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Volumn 1779, Issue 1, 2008, Pages 17-27

Transcriptional regulation of the human soluble epoxide hydrolase gene EPHX2

Author keywords

EPHX2; Epoxide hydrolase; Promoter; Transcription

Indexed keywords

5' FLANKING REGION; BASE SEQUENCE; CELL LINE; CHROMATIN IMMUNOPRECIPITATION; CYTOGENETICS; DNA PRIMERS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; EPOXIDE HYDROLASES; GC RICH SEQUENCE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENES, REPORTER; HUMANS; MOLECULAR SEQUENCE DATA; PLASMIDS; PROMOTER REGIONS (GENETICS); REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; TRANSCRIPTION INITIATION SITE; TRANSCRIPTION, GENETIC;

EID: 39449131197     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2007.11.005     Document Type: Article
Times cited : (31)

References (67)
  • 1
    • 0028939804 scopus 로고
    • Localization of the human soluble epoxide hydrolase gene (EPHX2) to chromosomal region 8p21-p12
    • Larsson C., White I., Johansson C., Stark A., and Meijer J. Localization of the human soluble epoxide hydrolase gene (EPHX2) to chromosomal region 8p21-p12. Hum. Genet. 95 (1995) 356-358
    • (1995) Hum. Genet. , vol.95 , pp. 356-358
    • Larsson, C.1    White, I.2    Johansson, C.3    Stark, A.4    Meijer, J.5
  • 2
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles
    • Morisseau C., and Hammock B.D. Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 311-333
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 3
    • 14644429730 scopus 로고    scopus 로고
    • Epoxide hydrolases: their roles and interactions with lipid metabolism
    • Newman J.W., Morisseau C., and Hammock B.D. Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog. Lipid Res. 44 (2005) 1-51
    • (2005) Prog. Lipid Res. , vol.44 , pp. 1-51
    • Newman, J.W.1    Morisseau, C.2    Hammock, B.D.3
  • 5
    • 0032238183 scopus 로고    scopus 로고
    • Functional role of epoxyeicosatrienoic acids and their production in astrocytes: approaches for gene transfer and therapy (review)
    • Medhora M., and Harder D. Functional role of epoxyeicosatrienoic acids and their production in astrocytes: approaches for gene transfer and therapy (review). Int. J. Mol. Med. 2 (1998) 661-669
    • (1998) Int. J. Mol. Med. , vol.2 , pp. 661-669
    • Medhora, M.1    Harder, D.2
  • 6
    • 0036080081 scopus 로고    scopus 로고
    • P-450 metabolites of arachidonic acid in the control of cardiovascular function
    • Roman R.J. P-450 metabolites of arachidonic acid in the control of cardiovascular function. Physiol. Rev. 82 (2002) 131-185
    • (2002) Physiol. Rev. , vol.82 , pp. 131-185
    • Roman, R.J.1
  • 7
    • 9944254760 scopus 로고    scopus 로고
    • Vascular protective effects of cytochrome p450 epoxygenase-derived eicosanoids
    • Spiecker M., and Liao J.K. Vascular protective effects of cytochrome p450 epoxygenase-derived eicosanoids. Arch. Biochem. Biophys. 433 (2005) 413-420
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 413-420
    • Spiecker, M.1    Liao, J.K.2
  • 8
    • 0037980428 scopus 로고    scopus 로고
    • The CYP P450 arachidonate monooxygenases: enzymatic relays for the control of kidney function and blood pressure
    • Capdevila J.H., Nakagawa K., and Holla V. The CYP P450 arachidonate monooxygenases: enzymatic relays for the control of kidney function and blood pressure. Adv. Exp. Med. Biol. 525 (2003) 39-46
    • (2003) Adv. Exp. Med. Biol. , vol.525 , pp. 39-46
    • Capdevila, J.H.1    Nakagawa, K.2    Holla, V.3
  • 9
    • 0037123925 scopus 로고    scopus 로고
    • Inhibition of vascular smooth muscle cell migration by cytochrome p450 epoxygenase-derived eicosanoids
    • Sun J., Sui X., Bradbury J.A., Zeldin D.C., Conte M.S., and Liao J.K. Inhibition of vascular smooth muscle cell migration by cytochrome p450 epoxygenase-derived eicosanoids. Circ. Res. 90 (2002) 1020-1027
    • (2002) Circ. Res. , vol.90 , pp. 1020-1027
    • Sun, J.1    Sui, X.2    Bradbury, J.A.3    Zeldin, D.C.4    Conte, M.S.5    Liao, J.K.6
  • 10
    • 0036179501 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase inhibition lowers arterial blood pressure in angiotensin II hypertension
    • Imig J.D., Zhao X., Capdevila J.H., Morisseau C., and Hammock B.D. Soluble epoxide hydrolase inhibition lowers arterial blood pressure in angiotensin II hypertension. Hypertension 39 (2002) 690-694
    • (2002) Hypertension , vol.39 , pp. 690-694
    • Imig, J.D.1    Zhao, X.2    Capdevila, J.H.3    Morisseau, C.4    Hammock, B.D.5
  • 12
    • 0033588034 scopus 로고    scopus 로고
    • Anti-inflammatory properties of cytochrome P450 epoxygenase-derived eicosanoids
    • Node K., Huo Y., Ruan X., Yang B., Spiecker M., Ley K., Zeldin D.C., and Liao J.K. Anti-inflammatory properties of cytochrome P450 epoxygenase-derived eicosanoids. Science 285 (1999) 1276-1279
    • (1999) Science , vol.285 , pp. 1276-1279
    • Node, K.1    Huo, Y.2    Ruan, X.3    Yang, B.4    Spiecker, M.5    Ley, K.6    Zeldin, D.C.7    Liao, J.K.8
  • 16
    • 33750529521 scopus 로고    scopus 로고
    • Inhibition of soluble epoxide hydrolase reduces LPS-induced thermal hyperalgesia and mechanical allodynia in a rat model of inflammatory pain
    • Inceoglu B., Jinks S.L., Schmelzer K.R., Waite T., Kim I.H., and Hammock B.D. Inhibition of soluble epoxide hydrolase reduces LPS-induced thermal hyperalgesia and mechanical allodynia in a rat model of inflammatory pain. Life Sci. 79 (2006) 2311-2319
    • (2006) Life Sci. , vol.79 , pp. 2311-2319
    • Inceoglu, B.1    Jinks, S.L.2    Schmelzer, K.R.3    Waite, T.4    Kim, I.H.5    Hammock, B.D.6
  • 18
    • 0037452577 scopus 로고    scopus 로고
    • The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity
    • Newman J.W., Morisseau C., Harris T.R., and Hammock B.D. The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 1558-1563
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 1558-1563
    • Newman, J.W.1    Morisseau, C.2    Harris, T.R.3    Hammock, B.D.4
  • 19
    • 24644432418 scopus 로고    scopus 로고
    • Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase
    • Tran K.L., Aronov P.A., Tanaka H., Newman J.W., Hammock B.D., and Morisseau C. Lipid sulfates and sulfonates are allosteric competitive inhibitors of the N-terminal phosphatase activity of the mammalian soluble epoxide hydrolase. Biochemistry 44 (2005) 12179-12187
    • (2005) Biochemistry , vol.44 , pp. 12179-12187
    • Tran, K.L.1    Aronov, P.A.2    Tanaka, H.3    Newman, J.W.4    Hammock, B.D.5    Morisseau, C.6
  • 20
    • 0020478359 scopus 로고
    • Purification of human liver cytosolic epoxide hydrolase and comparison to the microsomal enzyme
    • Wang P., Meijer J., and Guengerich F.P. Purification of human liver cytosolic epoxide hydrolase and comparison to the microsomal enzyme. Biochemistry 21 (1982) 5769-5776
    • (1982) Biochemistry , vol.21 , pp. 5769-5776
    • Wang, P.1    Meijer, J.2    Guengerich, F.P.3
  • 22
    • 0023791757 scopus 로고
    • Organ distribution of epoxide hydrolases in cytosolic and microsomal fractions of normal and nafenopin-treated male DBA/2 mice
    • Waechter F., Bentley P., Bieri F., Muakkassah-Kelly S., Staubli W., and Villermain M. Organ distribution of epoxide hydrolases in cytosolic and microsomal fractions of normal and nafenopin-treated male DBA/2 mice. Biochem. Pharmacol. 37 (1988) 3897-3903
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3897-3903
    • Waechter, F.1    Bentley, P.2    Bieri, F.3    Muakkassah-Kelly, S.4    Staubli, W.5    Villermain, M.6
  • 26
    • 0024086706 scopus 로고
    • Cytosolic epoxide hydrolase in human placenta
    • Wixtrom R.N., Silva M.H., and Hammock B.D. Cytosolic epoxide hydrolase in human placenta. Placenta 9 (1988) 559-563
    • (1988) Placenta , vol.9 , pp. 559-563
    • Wixtrom, R.N.1    Silva, M.H.2    Hammock, B.D.3
  • 27
    • 1842430562 scopus 로고    scopus 로고
    • Distribution of soluble epoxide hydrolase and of cytochrome P450 2C8, 2C9, and 2J2 in human tissues
    • Enayetallah A.E., French R.A., Thibodeau M.S., and Grant D.F. Distribution of soluble epoxide hydrolase and of cytochrome P450 2C8, 2C9, and 2J2 in human tissues. J. Histochem. Cytochem. 52 (2004) 447-454
    • (2004) J. Histochem. Cytochem. , vol.52 , pp. 447-454
    • Enayetallah, A.E.1    French, R.A.2    Thibodeau, M.S.3    Grant, D.F.4
  • 28
    • 0019318919 scopus 로고
    • Lipid epoxide hydrolase in rat lung preparations
    • Sevanian A., Stein R.A., and Mead J.F. Lipid epoxide hydrolase in rat lung preparations. Biochim. Biophys. Acta 614 (1980) 489-500
    • (1980) Biochim. Biophys. Acta , vol.614 , pp. 489-500
    • Sevanian, A.1    Stein, R.A.2    Mead, J.F.3
  • 30
    • 0024349122 scopus 로고
    • Characterization of distinct forms of cytochromes P-450, epoxide metabolizing enzymes and UDP-glucuronosyltransferases in rat skin
    • Pham M.A., Magdalou J., Totis M., Fournel-Gigleux S., Siest G., and Hammock B.D. Characterization of distinct forms of cytochromes P-450, epoxide metabolizing enzymes and UDP-glucuronosyltransferases in rat skin. Biochem. Pharmacol. 38 (1989) 2187-2194
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 2187-2194
    • Pham, M.A.1    Magdalou, J.2    Totis, M.3    Fournel-Gigleux, S.4    Siest, G.5    Hammock, B.D.6
  • 31
    • 0029150467 scopus 로고
    • Differential regulation of soluble epoxide hydrolase by clofibrate and sexual hormones in the liver and kidneys of mice
    • Pinot F., Grant D.F., Spearow J.L., Parker A.G., and Hammock B.D. Differential regulation of soluble epoxide hydrolase by clofibrate and sexual hormones in the liver and kidneys of mice. Biochem. Pharmacol. 50 (1995) 501-508
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 501-508
    • Pinot, F.1    Grant, D.F.2    Spearow, J.L.3    Parker, A.G.4    Hammock, B.D.5
  • 33
    • 0021073537 scopus 로고
    • Differential induction of cytosolic epoxide hydrolase, microsomal epoxide hydrolase, and glutathione S-transferase activities
    • Hammock B.D., and Ota K. Differential induction of cytosolic epoxide hydrolase, microsomal epoxide hydrolase, and glutathione S-transferase activities. Toxicol. Appl. Pharmacol. 71 (1983) 254-265
    • (1983) Toxicol. Appl. Pharmacol. , vol.71 , pp. 254-265
    • Hammock, B.D.1    Ota, K.2
  • 38
    • 0017332809 scopus 로고
    • Absence of HeLa cell contamination in 169 cell lines derived from human tumors
    • Fogh J., Wright W.C., and Loveless J.D. Absence of HeLa cell contamination in 169 cell lines derived from human tumors. J. Natl. Cancer Inst. 58 (1977) 209-214
    • (1977) J. Natl. Cancer Inst. , vol.58 , pp. 209-214
    • Fogh, J.1    Wright, W.C.2    Loveless, J.D.3
  • 40
    • 39449087129 scopus 로고
    • In vitro studies with HeLa cell line sensitive and resistant to actinomycin D
    • Goldstein M.N., Slotnick I.J., and Journey L.J. In vitro studies with HeLa cell line sensitive and resistant to actinomycin D. Ann. N. Y. Acad. Sci. 89 (1960) 474-483
    • (1960) Ann. N. Y. Acad. Sci. , vol.89 , pp. 474-483
    • Goldstein, M.N.1    Slotnick, I.J.2    Journey, L.J.3
  • 41
    • 0019966544 scopus 로고
    • Growth of human hepatoma cells lines with differentiated functions in chemically defined medium
    • Nakabayashi H., Taketa K., Miyano K., Yamane T., and Sato J. Growth of human hepatoma cells lines with differentiated functions in chemically defined medium. Cancer Res. 42 (1982) 3858-3863
    • (1982) Cancer Res. , vol.42 , pp. 3858-3863
    • Nakabayashi, H.1    Taketa, K.2    Miyano, K.3    Yamane, T.4    Sato, J.5
  • 42
    • 0020377792 scopus 로고
    • Comparative antiproliferative activity in vitro of natural interferons a and b for diploid and transformed human cells
    • Borden E.C., Hogan T.F., and Voelkel J.G. Comparative antiproliferative activity in vitro of natural interferons a and b for diploid and transformed human cells. Cancer Res. 42 (1982) 4948-4953
    • (1982) Cancer Res. , vol.42 , pp. 4948-4953
    • Borden, E.C.1    Hogan, T.F.2    Voelkel, J.G.3
  • 43
    • 0022492520 scopus 로고
    • Growth and metastasis of tumor cells isolated from a human renal cell carcinoma implanted into different organs of nude mice
    • Naito S., von Eschenbach A.C., Giavazzi R., and Fidler I.J. Growth and metastasis of tumor cells isolated from a human renal cell carcinoma implanted into different organs of nude mice. Cancer Res. 46 (1986) 4109-4115
    • (1986) Cancer Res. , vol.46 , pp. 4109-4115
    • Naito, S.1    von Eschenbach, A.C.2    Giavazzi, R.3    Fidler, I.J.4
  • 44
    • 0018718742 scopus 로고
    • Controlled synthesis of HBsAg in a differentiated human liver carcinoma-derived cell line
    • Aden D.P., Fogel A., Plotkin S., Damjanov I., and Knowles B.B. Controlled synthesis of HBsAg in a differentiated human liver carcinoma-derived cell line. Nature 282 (1979) 615-616
    • (1979) Nature , vol.282 , pp. 615-616
    • Aden, D.P.1    Fogel, A.2    Plotkin, S.3    Damjanov, I.4    Knowles, B.B.5
  • 45
    • 0015834582 scopus 로고
    • Isolation of high-molecular-weight DNA from mammalian cells
    • Gross-Bellard M., Oudet P., and Chambon P. Isolation of high-molecular-weight DNA from mammalian cells. Eur. J. Biochem. 36 (1973) 32-38
    • (1973) Eur. J. Biochem. , vol.36 , pp. 32-38
    • Gross-Bellard, M.1    Oudet, P.2    Chambon, P.3
  • 48
    • 0031579666 scopus 로고    scopus 로고
    • Transcription initiation from TATA-less promoters within eukaryotic protein-coding genes
    • Smale S.T. Transcription initiation from TATA-less promoters within eukaryotic protein-coding genes. Biochim. Biophys. Acta 1351 (1997) 73-88
    • (1997) Biochim. Biophys. Acta , vol.1351 , pp. 73-88
    • Smale, S.T.1
  • 49
    • 0021058853 scopus 로고
    • The promoter-specific transcription factor Sp1 binds to upstream sequences in the SV40 early promoter
    • Dynan W.S., and Tjian R. The promoter-specific transcription factor Sp1 binds to upstream sequences in the SV40 early promoter. Cell 35 (1983) 79-87
    • (1983) Cell , vol.35 , pp. 79-87
    • Dynan, W.S.1    Tjian, R.2
  • 50
    • 0023663884 scopus 로고
    • Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain
    • Kadonaga J.T., Carner K.R., Masiarz F.R., and Tjian R. Isolation of cDNA encoding transcription factor Sp1 and functional analysis of the DNA binding domain. Cell 51 (1987) 1079-1090
    • (1987) Cell , vol.51 , pp. 1079-1090
    • Kadonaga, J.T.1    Carner, K.R.2    Masiarz, F.R.3    Tjian, R.4
  • 51
    • 0000731879 scopus 로고
    • Affinity purification of sequence-specific DNA binding proteins
    • Kadonaga J.T., and Tjian R. Affinity purification of sequence-specific DNA binding proteins. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 5889-5893
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 5889-5893
    • Kadonaga, J.T.1    Tjian, R.2
  • 52
    • 0023007801 scopus 로고
    • Purification and biochemical characterization of the promoter-specific transcription factor, Sp1
    • Briggs M.R., Kadonaga J.T., Bell S.P., and Tjian R. Purification and biochemical characterization of the promoter-specific transcription factor, Sp1. Science 234 (1986) 47-52
    • (1986) Science , vol.234 , pp. 47-52
    • Briggs, M.R.1    Kadonaga, J.T.2    Bell, S.P.3    Tjian, R.4
  • 55
    • 39449123100 scopus 로고    scopus 로고
    • M.P. Hutchens, T. Nakano, J. Dunlap, R.J. Traystman, P.D. Hurn, N.J. Alkayed, Soluble epoxide hydrolase gene deletion reduces survival after cardiac arrest and cardiopulmonary resuscitation, Resuscitation (in press) (available online 28 August 2007).
  • 56
    • 0037387681 scopus 로고    scopus 로고
    • Cytochrome P450 2C9-derived epoxyeicosatrienoic acids induce angiogenesis via cross-talk with the epidermal growth factor receptor (EGFR)
    • Michaelis U.R., Fisslthaler B., Medhora M., Harder D., Fleming I., and Busse R. Cytochrome P450 2C9-derived epoxyeicosatrienoic acids induce angiogenesis via cross-talk with the epidermal growth factor receptor (EGFR). FASEB J. 17 (2003) 770-772
    • (2003) FASEB J. , vol.17 , pp. 770-772
    • Michaelis, U.R.1    Fisslthaler, B.2    Medhora, M.3    Harder, D.4    Fleming, I.5    Busse, R.6
  • 57
    • 39449097368 scopus 로고    scopus 로고
    • Distribution of soluble epoxide hydrolase, cytochrome P450 2C8, 2C9 and 2J2 in human malignant neoplasms
    • Enayetallah A.E., French R.A., and Grant D.F. Distribution of soluble epoxide hydrolase, cytochrome P450 2C8, 2C9 and 2J2 in human malignant neoplasms. J. Mol. Histol. 37 (2006) 133-141
    • (2006) J. Mol. Histol. , vol.37 , pp. 133-141
    • Enayetallah, A.E.1    French, R.A.2    Grant, D.F.3
  • 58
    • 39449131531 scopus 로고
    • Comparison of epoxide hydrases in the soluble and microsomal fractions of mammalian liver
    • Bhatnagar R.S. (Ed), Ann Arbor Science, Ann Arbor
    • Hammock B.D., Gill S.J., Mumby S.M., and Ota K. Comparison of epoxide hydrases in the soluble and microsomal fractions of mammalian liver. In: Bhatnagar R.S. (Ed). Molecular Basis of Environmental Toxicity (1980), Ann Arbor Science, Ann Arbor 229-272
    • (1980) Molecular Basis of Environmental Toxicity , pp. 229-272
    • Hammock, B.D.1    Gill, S.J.2    Mumby, S.M.3    Ota, K.4
  • 59
    • 0027056581 scopus 로고
    • A consensus DNA-binding site for the androgen receptor
    • Roche P.J., Hoare S.A., and Parker M.G. A consensus DNA-binding site for the androgen receptor. Mol. Endocrinol. 6 (1992) 2229-2235
    • (1992) Mol. Endocrinol. , vol.6 , pp. 2229-2235
    • Roche, P.J.1    Hoare, S.A.2    Parker, M.G.3
  • 60
    • 0030771852 scopus 로고    scopus 로고
    • DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. Importance of the 5′-flanking region
    • Juge-Aubry C., Pernin A., Favez T., Burger A.G., Wahli W., Meier C.A., and Desvergne B. DNA binding properties of peroxisome proliferator-activated receptor subtypes on various natural peroxisome proliferator response elements. Importance of the 5′-flanking region. J. Biol. Chem. 272 (1997) 25252-25259
    • (1997) J. Biol. Chem. , vol.272 , pp. 25252-25259
    • Juge-Aubry, C.1    Pernin, A.2    Favez, T.3    Burger, A.G.4    Wahli, W.5    Meier, C.A.6    Desvergne, B.7
  • 61
    • 0026747761 scopus 로고
    • Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA
    • Lewis J.D., Meehan R.R., Henzel W.J., Maurer-Fogy I., Jeppesen P., Klein F., and Bird A. Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA. Cell 69 (1992) 905-914
    • (1992) Cell , vol.69 , pp. 905-914
    • Lewis, J.D.1    Meehan, R.R.2    Henzel, W.J.3    Maurer-Fogy, I.4    Jeppesen, P.5    Klein, F.6    Bird, A.7
  • 62
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • Li E., Bestor T.H., and Jaenisch R. Targeted mutation of the DNA methyltransferase gene results in embryonic lethality. Cell 69 (1992) 915-926
    • (1992) Cell , vol.69 , pp. 915-926
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 64
    • 0037218919 scopus 로고    scopus 로고
    • Sp1- and Kruppel-like transcription factors
    • Kaczynski J., Cook T., and Urrutia R. Sp1- and Kruppel-like transcription factors. Genome Biol. 4 (2003) 206
    • (2003) Genome Biol. , vol.4 , pp. 206
    • Kaczynski, J.1    Cook, T.2    Urrutia, R.3
  • 65
    • 0022338074 scopus 로고
    • The regulation of cytosolic epoxide hydrolase in mice
    • Pichare M.M., and Gill S.S. The regulation of cytosolic epoxide hydrolase in mice. Biochem. Biophys. Res. Commun. 133 (1985) 233-238
    • (1985) Biochem. Biophys. Res. Commun. , vol.133 , pp. 233-238
    • Pichare, M.M.1    Gill, S.S.2
  • 66
    • 0027333030 scopus 로고
    • 14, 15-Epoxyeicosatrienoic acid metabolism in endothelial cells
    • VanRollins M., Kaduce T.L., Knapp H.R., and Spector A.A. 14, 15-Epoxyeicosatrienoic acid metabolism in endothelial cells. J. Lipid Res. 34 (1993) 1931-1942
    • (1993) J. Lipid Res. , vol.34 , pp. 1931-1942
    • VanRollins, M.1    Kaduce, T.L.2    Knapp, H.R.3    Spector, A.A.4
  • 67
    • 33344460020 scopus 로고    scopus 로고
    • Cell-specific subcellular localization of soluble epoxide hydrolase in human tissues
    • Enayetallah A.E., French R.A., Barber M., and Grant D.F. Cell-specific subcellular localization of soluble epoxide hydrolase in human tissues. J. Histochem. Cytochem. 54 (2006) 329-335
    • (2006) J. Histochem. Cytochem. , vol.54 , pp. 329-335
    • Enayetallah, A.E.1    French, R.A.2    Barber, M.3    Grant, D.F.4


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