Carboxylesterases: structure, function and polymorphism in mammals

This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we propose a novel nomenclature and classification of mammalian carboxylesterases on the basis of...

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Published inJournal of Pesticide Science Vol. 35; no. 3; pp. 218 - 228
Main Authors Satoh, Tetsuo, Hosokawa, Masakiyo
Format Journal Article
LanguageEnglish
Published Pesticide Science Society of Japan 01.01.2010
Subjects
carboxylesterase
classification
genetic polymorphism
molecular structure
novel biomarker
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Abstract This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we propose a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. Mechanisms of the regulation of the gene expression of carboxylesterases by xenobiotics, and the involvement of carboxylesterase in drug metabolism are also described. The novel biomarker for organophosphate pesticide exposure developed here is much more useful and reliable than cholinesterase inhibition.
AbstractList This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we propose a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. Mechanisms of the regulation of the gene expression of carboxylesterases by xenobiotics, and the involvement of carboxylesterase in drug metabolism are also described. The novel biomarker for organophosphate pesticide exposure developed here is much more useful and reliable than cholinesterase inhibition.
This review covers current developments in molecular-based studies of the structure and function of carboxylesterases. To allay the confusion of the classic classification of carboxylesterase isozymes, we propose a novel nomenclature and classification of mammalian carboxylesterases on the basis of molecular properties. Mechanisms of the regulation of the gene expression of carboxylesterases by xenobiotics, and the involvement of carboxylesterase in drug metabolism are also described. The novel biomarker for organophosphate pesticide exposure developed here is much more useful and reliable than cholinesterase inhibition. 「1. Introduction」 The present review highlights the importance of structure in delineating overall function, substrate specificity, regulation and localization of carboxylesterases (CEs). Structural considerations emerge from the genes encoding the family of enzymes. Sequence homology typically yields insights into the evolutionary relationship between the members and the conserved and divergent areas of sequence.
Author Satoh, Tetsuo
Hosokawa, Masakiyo
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  organization: Laboratory of Drug Metabolism and Biopharmaceutics, Faculty of Pharmaceutical Sciences, Chiba Institute of Science
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Cites_doi 10.1177/0960327107085349
10.1016/0888-7543(91)90020-F
10.1126/science.7661899
10.1016/0968-0004(90)90303-S
10.1042/bj3130821
10.1038/nsb790
10.1016/j.taap.2006.10.014
10.1006/bbrc.1997.6413
10.1021/bi00094a018
10.1021/bi0255625
10.1016/j.cbi.2006.07.001
10.1124/mol.107.036889
10.1182/blood.V78.2.506.bloodjournal782506
10.1006/abbi.1994.1531
10.1042/BJ20040765
10.1248/bpb.17.662
10.1006/bbrc.1994.2341
10.1006/abbi.1995.1157
10.1124/dmd.108.024018
10.1165/ajrcmb.20.6.3402
10.1016/0378-4274(95)03493-5
10.1016/j.toxlet.2009.12.009
10.1074/jbc.270.32.19128
10.1016/0006-2952(84)90176-X
10.1254/jjp.29.9
10.1080/03602530600952164
10.1016/S0021-9258(18)48230-0
10.1016/S1074-5521(03)00071-1
10.1124/dmd.104.000554
10.1074/jbc.272.23.14769
10.2133/dmpk.23.73
10.1006/abbi.2001.2346
10.1016/S0021-9258(18)43935-X
10.1016/j.tox.2008.09.019
10.1172/JCI119888
10.1016/0006-2952(92)90634-U
10.1006/taap.1997.8187
10.1016/0003-9861(80)90386-0
10.1016/S0022-2275(20)33863-3
10.1111/j.1349-7006.1991.tb02705.x
10.1042/bj2690451
10.1016/j.bcp.2005.01.017
10.1002/pro.5560020309
10.1006/geno.1993.1285
10.1124/dmd.108.024331
10.1146/annurev.pharmtox.38.1.257
10.1016/0006-291X(91)92005-5
10.1016/S0167-4781(96)00142-X
10.1016/S0003-9861(03)00286-8
10.2133/dmpk.21.173
10.1097/FPC.0b013e32830b0c5e
10.1016/S0021-9258(18)54952-8
10.1006/bbrc.1996.5912
10.1042/0264-6021:3380761
10.1016/0003-9861(90)90572-G
10.1124/jpet.106.111807
10.1191/0960327105ht532oa
10.3109/00498259309059427
10.1124/dmd.30.5.488
10.1016/j.lfs.2007.07.026
10.1016/j.abb.2006.01.015
10.1016/S0021-9258(18)63890-6
10.2131/jts.6.27
10.1111/j.1432-1033.1983.tb07424.x
10.1016/0024-3205(96)00065-3
10.1016/j.cbpb.2006.05.015
10.1291/hypres.28.719
10.1248/bpb.20.869
10.1016/0888-7543(91)90263-E
10.1016/j.bbrc.2008.02.120
10.1124/dmd.106.009381
10.1124/dmd.32.5.505
10.1006/abbi.1995.1121
10.1248/bpb.19.765
10.1124/mol.56.6.1346
10.1016/0006-2952(94)90461-8
10.1038/nsb919
10.1194/jlr.R200007-JLR200
10.1016/S0009-2797(99)00060-5
10.1016/S0014-5793(99)01111-4
10.1016/S0021-9258(18)69097-0
10.1124/dmd.104.000620
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Ichikawa General Hospital
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References 46) J. Ozols: J. Biol. Chem. 264, 12533–12545 (1989).
52) K. Watanabe, Y. Kayano, T. Matsunaga, I. Yamamoto and H. Yoshimura: Biochem. Mol. Biol. Int. 31, 25–30 (1993).
99) H. M. Dodds and L. P. Rivory: Mol. Pharmacol. 56, 1346–1353 (1999).
38) M. Mori, M. Hosokawa, Y. Ogasawara, E. Tsukada and K. Chiba: FEBS Lett. 458, 17–22 (1999).
12) T. Langmann, C. Aslanidis, M. Schuierer and G. Schmitz: Biochem. Biophys. Res. Commun. 230, 215–219 (1997).
11) M. R. Brzezinski, B. J. Spink, R. A. Dean, C. E. Berkman, J. R. Cashman and W. F. Bosron: Drug Metab. Dispos. 25, 1089–1096 (1997).
25) T. Satoh and M. Hosokawa: Chem. Biol. Interact. 162, 195–211 (2006).
70) T. Imai: Drug Metab Pharmacokinet. 21, 173–185 (2006).
102) T. Satoh, S. Suzuki, N. Kawai, T. Nakamura and M. Hosokawa: Chem. Biol. Interact. 119, 471–478 (1999).
34) T. Imai, M. Taketani, M. Shii, M. Hosokawa and K. Chiba: Drug Metab. Dispos. 34, 1734–1741 (2006).
101) H. Kikuchi, Y. Suzuki, Y. Hashimoto: J. Toxicol. Sci. 6, 27–35 (1981).
13) T. Langmann, A. Becker, C. Aslanidis, F. Notka, H. Ullrich, H. Schwer and G. Schmitz: Biochem. Biophys. Acta 1350, 65–74(1997).
23) T. Satoh and M. Hosokawa: Toxicol. Lett. 82, 439–445 (1995).
3) D. L. Kroetz, O. W. McBride and F. J. Gonzalez: Biochemistry 32, 11606–11617 (1993).
75) M. Hosokawa, T. Satoh, S. Ohkawara, S. Ohmori, T. Igarashi, K. Ueno and H. Kitagawa: Res. Commun. Chem. Pathol. Pharmacol. 46, 245–258 (1984).
92) S. Takahashi, M. Katoh, T. Saitoh, M. Nakajima and T. Yokoi: Drug Metab. Dispos. 37, 956–961 (2009).
93) L. Jaganathan and R. Boopathy: Indian J. Biochem. Biophys. 35, 142–147 (1998).
97) T. Y. Lynch, C. E. Mattes, A. Singh, R. M. Bradley, R. O. Brady and K. L. Dretchen: Toxicol. Appl. Pharmacol. 145, 363–371 (1997).
20) T. Furihata, M. Hosokawa, N. Koyano, T. Nakamura, T. Satoh and K. Chiba: Drug Metab. Dispos. 32, 1170–1177 (2004).
54) M. Robbi and H. Beaufay: J. Biol. Chem. 266, 20498–20503 (1991).
48) K. Aida, R. Moore and M. Negishi: Biochim. Biophys. Acta 1174, 72–74 (1993).
10) K. Kusano, T. Seko, S. Tanaka, Y. Shikata, T. Ando, S. Ida, M. Hosokawa, T. Satoh, T. Yuzuriha and T. Horie: Drug. Metab. Didpos. 24, 1186–1191(1996).
45) T. Furihara, M. Hosokawa, F. Nakata, T. Satoh and K. Chiba. Arch. Biochem. Biophys. 416, 101–109(2003).
86) T. Tabata, M. Katoh, S. Tokudome, M. Nakajima and T. Yokoi: Drug Metab. Dispos. 32, 1103–1110 (2004).
88) J. Zhang, J. C. Burnell, N. Dumaual and W. F. Bosron: J. Pharmacol. Exp. Ther. 290, 314–318 (1999).
105) K. Soltaninejad, K. Shadnis, M. Afkhami-Taghipour, R. Saljooghi, A. Mohanmmadirad and M. Abdollahi: Hum. Exp. Toxicol. 26, 963–966 (2007).
30) T. Prueksaritanont, L.M. Gorham, J. H. Hochman, L. O. Tran and K. P. Vyas: Drug Metab. Dispos. 24, 634–642 (1996).
37) P. M. Potter, C. A. Pawlik, C. L. Morton, C. W. Naeve and M. K. Danks: Cancer Res. 58, 2646–2651 (1998).
80) S. Takai, A. Matsuda, Y. Usami, T. Adachi, T. Sugiyama, Y. Katagiri, M. Tatematsu and K. Hirano: Biol. Pharm. Bull. 20, 869–873 (1997).
85) A. Kojima, N. R. Hackett, A. Ohwada and R. G. Crystal: J. Clin. Invest. 101, 1789–1796 (1998).
33) W. N. Aldridge WN: Chem. Biol. Interact. 87, 5–13 (1993).
83) M. K. Danks, C. L. Morton, C. A. Pawlik and P. M. Potter: Cancer Res. 58, 20–22 (1998).
96) C. Mattes, R. Bradley, E. Slaughter and S. Browne: Pharmacol. Lett. 58, 257–261 (1996).
57) M. Robbi, H. Beaufay and J. N. Octave: Biochem. J. 269, 451–458 (1990).
55) B. K. Tang and W. Kalow: Eur. J. Clin. Pharmacol. 47, 449–451 (1995).
69) T. J. Wallace, S. Ghosh and G. W. McLean: Am. J. Respir. Cell. Mol. Biol. 20, 1201–1208 (1999).
59) S. Medda, K. Takeuchi, D. Devore-Carter, O. von Deimling, E. Heymann and R. T. Swank: J. Biol. Chem. 262, 7248–7253 (1987).
43) J. Yang, D. Shi, D. Yang, X. Song and B. Yan: Mol. Pharmacol. 72, 686–694 (2007).
82) T. Satoh, M. Hosokawa, R. Atsumi, W. Suzuki, H. Hakusui and E. Nagai: Biol. Pharm. Bull. 17, 662–664 (1994).
32) C. M. Mansbach, and P. Nevin: J. Lipid Res. 39, 963–968 (1998).
41) R. Humerickhouse, K. Lohrbach, L. Li, W. F. Bosron and M. E. Dolan: Cancer Res. 60, 1189–1192 (2000).
49) S. P. Sanghani, S. K. Quinney, T. B. Fredenburg, W. I. Davis, D. J. Murry and W .F. Bosron: Drug Metab. Dispos. 32, 505–511 (2004).
22) T. Furihata, M. Hosokawa, A. Fujii, M. Derbel, T. Satoh and K. Chiba: Biochem. Pharmacol. 69, 1287–1297 (2005).
68) S. Bencharit, C. L. Morton, Y. Xue, P. M. Potter and M. R. Redinbo: Nat. Struct. Biol. 10, 349–356 (2003).
8) B. Yan, D. Yang, P. Bullock and A. Parkinson: J. Biol. Chem. 270, 19128–19134 (1995).
50) M. Miyazaki, T. Yamashita, M. Hosokawa, H. Taira and A. Suzuki: Comp. Biochem. Physiol. Biochem. Mol. Biol. 145, 270–277 (2006).
2) M. Hosokawa: Xenobiotic Metab. Dispos. 5, 185–195 (1990).
28) M. Hosokawa, K. Hirata, F. Nakata, T. Suga and T. Satoh: Drug Metab. Dispos. 22, 889–894 (1994).
100) M. Yoshimura, T. Kimura, M. Ishii, K. Ishii, T. Matsuura, E. Geshi, M. Hosokawa and M. Muramatsu: Biochem. Biophys. Res. Commun. 369, 939–942 (2008).
79) R. Lehner, Z. Cui and D. E. Vance: Biochem. J. 338, 761–768 (1999).
1) M. Cygler, J. D. Schrag, J. L. Sussman, M. Harel, I. Silman, M. K. Gentry and B. P. Doctor BP: Protein Sci. 2, 366–382 (1993).
76) K. Hattori, M. Igarashi, M. Itoh, H. Tomisawa and M. Tateishi: Biochem. Pharmacol. 43, 1921–1927 (1992).
63) P. A. Frey, S. A. Whitt and J. B. Tobin: Science 264, 1927–1930 (1994).
6) B. Yan, D. Yang, M. Brady and A. Parkinson: J. Biol. Chem. 269, 29688–29696 (1994).
56) G. Korza and J. Ozols: J. Biol. Chem. 263, 3486–3495 (1998).
91) A. Ose, M. Ito, H. Kusuhara, K. Yamatsugu, M. Kanai, M. Shibasaki, M. Hosokawa, J. D. Schuetz and Y. Sugiyama: Drug Metab. Dispos. 37, 315–321 (2009).
40) H. Schwer, T. Langmann, R. Daig, A. Becker, C. Aslanidis and G. Schmitz: Biochem. Biophys. Res. Commun. 233, 117–120 (1997).
73) T. Fukami, M. Nakajima, T. Maruichi, S. Takahashi, M. Takamiya, Y. Aoki, H. L. McLeod and T. Yokoi: Pharmacogenet. Genomics 18, 911–920 (2008).
9) B. Yan, D. Yang and A. Parkinson: (1995). Arch. Biochem. Biophys. 317, 222–234 (1995).
17) T. Maki, M. Hosokawa, T. Satoh and K. Sato: Jpn. J. Cancer Res. 88, 800–806 (1991).
64) M. Alam, D. E. Vance and R. Lehner: Biochemistry 41, 6679–6687 (2002).
35) M. Ovnic, K. Tepperman, S. Medda, R. W. Elliott, D. A. Stephenson, S. G. Grant and R. E. Ganschow: Genomics 9, 344–354 (1991).
26) M. Hosokawa, T. Furihata, Y. Yaginuma, N. Yamamoto, N. Koyano, A. Fujii, Y. Nagahara, T. Satoh and K. Chiba: Drug Metab. Rev. 39, 1–15 (2007).
65) S. Bencharit, C. L. Morton, E. L. Howard-Williams, M. K. Danks, P. M. Potter and M. R. Redinbo: Nat. Struct. Biol. 9, 337–342 (2002).
66) H. Wong and M. C. Schotz: J. Lipid Res. 43, 993–999 (2002).
89) T. Satoh, P. Taylor, W. F. Bosron, S. P. Sanghani, M. Hosokawa and B. N. La Du: Drug Metab. Dispos. 30, 488–493 (2002).
104) S. H. Iynayat-Hussain, S. H. Lubis, N. Ibrahim, M. Sakian, A. R. Ghazali, N. S. Ali, M. Sersi, L. M. Toong, A. M. Zainal, S. Hashim, M. S. Ghazali, M. N. Saidin, A. R. A. Rahman, M. J. M. Rafaai, S. Omar, R. Rapiai, R. Othman, L. T. Chan, A. Omar, R. Rapiai, R. Othman, L. T. Chan, A. Johari, W. H. Soon, A. R. Salleh and T. Satoh: Toxicol. Appl. Pharmacol. 219, 210–216 (2007).
77) M. Hosokawa and T. Satoh: Xenobiotica 23, 1125–1133 (1993).
19) M. Hosokawa, K. Suzuki, D. Takahashi, M. Mori, T. Satoh and K. Chiba: Arch. Biochem. Biophys. 389, 245–253 (2001).
14) P. Ellinghaus, U. Seedorf and G. Assmann: Biochim. Biophys. Acta 1397, 175–179 (1998).
74) M. Hosokawa, Y. Endo, M. Fujisawa, S. Hara, N. Iwata, Y. Sato and T. Satoh: Drug. Metab. Dispos. 23, 1022–1027 (1995).
71) T. Furihata, M. Hosokawa, M. Masuda, T. Satoh and K. Chiba: Arch Biochem. Biophys. 447, 107–117 (2006).
24) T. Satoh and M. Hosokawa: Annu. Rev. Pharmacol. Toxicol. 38, 257–288 (1998).
47) T. Sone, M. Isobe, E. Takabatake and C. Y. Wang: Biochim. Biophys. Acta 1207, 138–142 (1994).
4) M. R. Brzezinski, T. L. Abraham, C. L. Stone, R. A. Dean and W. F. Bosron: Biochem. Pharmacol. 48, 1747–1755 (1994).
44) D. Shi, J. Yang, D. Yang and B. Yan: Toxicology 254, 97–105 (2008).
95) E. V. Pindel, N. Y. Kedishvili, T. L. Abraham, M. R. Brezezinski, J. Zhang, R. A. Dean and W. F. Bosron: J. Biol. Chem. 272, 14769–14775 (1997).
53) H. R. Pelham: Trends Biochem. Sci. 15, 483–486 (1990).
62) G. von Heijne: Eur. J. Biochem. 133, 17–21 (1983).
36) F. Zschunke, A. Salmassi, H. Kreipe, F. Buck, M. R. Parwaresch and H. J. Radzun: Blood 78, 506–512 (1991).
106) J. Ueyama, T. Satoh, T. Kondo, K. Takagi, E. Shibata, M. Goto, A. Kimata, I. Saito, T. Hasegawa, S. Wakusawa and M. Kamijima: Toxicol. Lett. 193, 115–119 (2010).
16) R. Mentlein and E. Heymann: Biochem. Pharmacol. 33, 1243–1248 (1984).
18) M. Hosokawa and T. Satoh: 7th North American ISSX Meeting, San Diego (1996).
5) E. W. Morgan, B. Yan, D. Greenway, D. R. Petersen and A. Parkinson: Arch. Biochem. Biophys. 315, 495–512 (1994).
81) E. Geshi, T. Kimura, M. Yoshimura, H. Suzuki, S. Koba, T. Sakai, T. Saito, A. Koga, M. Muramatsu and T. Katagiri: Hypertens Res. 28, 719–725 (2005).
27) M. Hosokawa, T. Maki and T. Satoh: Mol. Pharmacol. 31, 579–584 (1987).
84) S. M. Guichard, C. L. Morton, E. J. Krull, C. F. Stewart, M. K. Danks and P. M. Potter: Clin. Cancer Res. 4, 3089–3094 (1998).
39) M. Robbi, R. Van Schaftingen and H. Beaufay: Biochem. J. 313, 821–826 (1996).
31) M. Inoue, M. Morikawa, M. Tsuboi and M. Sugiura: Jpn. J. Pharmacol. 29, 9–16 (1979).
15) R. Mentlein, S. Heiland and E. Heymann: Arch. Biochem. Biophys. 200, 547–559 (1980).
7) B. Yan, D. Yang, M. Brady and A. Parkinson: Arch. Biochem. Biophys. 316, 899–908 (1995).
78) M. Derbel, M. Hosokawa and T. Satoh T: Biol. Pharam. Bull. 19, 765–767 (1996).
21) T. Furihata, M. Hosokawa, T. Satoh and K. Chiba: Biochem. J. 384, 101–110 (2004).
72) M. Hosokawa, T. Furihata, Y. Yaginuma, N. Yamamoto, N. Watanabe, E. Tsukada, Y. Ohhata, K. Kobayashi, T. Satoh and K. Chiba: Drug Metab.Pharmacokinet. 23, 73–84 (2008).
94) R. S. Rush, A. R. Main, B. F.
89
(77) 1993; 23
(28) 1994; 22
90
(14) 1998; 1397
91
92
95
96
97
10
12
13
15
16
17
18
19
1
2
3
4
5
7
8
9
(55) 1995; 47
20
21
22
23
24
25
26
ZHANG J (88) 1999; 290
29
(101) 1981; 6
DODDS H M (99) 1999; 56
(59) 1987; 262
(48) 1993; 1174
31
34
35
36
37
38
WALLACE T J (69) 1999; 20
HUMERICKHOUSE R (41) 2000; 60
(47) 1994; 1207
(87) 1996; 279
(74) 1995; 23
(54) 1991; 266
(75) 1984; 46
40
42
43
44
45
49
(52) 1993; 31
(57) 1990; 269
(39) 1996; 313
SATOH T (82) 1994; 17
50
51
53
56
58
TAKAI S (80) 1997; 20
(94) 1981; 216
(30) 1996; 24
(33) 1993; 87
(11) 1997; 25
(32) 1998; 39
60
61
62
63
64
65
(93) 1998; 35
66
67
68
(46) 1989; 264
70
71
72
73
76
78
(6) 1994; 269
79
(27) 1987; 31
(83) 1998; 58
MORTON C L (98) 1999; 59
100
102
103
104
105
106
81
84
85
86
References_xml – volume: 35
  start-page: 142
  issn: 0301-1208
  issue: 3
  year: 1998
  ident: 93
– ident: 105
  doi: 10.1177/0960327107085349
– volume: 60
  start-page: 1189
  issn: 0008-5472
  issue: 5
  year: 2000
  ident: 41
  contributor:
    fullname: HUMERICKHOUSE R
– ident: 60
  doi: 10.1016/0888-7543(91)90020-F
– ident: 63
  doi: 10.1126/science.7661899
– ident: 53
  doi: 10.1016/0968-0004(90)90303-S
– volume: 313
  start-page: 821
  issn: 0264-6021
  issue: 3
  year: 1996
  ident: 39
  doi: 10.1042/bj3130821
– ident: 65
  doi: 10.1038/nsb790
– ident: 104
  doi: 10.1016/j.taap.2006.10.014
– ident: 40
  doi: 10.1006/bbrc.1997.6413
– volume: 25
  start-page: 1089
  issn: 0090-9556
  issue: 9
  year: 1997
  ident: 11
– ident: 3
  doi: 10.1021/bi00094a018
– ident: 64
  doi: 10.1021/bi0255625
– volume: 58
  start-page: 20
  issn: 0008-5472
  issue: 1
  year: 1998
  ident: 83
– ident: 25
  doi: 10.1016/j.cbi.2006.07.001
– ident: 43
  doi: 10.1124/mol.107.036889
– ident: 36
  doi: 10.1182/blood.V78.2.506.bloodjournal782506
– ident: 5
  doi: 10.1006/abbi.1994.1531
– ident: 21
  doi: 10.1042/BJ20040765
– volume: 31
  start-page: 579
  issn: 0026-895X
  issue: 6
  year: 1987
  ident: 27
– volume: 17
  start-page: 662
  issn: 0918-6158
  issue: 5
  year: 1994
  ident: 82
  doi: 10.1248/bpb.17.662
  contributor:
    fullname: SATOH T
– volume: 24
  start-page: 634
  issn: 0090-9556
  issue: 6
  year: 1996
  ident: 30
– volume: 1207
  start-page: 138
  issn: 0005-2728
  issue: 1
  year: 1994
  ident: 47
– ident: 18
– ident: 58
  doi: 10.1006/bbrc.1994.2341
– ident: 9
  doi: 10.1006/abbi.1995.1157
– ident: 91
  doi: 10.1124/dmd.108.024018
– volume: 20
  start-page: 1201
  issn: 1044-1549
  issue: 6
  year: 1999
  ident: 69
  doi: 10.1165/ajrcmb.20.6.3402
  contributor:
    fullname: WALLACE T J
– ident: 37
– ident: 23
  doi: 10.1016/0378-4274(95)03493-5
– ident: 106
  doi: 10.1016/j.toxlet.2009.12.009
– ident: 10
– volume: 23
  start-page: 1022
  issn: 0090-9556
  issue: 10
  year: 1995
  ident: 74
– ident: 8
  doi: 10.1074/jbc.270.32.19128
– ident: 16
  doi: 10.1016/0006-2952(84)90176-X
– ident: 31
  doi: 10.1254/jjp.29.9
– ident: 26
  doi: 10.1080/03602530600952164
– volume: 87
  start-page: 5
  issn: 0009-2797
  issue: 1/3
  year: 1993
  ident: 33
– volume: 46
  start-page: 245
  issn: 0034-5164
  issue: 2
  year: 1984
  ident: 75
– volume: 262
  start-page: 7248
  issn: 0021-9258
  issue: 15
  year: 1987
  ident: 59
  doi: 10.1016/S0021-9258(18)48230-0
– ident: 67
  doi: 10.1016/S1074-5521(03)00071-1
– ident: 86
  doi: 10.1124/dmd.104.000554
– ident: 95
  doi: 10.1074/jbc.272.23.14769
– ident: 72
  doi: 10.2133/dmpk.23.73
– ident: 19
  doi: 10.1006/abbi.2001.2346
– volume: 269
  start-page: 29688
  issn: 0021-9258
  issue: 47
  year: 1994
  ident: 6
  doi: 10.1016/S0021-9258(18)43935-X
– ident: 44
  doi: 10.1016/j.tox.2008.09.019
– volume: 47
  start-page: 449
  issn: 0031-6970
  issue: 5
  year: 1995
  ident: 55
– ident: 85
  doi: 10.1172/JCI119888
– volume: 1397
  start-page: 175
  issn: 0005-2728
  issue: 2
  year: 1998
  ident: 14
– ident: 76
  doi: 10.1016/0006-2952(92)90634-U
– volume: 216
  start-page: 586
  issn: 0022-3565
  issue: 3
  year: 1981
  ident: 94
– volume: 1174
  start-page: 72
  issn: 0005-2728
  issue: 1
  year: 1993
  ident: 48
– ident: 2
– ident: 97
  doi: 10.1006/taap.1997.8187
– ident: 15
  doi: 10.1016/0003-9861(80)90386-0
– volume: 39
  start-page: 963
  issn: 0022-2275
  issue: 5
  year: 1998
  ident: 32
  doi: 10.1016/S0022-2275(20)33863-3
– ident: 17
  doi: 10.1111/j.1349-7006.1991.tb02705.x
– volume: 269
  start-page: 451
  issn: 0264-6021
  issue: 2
  year: 1990
  ident: 57
  doi: 10.1042/bj2690451
– ident: 22
  doi: 10.1016/j.bcp.2005.01.017
– ident: 1
  doi: 10.1002/pro.5560020309
– ident: 61
  doi: 10.1006/geno.1993.1285
– ident: 92
  doi: 10.1124/dmd.108.024331
– volume: 279
  start-page: 713
  issn: 0022-3565
  issue: 2
  year: 1996
  ident: 87
– ident: 24
  doi: 10.1146/annurev.pharmtox.38.1.257
– ident: 51
  doi: 10.1016/0006-291X(91)92005-5
– ident: 13
  doi: 10.1016/S0167-4781(96)00142-X
– ident: 45
  doi: 10.1016/S0003-9861(03)00286-8
– ident: 70
  doi: 10.2133/dmpk.21.173
– ident: 73
  doi: 10.1097/FPC.0b013e32830b0c5e
– volume: 290
  start-page: 314
  issn: 0022-3565
  issue: 1
  year: 1999
  ident: 88
  contributor:
    fullname: ZHANG J
– volume: 266
  start-page: 20498
  issn: 0021-9258
  issue: 30
  year: 1991
  ident: 54
  doi: 10.1016/S0021-9258(18)54952-8
– ident: 12
  doi: 10.1006/bbrc.1996.5912
– ident: 79
  doi: 10.1042/0264-6021:3380761
– ident: 29
  doi: 10.1016/0003-9861(90)90572-G
– ident: 90
  doi: 10.1124/jpet.106.111807
– ident: 103
  doi: 10.1191/0960327105ht532oa
– volume: 31
  start-page: 25
  issn: 1039-9712
  issue: 1
  year: 1993
  ident: 52
– volume: 23
  start-page: 1125
  issn: 0049-8254
  issue: 10
  year: 1993
  ident: 77
  doi: 10.3109/00498259309059427
– ident: 89
  doi: 10.1124/dmd.30.5.488
– ident: 42
  doi: 10.1016/j.lfs.2007.07.026
– ident: 71
  doi: 10.1016/j.abb.2006.01.015
– volume: 22
  start-page: 889
  issn: 0090-9556
  issue: 6
  year: 1994
  ident: 28
– volume: 264
  start-page: 12533
  issn: 0021-9258
  issue: 21
  year: 1989
  ident: 46
  doi: 10.1016/S0021-9258(18)63890-6
– volume: 6
  start-page: 27
  issn: 0388-1350
  issue: 1
  year: 1981
  ident: 101
  doi: 10.2131/jts.6.27
– ident: 62
  doi: 10.1111/j.1432-1033.1983.tb07424.x
– ident: 96
  doi: 10.1016/0024-3205(96)00065-3
– ident: 50
  doi: 10.1016/j.cbpb.2006.05.015
– ident: 81
  doi: 10.1291/hypres.28.719
– volume: 20
  start-page: 869
  issn: 0918-6158
  issue: 8
  year: 1997
  ident: 80
  doi: 10.1248/bpb.20.869
  contributor:
    fullname: TAKAI S
– ident: 35
  doi: 10.1016/0888-7543(91)90263-E
– ident: 100
  doi: 10.1016/j.bbrc.2008.02.120
– ident: 34
  doi: 10.1124/dmd.106.009381
– ident: 49
  doi: 10.1124/dmd.32.5.505
– ident: 7
  doi: 10.1006/abbi.1995.1121
– ident: 78
  doi: 10.1248/bpb.19.765
– volume: 56
  start-page: 1346
  issn: 0026-895X
  issue: 6
  year: 1999
  ident: 99
  doi: 10.1124/mol.56.6.1346
  contributor:
    fullname: DODDS H M
– volume: 59
  start-page: 1458
  issn: 0008-5472
  issue: 7
  year: 1999
  ident: 98
  contributor:
    fullname: MORTON C L
– ident: 4
  doi: 10.1016/0006-2952(94)90461-8
– ident: 68
  doi: 10.1038/nsb919
– ident: 66
  doi: 10.1194/jlr.R200007-JLR200
– ident: 102
  doi: 10.1016/S0009-2797(99)00060-5
– ident: 84
– ident: 38
  doi: 10.1016/S0014-5793(99)01111-4
– ident: 56
  doi: 10.1016/S0021-9258(18)69097-0
– ident: 20
  doi: 10.1124/dmd.104.000620
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SubjectTerms carboxylesterase
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