analysis. Proteins, 55, 846-855.
    • (2004) Proteins , vol.55 , pp. 846-855
    • Barth, S.1    Fischer, M.2    Schmid, R.D.3    Pleiss, J.4
  • 79
    • 73449142847 scopus 로고    scopus 로고
    • Contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth
    • Oguro, A., Sakamoto, K., Suzuki, S., and Imaoka, S. (2009) Contribution of hydrolase and phosphatase domains in soluble epoxide hydrolase to vascular endothelial growth factor expression and cell growth. Biol. Pharm. Bull., 32, 1962-1967.
    • (2009) Biol. Pharm. Bull , vol.32 , pp. 1962-1967
    • Oguro, A.1    Sakamoto, K.2    Suzuki, S.3    Imaoka, S.4
  • 80
    • 66649116553 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase, a target with multiple opportunities for cardiovascular drug discovery
    • Marino, J.P., Jr (2009) Soluble epoxide hydrolase, a target with multiple opportunities for cardiovascular drug discovery. Curr. Top. Med. Chem., 9, 452-463.
    • (2009) Curr. Top. Med. Chem , vol.9 , pp. 452-463
    • Marino Jr., J.P.1
  • 81
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases:mechanisms, inhibitor designs, and biological roles
    • Morisseau, C. and Hammock, B.D. (2005) Epoxide hydrolases:mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol., 45, 311-333.
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 84
    • 0034761623 scopus 로고    scopus 로고
    • Leukotoxin-diol:a putative toxic mediator involved in acute respiratory distress syndrome
    • Zheng, J., Plopper, C.G., Lakritz, J., Storms, D.H., and Hammock, B.D. (2001) Leukotoxin-diol:a putative toxic mediator involved in acute respiratory distress syndrome. Am. J. Respir. Cell Mol. Biol., 25, 434-438.
    • (2001) Am. J. Respir. Cell Mol. Biol , vol.25 , pp. 434-438
    • Zheng, J.1    Plopper, C.G.2    Lakritz, J.3    Storms, D.H.4    Hammock, B.D.5
  • 85
    • 70349636047 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases
    • Imig, J.D. and Hammock, B.D. (2009) Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases. Nat. Rev. Drug Discov., 8, 794-805.
    • (2009) Nat. Rev. Drug Discov , vol.8 , pp. 794-805
    • Imig, J.D.1    Hammock, B.D.2
  • 86
    • 77958468395 scopus 로고    scopus 로고
    • Targeting epoxides for organ damage in hypertension
    • Imig, J.D. (2010) Targeting epoxides for organ damage in hypertension. J. Cardiovasc. Pharmacol., 56, 329-335.
    • (2010) J. Cardiovasc. Pharmacol , vol.56 , pp. 329-335
    • Imig, J.D.1
  • 87
    • 64249112966 scopus 로고    scopus 로고
    • Mammalian epoxide hydrolases in xenobiotic metabolism and signalling
    • Decker, M., Arand, M., and Cronin, A. (2009) Mammalian epoxide hydrolases in xenobiotic metabolism and signalling. Arch. Toxicol., 83, 297-318.
    • (2009) Arch. Toxicol , vol.83 , pp. 297-318
    • Decker, M.1    Arand, M.2    Cronin, A.3
  • 88
    • 69549084345 scopus 로고    scopus 로고
    • Alpha/ beta hydrolase fold:an update
    • Carr, P.D. and Ollis, D.L. (2009) Alpha/ beta hydrolase fold:an update. Protein Pept. Lett., 16, 1137-1148.
    • (2009) Protein Pept. Lett , vol.16 , pp. 1137-1148
    • Carr, P.D.1    Ollis, D.L.2
  • 90
    • 51849151991 scopus 로고    scopus 로고
    • Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase:implications for M1 aminopeptidases and inhibitor design
    • Tholander, F., Muroya, A., Roques, B.P., Fournié-Zaluski, M.C., Thunnissen, M.M., and Haeggström, J.Z. (2008) Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase:implications for M1 aminopeptidases and inhibitor design. Chem. Biol., 15, 920-929.
    • (2008) Chem. Biol , vol.15 , pp. 920-929
    • Tholander, F.1    Muroya, A.2    Roques, B.P.3    Fournié-Zaluski, M.C.4    Thunnissen, M.M.5    Haeggström, J.Z.6
  • 91
    • 77955799773 scopus 로고    scopus 로고
    • Identification and pharmacological characterization of cholesterol-5,6-epoxide hydrolase as a target for tamoxifen and AEBS ligands
    • de Medina, P., Paillasse, M.R., Segala, G., Poirot, M., and Silvente-Poirot, S. (2010) Identification and pharmacological characterization of cholesterol-5,6-epoxide hydrolase as a target for tamoxifen and AEBS ligands. Proc. Natl. Acad. Sci. USA, 107, 13520-13525.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13520-13525
    • De Medina, P.1    Paillasse, M.R.2    Segala, G.3    Poirot, M.4    Silvente-Poirot, S.5
  • 92
    • 61449118867 scopus 로고    scopus 로고
    • The paraoxonases:role in human diseases and methodological difficulties in measurement
    • Camps, J., Marsillach, J., and Joven, J. (2009) The paraoxonases:role in human diseases and methodological difficulties in measurement. Crit. Rev. Clin. Lab. Sci., 46, 83-106.
    • (2009) Crit. Rev. Clin. Lab. Sci , vol.46 , pp. 83-106
    • Camps, J.1    Marsillach, J.2    Joven, J.3
  • 93
    • 33646373929 scopus 로고    scopus 로고
    • The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
    • Khersonsky, O. and Tawfik, D.S. (2006) The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases. J. Biol. Chem., 281, 7649-7656.
    • (2006) J. Biol. Chem , vol.281 , pp. 7649-7656
    • Khersonsky, O.1    Tawfik, D.S.2
  • 94
    • 77955516506 scopus 로고    scopus 로고
    • Lactonases with organophosphatase activity:structural and evolutionary perspectives
    • Draganov, D.I. (2010) Lactonases with organophosphatase activity:structural and evolutionary perspectives. Chem. Biol. Interact., 187, 370-372.
    • (2010) Chem. Biol. Interact , vol.187 , pp. 370-372
    • Draganov, D.I.1
  • 95
    • 71449093018 scopus 로고    scopus 로고
    • Paraoxonases:structure, gene polymorphism and role in coronary artery disease
    • Gupta, N., Gill, K., and Singh, S. (2009) Paraoxonases:structure, gene polymorphism and role in coronary artery disease. Indian J. Med. Res., 130, 361-368.
    • (2009) Indian J. Med. Res , vol.130 , pp. 361-368
    • Gupta, N.1    Gill, K.2    Singh, S.3
  • 97
    • 0037443799 scopus 로고    scopus 로고
    • Paraoxonase (PON1) deficiency is associated with increased macrophage oxidative stress:studies in PON1-knockout mice
    • Rozenberg, O., Rosenblat, M., Coleman, R., Shih, D.M., and Aviram, M. (2003) Paraoxonase (PON1) deficiency is associated with increased macrophage oxidative stress:studies in PON1-knockout mice. Free Radic. Biol. Med., 34, 774-784.
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 774-784
    • Rozenberg, O.1    Rosenblat, M.2    Coleman, R.3    Shih, D.M.4    Aviram, M.5
  • 99
    • 0031920093 scopus 로고    scopus 로고
    • Paraoxonase has a major role in the hydrolysis of prulifloxacin (NM441), a prodrug of a new antibacterial agent
    • Tougou, K., Nakamura, A., Watanabe, S., Okuyama, Y., and Morino, A. (1998) Paraoxonase has a major role in the hydrolysis of prulifloxacin (NM441), a prodrug of a new antibacterial agent. Drug Metab. Dispos., 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
  • 102
    • 62549166186 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) modulates the toxicity of mixed organophosphorus compounds
    • Jansen, K.L., Cole, T.B., Park, S.S., Furlong, C.E., and Costa, L.G. (2009) Paraoxonase 1 (PON1) modulates the toxicity of mixed organophosphorus compounds. Toxicol. Appl. Pharmacol., 236, 142-153.
    • (2009) Toxicol. Appl. Pharmacol , vol.236 , pp. 142-153
    • Jansen, K.L.1    Cole, T.B.2    Park, S.S.3    Furlong, C.E.4    Costa, L.G.5
  • 103
    • 0029937118 scopus 로고    scopus 로고
    • The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family
    • Primo-Parmo, S.L., Sorenson, R.C., Teiber, J., and La Du, B.N. (1996) The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics, 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
  • 105
    • 0037375932 scopus 로고    scopus 로고
    • Expression of major HDL-associated antioxidant PON-1 is gender dependent and regulated during inflammation
    • bin Ali, A., Zhang, Q., Lim, Y.K., Fang, D., Retnam, L., and Lim, S.K. (2003) Expression of major HDL-associated antioxidant PON-1 is gender dependent and regulated during inflammation. Free Radic. Biol. Med., 34, 824-829.
    • (2003) Free Radic. Biol. Med , vol.34 , pp. 824-829
    • Bin Ali, A.1    Zhang, Q.2    Lim, Y.K.3    Fang, D.4    Retnam, L.5    Lim, S.K.6
  • 107
    • 2942600176 scopus 로고    scopus 로고
    • Dietary polyphenols increase paraoxonase 1 gene expression by an aryl hydrocarbon receptor-dependent mechanism
    • Gouédard, C., Barouki, R., and Morel, Y. (2004) Dietary polyphenols increase paraoxonase 1 gene expression by an aryl hydrocarbon receptor-dependent mechanism. Mol. Cell. Biol., 24, 5209-5222.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 5209-5222
    • Gouédard, C.1    Barouki, R.2    Morel, Y.3
  • 108
    • 36048994061 scopus 로고    scopus 로고
    • Macrophage paraoxonase 2 (PON2) expression is up-regulated by pomegranate juice phenolic antioxidants via PPAR gamma and AP-1 pathway activation
    • Shiner, M., Fuhrman, B., and Aviram, M. (2007) Macrophage paraoxonase 2 (PON2) expression is up-regulated by pomegranate juice phenolic antioxidants via PPAR gamma and AP-1 pathway activation. Atherosclerosis, 195, 313-321.
    • (2007) Atherosclerosis , vol.195 , pp. 313-321
    • Shiner, M.1    Fuhrman, B.2    Aviram, M.3
  • 110
    • 0344951233 scopus 로고    scopus 로고
    • Opposite regulation of the human paraoxonase-1 gene PON-1 by fenofibrate and statins
    • Gouédard, C., Koum-Besson, N., Barouki, R., and Morel, Y. (2003) Opposite regulation of the human paraoxonase-1 gene PON-1 by fenofibrate and statins. Mol. Pharmacol., 63, 945-956.
    • (2003) Mol. Pharmacol , vol.63 , pp. 945-956
    • Gouédard, C.1    Koum-Besson, N.2    Barouki, R.3    Morel, Y.4
  • 111
    • 77954314023 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) deficiency in mice is associated with reduced expression of macrophage SR-BI and consequently the loss of HDL cytoprotection against apoptosis
    • Fuhrman, B., Gantman, A., and Aviram, M. (2010) Paraoxonase 1 (PON1) deficiency in mice is associated with reduced expression of macrophage SR-BI and consequently the loss of HDL cytoprotection against apoptosis. Atherosclerosis, 211, 61-68.
    • (2010) Atherosclerosis , vol.211 , pp. 61-68
    • Fuhrman, B.1    Gantman, A.2    Aviram, M.3
  • 112
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • Khersonsky, O. and Tawfik, D.S. (2005) Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry, 44, 6371-6382.
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 113
    • 79951688566 scopus 로고    scopus 로고
    • The role of paraoxonase 1 in the detoxification of homocysteine thiolactone
    • Jakubowski, H. (2010) The role of paraoxonase 1 in the detoxification of homocysteine thiolactone. Adv. Exp. Med. Biol., 660, 113-127.
    • (2010) Adv. Exp. Med. Biol , vol.660 , pp. 113-127
    • Jakubowski, H.1
  • 114
    • 0042261695 scopus 로고    scopus 로고
    • Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3
    • Teiber, J.F., Draganov, D.I., and La Du, B.N. (2003) Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3. Biochem. Pharmacol., 66, 887-896.
    • (2003) Biochem. Pharmacol , vol.66 , pp. 887-896
    • Teiber, J.F.1    Draganov, D.I.2    La Du, B.N.3
  • 115
    • 33746773687 scopus 로고    scopus 로고
    • Effects of some antibiotics on paraoxonase from human serum in vitro and from mouse serum and liver
    • Sinan, S., Kockar, F., Gencer, N., Yildirim, H., and Arslan, O. (2006) Effects of some antibiotics on paraoxonase from human serum in vitro and from mouse serum and liver in vivo. Biol. Pharm. Bull., 29, 1559-1563.
    • (2006) in vivo. Biol. Pharm. Bull , vol.29 , pp. 1559-1563
    • Sinan, S.1    Kockar, F.2    Gencer, N.3    Yildirim, H.4    Arslan, O.5
  • 116
    • 77956191110 scopus 로고    scopus 로고
    • Some cardiovascular therapeutics inhibit paraoxonase 1 (PON1) from human serum
    • Işgör, M.M. and Beydemir, S. (2010) Some cardiovascular therapeutics inhibit paraoxonase 1 (PON1) from human serum. Eur. J. Pharmacol., 645, 135-142.
    • (2010) Eur. J. Pharmacol , vol.645 , pp. 135-142
    • Işgör, M.M.1    Beydemir, S.2
  • 117
    • 33745130045 scopus 로고    scopus 로고
    • Differential effect of lysophospholipids on activities of human plasma paraoxonase1, either soluble or lipid-bound
    • Park, C.H., Nguyen, S.D., Kim, M.R., Jeong, T.S., and Sok, D.E. (2006) Differential effect of lysophospholipids on activities of human plasma paraoxonase1, either soluble or lipid-bound. Lipids, 41, 371-380.
    • (2006) Lipids , vol.41 , pp. 371-380
    • Park, C.H.1    Nguyen, S.D.2    Kim, M.R.3    Jeong, T.S.4    Sok, D.E.5
  • 118
    • 60249083427 scopus 로고    scopus 로고
    • Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1)
    • Nguyen, S.D., Hung, N.D., Cheon-Ho, P., Ree, K.M., and Dai-Eun, S. (2009) Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1). Biochim. Biophys. Acta, 1790, 155-160.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 155-160
    • Nguyen, S.D.1    Hung, N.D.2    Cheon-Ho, P.3    Ree, K.M.4    Dai-Eun, S.5
  • 119
    • 58949104723 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors:inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates
    • Isik, S., Kockar, F., Aydin, M., Arslan, O., Guler, O.O., Innocenti, A., Scozzafava, A., and Supuran, C.T. (2009) Carbonic anhydrase inhibitors:inhibition of the beta-class enzyme from the yeast Saccharomyces cerevisiae with sulfonamides and sulfamates. Bioorg. Med. Chem., 17, 1158-1163.
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 1158-1163
    • Isik, S.1    Kockar, F.2    Aydin, M.3    Arslan, O.4    Guler, O.O.5    Innocenti, A.6    Scozzafava, A.7    Supuran, C.T.8
  • 120
    • 77649234636 scopus 로고    scopus 로고
    • Effects of cholinesterase inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzheimer's disease:a review of recent clinical studies
    • Darreh-Shori, T. and Soininen, H. (2010) Effects of cholinesterase inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzheimer's disease:a review of recent clinical studies. Curr. Alzheimer Res., 7, 67-73.
    • (2010) Curr. Alzheimer Res , vol.7 , pp. 67-73
    • Darreh-Shori, T.1    Soininen, H.2
  • 122
    • 77349107604 scopus 로고    scopus 로고
    • Study of a cyclopamine glucuronide prodrug for the selective chemotherapy of glioblastoma
    • Hamon, F., Renoux, B., Chadéneau, C., Muller, J.M., and Papot, S. (2010) Study of a cyclopamine glucuronide prodrug for the selective chemotherapy of glioblastoma. Eur.J. Med. Chem., 45, 1678-1682.
    • (2010) Eur.J. Med. Chem , vol.45 , pp. 1678-1682
    • Hamon, F.1    Renoux, B.2    Chadéneau, C.3    Muller, J.M.4    Papot, S.5
  • 124
    • 76749118433 scopus 로고    scopus 로고
    • Tanezumab, a recombinant humanized mAb against nerve growth factor for the treatment of acute and chronic pain
    • Cattaneo, A. (2010) Tanezumab, a recombinant humanized mAb against nerve growth factor for the treatment of acute and chronic pain. Curr. Opin. Mol. Ther., 12, 94-106.
    • (2010) Curr. Opin. Mol. Ther , vol.12 , pp. 94-106
    • Cattaneo, A.1
  • 125
    • 44049083306 scopus 로고    scopus 로고
    • Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase
    • Lai, L., Xu, Z., Zhou, J., Lee, K.D., and Amidon, G.L. (2008) Molecular basis of prodrug activation by human valacyclovirase, an alpha-amino acid ester hydrolase. J. Biol. Chem., 283, 9318-9327.
    • (2008) J. Biol. Chem , vol.283 , pp. 9318-9327
    • Lai, L.1    Xu, Z.2    Zhou, J.3    Lee, K.D.4    Amidon, G.L.5


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