Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins

Mammalian carboxylesterase (CES or Ces) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused co...

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Published inMammalian genome Vol. 21; no. 9-10; pp. 427 - 441
Main Authors Holmes, Roger S, Wright, Matthew W, Laulederkind, Stanley J. F, Cox, Laura A, Hosokawa, Masakiyo, Imai, Teruko, Ishibashi, Shun, Lehner, Richard, Miyazaki, Masao, Perkins, Everett J, Potter, Phillip M, Redinbo, Matthew R, Robert, Jacques, Satoh, Tetsuo, Yamashita, Tetsuro, Yan, Bingfan, Yokoi, Tsuyoshi, Zechner, Rudolf, Maltais, Lois J
Format Journal Article
LanguageEnglish
Published New York New York : Springer-Verlag 01.10.2010
Springer-Verlag
Springer Nature B.V
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Abstract Mammalian carboxylesterase (CES or Ces) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused confusion in naming rodent Ces genes. This article describes a new nomenclature system for human, mouse, and rat carboxylesterase genes that identifies homolog gene families and allocates a unique name for each gene. The guidelines of human, mouse, and rat gene nomenclature committees were followed and “CES” (human) and “Ces” (mouse and rat) root symbols were used followed by the family number (e.g., human CES1). Where multiple genes were identified for a family or where a clash occurred with an existing gene name, a letter was added (e.g., human CES4A; mouse and rat Ces1a) that reflected gene relatedness among rodent species (e.g., mouse and rat Ces1a). Pseudogenes were named by adding “P” and a number to the human gene name (e.g., human CES1P1) or by using a new letter followed by ps for mouse and rat Ces pseudogenes (e.g., Ces2d-ps). Gene transcript isoforms were named by adding the GenBank accession ID to the gene symbol (e.g., human CES1_AB119995 or mouse Ces1e_BC019208). This nomenclature improves our understanding of human, mouse, and rat CES/Ces gene families and facilitates research into the structure, function, and evolution of these gene families. It also serves as a model for naming CES genes from other mammalian species.
AbstractList Mammalian carboxylesterase (CES or Ces) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused confusion in naming rodent Ces genes. This article describes a new nomenclature system for human, mouse, and rat carboxylesterase genes that identifies homolog gene families and allocates a unique name for each gene. The guidelines of human, mouse, and rat gene nomenclature committees were followed and "CES" (human) and "Ces" (mouse and rat) root symbols were used followed by the family number (e.g., human CES1). Where multiple genes were identified for a family or where a clash occurred with an existing gene name, a letter was added (e.g., human CES4A; mouse and rat Ces1a) that reflected gene relatedness among rodent species (e.g., mouse and rat Ces1a). Pseudogenes were named by adding "P" and a number to the human gene name (e.g., human CES1P1) or by using a new letter followed by ps for mouse and rat Ces pseudogenes (e.g., Ces2d-ps). Gene transcript isoforms were named by adding the GenBank accession ID to the gene symbol (e.g., human CES1_AB119995 or mouse Ces1e_BC019208). This nomenclature improves our understanding of human, mouse, and rat CES/Ces gene families and facilitates research into the structure, function, and evolution of these gene families. It also serves as a model for naming CES genes from other mammalian species.[PUBLICATION ABSTRACT]
Mammalian carboxylesterase (CES or Ces) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused confusion in naming rodent Ces genes. This article describes a new nomenclature system for human, mouse, and rat carboxylesterase genes that identifies homolog gene families and allocates a unique name for each gene. The guidelines of human, mouse, and rat gene nomenclature committees were followed and “CES” (human) and “Ces” (mouse and rat) root symbols were used followed by the family number (e.g., human CES1). Where multiple genes were identified for a family or where a clash occurred with an existing gene name, a letter was added (e.g., human CES4A; mouse and rat Ces1a) that reflected gene relatedness among rodent species (e.g., mouse and rat Ces1a). Pseudogenes were named by adding “P” and a number to the human gene name (e.g., human CES1P1) or by using a new letter followed by ps for mouse and rat Ces pseudogenes (e.g., Ces2d-ps). Gene transcript isoforms were named by adding the GenBank accession ID to the gene symbol (e.g., human CES1_AB119995 or mouse Ces1e_BC019208). This nomenclature improves our understanding of human, mouse, and rat CES/Ces gene families and facilitates research into the structure, function, and evolution of these gene families. It also serves as a model for naming CES genes from other mammalian species.
Mammalian carboxylesterase ( CES or Ces ) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused confusion in naming rodent Ces genes. This article describes a new nomenclature system for human, mouse, and rat carboxylesterase genes that identifies homolog gene families and allocates a unique name for each gene. The guidelines of human, mouse, and rat gene nomenclature committees were followed and “ CES ” (human) and “ Ces ” (mouse and rat) root symbols were used followed by the family number (e.g., human CES1 ). Where multiple genes were identified for a family or where a clash occurred with an existing gene name, a letter was added (e.g., human CES4A ; mouse and rat Ces1a ) that reflected gene relatedness among rodent species (e.g., mouse and rat Ces1a ). Pseudogenes were named by adding “ P ” and a number to the human gene name (e.g., human CES1P1 ) or by using a new letter followed by ps for mouse and rat Ces pseudogenes (e.g., Ces2d-ps ). Gene transcript isoforms were named by adding the GenBank accession ID to the gene symbol (e.g., human CES1_AB119995 or mouse Ces1e_BC019208 ). This nomenclature improves our understanding of human, mouse, and rat CES / Ces gene families and facilitates research into the structure, function, and evolution of these gene families. It also serves as a model for naming CES genes from other mammalian species.
Mammalian carboxylesterase ( CES or Ces ) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least five gene families. Tandem duplications have added more genes for some families, particularly for mouse and rat genomes, which has caused confusion in naming rodent Ces genes. This article describes a new nomenclature system for human, mouse, and rat carboxylesterase genes that identifies homolog gene families and allocates a unique name for each gene. The guidelines of human, mouse, and rat gene nomenclature committees were followed and “ CES ” (human) and “ Ces ” (mouse and rat) root symbols were used followed by the family number (e.g., human CES1 ). Where multiple genes were identified for a family or where a clash occurred with an existing gene name, a letter was added (e.g., human CES4A ; mouse and rat Ces1a ) that reflected gene relatedness among rodent species (e.g., mouse and rat Ces1a ). Pseudogenes were named by adding “ P ” and a number to the human gene name (e.g., human CES1P1 ) or by using a new letter followed by ps for mouse and rat Ces pseudogenes (e.g., Ces2d - ps ). Gene transcript isoforms were named by adding the GenBank accession ID to the gene symbol (e.g., human CES1_AB119995 or mouse Ces1e_BC019208 ). This nomenclature improves our understanding of human, mouse, and rat CES/Ces gene families and facilitates research into the structure, function, and evolution of these gene families. It also serves as a model for naming CES genes from other mammalian species.
Author Yokoi, Tsuyoshi
Potter, Phillip M
Miyazaki, Masao
Redinbo, Matthew R
Perkins, Everett J
Lehner, Richard
Yamashita, Tetsuro
Holmes, Roger S
Yan, Bingfan
Wright, Matthew W
Cox, Laura A
Satoh, Tetsuo
Maltais, Lois J
Laulederkind, Stanley J. F
Hosokawa, Masakiyo
Imai, Teruko
Ishibashi, Shun
Robert, Jacques
Zechner, Rudolf
Author_xml – sequence: 1
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  fullname: Cox, Laura A
– sequence: 5
  fullname: Hosokawa, Masakiyo
– sequence: 6
  fullname: Imai, Teruko
– sequence: 7
  fullname: Ishibashi, Shun
– sequence: 8
  fullname: Lehner, Richard
– sequence: 9
  fullname: Miyazaki, Masao
– sequence: 10
  fullname: Perkins, Everett J
– sequence: 11
  fullname: Potter, Phillip M
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  fullname: Redinbo, Matthew R
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  fullname: Robert, Jacques
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  fullname: Satoh, Tetsuo
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  fullname: Yamashita, Tetsuro
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/20931200$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1124/dmd.106.013862
10.1016/S0169-5002(03)00223-X
10.2133/dmpk.23.73
10.1016/S0003-9861(03)00286-8
10.1007/s00280-005-1027-y
10.1002/pro.5560020309
10.1042/BJ20021446
10.1016/j.chembiol.2006.08.013
10.1016/S1055-7903(03)00113-1
10.1101/gr.2596504
10.1016/j.ygeno.2004.07.008
10.1038/nsb919
10.1124/dmd.30.5.488
10.1042/0264-6021:3430001
10.1074/jbc.272.23.14769
10.1146/annurev.pharmtox.38.1.257
10.1016/j.ympev.2010.05.018
10.3390/molecules13020412
10.1006/abbi.1993.1143
10.1038/nature02426
10.2133/dmpk.21.173
10.1074/jbc.M413585200
10.1074/jbc.270.6.2630
10.1091/mbc.E04-03-0224
10.1021/bi00094a018
10.1074/jbc.M802686200
10.1124/mol.109.062356
10.1095/biolreprod.105.046847
10.1053/plac.1999.0407
10.1186/1471-2148-8-54
10.1006/bbrc.1997.6413
10.1093/nar/gkp939
10.1097/FPC.0b013e32830b0c5e
10.1016/j.jmb.2005.07.016
10.1016/j.cbd.2008.05.002
10.1016/j.bbrc.2008.02.120
10.2337/db05-0585
10.1046/j.1432-1033.2002.03121.x
10.1093/abbs/gmp075
10.1016/j.jmb.2006.08.025
10.1006/geno.1993.1285
10.1111/j.1432-1033.1983.tb07424.x
10.1016/j.cbd.2009.03.002
10.1074/jbc.M706841200
10.1016/j.lfs.2007.07.026
10.1111/j.1432-1033.1983.tb07828.x
10.1007/s10709-010-9438-z
10.1021/jm7011479
10.1006/bbrc.1994.2341
10.1124/jpet.104.067116
10.1124/jpet.103.056499
10.1016/S0006-291X(88)80513-8
10.1194/jlr.M000950
10.1016/j.bcp.2007.01.031
10.1111/j.1600-0684.2008.00315.x
10.1080/03602530600952164
10.1124/dmd.32.5.505
10.1016/0305-0491(85)90475-4
10.3109/03602538708994129
10.1016/S1359-6446(05)03383-0
10.1016/j.bbrc.2006.08.013
10.1016/j.cbi.2006.07.001
10.1097/01.fpc.0000230110.18957.50
10.1016/0888-7543(91)90020-F
10.1016/0378-4274(95)03493-5
10.1016/S0022-2275(20)35740-0
10.1152/ajplung.1998.275.5.L969
10.1016/j.bbalip.2009.07.006
10.1016/S0022-2275(20)31590-X
10.1007/s10822-010-9373-1
10.1016/S0021-9258(18)55139-5
10.1074/jbc.270.20.11912
10.1152/physiolgenomics.2000.2.1.1
10.1248/bpb.20.869
10.1016/S0021-9258(18)45149-6
10.1016/0167-4781(93)90093-S
10.1042/bj3430001
10.1042/bj2690451
10.1016/S0167-4781(96)00142-X
10.1042/bj20021446
10.1016/S0167-4781(98)00023-2
10.1016/S1388-1981(01)00133-0
10.1161/01.ATV.14.8.1346
10.1016/0005-2760(95)00184-0
10.1091/mbc.e04-03-0224
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Copyright Springer Science+Business Media, LLC 2010
Springer Science+Business Media, LLC 2010 2010
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Issue 9-10
Keywords Side Door
Transcript Isoforms
Cholesteryl Ester Hydrolase
Homolog Gene Family
Cholesteryl Ester Hydrolase Activity
Language English
License http://www.springer.com/tdm
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Notes http://dx.doi.org/10.1007/s00335-010-9284-4
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PMID 20931200
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PublicationDate 2010-10-00
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  year: 2010
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PublicationPlace New York
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PublicationTitle Mammalian genome
PublicationTitleAbbrev Mamm Genome
PublicationTitleAlternate Mamm Genome
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References Redinbo, Potter (CR55) 2005; 10
Morton, Iacono, Hyatt, Taylor, Cheshire (CR46) 2005; 56
Lockridge, Adkins, La Due (CR41) 1987; 262
Sanghani, Davis, Dumaual, Mahrenholz, Bosron (CR60) 2002; 269
Bencharit, Edwards, Morton, Howard-Williams, Kuhn (CR5) 2006; 363
Linke, Dawson, Harrison (CR40) 2005; 280
Rhead, Karolchik, Kuhn, Hinrichs, Zweig (CR56) 2010; 38
Schewer, Langmann, Daig, Becker, Aslandis (CR65) 1997; 233
Imai (CR32) 2006; 21
Robbi, Beaufay (CR57) 1994; 203
Holmes, Cox, VandeBerg (CR26) 2009; 4
Hosokawa, Furihata, Yaginuma, Yamamoto, Kayano (CR29) 2007; 39
Yan, Matoney, Yang (CR82) 1999; 20
Ellingham, Seedorf, Assmann (CR12) 1998; 1397
Shibita, Takagi, Kitajima, Kuroda, Omura (CR67) 1993; 17
Furihata, Hosokawa, Nakata, Satoh, Chiba (CR15) 2003; 416
Gibbs, Weinstock, Metzker, Muzny, Sodergren (CR19) 2004; 428
Taketani, Shii, Ohura, Ninomiya, Imai (CR70) 2007; 81
Holmes, Cox, VandeBerg (CR27) 2010; 138
Robbi, Beaufay, Octave (CR58) 1990; 269
Tsujita, Okuda (CR74) 1993; 34
Dolinsky, Sipione, Lehner, Vance (CR9) 2001; 1532
Okazaki, Igarashi, Nishi, Tajima, Sekiya (CR50) 2006; 55
Holmes, Glenn, VandeBerg, Cox (CR25) 2009; 38
Masaki, Hashimoto, Imai (CR43) 2007; 35
Wang, Gilham, Lehner (CR78) 2007; 282
Satoh, Hosokawa (CR62) 1998; 38
Holmes, Chan, Cox, Murphy, VandeBerg (CR23) 2008; 8
Woodburne, Rich, Springer (CR80) 2003; 28
Miyazaki, Yamashita, Suzuki, Saito, Soeta (CR45) 2006; 13
Barthel, Torres, Hyatt, Edwards, Hatfield (CR2) 2008; 51
Vanlith, Haller, Vanhoof, Vanderwouw, Vanzutphen (CR75) 1993; 301
Hosokawa (CR28) 2008; 13
Munger, Shi, Mark, Chin, Gerard (CR47) 1991; 266
Holmes, VandeBerg, Cox (CR24) 2009; 4
Vistoli, Pedretti, Mazzolari, Testa (CR76) 2010; 24
Potter, Wolverton, Morton, Wierdl, Danks (CR54) 1998; 58
Miyazaki, Kamiie, Soeta, Taira, Yamashita (CR44) 2003; 370
Ecroyd, Belghazi, Dacheux, Miyazaki, Yamashita (CR11) 2006; 74
Hosokawa, Furihata, Yaginuma, Yamamoto, Watanabe (CR30) 2008; 23
Williams, Wang, Wrighton, Qian, Perkins (CR79) 2010; 57
Kroetz, McBride, Gonzalez (CR36) 1993; 32
Ohtsuka, Inoue, Kameyama (CR49) 2003; 41
Ko, Erickson, Lehner (CR34) 2009; 1791
Becker, Bottcher, Lackner, Fehringer, Notka (CR3) 1994; 14
Gilham, Alam, Gao, Vance, Lehner (CR20) 2005; 16
Tanimoto, Kaneyasu, Shimokuni, Hiyama, Nishiyama (CR71) 2007; 17
Pindel, Kedishvili, Abraham, Brezinski, Zhang (CR53) 1997; 272
Satoh, Taylor, Bosron, Sanghani, Hosokawa (CR64) 2002; 30
Takai, Matsuda, Usami, Adachi, Sugiyama (CR69) 1997; 20
(CR72) 2004; 14
von Heijne (CR77) 1983; 133
Sanghani, Quinney, Fredenberg, Davis, Murray (CR61) 2004; 32
Marsh, Xiao, Yu, Ahluwalia, Minton (CR42) 2004; 84
Mutch, Nave, McCracken, Zech, Williams (CR48) 2007; 73
Okazaki, Igarashi, Nishi, Sekiya, Tajima (CR51) 2008; 283
Bencharit, Morton, Xue, Potter, Redinbo (CR4) 2003; 10
Berning, De Looze, von Deimling (CR6) 1985; 80
Leinweber (CR39) 1987; 18
Ovnic, Swank, Fletcher, Zhen, Novak (CR52) 1991; 11
Thierry-Mieg, Thierry-Mieg (CR73) 2006; 7
Robbi, Beaufay (CR101) 1993; 137
Genetta, D’Eustachio, Kadner, Finlay (CR16) 1988; 151
Satoh, Hosokawa (CR102) 1995; 82–83
Zhang, Hu, Zhu, Liu, Zhou (CR84) 2009; 41
Lehner, Vance (CR38) 1999; 343
Ruppert, Bagheri, Markart, Schmidt, Seegar (CR59) 2006; 348
Donoghue, Benton (CR10) 2007; 22
Langmann, Becker, Aslanidis, Notka, Ulrich (CR37) 1997; 1350
Imai, Yoshigae, Hosokawa, Chiba, Otagiri (CR33) 2003; 307
Aida, Moore, Negishi (CR1) 1993; 1174
Fleming, Bencharit, Edwards, Hyatt, Tsurkan (CR13) 2005; 352
Satoh, Hosokawa (CR63) 2006; 162
Ghosh, Mallonee, Grogan (CR18) 1995; 1259
Yoshimura, Kimura, Ishii, Ishii, Matsuura (CR83) 2008; 369
Holmes, Cox, VandeBerg (CR22) 2008; 3
Sun, Murry, Sanghani, Davis, Kedishvilli (CR68) 2004; 310
Ghosh (CR17) 2000; 2
Diczfalusy, Bjorkkem, Einarsson, Hillebrant, Alexson (CR8) 2001; 42
Hemmert, Otto, Wierdl, Edwards, Fleming (CR21) 2010; 77
Schreiber, Taschler, Wolinski, Seper, Tamegger (CR66) 2009; 50
Zhen, Rusiniak, Swank (CR85) 1995; 270
Humerickhouse, Lohrbach, Li, Bosron, Dolan (CR31) 2000; 60
Cygler, Schrag, Sussman, Harel, Silman (CR7) 1993; 2
Xu, Zhang, Ma, MacLeod (CR81) 2002; 8
Fukami, Nakajima, Maruichi, Takahashi, Takamiya (CR14) 2008; 18
Krishnasamy, Teng, Dhand, Schultz, Gross (CR35) 1998; 275
M Yoshimura (9284_CR83) 2008; 369
JS Munger (9284_CR47) 1991; 266
Z Sun (9284_CR68) 2004; 310
K Masaki (9284_CR43) 2007; 35
RS Holmes (9284_CR24) 2009; 4
G Heijne von (9284_CR77) 1983; 133
T Linke (9284_CR40) 2005; 280
A Becker (9284_CR3) 1994; 14
9284_CR76
R Krishnasamy (9284_CR35) 1998; 275
S Ghosh (9284_CR18) 1995; 1259
T Furihata (9284_CR15) 2003; 416
T Tsujita (9284_CR74) 1993; 34
9284_CR73
L Zhang (9284_CR84) 2009; 41
T Imai (9284_CR33) 2003; 307
M Miyazaki (9284_CR44) 2003; 370
G Xu (9284_CR81) 2002; 8
S Ghosh (9284_CR17) 2000; 2
EV Pindel (9284_CR53) 1997; 272
M Taketani (9284_CR70) 2007; 81
TL Genetta (9284_CR16) 1988; 151
O Lockridge (9284_CR41) 1987; 262
MR Redinbo (9284_CR55) 2005; 10
S Marsh (9284_CR42) 2004; 84
T Satoh (9284_CR64) 2002; 30
MA Diczfalusy (9284_CR8) 2001; 42
KW Ko (9284_CR34) 2009; 1791
B Rhead (9284_CR56) 2010; 38
R Humerickhouse (9284_CR31) 2000; 60
R Lehner (9284_CR38) 1999; 343
S Bencharit (9284_CR4) 2003; 10
D Gilham (9284_CR20) 2005; 16
K Aida (9284_CR1) 1993; 1174
H Ohtsuka (9284_CR49) 2003; 41
H Ecroyd (9284_CR11) 2006; 74
FJ Leinweber (9284_CR39) 1987; 18
M Robbi (9284_CR101) 1993; 137
K Tanimoto (9284_CR71) 2007; 17
T Satoh (9284_CR63) 2006; 162
L Zhen (9284_CR85) 1995; 270
C Ruppert (9284_CR59) 2006; 348
RS Holmes (9284_CR27) 2010; 138
M Hosokawa (9284_CR29) 2007; 39
CL Morton (9284_CR46) 2005; 56
S Bencharit (9284_CR5) 2006; 363
RS Holmes (9284_CR23) 2008; 8
The MGC Project Team (9284_CR72) 2004; 14
BL Barthel (9284_CR2) 2008; 51
M Ovnic (9284_CR52) 1991; 11
R Schreiber (9284_CR66) 2009; 50
SP Sanghani (9284_CR60) 2002; 269
AC Hemmert (9284_CR21) 2010; 77
E Mutch (9284_CR48) 2007; 73
SP Sanghani (9284_CR61) 2004; 32
PM Potter (9284_CR54) 1998; 58
H Wang (9284_CR78) 2007; 282
DL Kroetz (9284_CR36) 1993; 32
T Fukami (9284_CR14) 2008; 18
MO Woodburne (9284_CR80) 2003; 28
RA Gibbs (9284_CR19) 2004; 428
T Langmann (9284_CR37) 1997; 1350
RS Holmes (9284_CR25) 2009; 38
M Robbi (9284_CR57) 1994; 203
B Yan (9284_CR82) 1999; 20
ET Williams (9284_CR79) 2010; 57
PCJ Donoghue (9284_CR10) 2007; 22
S Takai (9284_CR69) 1997; 20
M Robbi (9284_CR58) 1990; 269
HA Vanlith (9284_CR75) 1993; 301
CD Fleming (9284_CR13) 2005; 352
H Schewer (9284_CR65) 1997; 233
M Cygler (9284_CR7) 1993; 2
F Shibita (9284_CR67) 1993; 17
M Hosokawa (9284_CR28) 2008; 13
M Miyazaki (9284_CR45) 2006; 13
T Satoh (9284_CR102) 1995; 82–83
W Berning (9284_CR6) 1985; 80
H Okazaki (9284_CR51) 2008; 283
P Ellingham (9284_CR12) 1998; 1397
T Satoh (9284_CR62) 1998; 38
VW Dolinsky (9284_CR9) 2001; 1532
M Hosokawa (9284_CR30) 2008; 23
RS Holmes (9284_CR22) 2008; 3
T Imai (9284_CR32) 2006; 21
RS Holmes (9284_CR26) 2009; 4
H Okazaki (9284_CR50) 2006; 55
References_xml – volume: 35
  start-page: 1089
  year: 2007
  end-page: 1095
  ident: CR43
  article-title: Intestinal first-pass metabolism via carboxylesterase in rat jejunum and intestine
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.106.013862
  contributor:
    fullname: Imai
– volume: 41
  start-page: 87
  year: 2003
  end-page: 198
  ident: CR49
  article-title: Intracellular conversion of irinotecan to its active form, SN-38, by native carboxylesterase in human non-small cell lung cancer
  publication-title: Lung Cancer
  doi: 10.1016/S0169-5002(03)00223-X
  contributor:
    fullname: Kameyama
– volume: 14
  start-page: 1346
  year: 1994
  end-page: 1355
  ident: CR3
  article-title: Purification, cloning and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase
  publication-title: Arterioscler Thromb
  contributor:
    fullname: Notka
– volume: 23
  start-page: 73
  year: 2008
  end-page: 84
  ident: CR30
  article-title: Structural organization and characterization of the regulatory element of the human carboxylesterase ( and ) genes
  publication-title: Drug Metab Pharmacokinet
  doi: 10.2133/dmpk.23.73
  contributor:
    fullname: Watanabe
– volume: 416
  start-page: 101
  year: 2003
  end-page: 109
  ident: CR15
  article-title: Purification, molecular cloning, and functional expression of inducible liver acylcarnitine hydrolase in C57BL/6 mouse, belonging to the carboxylesterase multigene family
  publication-title: Arch Biochem Biophys
  doi: 10.1016/S0003-9861(03)00286-8
  contributor:
    fullname: Chiba
– volume: 56
  start-page: 629
  year: 2005
  end-page: 636
  ident: CR46
  article-title: Activation and antitumor activity of CPT-11 in plasma esterase-deficient mice
  publication-title: Cancer Chemother Pharmacol
  doi: 10.1007/s00280-005-1027-y
  contributor:
    fullname: Cheshire
– volume: 2
  start-page: 1
  year: 2000
  end-page: 8
  ident: CR17
  article-title: Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing and expression of full-length cDNA
  publication-title: Physiol Genomics
  contributor:
    fullname: Ghosh
– volume: 2
  start-page: 366
  year: 1993
  end-page: 382
  ident: CR7
  article-title: Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases and related proteins
  publication-title: Protein Sci
  doi: 10.1002/pro.5560020309
  contributor:
    fullname: Silman
– volume: 370
  start-page: 101
  year: 2003
  end-page: 110
  ident: CR44
  article-title: Molecular cloning and characterization of a novel carboxylesterase-like protein that is physiologically present at high concentrations in the urine of domestic cats ( )
  publication-title: Biochem J
  doi: 10.1042/BJ20021446
  contributor:
    fullname: Yamashita
– volume: 13
  start-page: 1070
  year: 2006
  end-page: 1079
  ident: CR45
  article-title: A major urinary protein of the domestic cat regulates the production of felinine, a putative pheromone precursor
  publication-title: Chem Biol
  doi: 10.1016/j.chembiol.2006.08.013
  contributor:
    fullname: Soeta
– volume: 28
  start-page: 360
  year: 2003
  end-page: 385
  ident: CR80
  article-title: The evolution of tribospheny and the antiquity of mammalian clades
  publication-title: Mol Phylogenet Evol
  doi: 10.1016/S1055-7903(03)00113-1
  contributor:
    fullname: Springer
– volume: 1174
  start-page: 72
  year: 1993
  end-page: 74
  ident: CR1
  article-title: Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Negishi
– volume: 14
  start-page: 2121
  year: 2004
  end-page: 2127
  ident: CR72
  article-title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)
  publication-title: Genome Res
  doi: 10.1101/gr.2596504
– volume: 84
  start-page: 661
  year: 2004
  end-page: 668
  ident: CR42
  article-title: Pharmacogenomic assessment of carboxylesterases 1 and 2
  publication-title: Genomics
  doi: 10.1016/j.ygeno.2004.07.008
  contributor:
    fullname: Minton
– volume: 10
  start-page: 349
  year: 2003
  end-page: 356
  ident: CR4
  article-title: Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme
  publication-title: Nat Struct Biol
  doi: 10.1038/nsb919
  contributor:
    fullname: Redinbo
– volume: 20
  start-page: 869
  year: 1997
  end-page: 873
  ident: CR69
  article-title: Hydrolytic profile for ester- or amide-linkage by carboxylesterases pI 5.3 and 4.5 from human liver
  publication-title: Biol Pharm Bull
  contributor:
    fullname: Sugiyama
– volume: 30
  start-page: 488
  year: 2002
  end-page: 493
  ident: CR64
  article-title: Current progress on esterases: from molecular structure to function
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.30.5.488
  contributor:
    fullname: Hosokawa
– volume: 343
  start-page: 1
  year: 1999
  end-page: 10
  ident: CR38
  article-title: Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol
  publication-title: Biochem J
  doi: 10.1042/0264-6021:3430001
  contributor:
    fullname: Vance
– volume: 272
  start-page: 14769
  year: 1997
  end-page: 14775
  ident: CR53
  article-title: Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin
  publication-title: J Biol Chem
  doi: 10.1074/jbc.272.23.14769
  contributor:
    fullname: Zhang
– volume: 38
  start-page: 257
  year: 1998
  end-page: 288
  ident: CR62
  article-title: The mammalian carboxylesterases: from molecules to functions
  publication-title: Ann Rev Pharmacol Toxicol
  doi: 10.1146/annurev.pharmtox.38.1.257
  contributor:
    fullname: Hosokawa
– volume: 57
  start-page: 23
  issue: 1
  year: 2010
  end-page: 34
  ident: CR79
  article-title: Genomic analysis of the carboxylesterases: identification and classification of novel forms
  publication-title: Mol Phylogenet Evol
  doi: 10.1016/j.ympev.2010.05.018
  contributor:
    fullname: Perkins
– volume: 1791
  start-page: 1133
  year: 2009
  end-page: 1143
  ident: CR34
  article-title: Es-x/Ces1 prevents triacylglycerol accumulation in McArdle-RH7777 hepatocytes
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Lehner
– volume: 13
  start-page: 412
  year: 2008
  end-page: 431
  ident: CR28
  article-title: Structure and catalytic properties of carboxylesterase isozymes involved in metabolic activation of prodrugs
  publication-title: Molecules
  doi: 10.3390/molecules13020412
  contributor:
    fullname: Hosokawa
– volume: 301
  start-page: 265
  year: 1993
  end-page: 274
  ident: CR75
  article-title: Characterization of rat plasma esterase ES-1A concerning its molecular and catalytic properties
  publication-title: Arch Biochem Biophys
  doi: 10.1006/abbi.1993.1143
  contributor:
    fullname: Vanzutphen
– volume: 428
  start-page: 493
  year: 2004
  end-page: 521
  ident: CR19
  article-title: Genome sequence of the Brown Norway rat yields insights into mammalian evolution
  publication-title: Nature
  doi: 10.1038/nature02426
  contributor:
    fullname: Sodergren
– volume: 21
  start-page: 173
  year: 2006
  end-page: 185
  ident: CR32
  article-title: Human carboxylesterase isozymes: catalytic properties and rational drug design
  publication-title: Drug Metab Pharmacokinet
  doi: 10.2133/dmpk.21.173
  contributor:
    fullname: Imai
– volume: 8
  start-page: 2605
  year: 2002
  end-page: 2611
  ident: CR81
  article-title: Human carboxylesterase 2 is commonly expressed in tumor tissue and is correlated with the activation of irinotecan
  publication-title: Clin Cancer Res
  contributor:
    fullname: MacLeod
– volume: 280
  start-page: 23287
  year: 2005
  end-page: 23294
  ident: CR40
  article-title: Isolation and characterization of a microsomal retinyl ester hydrolase
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M413585200
  contributor:
    fullname: Harrison
– volume: 270
  start-page: 11912
  year: 1995
  end-page: 11920
  ident: CR85
  article-title: The beta-glucuronidase propeptide contains a serpin-related octamer necessary for complex formation with egasyn esterase and for retention within the endoplasmic reticulum
  publication-title: J Biol Chem
  doi: 10.1074/jbc.270.6.2630
  contributor:
    fullname: Swank
– volume: 16
  start-page: 984
  year: 2005
  end-page: 996
  ident: CR20
  article-title: Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.E04-03-0224
  contributor:
    fullname: Lehner
– volume: 32
  start-page: 11606
  year: 1993
  end-page: 11617
  ident: CR36
  article-title: Glycosylation-dependent activity of Baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms
  publication-title: Biochemistry
  doi: 10.1021/bi00094a018
  contributor:
    fullname: Gonzalez
– volume: 1397
  start-page: 175
  year: 1998
  end-page: 179
  ident: CR12
  article-title: Cloning and sequencing of a novel murine liver carboxylesterase cDNA
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Assmann
– volume: 283
  start-page: 33357
  year: 2008
  end-page: 33364
  ident: CR51
  article-title: Identification of neutral cholesterol hydrolase, a key enzyme removing cholesterol from macrophages
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M802686200
  contributor:
    fullname: Tajima
– volume: 77
  start-page: 508
  year: 2010
  end-page: 516
  ident: CR21
  article-title: Human carboxylesterase 1 stereoselectively binds the nerve agent cyclosarin and spontaneously hydrolyzes the nerve agent sarin
  publication-title: Mol Pharmacol
  doi: 10.1124/mol.109.062356
  contributor:
    fullname: Fleming
– volume: 74
  start-page: 439
  year: 2006
  end-page: 447
  ident: CR11
  article-title: An epididymal form of cauxin, a carboxylesterase-like enzyme, is present and active in mammalian male reproductive fluids
  publication-title: Biol Reprod
  doi: 10.1095/biolreprod.105.046847
  contributor:
    fullname: Yamashita
– volume: 20
  start-page: 517
  year: 1999
  end-page: 525
  ident: CR82
  article-title: Human carboxylesterases in term placenta: enzymatic characterization, molecular cloning and evidence for the existence of multiple forms
  publication-title: Placenta
  doi: 10.1053/plac.1999.0407
  contributor:
    fullname: Yang
– volume: 8
  start-page: 54
  year: 2008
  ident: CR23
  article-title: Opossum carboxylesterases: sequences, phylogeny and evidence for CES duplication events predating the marsupial-eutherian common ancestor
  publication-title: BMC Evol Biol
  doi: 10.1186/1471-2148-8-54
  contributor:
    fullname: VandeBerg
– volume: 233
  start-page: 117
  year: 1997
  end-page: 120
  ident: CR65
  article-title: Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.1997.6413
  contributor:
    fullname: Aslandis
– volume: 38
  start-page: D613
  year: 2010
  end-page: D619
  ident: CR56
  article-title: The UCSC Genome Browser database: update 2010
  publication-title: Nucl Acids Res
  doi: 10.1093/nar/gkp939
  contributor:
    fullname: Zweig
– volume: 1532
  start-page: 162
  year: 2001
  end-page: 172
  ident: CR9
  article-title: The cloning and expression of murine triacylglycerol hydrolase cDNA and the structure of the corresponding gene
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Vance
– volume: 18
  start-page: 911
  year: 2008
  end-page: 920
  ident: CR14
  article-title: Structure and characterization of human carboxylesterase 1A1, 1A2 and 1A3 genes
  publication-title: Pharm Genomics
  doi: 10.1097/FPC.0b013e32830b0c5e
  contributor:
    fullname: Takamiya
– volume: 34
  start-page: 1773
  year: 1993
  end-page: 1781
  ident: CR74
  article-title: Palmitoyl-coenzyme A hydrolyzing activity in rat kidney and its relationship with carboxylesterase
  publication-title: J Lipid Res
  contributor:
    fullname: Okuda
– volume: 352
  start-page: 165
  year: 2005
  end-page: 177
  ident: CR13
  article-title: Structural insights into drug processing by human carboxylesterase 1: tamoxifen, Mevastatin, and inhibition by Benzil
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2005.07.016
  contributor:
    fullname: Tsurkan
– volume: 60
  start-page: 1189
  year: 2000
  end-page: 1192
  ident: CR31
  article-title: Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms h-CE1 and hCE-2
  publication-title: Cancer Res
  contributor:
    fullname: Dolan
– volume: 3
  start-page: 195
  year: 2008
  end-page: 204
  ident: CR22
  article-title: Mammalian carboxylesterase 5: comparative biochemistry and genomics
  publication-title: Comp Biochem Physiol D Genomics Proteomics
  doi: 10.1016/j.cbd.2008.05.002
  contributor:
    fullname: VandeBerg
– volume: 369
  start-page: 939
  year: 2008
  end-page: 942
  ident: CR83
  article-title: Functional polymorphisms in carboxylesterase1A2 ( ) gene involves specific protein 1 (Sp1) binding sites
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/j.bbrc.2008.02.120
  contributor:
    fullname: Matsuura
– volume: 4
  start-page: 54
  year: 2009
  end-page: 65
  ident: CR26
  article-title: Horse carboxylesterases: evidence for six CES1 and four families of CES genes on chromosome 3
  publication-title: Comp Biochem Physiol
  contributor:
    fullname: VandeBerg
– volume: 55
  start-page: 2091
  year: 2006
  end-page: 2097
  ident: CR50
  article-title: Identification of a novel member of the carboxylesterase family that hydrolyzes triacylglycerol. A potential role in adipocyte lipolysis
  publication-title: Diabetes
  doi: 10.2337/db05-0585
  contributor:
    fullname: Sekiya
– volume: 269
  start-page: 4387
  year: 2002
  end-page: 4398
  ident: CR60
  article-title: Identification of microsomal rat liver carboxylesterases and their activity with retinyl palmitate
  publication-title: Eur J Biochem
  doi: 10.1046/j.1432-1033.2002.03121.x
  contributor:
    fullname: Bosron
– volume: 41
  start-page: 809
  year: 2009
  end-page: 815
  ident: CR84
  article-title: Identification and characterization of an epididymis-specific gene,
  publication-title: Acta Biochim Biophys Sin
  doi: 10.1093/abbs/gmp075
  contributor:
    fullname: Zhou
– volume: 266
  start-page: 18832
  year: 1991
  end-page: 18838
  ident: CR47
  article-title: A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases
  publication-title: J Biol Chem
  contributor:
    fullname: Gerard
– volume: 363
  start-page: 201
  year: 2006
  end-page: 214
  ident: CR5
  article-title: Multisite promiscuity in the processing of endogenous substrates by human carboxylesterase 1
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2006.08.025
  contributor:
    fullname: Kuhn
– volume: 17
  start-page: 76
  year: 1993
  end-page: 82
  ident: CR67
  article-title: Molecular cloning and characterization of a human carboxylesterase gene
  publication-title: Genomics
  doi: 10.1006/geno.1993.1285
  contributor:
    fullname: Omura
– volume: 133
  start-page: 17
  year: 1983
  end-page: 21
  ident: CR77
  article-title: Patterns of amino acids near signal-sequence cleavage sites
  publication-title: Eur J Biochem
  doi: 10.1111/j.1432-1033.1983.tb07424.x
  contributor:
    fullname: von Heijne
– volume: 4
  start-page: 209
  year: 2009
  end-page: 217
  ident: CR24
  article-title: A new class of mammalian carboxylesterase
  publication-title: Comp Biochem Physiol Part D Genomics Proteomics
  doi: 10.1016/j.cbd.2009.03.002
  contributor:
    fullname: Cox
– volume: 282
  start-page: 33218
  year: 2007
  end-page: 33226
  ident: CR78
  article-title: Proteomic and lipid characterization of apo-lipoprotein B-free luminal lipid droplets from mouse liver microsomes: implications for very low density lipoprotein assembly
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M706841200
  contributor:
    fullname: Lehner
– volume: 81
  start-page: 924
  year: 2007
  end-page: 932
  ident: CR70
  article-title: Carboxylesterase in the liver and small intestine of experimental animals and human
  publication-title: Life Sci
  doi: 10.1016/j.lfs.2007.07.026
  contributor:
    fullname: Imai
– volume: 22
  start-page: 424
  year: 2007
  end-page: 630
  ident: CR10
  article-title: Rocks and clocks: calibrating the tree of life using fossils and molecules
  publication-title: Trends Genet
  contributor:
    fullname: Benton
– volume: 137
  start-page: 293
  year: 1993
  end-page: 301
  ident: CR101
  article-title: Purification and characterization of various esterases from rat liver
  publication-title: Eur J Biochem
  doi: 10.1111/j.1432-1033.1983.tb07828.x
  contributor:
    fullname: Beaufay
– volume: 138
  start-page: 695
  issue: 7
  year: 2010
  end-page: 708
  ident: CR27
  article-title: Mammalian carboxylesterase 3: comparative genomics and proteomics
  publication-title: Genetica
  doi: 10.1007/s10709-010-9438-z
  contributor:
    fullname: VandeBerg
– volume: 51
  start-page: 298
  year: 2008
  end-page: 304
  ident: CR2
  article-title: Identification of human intestinal carboxylesterase as the primary enzyme for activation of a doxazoline carbamate prodrug
  publication-title: J Med Chem
  doi: 10.1021/jm7011479
  contributor:
    fullname: Hatfield
– volume: 203
  start-page: 1404
  year: 1994
  end-page: 1411
  ident: CR57
  article-title: Cloning and sequencing of rat liver carboxylesterase ES-3 (egasyn)
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.1994.2341
  contributor:
    fullname: Beaufay
– volume: 310
  start-page: 469
  year: 2004
  end-page: 476
  ident: CR68
  article-title: Methylphenadate is stereoselectively hydrolyzed by human carboxylesterase CES1A1
  publication-title: J Pharmcol Exp Ther
  doi: 10.1124/jpet.104.067116
  contributor:
    fullname: Kedishvilli
– volume: 307
  start-page: 1234
  year: 2003
  end-page: 1242
  ident: CR33
  article-title: Evidence for the involvement of a pulmonary first-pass effect via carboxylesterase in the disposition of a propanolol ester derivative after intravenous administration
  publication-title: J Pharmacol Exp Ther
  doi: 10.1124/jpet.103.056499
  contributor:
    fullname: Otagiri
– volume: 269
  start-page: 451
  year: 1990
  end-page: 458
  ident: CR58
  article-title: Nucleotide sequence of cDNA coding for rat liver pI 6.1 esterase (ES-10), a carboxylesterase located in the lumen of the endoplasmic reticulum
  publication-title: Biochem J
  contributor:
    fullname: Octave
– volume: 151
  start-page: 1364
  year: 1988
  end-page: 1370
  ident: CR16
  article-title: cDNA cloning of esterase 1, the major esterase activity in mouse plasma
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/S0006-291X(88)80513-8
  contributor:
    fullname: Finlay
– volume: 1259
  start-page: 305
  year: 1995
  end-page: 312
  ident: CR18
  article-title: Molecular cloning and expression of rat hepatic neutral cholesteryl ester hydrolase
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Grogan
– volume: 1350
  start-page: 65
  year: 1997
  end-page: 74
  ident: CR37
  article-title: Structural organization and characterization of the promoter region of a human carboxylesterase gene
  publication-title: Biochim Biophys Acta
  contributor:
    fullname: Ulrich
– volume: 262
  start-page: 12945
  year: 1987
  end-page: 12952
  ident: CR41
  article-title: Location of disulfide bonds within the sequence of human serum cholinesterase
  publication-title: J Biol Chem
  contributor:
    fullname: La Due
– volume: 50
  start-page: 2514
  year: 2009
  end-page: 2523
  ident: CR66
  article-title: Esterase 22 and beta-glucuronidase hydrolyze retinoids in mouse liver
  publication-title: J Lipid Res
  doi: 10.1194/jlr.M000950
  contributor:
    fullname: Tamegger
– volume: 73
  start-page: 1657
  year: 2007
  end-page: 1664
  ident: CR48
  article-title: The role of esterases in the metabolism of ciclesinide to deisobutyrl-ciclesonide in human tissue
  publication-title: Biochem Pharmacol
  doi: 10.1016/j.bcp.2007.01.031
  contributor:
    fullname: Williams
– volume: 24
  start-page: 771
  issue: 9
  year: 2010
  end-page: 787
  ident: CR76
  article-title: Homology modelling and metabolism prediction of human carboxylesterase-2 using docking analyses by GriDock: a parallelized tool based on AutoDock 4.0
  publication-title: J Comput Aided Mol Des
  contributor:
    fullname: Testa
– volume: 58
  start-page: 3627
  year: 1998
  end-page: 3632
  ident: CR54
  article-title: Cellular localization domains of a rabbit and human carboxylesterase: influence on irinotecan (CPT-11) metabolism by the rabbit enzyme
  publication-title: Cancer Res
  contributor:
    fullname: Danks
– volume: 38
  start-page: 27
  year: 2009
  end-page: 38
  ident: CR25
  article-title: Baboon carboxylesterases 1 and 2: sequences, structures and phylogenetic relationships with human and other primate carboxylesterases
  publication-title: J Med Primatol
  doi: 10.1111/j.1600-0684.2008.00315.x
  contributor:
    fullname: Cox
– volume: 42
  start-page: 1025
  year: 2001
  end-page: 1032
  ident: CR8
  article-title: Characterization of enzymes involved in formation of ethyl esters of long-chain fatty acids
  publication-title: J Lipid Res
  contributor:
    fullname: Alexson
– volume: 39
  start-page: 1
  year: 2007
  end-page: 15
  ident: CR29
  article-title: Genomic structure and transcriptional regulation of the rat, mouse and human carboxylesterase genes
  publication-title: Drug Metab Rev
  doi: 10.1080/03602530600952164
  contributor:
    fullname: Kayano
– volume: 32
  start-page: 505
  year: 2004
  end-page: 511
  ident: CR61
  article-title: Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N(5-aminopentanoic acid)-1-piperidino] carbonyloxycampothecin and 7-ethyl-10-[4-(1-piperidino)-1 amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.32.5.505
  contributor:
    fullname: Murray
– volume: 80
  start-page: 859
  year: 1985
  end-page: 865
  ident: CR6
  article-title: Identification and development of a genetically closely linked carboxylesterase gene family of the mouse liver
  publication-title: Comp Biochem Physiol
  doi: 10.1016/0305-0491(85)90475-4
  contributor:
    fullname: von Deimling
– volume: 18
  start-page: 379
  year: 1987
  end-page: 439
  ident: CR39
  article-title: Possible physiological roles of carboxyl ester hydrolases
  publication-title: Drug Metab Rev
  doi: 10.3109/03602538708994129
  contributor:
    fullname: Leinweber
– volume: 10
  start-page: 313
  year: 2005
  end-page: 320
  ident: CR55
  article-title: Mammalian carboxylesterases: from drug targets to protein therapeutics
  publication-title: Drug Discov Today
  doi: 10.1016/S1359-6446(05)03383-0
  contributor:
    fullname: Potter
– volume: 275
  start-page: L969
  year: 1998
  end-page: L975
  ident: CR35
  article-title: Molecular cloning, characterization and differential expression pattern of mouse lung surfactant convertase
  publication-title: Am J Physiol Lung Mol Cell Biol
  contributor:
    fullname: Gross
– volume: 348
  start-page: 1449
  year: 2006
  end-page: 1454
  ident: CR59
  article-title: Liver carboxylesterase cleaves surfactant protein (SP-B) and promotes surfactant subtype conversion
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/j.bbrc.2006.08.013
  contributor:
    fullname: Seegar
– volume: 162
  start-page: 195
  year: 2006
  end-page: 211
  ident: CR63
  article-title: Structure, function and regulation of carboxylesterases
  publication-title: Chem Biol Interact
  doi: 10.1016/j.cbi.2006.07.001
  contributor:
    fullname: Hosokawa
– volume: 7
  start-page: S12
  issue: Suppl 1
  year: 2006
  end-page: S14
  ident: CR73
  article-title: AceView: a comprehensive cDNA-supported gene and transcripts annotation
  publication-title: Genome Biol
  contributor:
    fullname: Thierry-Mieg
– volume: 17
  start-page: 1
  year: 2007
  end-page: 10
  ident: CR71
  article-title: Human carboxylesterase 1A2 expressed from carboxylesterase 1A1 and 1A2 genes is a potent predictor of CPT-11 cytotoxicity in vitro
  publication-title: Pharm Genomics
  doi: 10.1097/01.fpc.0000230110.18957.50
  contributor:
    fullname: Nishiyama
– volume: 11
  start-page: 956
  year: 1991
  end-page: 967
  ident: CR52
  article-title: Characterization and functional expression of a cDNA encoding egasyn (esterase-22): the endoplasmic reticulum-targeting protein of beta-glucuronidase
  publication-title: Genomics
  doi: 10.1016/0888-7543(91)90020-F
  contributor:
    fullname: Novak
– volume: 82–83
  start-page: 439
  year: 1995
  end-page: 445
  ident: CR102
  article-title: Molecular aspects of carboxylesterase isoforms in comparison with other esterases
  publication-title: Toxicol Letters
  doi: 10.1016/0378-4274(95)03493-5
  contributor:
    fullname: Hosokawa
– volume: 280
  start-page: 23287
  year: 2005
  ident: 9284_CR40
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M413585200
  contributor:
    fullname: T Linke
– volume: 50
  start-page: 2514
  year: 2009
  ident: 9284_CR66
  publication-title: J Lipid Res
  doi: 10.1194/jlr.M000950
  contributor:
    fullname: R Schreiber
– volume: 34
  start-page: 1773
  year: 1993
  ident: 9284_CR74
  publication-title: J Lipid Res
  doi: 10.1016/S0022-2275(20)35740-0
  contributor:
    fullname: T Tsujita
– volume: 162
  start-page: 195
  year: 2006
  ident: 9284_CR63
  publication-title: Chem Biol Interact
  doi: 10.1016/j.cbi.2006.07.001
  contributor:
    fullname: T Satoh
– volume: 275
  start-page: L969
  year: 1998
  ident: 9284_CR35
  publication-title: Am J Physiol Lung Mol Cell Biol
  doi: 10.1152/ajplung.1998.275.5.L969
  contributor:
    fullname: R Krishnasamy
– volume: 310
  start-page: 469
  year: 2004
  ident: 9284_CR68
  publication-title: J Pharmcol Exp Ther
  doi: 10.1124/jpet.104.067116
  contributor:
    fullname: Z Sun
– volume: 369
  start-page: 939
  year: 2008
  ident: 9284_CR83
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/j.bbrc.2008.02.120
  contributor:
    fullname: M Yoshimura
– volume: 283
  start-page: 33357
  year: 2008
  ident: 9284_CR51
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M802686200
  contributor:
    fullname: H Okazaki
– volume: 77
  start-page: 508
  year: 2010
  ident: 9284_CR21
  publication-title: Mol Pharmacol
  doi: 10.1124/mol.109.062356
  contributor:
    fullname: AC Hemmert
– volume: 18
  start-page: 379
  year: 1987
  ident: 9284_CR39
  publication-title: Drug Metab Rev
  doi: 10.3109/03602538708994129
  contributor:
    fullname: FJ Leinweber
– volume: 58
  start-page: 3627
  year: 1998
  ident: 9284_CR54
  publication-title: Cancer Res
  contributor:
    fullname: PM Potter
– volume: 4
  start-page: 209
  year: 2009
  ident: 9284_CR24
  publication-title: Comp Biochem Physiol Part D Genomics Proteomics
  doi: 10.1016/j.cbd.2009.03.002
  contributor:
    fullname: RS Holmes
– volume: 21
  start-page: 173
  year: 2006
  ident: 9284_CR32
  publication-title: Drug Metab Pharmacokinet
  doi: 10.2133/dmpk.21.173
  contributor:
    fullname: T Imai
– volume: 1791
  start-page: 1133
  year: 2009
  ident: 9284_CR34
  publication-title: Biochim Biophys Acta
  doi: 10.1016/j.bbalip.2009.07.006
  contributor:
    fullname: KW Ko
– volume: 282
  start-page: 33218
  year: 2007
  ident: 9284_CR78
  publication-title: J Biol Chem
  doi: 10.1074/jbc.M706841200
  contributor:
    fullname: H Wang
– volume: 73
  start-page: 1657
  year: 2007
  ident: 9284_CR48
  publication-title: Biochem Pharmacol
  doi: 10.1016/j.bcp.2007.01.031
  contributor:
    fullname: E Mutch
– volume: 81
  start-page: 924
  year: 2007
  ident: 9284_CR70
  publication-title: Life Sci
  doi: 10.1016/j.lfs.2007.07.026
  contributor:
    fullname: M Taketani
– volume: 20
  start-page: 517
  year: 1999
  ident: 9284_CR82
  publication-title: Placenta
  contributor:
    fullname: B Yan
– volume: 42
  start-page: 1025
  year: 2001
  ident: 9284_CR8
  publication-title: J Lipid Res
  doi: 10.1016/S0022-2275(20)31590-X
  contributor:
    fullname: MA Diczfalusy
– volume: 38
  start-page: 257
  year: 1998
  ident: 9284_CR62
  publication-title: Ann Rev Pharmacol Toxicol
  doi: 10.1146/annurev.pharmtox.38.1.257
  contributor:
    fullname: T Satoh
– ident: 9284_CR76
  doi: 10.1007/s10822-010-9373-1
– volume: 22
  start-page: 424
  year: 2007
  ident: 9284_CR10
  publication-title: Trends Genet
  contributor:
    fullname: PCJ Donoghue
– volume: 151
  start-page: 1364
  year: 1988
  ident: 9284_CR16
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/S0006-291X(88)80513-8
  contributor:
    fullname: TL Genetta
– volume: 38
  start-page: 27
  year: 2009
  ident: 9284_CR25
  publication-title: J Med Primatol
  doi: 10.1111/j.1600-0684.2008.00315.x
  contributor:
    fullname: RS Holmes
– volume: 266
  start-page: 18832
  year: 1991
  ident: 9284_CR47
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)55139-5
  contributor:
    fullname: JS Munger
– volume: 8
  start-page: 2605
  year: 2002
  ident: 9284_CR81
  publication-title: Clin Cancer Res
  contributor:
    fullname: G Xu
– volume: 82–83
  start-page: 439
  year: 1995
  ident: 9284_CR102
  publication-title: Toxicol Letters
  doi: 10.1016/0378-4274(95)03493-5
  contributor:
    fullname: T Satoh
– volume: 233
  start-page: 117
  year: 1997
  ident: 9284_CR65
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.1997.6413
  contributor:
    fullname: H Schewer
– volume: 2
  start-page: 366
  year: 1993
  ident: 9284_CR7
  publication-title: Protein Sci
  doi: 10.1002/pro.5560020309
  contributor:
    fullname: M Cygler
– volume: 3
  start-page: 195
  year: 2008
  ident: 9284_CR22
  publication-title: Comp Biochem Physiol D Genomics Proteomics
  doi: 10.1016/j.cbd.2008.05.002
  contributor:
    fullname: RS Holmes
– volume: 270
  start-page: 11912
  year: 1995
  ident: 9284_CR85
  publication-title: J Biol Chem
  doi: 10.1074/jbc.270.20.11912
  contributor:
    fullname: L Zhen
– volume: 2
  start-page: 1
  year: 2000
  ident: 9284_CR17
  publication-title: Physiol Genomics
  doi: 10.1152/physiolgenomics.2000.2.1.1
  contributor:
    fullname: S Ghosh
– volume: 32
  start-page: 11606
  year: 1993
  ident: 9284_CR36
  publication-title: Biochemistry
  doi: 10.1021/bi00094a018
  contributor:
    fullname: DL Kroetz
– volume: 20
  start-page: 869
  year: 1997
  ident: 9284_CR69
  publication-title: Biol Pharm Bull
  doi: 10.1248/bpb.20.869
  contributor:
    fullname: S Takai
– volume: 18
  start-page: 911
  year: 2008
  ident: 9284_CR14
  publication-title: Pharm Genomics
  doi: 10.1097/FPC.0b013e32830b0c5e
  contributor:
    fullname: T Fukami
– volume: 307
  start-page: 1234
  year: 2003
  ident: 9284_CR33
  publication-title: J Pharmacol Exp Ther
  doi: 10.1124/jpet.103.056499
  contributor:
    fullname: T Imai
– volume: 56
  start-page: 629
  year: 2005
  ident: 9284_CR46
  publication-title: Cancer Chemother Pharmacol
  doi: 10.1007/s00280-005-1027-y
  contributor:
    fullname: CL Morton
– ident: 9284_CR73
– volume: 80
  start-page: 859
  year: 1985
  ident: 9284_CR6
  publication-title: Comp Biochem Physiol
  contributor:
    fullname: W Berning
– volume: 41
  start-page: 809
  year: 2009
  ident: 9284_CR84
  publication-title: Acta Biochim Biophys Sin
  doi: 10.1093/abbs/gmp075
  contributor:
    fullname: L Zhang
– volume: 28
  start-page: 360
  year: 2003
  ident: 9284_CR80
  publication-title: Mol Phylogenet Evol
  doi: 10.1016/S1055-7903(03)00113-1
  contributor:
    fullname: MO Woodburne
– volume: 262
  start-page: 12945
  year: 1987
  ident: 9284_CR41
  publication-title: J Biol Chem
  doi: 10.1016/S0021-9258(18)45149-6
  contributor:
    fullname: O Lockridge
– volume: 272
  start-page: 14769
  year: 1997
  ident: 9284_CR53
  publication-title: J Biol Chem
  doi: 10.1074/jbc.272.23.14769
  contributor:
    fullname: EV Pindel
– volume: 10
  start-page: 313
  year: 2005
  ident: 9284_CR55
  publication-title: Drug Discov Today
  doi: 10.1016/S1359-6446(05)03383-0
  contributor:
    fullname: MR Redinbo
– volume: 1174
  start-page: 72
  year: 1993
  ident: 9284_CR1
  publication-title: Biochim Biophys Acta
  doi: 10.1016/0167-4781(93)90093-S
  contributor:
    fullname: K Aida
– volume: 343
  start-page: 1
  year: 1999
  ident: 9284_CR38
  publication-title: Biochem J
  doi: 10.1042/bj3430001
  contributor:
    fullname: R Lehner
– volume: 13
  start-page: 1070
  year: 2006
  ident: 9284_CR45
  publication-title: Chem Biol
  doi: 10.1016/j.chembiol.2006.08.013
  contributor:
    fullname: M Miyazaki
– volume: 13
  start-page: 412
  year: 2008
  ident: 9284_CR28
  publication-title: Molecules
  doi: 10.3390/molecules13020412
  contributor:
    fullname: M Hosokawa
– volume: 51
  start-page: 298
  year: 2008
  ident: 9284_CR2
  publication-title: J Med Chem
  doi: 10.1021/jm7011479
  contributor:
    fullname: BL Barthel
– volume: 11
  start-page: 956
  year: 1991
  ident: 9284_CR52
  publication-title: Genomics
  doi: 10.1016/0888-7543(91)90020-F
  contributor:
    fullname: M Ovnic
– volume: 137
  start-page: 293
  year: 1993
  ident: 9284_CR101
  publication-title: Eur J Biochem
  doi: 10.1111/j.1432-1033.1983.tb07828.x
  contributor:
    fullname: M Robbi
– volume: 269
  start-page: 451
  year: 1990
  ident: 9284_CR58
  publication-title: Biochem J
  doi: 10.1042/bj2690451
  contributor:
    fullname: M Robbi
– volume: 1350
  start-page: 65
  year: 1997
  ident: 9284_CR37
  publication-title: Biochim Biophys Acta
  doi: 10.1016/S0167-4781(96)00142-X
  contributor:
    fullname: T Langmann
– volume: 14
  start-page: 2121
  year: 2004
  ident: 9284_CR72
  publication-title: Genome Res
  doi: 10.1101/gr.2596504
  contributor:
    fullname: The MGC Project Team
– volume: 428
  start-page: 493
  year: 2004
  ident: 9284_CR19
  publication-title: Nature
  doi: 10.1038/nature02426
  contributor:
    fullname: RA Gibbs
– volume: 370
  start-page: 101
  year: 2003
  ident: 9284_CR44
  publication-title: Biochem J
  doi: 10.1042/bj20021446
  contributor:
    fullname: M Miyazaki
– volume: 55
  start-page: 2091
  year: 2006
  ident: 9284_CR50
  publication-title: Diabetes
  doi: 10.2337/db05-0585
  contributor:
    fullname: H Okazaki
– volume: 301
  start-page: 265
  year: 1993
  ident: 9284_CR75
  publication-title: Arch Biochem Biophys
  doi: 10.1006/abbi.1993.1143
  contributor:
    fullname: HA Vanlith
– volume: 1397
  start-page: 175
  year: 1998
  ident: 9284_CR12
  publication-title: Biochim Biophys Acta
  doi: 10.1016/S0167-4781(98)00023-2
  contributor:
    fullname: P Ellingham
– volume: 10
  start-page: 349
  year: 2003
  ident: 9284_CR4
  publication-title: Nat Struct Biol
  doi: 10.1038/nsb919
  contributor:
    fullname: S Bencharit
– volume: 57
  start-page: 23
  issue: 1
  year: 2010
  ident: 9284_CR79
  publication-title: Mol Phylogenet Evol
  doi: 10.1016/j.ympev.2010.05.018
  contributor:
    fullname: ET Williams
– volume: 352
  start-page: 165
  year: 2005
  ident: 9284_CR13
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2005.07.016
  contributor:
    fullname: CD Fleming
– volume: 23
  start-page: 73
  year: 2008
  ident: 9284_CR30
  publication-title: Drug Metab Pharmacokinet
  doi: 10.2133/dmpk.23.73
  contributor:
    fullname: M Hosokawa
– volume: 17
  start-page: 76
  year: 1993
  ident: 9284_CR67
  publication-title: Genomics
  doi: 10.1006/geno.1993.1285
  contributor:
    fullname: F Shibita
– volume: 35
  start-page: 1089
  year: 2007
  ident: 9284_CR43
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.106.013862
  contributor:
    fullname: K Masaki
– volume: 1532
  start-page: 162
  year: 2001
  ident: 9284_CR9
  publication-title: Biochim Biophys Acta
  doi: 10.1016/S1388-1981(01)00133-0
  contributor:
    fullname: VW Dolinsky
– volume: 30
  start-page: 488
  year: 2002
  ident: 9284_CR64
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.30.5.488
  contributor:
    fullname: T Satoh
– volume: 416
  start-page: 101
  year: 2003
  ident: 9284_CR15
  publication-title: Arch Biochem Biophys
  doi: 10.1016/S0003-9861(03)00286-8
  contributor:
    fullname: T Furihata
– volume: 348
  start-page: 1449
  year: 2006
  ident: 9284_CR59
  publication-title: Biochem Biophys Res Commun
  doi: 10.1016/j.bbrc.2006.08.013
  contributor:
    fullname: C Ruppert
– volume: 14
  start-page: 1346
  year: 1994
  ident: 9284_CR3
  publication-title: Arterioscler Thromb
  doi: 10.1161/01.ATV.14.8.1346
  contributor:
    fullname: A Becker
– volume: 8
  start-page: 54
  year: 2008
  ident: 9284_CR23
  publication-title: BMC Evol Biol
  doi: 10.1186/1471-2148-8-54
  contributor:
    fullname: RS Holmes
– volume: 41
  start-page: 87
  year: 2003
  ident: 9284_CR49
  publication-title: Lung Cancer
  doi: 10.1016/S0169-5002(03)00223-X
  contributor:
    fullname: H Ohtsuka
– volume: 133
  start-page: 17
  year: 1983
  ident: 9284_CR77
  publication-title: Eur J Biochem
  doi: 10.1111/j.1432-1033.1983.tb07424.x
  contributor:
    fullname: G Heijne von
– volume: 84
  start-page: 661
  year: 2004
  ident: 9284_CR42
  publication-title: Genomics
  doi: 10.1016/j.ygeno.2004.07.008
  contributor:
    fullname: S Marsh
– volume: 4
  start-page: 54
  year: 2009
  ident: 9284_CR26
  publication-title: Comp Biochem Physiol
  contributor:
    fullname: RS Holmes
– volume: 363
  start-page: 201
  year: 2006
  ident: 9284_CR5
  publication-title: J Mol Biol
  doi: 10.1016/j.jmb.2006.08.025
  contributor:
    fullname: S Bencharit
– volume: 1259
  start-page: 305
  year: 1995
  ident: 9284_CR18
  publication-title: Biochim Biophys Acta
  doi: 10.1016/0005-2760(95)00184-0
  contributor:
    fullname: S Ghosh
– volume: 138
  start-page: 695
  issue: 7
  year: 2010
  ident: 9284_CR27
  publication-title: Genetica
  doi: 10.1007/s10709-010-9438-z
  contributor:
    fullname: RS Holmes
– volume: 17
  start-page: 1
  year: 2007
  ident: 9284_CR71
  publication-title: Pharm Genomics
  doi: 10.1097/01.fpc.0000230110.18957.50
  contributor:
    fullname: K Tanimoto
– volume: 16
  start-page: 984
  year: 2005
  ident: 9284_CR20
  publication-title: Mol Biol Cell
  doi: 10.1091/mbc.e04-03-0224
  contributor:
    fullname: D Gilham
– volume: 38
  start-page: D613
  year: 2010
  ident: 9284_CR56
  publication-title: Nucl Acids Res
  doi: 10.1093/nar/gkp939
  contributor:
    fullname: B Rhead
– volume: 269
  start-page: 4387
  year: 2002
  ident: 9284_CR60
  publication-title: Eur J Biochem
  doi: 10.1046/j.1432-1033.2002.03121.x
  contributor:
    fullname: SP Sanghani
– volume: 203
  start-page: 1404
  year: 1994
  ident: 9284_CR57
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.1994.2341
  contributor:
    fullname: M Robbi
– volume: 74
  start-page: 439
  year: 2006
  ident: 9284_CR11
  publication-title: Biol Reprod
  doi: 10.1095/biolreprod.105.046847
  contributor:
    fullname: H Ecroyd
– volume: 32
  start-page: 505
  year: 2004
  ident: 9284_CR61
  publication-title: Drug Metab Dispos
  doi: 10.1124/dmd.32.5.505
  contributor:
    fullname: SP Sanghani
– volume: 39
  start-page: 1
  year: 2007
  ident: 9284_CR29
  publication-title: Drug Metab Rev
  doi: 10.1080/03602530600952164
  contributor:
    fullname: M Hosokawa
– volume: 60
  start-page: 1189
  year: 2000
  ident: 9284_CR31
  publication-title: Cancer Res
  contributor:
    fullname: R Humerickhouse
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Snippet Mammalian carboxylesterase (CES or Ces) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at least...
Mammalian carboxylesterase ( CES or Ces ) genes encode enzymes that participate in xenobiotic, drug, and lipid metabolism in the body and are members of at...
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SourceType Open Access Repository
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StartPage 427
SubjectTerms Amino Acid Sequence
Animal Genetics and Genomics
Animals
Biomedical and Life Sciences
Carboxylesterase - genetics
Cell Biology
Genes
Human Genetics
Humans
Life Sciences
Mice
Multigene Family
Protein Isoforms - genetics
Pseudogenes
Rats
Sequence Homology
Terminology as Topic
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Title Recommended nomenclature for five mammalian carboxylesterase gene families: human, mouse, and rat genes and proteins
URI https://link.springer.com/article/10.1007/s00335-010-9284-4
https://www.ncbi.nlm.nih.gov/pubmed/20931200
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https://search.proquest.com/docview/762685606
https://search.proquest.com/docview/856769154
https://pubmed.ncbi.nlm.nih.gov/PMC3127206
Volume 21
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