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Volumn 4, Issue 3, 2009, Pages 209-217

A new class of mammalian carboxylesterase CES6

Author keywords

Amino acid sequence; Carboxylesterase; CES6; Drug detoxification; Genomics; Mammals

Indexed keywords

ASPARAGINE; CARBOXYLESTERASE; CARBOXYLESTERASE 1; CARBOXYLESTERASE 2; CARBOXYLESTERASE 3; CARBOXYLESTERASE 5; CARBOXYLESTERASE 6; CHOLESTEROL; GLUTAMIC ACID; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 67650224824     PISSN: 1744117X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbd.2009.03.002     Document Type: Article
Times cited : (22)

References (63)
  • 1
    • 0017187771 scopus 로고
    • Nonoxidative enzymes in the metabolism of insecticides
    • Ahmad S., and Forgash A.J. Nonoxidative enzymes in the metabolism of insecticides. Drug Metab. Rev. 5 (1976) 141-164
    • (1976) Drug Metab. Rev. , vol.5 , pp. 141-164
    • Ahmad, S.1    Forgash, A.J.2
  • 4
    • 0028167775 scopus 로고
    • Purification, cloning and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase
    • Becker A., Bottcher A., Lackner K.J., Fehringer P., Notka F., Aslandis C., and Schmitz. Purification, cloning and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. Arterioscler. Thromb. 14 (1994) 1346-1355
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 1346-1355
    • Becker, A.1    Bottcher, A.2    Lackner, K.J.3    Fehringer, P.4    Notka, F.5    Aslandis, C.6    Schmitz7
  • 6
    • 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. Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. Nat. Struct. Biol., 10 (2003) 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
  • 8
    • 67650239365 scopus 로고    scopus 로고
    • Bovine Genome Project
    • Bovine Genome Project., 2008, http://www.hgsc.bcm.tmc.edu/projects/bovine/.
    • (2008)
  • 10
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases and related proteins
    • Cygler M., Schrag J.D., Sussman J.L., Harel M., Silman I., Gentry M.K., and Dostor B.P. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases and related proteins. Protein Sci 2 (1993) 366-382
    • (1993) Protein Sci , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Dostor, B.P.7
  • 11
    • 0034948044 scopus 로고    scopus 로고
    • Characterization of enzymes involved in formation of ethyl esters of long-chain fatty acids
    • Diczfalusy M.A., Bjorkkem I., Einarsson C., Hillebrant C.G., and Alexson S.E. Characterization of enzymes involved in formation of ethyl esters of long-chain fatty acids. J Lipid Res. 42 (2001) 1025-1032
    • (2001) J Lipid Res. , vol.42 , pp. 1025-1032
    • Diczfalusy, M.A.1    Bjorkkem, I.2    Einarsson, C.3    Hillebrant, C.G.4    Alexson, S.E.5
  • 12
    • 0035967790 scopus 로고    scopus 로고
    • The cloning and expression of murine triacylglycerol hydrolase cDNA and the structure of the corresponding gene
    • Dolinsky V.W., Sipione S., Lehner R., and Vance D.E. The cloning and expression of murine triacylglycerol hydrolase cDNA and the structure of the corresponding gene. Biochim. Biophys. Acta 1532 (2001) 162-172
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 162-172
    • Dolinsky, V.W.1    Sipione, S.2    Lehner, R.3    Vance, D.E.4
  • 13
    • 31044455085 scopus 로고    scopus 로고
    • An epididymal form of cauxin, a carboxylesterase-like enzyme, is present and active in mammalian male reproductive fluids
    • Ecroyd H., Belghazi M., Dacheux J.-L., Miyazaki M., Yamashita T., and Gatti J.-L. An epididymal form of cauxin, a carboxylesterase-like enzyme, is present and active in mammalian male reproductive fluids. Biol. Reprod. 74 (2006) 439-447
    • (2006) Biol. Reprod. , vol.74 , pp. 439-447
    • Ecroyd, H.1    Belghazi, M.2    Dacheux, J.-L.3    Miyazaki, M.4    Yamashita, T.5    Gatti, J.-L.6
  • 14
    • 34248531753 scopus 로고    scopus 로고
    • Locating proteins in the cell using TargetP, SignalP and related tools
    • Emanuelsson O., Brunak S., von Heijne G., and Nielsen H. Locating proteins in the cell using TargetP, SignalP and related tools. Nat Protoc 2 (2007) 953-971
    • (2007) Nat Protoc , vol.2 , pp. 953-971
    • Emanuelsson, O.1    Brunak, S.2    von Heijne, G.3    Nielsen, H.4
  • 16
    • 0034707495 scopus 로고    scopus 로고
    • Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing and expression of full-length cDNA
    • Ghosh S. Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing and expression of full-length cDNA. Physiol. Genomics 2 (2000) 1-8
    • (2000) Physiol. Genomics , vol.2 , pp. 1-8
    • Ghosh, S.1
  • 17
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer. An environment for comparative protein modeling
    • Gue N., and Peitsch M.C. SWISS-MODEL and the Swiss-Pdb viewer. An environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Gue, N.1    Peitsch, M.C.2
  • 18
    • 0033385681 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of the prodrug oseltamivir and its active metabolite Ro 64-0802
    • He G., Massarella J., and Ward P. Clinical pharmacokinetics of the prodrug oseltamivir and its active metabolite Ro 64-0802. Clin. Pharmacokinet. 37 (1999) 471-484
    • (1999) Clin. Pharmacokinet. , vol.37 , pp. 471-484
    • He, G.1    Massarella, J.2    Ward, P.3
  • 19
    • 58549114905 scopus 로고    scopus 로고
    • Baboon carboxylesterases 1 and 2: sequences, structures and phylogenetics relationships with human and other primate carboxylesterases
    • Holmes R.S., Glenn J.P., Vandeberg J.L., and Cox L.A. Baboon carboxylesterases 1 and 2: sequences, structures and phylogenetics relationships with human and other primate carboxylesterases. J. Med. Primatol. 38 (2009) 27-38
    • (2009) J. Med. Primatol. , vol.38 , pp. 27-38
    • Holmes, R.S.1    Glenn, J.P.2    Vandeberg, J.L.3    Cox, L.A.4
  • 20
    • 48049114394 scopus 로고    scopus 로고
    • Mammalian carboxylesterase 5: comparative biochemistry and genomics
    • Holmes R.S., Cox L.A., and VandeBerg J.L. Mammalian carboxylesterase 5: comparative biochemistry and genomics. Com. Biochem. Physiol. Part D 3 (2008) 195-204
    • (2008) Com. Biochem. Physiol. Part D , vol.3 , pp. 195-204
    • Holmes, R.S.1    Cox, L.A.2    VandeBerg, J.L.3
  • 21
    • 40749112803 scopus 로고    scopus 로고
    • Opossum carboxylesterases: sequences, phylogeny and evidence for CES duplication events predating the marsupial-eutherian common ancestor
    • Holmes R.S., Chan J., Cox L.A., Murphy W.M., and VandeBerg J.L. Opossum carboxylesterases: sequences, phylogeny and evidence for CES duplication events predating the marsupial-eutherian common ancestor. BMC Evol. Biol. 8 (2008) 54
    • (2008) BMC Evol. Biol. , vol.8 , pp. 54
    • Holmes, R.S.1    Chan, J.2    Cox, L.A.3    Murphy, W.M.4    VandeBerg, J.L.5
  • 23
    • 0034162687 scopus 로고    scopus 로고
    • Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms h-CE1 and hCE-2
    • Humerickhouse R., Lohrbach K., Li L., Bosron W.F., and Dolan M.E. Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms h-CE1 and hCE-2. Cancer Res. 60 (2000) 1189-1192
    • (2000) Cancer Res. , vol.60 , pp. 1189-1192
    • Humerickhouse, R.1    Lohrbach, K.2    Li, L.3    Bosron, W.F.4    Dolan, M.E.5
  • 24
    • 33749030999 scopus 로고    scopus 로고
    • Human carboxylesterase isozymes: catalytic properties and rational drug design
    • Imai T. Human carboxylesterase isozymes: catalytic properties and rational drug design. Drug Metab. Pharmacogenet. 21 (2006) 173-185
    • (2006) Drug Metab. Pharmacogenet. , vol.21 , pp. 173-185
    • Imai, T.1
  • 25
    • 0344304751 scopus 로고    scopus 로고
    • Evidence for the involvement of a pulmonary first-pass effect via carboxylesterase in the disposition of a propanolol ester derivative after intravenous administration
    • Imai T., Yoshigae Y., Hosokawa M., Chiba K., and Oragiri M. Evidence for the involvement of a pulmonary first-pass effect via carboxylesterase in the disposition of a propanolol ester derivative after intravenous administration. J. Pharmacol. Exp. Ther. 307 (2003) 1234-1242
    • (2003) J. Pharmacol. Exp. Ther. , vol.307 , pp. 1234-1242
    • Imai, T.1    Yoshigae, Y.2    Hosokawa, M.3    Chiba, K.4    Oragiri, M.5
  • 27
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL repository of three dimensional protein structure homology models
    • Kopp J., and Schwede T. The SWISS-MODEL repository of three dimensional protein structure homology models. Nucleic Acids Res. 32 (2004) D230-D234
    • (2004) Nucleic Acids Res. , vol.32
    • Kopp, J.1    Schwede, T.2
  • 29
    • 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. Glycosylation-dependent activity of Baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry 32 (1993) 11606-11617
    • (1993) Biochemistry , vol.32 , pp. 11606-11617
    • Kroetz, D.L.1    McBride, O.W.2    Gonzalez, F.J.3
  • 32
    • 0023614883 scopus 로고
    • Possible physiological roles of carboxyl ester hydrolases
    • Leinweber F.J. Possible physiological roles of carboxyl ester hydrolases. Drug Metab. Rev. 18 (1987) 379-439
    • (1987) Drug Metab. Rev. , vol.18 , pp. 379-439
    • Leinweber, F.J.1
  • 33
    • 0023489795 scopus 로고
    • Location of disulfide bonds within the sequence of human serum cholinesterase
    • Lockridge O., Adkins S., and La Due B.N. Location of disulfide bonds within the sequence of human serum cholinesterase. J. Biol. Chem. 262 (1987) 12945-12952
    • (1987) J. Biol. Chem. , vol.262 , pp. 12945-12952
    • Lockridge, O.1    Adkins, S.2    La Due, B.N.3
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L.J., Bryson K., and Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics 16 (2000) 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 36
    • 0037442521 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel carboxylesterase-like protein that is physiologically present at high concentrations in the urine of domestic cats (Felis catus)
    • Miyazaki M., Kamiie K., Soeta S., Taira H., and Yamashita T. Molecular cloning and characterization of a novel carboxylesterase-like protein that is physiologically present at high concentrations in the urine of domestic cats (Felis catus). Biochem. J. 370 (2003) 101-110
    • (2003) Biochem. J. , vol.370 , pp. 101-110
    • Miyazaki, M.1    Kamiie, K.2    Soeta, S.3    Taira, H.4    Yamashita, T.5
  • 37
    • 33749660434 scopus 로고    scopus 로고
    • A major urinary protein of the domestic cat regulates the production the production of felinine, a putative pheromone precursor
    • Miyazaki M., Yamashita T., Suzuki Y., Saito Y., Soeta S., Taira H., and Suzuki A. A major urinary protein of the domestic cat regulates the production the production of felinine, a putative pheromone precursor. Chem. Biol. 13 (2006) 10171-10179
    • (2006) Chem. Biol. , vol.13 , pp. 10171-10179
    • Miyazaki, M.1    Yamashita, T.2    Suzuki, Y.3    Saito, Y.4    Soeta, S.5    Taira, H.6    Suzuki, A.7
  • 38
    • 1542563409 scopus 로고    scopus 로고
    • Initial sequencing and comparative analysis of the mouse genome
    • Mouse Sequencing Consortium. Initial sequencing and comparative analysis of the mouse genome. Nature 420 (2002) 520-562
    • (2002) Nature , vol.420 , pp. 520-562
    • Mouse Sequencing Consortium1
  • 39
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S., and Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48 (1987) 899-907
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 41
    • 0037829150 scopus 로고    scopus 로고
    • Intracellular conversion of irinotecan to its active form, SN-38, by native carboxylesterase in human non-small cell lung cancer
    • Ohtsuka K., Inoue S., Kameyama M., Kanetoshi A., Toru F., Kazuo T., Yoshikazu A., and Akira S. Intracellular conversion of irinotecan to its active form, SN-38, by native carboxylesterase in human non-small cell lung cancer. Lung Cancer 41 (2003) 187-198
    • (2003) Lung Cancer , vol.41 , pp. 187-198
    • Ohtsuka, K.1    Inoue, S.2    Kameyama, M.3    Kanetoshi, A.4    Toru, F.5    Kazuo, T.6    Yoshikazu, A.7    Akira, S.8
  • 42
    • 0024380746 scopus 로고
    • Isolation, properties, and the complete amino acid sequence of a second form of 60-kDa glycoprotein esterase. Orientation of the 60-kDa proteins in the microsomal membrane
    • Ozols J. Isolation, properties, and the complete amino acid sequence of a second form of 60-kDa glycoprotein esterase. Orientation of the 60-kDa proteins in the microsomal membrane. J. Biol. Chem. 264 (1989) 12533-12545
    • (1989) J. Biol. Chem. , vol.264 , pp. 12533-12545
    • Ozols, J.1
  • 43
    • 0029004590 scopus 로고
    • Protein modeling by E-mail
    • Peitsch M.C. Protein modeling by E-mail. Biotechnology 13 (1995) 658-660
    • (1995) Biotechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 44
    • 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 A., Dean R.A., and Bosron W.F. Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J. Biol. Chem. 272 (1997) 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, A.5    Dean, R.A.6    Bosron, W.F.7
  • 45
    • 1842684068 scopus 로고    scopus 로고
    • Genome sequence of the brown Norway rat yields insights into mammalian evolution
    • Rat Genome Sequencing Project Consortium. Genome sequence of the brown Norway rat yields insights into mammalian evolution. Nature 428 (2004) 493-521
    • (2004) Nature , vol.428 , pp. 493-521
    • Rat Genome Sequencing Project Consortium1
  • 46
    • 14644422580 scopus 로고    scopus 로고
    • Mammalian carboxylesterases: from drug targets to protein therapeutics
    • Redinbo M.R., and Potter P.N. Mammalian carboxylesterases: from drug targets to protein therapeutics. Drug Discov. Today 10 (2005) 313-320
    • (2005) Drug Discov. Today , vol.10 , pp. 313-320
    • Redinbo, M.R.1    Potter, P.N.2
  • 47
    • 0025757377 scopus 로고
    • The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum
    • Robbi M., and Beaufay H. The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum. J. Biol. Chem. 266 (1983) 20498-20503
    • (1983) J. Biol. Chem. , vol.266 , pp. 20498-20503
    • Robbi, M.1    Beaufay, H.2
  • 48
  • 49
    • 2042544103 scopus 로고    scopus 로고
    • 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
    • Sanghani S.P., Quinney S.K., Fredenberg T.B., Davis W.I., Murry D.J., and Bosron W.F. 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. Drug Metab. Dispos. 32 (2004) 505-511
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 505-511
    • Sanghani, S.P.1    Quinney, S.K.2    Fredenberg, T.B.3    Davis, W.I.4    Murry, D.J.5    Bosron, W.F.6
  • 50
    • 0031800635 scopus 로고    scopus 로고
    • The mammalian carboxylesterases: from molecules to functions
    • Satoh T., and Hosokawa M. The mammalian carboxylesterases: from molecules to functions. Annu. Rev. Pharmacol. Toxicol. 38 (1998) 257-288
    • (1998) Annu. Rev. Pharmacol. Toxicol. , vol.38 , pp. 257-288
    • Satoh, T.1    Hosokawa, M.2
  • 52
    • 0031557664 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver
    • Schewer H., Langmann T., Daig R., Becker A., Aslandis C., and Schmitz G. Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver. Biochem. Biophys. Res. Commun. 233 (1997) 117-120
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 117-120
    • Schewer, H.1    Langmann, T.2    Daig, R.3    Becker, A.4    Aslandis, C.5    Schmitz, G.6
  • 53
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 54
    • 0027265572 scopus 로고
    • Molecular cloning and characterization of a human carboxylesterase gene
    • Shibita F., Takagi Y., Kitajima M., Kuroda T., and Omura T. Molecular cloning and characterization of a human carboxylesterase gene. Genomics 17 (1993) 76-82
    • (1993) Genomics , vol.17 , pp. 76-82
    • Shibita, F.1    Takagi, Y.2    Kitajima, M.3    Kuroda, T.4    Omura, T.5
  • 55
    • 4644368419 scopus 로고    scopus 로고
    • Identification of the cytosolic carboxylesterase catalyzing the 5'-deoxy-5-fluorocytidine formation from capecitabine in human liver
    • Tabata T., Katoh M., Tokudome S., Nakajima M., and Yokoi T. Identification of the cytosolic carboxylesterase catalyzing the 5'-deoxy-5-fluorocytidine formation from capecitabine in human liver. Drug Metab. Dispos. 32 (2004) 1103-1110
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1103-1110
    • Tabata, T.1    Katoh, M.2    Tokudome, S.3    Nakajima, M.4    Yokoi, T.5
  • 57
    • 33748486517 scopus 로고    scopus 로고
    • AceView: A comprehensive cDNA-supported gene and transcripts annotation
    • Thierry-Mieg D., and Thierry-Mieg J. AceView: A comprehensive cDNA-supported gene and transcripts annotation. Genome Biol. 7 (2006) S12
    • (2006) Genome Biol. , vol.7
    • Thierry-Mieg, D.1    Thierry-Mieg, J.2
  • 58
    • 39549101237 scopus 로고    scopus 로고
    • Large scale identification of human genes implicated in eepidermal barrier function
    • Toulza E., de Daruvar N.R., Wincker P., Serre G., and Guerrin M. Large scale identification of human genes implicated in eepidermal barrier function. Genome Biol. 8 (2007) R107
    • (2007) Genome Biol. , vol.8
    • Toulza, E.1    de Daruvar, N.R.2    Wincker, P.3    Serre, G.4    Guerrin, M.5
  • 59
    • 0027453736 scopus 로고
    • Palmitoyl-coenzyme A hydrolyzing activity in rat kidney and its relationship with carboxylesterase
    • Tsujita T., and Okuda H. Palmitoyl-coenzyme A hydrolyzing activity in rat kidney and its relationship with carboxylesterase. J. Lipid Res. 34 (1993) 1773-1781
    • (1993) J. Lipid Res. , vol.34 , pp. 1773-1781
    • Tsujita, T.1    Okuda, H.2
  • 60
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur. J. Biochem. 133 (1983) 17-21
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • von Heijne, G.1
  • 61
    • 36349017062 scopus 로고    scopus 로고
    • Proteomic and lipid characterization of apo-lipoprotein B-free luminal lipid droplets from mouse liver microsomes: implications for very low density lipoprotein assembly
    • Wang H., Gilham D., and Lehner R. Proteomic and lipid characterization of apo-lipoprotein B-free luminal lipid droplets from mouse liver microsomes: implications for very low density lipoprotein assembly. J. Biol. Chem. 282 (2007) 33218-33226
    • (2007) J. Biol. Chem. , vol.282 , pp. 33218-33226
    • Wang, H.1    Gilham, D.2    Lehner, R.3
  • 62
    • 0141609681 scopus 로고    scopus 로고
    • The evolution of tribospheny and the antiquity of mammalian clades
    • Woodburne M.O., Rich T.H., and Springer M.S. The evolution of tribospheny and the antiquity of mammalian clades. Mol. Phylogenet. Evol. 28 (2003) 360-385
    • (2003) Mol. Phylogenet. Evol. , vol.28 , pp. 360-385
    • Woodburne, M.O.1    Rich, T.H.2    Springer, M.S.3
  • 63
    • 0028977992 scopus 로고
    • The beta-glucuronidase propeptide contains a serpin-related octamer necessary for complex formation with egasyn esterase and for retention within the endoplasmic reticulum
    • Zhen L., Rusiniak M.E., and Swank R.T. The beta-glucuronidase propeptide contains a serpin-related octamer necessary for complex formation with egasyn esterase and for retention within the endoplasmic reticulum. J. Biol. Chem. 270 (1995) 11912-11920
    • (1995) J. Biol. Chem. , vol.270 , pp. 11912-11920
    • Zhen, L.1    Rusiniak, M.E.2    Swank, R.T.3


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