메뉴 건너뛰기




Volumn 109-111, Issue , 2014, Pages 14-22

Why do a wide variety of animals retain multiple isoforms of cyclooxygenase?

Author keywords

Animal kingdom; Cyclooxygenase; Evolution; Genome duplication; Prostanoids

Indexed keywords

ARACHIDONIC ACID; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; OXYGENASE; PEROXIDASE; PHOSPHOLIPASE A2; PROSTAGLANDIN SYNTHASE; PROSTANOID; ISOENZYME;

EID: 84901620287     PISSN: 10988823     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.prostaglandins.2014.03.002     Document Type: Review
Times cited : (12)

References (86)
  • 1
    • 0038107709 scopus 로고    scopus 로고
    • Production of eicosanoids and other oxylipins by pathogenic eukaryotic microbes
    • DOI 10.1128/CMR.16.3.517-533.2003
    • M.C. Noverr, J.R. Erb-Downward, and G.B. Huffnagle Production of eicosanoids and other oxylipins by pathogenic eukaryotic microbes Clin Microbiol Rev 16 2003 517 533 http://www.ncbi.nlm.nih.gov/pubmed/12857780 http://cmr.asm.org/content/16/3/517.full.pdf (Pubitemid 36871319)
    • (2003) Clinical Microbiology Reviews , vol.16 , Issue.3 , pp. 517-533
    • Noverr, M.C.1    Erb-Downward, J.R.2    Huffnagle, G.B.3
  • 2
    • 0033708105 scopus 로고    scopus 로고
    • Molecular evolution of the myeloperoxidase family
    • H. Daiyasu, and H. Toh Molecular evolution of the myeloperoxidase family J Mol Evol 51 2000 433 445 http://www.ncbi.nlm.nih.gov/pubmed/11080366
    • (2000) J Mol Evol , vol.51 , pp. 433-445
    • Daiyasu, H.1    Toh, H.2
  • 3
    • 0345686711 scopus 로고    scopus 로고
    • Identification and characterization of a cyclooxygenase-like enzyme from Entamoeba histolytica
    • DOI 10.1073/pnas.1835863100
    • I. Dey, K. Keller, A. Belley, and K. Chadee Identification and characterization of a cyclooxygenase-like enzyme from Entamoeba histolytica Proc Natl Acad Sci U S A 100 2003 13561 13566 10.1073/pnas.1835863100 http://www.ncbi.nlm.nih.gov/pubmed/14585927 http://www.pnas.org/content/100/23/ 13561.full.pdf (Pubitemid 37444781)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.23 , pp. 13561-13566
    • Dey, I.1    Keller, K.2    Belley, A.3    Chadee, K.4
  • 4
    • 46449130668 scopus 로고    scopus 로고
    • The peroxidase-cyclooxygenase superfamily: Reconstructed evolution of critical enzymes of the innate immune system
    • DOI 10.1002/prot.21950
    • M. Zamocky, C. Jakopitsch, P.G. Furtmüller, C. Dunand, and C. Obinger The peroxidase-cyclooxygenase superfamily: reconstructed evolution of critical enzymes of the innate immune system Proteins 72 2008 589 605 10.1002/prot.21950 http://www.ncbi.nlm.nih.gov/pubmed/18247411 http://onlinelibrary.wiley.com/store/10.1002/prot.21950/asset/21950-ftp.pdf?v= 1&t=hs2jd0xm&s=98a6c75c2602467b2c9ce3f17765c71a4b9f05d3 (Pubitemid 351928514)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.2 , pp. 589-605
    • Zamocky, M.1    Jakopitsch, C.2    Furtmuller, P.G.3    Dunand, C.4    Obinger, C.5
  • 5
    • 0028009093 scopus 로고
    • 2 synthase-1
    • DOI 10.1038/367243a0
    • 2 synthase-1 Nature 367 1994 243 249 10.1038/367243a0 http://www.ncbi.nlm.nih.gov/pubmed/8121489 http://www.nature.com/nature/journal/v367/n6460/abs/367243a0.html (Pubitemid 24051139)
    • (1994) Nature , vol.367 , Issue.6460 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 6
    • 0028913379 scopus 로고
    • Localization of prostaglandin endoperoxide synthase-1 to the endoplasmic reticulum and nuclear envelope is independent of its C-terminal tetrapeptide-PTEL
    • 10.1006/abbi.1995.1188 http://ac.els-cdn.com/S0003986185711885/1-s2.0- S0003986185711885-main.pdf?-tid=ecd84468-9923-11e3-9ea2-00000aacb360&acdnat= 1392786712-30e80af11a4a04f4a2b0358ac773aa36
    • M.K. Regier, J.C. Otto, D.L. DeWitt, and W.L. Smith Localization of prostaglandin endoperoxide synthase-1 to the endoplasmic reticulum and nuclear envelope is independent of its C-terminal tetrapeptide-PTEL Arch Biochem Biophys 317 1995 457 463 10.1006/abbi.1995.1188 http://www.ncbi.nlm.nih.gov/pubmed/ 7893163 http://ac.els-cdn.com/S0003986185711885/1-s2.0-S0003986185711885-main. pdf?-tid=ecd84468-9923-11e3-9ea2-00000aacb360&acdnat=1392786712- 30e80af11a4a04f4a2b0358ac773aa36
    • (1995) Arch Biochem Biophys , vol.317 , pp. 457-463
    • Regier, M.K.1    Otto, J.C.2    Dewitt, D.L.3    Smith, W.L.4
  • 7
    • 0032701224 scopus 로고    scopus 로고
    • The cyclooxygenase isoforms: Structural insights into the conversion of arachidonic acid to prostaglandins
    • DOI 10.1016/S1388-1981(99)00147-X, PII S138819819900147X
    • R.M. Garavito, and D.L. DeWitt The cyclooxygenase isoforms: structural insights into the conversion of arachidonic acid to prostaglandins Biochim Biophys Acta 1441 1999 278 287 http://www.ncbi.nlm.nih.gov/pubmed/10570255 (Pubitemid 29537747)
    • (1999) Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids , vol.1441 , Issue.2-3 , pp. 278-287
    • Garavito, R.M.1    Dewitt, D.L.2
  • 8
    • 0030479496 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2
    • DOI 10.1074/jbc.271.52.33157
    • W.L. Smith, R.M. Garavito, and D.L. DeWitt Prostaglandin endoperoxide H synthases (cyclooxygenases)-1 and -2 J Biol Chem 271 1996 33157 33160 http://www.ncbi.nlm.nih.gov/pubmed/8969167 http://www.jbc.org/content/271/52/ 33157.full.pdf (Pubitemid 27010118)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.52 , pp. 33157-33160
    • Smith, W.L.1    Garavito, R.M.2    DeWitt, D.L.3
  • 9
    • 0001299961 scopus 로고
    • Acetylation of prostaglandin synthase by aspirin
    • http://www.pnas.org/content/72/8/3073.full.pdf
    • G.J. Roth, N. Stanford, and P.W. Majerus Acetylation of prostaglandin synthase by aspirin Proc Natl Acad Sci U S A 72 1975 3073 3076 http://www.ncbi.nlm.nih.gov/pubmed/810797 http://www.pnas.org/content/72/8/3073. full.pdf
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 3073-3076
    • Roth, G.J.1    Stanford, N.2    Majerus, P.W.3
  • 10
    • 0023968630 scopus 로고
    • Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence
    • http://www.pnas.org/content/85/5/1412.full.pdf
    • D.L. DeWitt, and W.L. Smith Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence Proc Natl Acad Sci U S A 85 1988 1412 1416 http://www.ncbi.nlm.nih.gov/ pubmed/3125548 http://www.pnas.org/content/85/5/1412.full.pdf
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 1412-1416
    • Dewitt, D.L.1    Smith, W.L.2
  • 11
    • 0017070560 scopus 로고
    • Purification of prostaglandin endoperoxide synthase from bovine vesicular gland microsomes
    • T. Miyamoto, N. Ogino, S. Yamamoto, and O. Hayaishi Purification of prostaglandin endoperoxide synthase from bovine vesicular gland microsomes J Biol Chem 251 1976 2629 2636 http://www.ncbi.nlm.nih.gov/pubmed/816795
    • (1976) J Biol Chem , vol.251 , pp. 2629-2636
    • Miyamoto, T.1    Ogino, N.2    Yamamoto, S.3    Hayaishi, O.4
  • 12
    • 27544510764 scopus 로고    scopus 로고
    • Cellular and molecular biology of prostacyclin synthase
    • DOI 10.1016/j.bbrc.2005.08.021, PII S0006291X05017109
    • K.K. Wu, and J.Y. Liou Cellular and molecular biology of prostacyclin synthase Biochem Biophys Res Commun 338 2005 45 52 10.1016/j.bbrc.2005.08.021 http://www.ncbi.nlm.nih.gov/pubmed/16115610 http://ac.els-cdn.com/ S0006291X05017109/1-s2.0-S0006291X05017109-main.pdf?-tid=07ad22e0-9924-11e3- 9532-00000aacb362&acdnat=1392786757-ba12b7cf0d7601a6149d437f76662613 (Pubitemid 41540535)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 45-52
    • Wu, K.K.1    Liou, J.-Y.2
  • 13
    • 0036669427 scopus 로고    scopus 로고
    • Thromboxane synthase: Structure and function of protein and gene
    • DOI 10.1016/S0090-6980(02)00045-X, PII S009069800200045X
    • L.H. Wang, and R.J. Kulmacz Thromboxane synthase: structure and function of protein and gene Prostaglandins Other Lipid Mediat 68-69 2002 409 422 http://www.ncbi.nlm.nih.gov/pubmed/12432933 (Pubitemid 35247411)
    • (2002) Prostaglandins and Other Lipid Mediators , vol.68-69 , pp. 409-422
    • Wang, L.-H.1    Kulmacz, R.J.2
  • 14
    • 0036669560 scopus 로고    scopus 로고
    • Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence
    • DOI 10.1016/S0090-6980(02)00042-4, PII S0090698002000424
    • Y. Urade, and N. Eguchi Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence Prostaglandins Other Lipid Mediat 68-69 2002 375 382 http://www.ncbi.nlm.nih.gov/pubmed/12432930 (Pubitemid 35247408)
    • (2002) Prostaglandins and Other Lipid Mediators , vol.68-69 , pp. 375-382
    • Urade, Y.1    Eguchi, N.2
  • 16
    • 82955194895 scopus 로고    scopus 로고
    • 2)
    • 10.1093/jb/mvr116 http://jb.oxfordjournals.org/content/150/6/593.full.pdf
    • 2) J Biochem 150 2011 593 596 10.1093/jb/mvr116 http://www.ncbi.nlm.nih.gov/pubmed/21926128 http://jb.oxfordjournals.org/ content/150/6/593.full.pdf
    • (2011) J Biochem , vol.150 , pp. 593-596
    • Watanabe, K.1
  • 17
    • 1942502821 scopus 로고    scopus 로고
    • Prostanoids and prostanoid receptors in signal transduction
    • DOI 10.1016/j.biocel.2003.08.006, PII S1357272503002966
    • C.L. Bos, D.J. Richel, T. Ritsema, M.P. Peppelenbosch, and H.H. Versteeg Prostanoids and prostanoid receptors in signal transduction Int J Biochem Cell Biol 36 2004 1187 1205 10.1016/j.biocel.2003.08.006 http://www.ncbi.nlm.nih.gov/ pubmed/15109566 http://ac.els-cdn.com/S1357272503002966/1-s2.0- S1357272503002966-main.pdf?-tid=c9b065f6-9923-11e3-852f-00000aacb361&acdnat= 1392786653-41763da1c29b37213de9c8b1495d3189 (Pubitemid 38515660)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.7 , pp. 1187-1205
    • Bos, C.L.1    Richel, D.J.2    Ritsema, T.3    Peppelenbosch, M.P.4    Versteeg, H.H.5
  • 21
    • 0034971264 scopus 로고    scopus 로고
    • Why there are two cyclooxygenase isozymes
    • W.L. Smith, and R. Langenbach Why there are two cyclooxygenase isozymes J Clin Invest 107 2001 1491 1495 10.1172/JCI13271 http://www.ncbi.nlm.nih.gov/ pubmed/11413152 http://www.jci.org/articles/view/13271 (Pubitemid 32574631)
    • (2001) Journal of Clinical Investigation , vol.107 , Issue.12 , pp. 1491-1495
    • Smith, W.L.1    Langenbach, R.2
  • 22
    • 0036724038 scopus 로고    scopus 로고
    • Cyclooxygenase cloning in dogfish shark. Squalus acanthias, and its role in rectal gland Cl secretion
    • 10.1152/ajpregu.00743.2001 http://ajpregu.physiology.org/content/ajpregu/ 283/3/R631.full.pdf
    • T. Yang, S.J. Forrest, and N. Stine et al. Cyclooxygenase cloning in dogfish shark. Squalus acanthias, and its role in rectal gland Cl secretion Am J Physiol Regul Integr Comp Physiol 283 2002 R631 R637 10.1152/ajpregu.00743.2001 http://www.ncbi.nlm.nih.gov/pubmed/12184997 http://ajpregu.physiology.org/ content/ajpregu/283/3/R631.full.pdf
    • (2002) Am J Physiol Regul Integr Comp Physiol , vol.283
    • Yang, T.1    Forrest, S.J.2    Stine, N.3
  • 23
    • 0015528236 scopus 로고
    • Prostaglandin controls neuromuscular transmission in guinea-pig vas deferens
    • P. Hedqvist, and U.S. von Euler Prostaglandin controls neuromuscular transmission in guinea-pig vas deferens Nat: New Biol 236 1972 113 115 http://www.ncbi.nlm.nih.gov/pubmed/4337119
    • (1972) Nat: New Biol , vol.236 , pp. 113-115
    • Hedqvist, P.1    Von Euler, U.S.2
  • 24
    • 0027976623 scopus 로고
    • 2-mediated amplification mechanism in thrombin-induced rabbit platelet activation
    • 2-mediated amplification mechanism in thrombin-induced rabbit platelet activation Platelets 5 1994 20 28 10.3109/09537109409006037 http://www.ncbi.nlm.nih.gov/pubmed/ 21043740 http://informahealthcare.com/doi/abs/10.3109/09537109409006037 (Pubitemid 24044415)
    • (1994) Platelets , vol.5 , Issue.1 , pp. 20-28
    • Kawamura, M.1    Huang, A.2    Harada, Y.3    Katori, M.4
  • 25
    • 0015890986 scopus 로고
    • Prostaglandins as potentiators of increased vascular permeability in inflammation
    • T.J. Williams, and J. Morley Prostaglandins as potentiators of increased vascular permeability in inflammation Nature 246 1973 215 217 http://www.ncbi.nlm.nih.gov/pubmed/4271544
    • (1973) Nature , vol.246 , pp. 215-217
    • Williams, T.J.1    Morley, J.2
  • 26
    • 0017770145 scopus 로고
    • Role of prostaglandin-mediated vasodilatation in inflammation
    • T.J. Williams, and M.J. Peck Role of prostaglandin-mediated vasodilatation in inflammation Nature 270 1977 530 532 http://www.ncbi.nlm.nih. gov/pubmed/593374
    • (1977) Nature , vol.270 , pp. 530-532
    • Williams, T.J.1    Peck, M.J.2
  • 27
    • 0018332385 scopus 로고
    • 2 and the vascular changes of inflammation
    • 2 and the vascular changes of inflammation Br J Pharmacol 65 1979 517 524 http://www.ncbi.nlm.nih.gov/pubmed/371730 (Pubitemid 9119649)
    • (1979) British Journal of Pharmacology , vol.65 , Issue.3 , pp. 517-524
    • Williams, T.J.1
  • 29
    • 0022854091 scopus 로고
    • Potentiation of bradykinin-induced nociceptive response by arachidonate metabolites in dogs
    • Y. Hori, M. Katori, Y. Harada, Y. Uchida, and K. Tanaka Potentiation of bradykinin-induced nociceptive response by arachidonate metabolites in dogs Eur J Pharmacol 132 1986 47 52 http://www.ncbi.nlm.nih.gov/pubmed/3028834 (Pubitemid 17229968)
    • (1986) European Journal of Pharmacology , vol.132 , Issue.1 , pp. 47-52
    • Hori, Y.1    Katori, M.2    Harada, Y.3
  • 30
    • 84861875788 scopus 로고    scopus 로고
    • Prostaglandins and chronic inflammation
    • 10.1016/j.tips.2012.02.004 http://ac.els-cdn.com/S0165614712000302/1-s2. 0-S0165614712000302-main.pdf?-tid=9ad616a4-3d3e-11e3-828b- 00000aacb35f&acdnat=1382682664-1b9a21005d8f6e1b9afb77ee3a11fc8d
    • T. Aoki, and S. Narumiya Prostaglandins and chronic inflammation Trends Pharmacol Sci 33 2012 304 311 10.1016/j.tips.2012.02.004 http://www.ncbi.nlm. nih.gov/pubmed/22464140 http://ac.els-cdn.com/S0165614712000302/1-s2.0- S0165614712000302-main.pdf?-tid=9ad616a4-3d3e-11e3-828b-00000aacb35f&acdnat= 1382682664-1b9a21005d8f6e1b9afb77ee3a11fc8d
    • (2012) Trends Pharmacol Sci , vol.33 , pp. 304-311
    • Aoki, T.1    Narumiya, S.2
  • 31
    • 0023855416 scopus 로고
    • Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)
    • J.P. Merlie, D. Fagan, J. Mudd, and P. Needleman Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase) J Biol Chem 263 1988 3550 3553 http://www.ncbi.nlm.nih.gov/pubmed/2831188 (Pubitemid 18078940)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.8 , pp. 3550-3553
    • Merlie, J.P.1    Fagan, D.2    Mudd, J.3    Needleman, P.4
  • 32
    • 0023915232 scopus 로고
    • Primary structure of sheep prostaglandin endoperoxide synthase deduced from cDNA sequence
    • http://ac.els-cdn.com/0014579388808470/1-s2.0-0014579388808470-main.pdf? -tid=9985e5da-3d3f-11e3-8c18-00000aacb35f&acdnat=1382683092- e125bab169b7cb7ba4ca7046ba1b9142
    • C. Yokoyama, T. Takai, and T. Tanabe Primary structure of sheep prostaglandin endoperoxide synthase deduced from cDNA sequence FEBS Lett 231 1988 347 351 http://www.ncbi.nlm.nih.gov/pubmed/3129310 http://ac.els-cdn.com/ 0014579388808470/1-s2.0-0014579388808470-main.pdf?-tid=9985e5da-3d3f-11e3-8c18- 00000aacb35f&acdnat=1382683092-e125bab169b7cb7ba4ca7046ba1b9142
    • (1988) FEBS Lett , vol.231 , pp. 347-351
    • Yokoyama, C.1    Takai, T.2    Tanabe, T.3
  • 33
    • 0027469850 scopus 로고
    • Expression of the protein product of the prostaglandin synthase-2/TIS10 gene in mitogen-stimulated Swiss 3T3 cells
    • D.A. Kujubu, S.T. Reddy, B.S. Fletcher, and H.R. Herschman Expression of the protein product of the prostaglandin synthase-2/TIS10 gene in mitogen-stimulated Swiss 3T3 cells J Biol Chem 268 1993 5425 5430 http://www.ncbi.nlm.nih.gov/pubmed/8449903 (Pubitemid 23090858)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.8 , pp. 5425-5430
    • Kujubu, D.A.1    Reddy, S.T.2    Fletcher, B.S.3    Herschman, H.R.4
  • 34
    • 34247505895 scopus 로고    scopus 로고
    • Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation
    • DOI 10.1016/j.plipres.2007.01.001, PII S0163782707000021
    • Y.J. Kang, U.R. Mbonye, C.J. DeLong, M. Wada, and W.L. Smith Regulation of intracellular cyclooxygenase levels by gene transcription and protein degradation Prog Lipid Res 46 2007 108 125 10.1016/j.plipres.2007.01.001 http://www.ncbi.nlm.nih.gov/pubmed/17316818 http://ac.els-cdn.com/ S0163782707000021/1-s2.0-S0163782707000021-main.pdf?-tid=d29acd8c-9923-11e3- aba9-00000aab0f02&acdnat=1392786668-10ad45fa9dbba4a39b26b6e43a9ff296 (Pubitemid 46661865)
    • (2007) Progress in Lipid Research , vol.46 , Issue.2 , pp. 108-125
    • Kang, Y.-J.1    Mbonye, U.R.2    DeLong, C.J.3    Wada, M.4    Smith, W.L.5
  • 35
    • 0028218504 scopus 로고
    • Prostacyclin synthesis in ovine pulmonary artery is developmentally regulated by changes in cyclooxygenase-1 gene expression
    • T.S. Brannon, A.J. North, L.B. Wells, and P.W. Shaul Prostacyclin synthesis in ovine pulmonary artery is developmentally regulated by changes in cyclooxygenase-1 gene expression J Clin Invest 93 1994 2230 2235 10.1172/JCI117220 http://www.ncbi.nlm.nih.gov/pubmed/8182155 http://www.jci.org/articles/view/117220 (Pubitemid 24143106)
    • (1994) Journal of Clinical Investigation , vol.93 , Issue.5 , pp. 2230-2235
    • Brannon, T.S.1    North, A.J.2    Wells, L.B.3    Shaul, P.W.4
  • 36
    • 20344364611 scopus 로고    scopus 로고
    • Cyclooxygenase-1 signaling is required for vascular tube formation during development
    • DOI 10.1016/j.ydbio.2005.03.014, PII S0012160605001831
    • Y.I. Cha, S.H. Kim, L. Solnica-Krezel, and R.N. Dubois Cyclooxygenase-1 signaling is required for vascular tube formation during development Dev Biol 282 2005 274 283 10.1016/j.ydbio.2005.03.014 http://www.ncbi.nlm.nih.gov/pubmed/ 15936346 http://ac.els-cdn.com/S0012160605001831/1-s2.0-S0012160605001831-main. pdf?-tid=b837ddb8-3d3e-11e3-bd34-00000aab0f6b&acdnat=1382682713- 570cf328522aaf850cef16144ce46f3a (Pubitemid 40779944)
    • (2005) Developmental Biology , vol.282 , Issue.1 , pp. 274-283
    • Cha, Y.I.1    Kim, S.-H.2    Solnica-Krezel, L.3    DuBois, R.N.4
  • 37
    • 27544489924 scopus 로고    scopus 로고
    • An intronic enhancer regulates cyclooxygenase-1 gene expression
    • DOI 10.1016/j.bbrc.2005.07.184, PII S0006291X05016876
    • C.J. DeLong, and W.L. Smith An intronic enhancer regulates cyclooxygenase-1 gene expression Biochem Biophys Res Commun 338 2005 53 61 10.1016/j.bbrc.2005.07.184 http://www.ncbi.nlm.nih.gov/pubmed/16105649 http://ac.els-cdn.com/S0006291X05016876/1-s2.0-S0006291X05016876-main.pdf?-tid= c4ba2afa-3d3e-11e3-b511-00000aacb35e&acdnat=1382682735- d0c9169419127b2849fa1b86bbebb107 (Pubitemid 41540536)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 53-61
    • DeLong, C.J.1    Smith, W.L.2
  • 39
    • 0025871150 scopus 로고
    • TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue
    • D.A. Kujubu, B.S. Fletcher, B.C. Varnum, R.W. Lim, and H.R. Herschman TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue J Biol Chem 266 1991 12866 12872 http://www.ncbi.nlm.nih.gov/pubmed/1712772
    • (1991) J Biol Chem , vol.266 , pp. 12866-12872
    • Kujubu, D.A.1    Fletcher, B.S.2    Varnum, B.C.3    Lim, R.W.4    Herschman, H.R.5
  • 40
    • 0026322957 scopus 로고
    • A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein
    • M.K. O'Banion, H.B. Sadowski, V. Winn, and D.A. Young A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein J Biol Chem 266 1991 23261 23267 http://www.ncbi.nlm.nih.gov/pubmed/ 1744122 (Pubitemid 21908788)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.34 , pp. 23261-23267
    • O'Banion, M.K.1    Sadowski, H.B.2    Winn, V.3    Young, D.A.4
  • 41
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • 10.1146/annurev.biochem.69.1.145
    • W.L. Smith, D.L. DeWitt, and R.M. Garavito Cyclooxygenases: structural, cellular, and molecular biology Annu Rev Biochem 69 2000 145 182 10.1146/annurev.biochem.69.1.145 http://www.ncbi.nlm.nih.gov/pubmed/10966456
    • (2000) Annu Rev Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    Dewitt, D.L.2    Garavito, R.M.3
  • 42
    • 43749094995 scopus 로고    scopus 로고
    • Two distinct pathways for cyclooxygenase-2 protein degradation
    • 10.1074/jbc.M710137200 http://www.jbc.org/content/283/13/8611.full.pdf
    • U.R. Mbonye, C. Yuan, and C.E. Harris et al. Two distinct pathways for cyclooxygenase-2 protein degradation J Biol Chem 283 2008 8611 8623 10.1074/jbc.M710137200 http://www.ncbi.nlm.nih.gov/pubmed/18203712 http://www.jbc.org/content/283/13/8611.full.pdf
    • (2008) J Biol Chem , vol.283 , pp. 8611-8623
    • Mbonye, U.R.1    Yuan, C.2    Harris, C.E.3
  • 43
    • 0029899186 scopus 로고    scopus 로고
    • A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors
    • DOI 10.1074/jbc.271.26.15810
    • J.K. Gierse, J.J. McDonald, S.D. Hauser, S.H. Rangwala, C.M. Koboldt, and K. Seibert A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors J Biol Chem 271 1996 15810 15814 http://www.ncbi.nlm.nih.gov/pubmed/8663121 http://www.jbc.org/content/271/26/15810.full.pdf (Pubitemid 26225362)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15810-15814
    • Gierse, J.K.1    McDonald, J.J.2    Hauser, S.D.3    Rangwala, S.H.4    Koboldt, C.M.5    Seibert, K.6
  • 45
    • 54149112779 scopus 로고    scopus 로고
    • Gene duplications and losses within the cyclooxygenase family of teleosts and other chordates
    • 10.1093/molbev/msn183 http://mbe.oxfordjournals.org/content/25/11/2349. full.pdf
    • J.C. Havird, M.M. Miyamoto, K.P. Choe, and D.H. Evans Gene duplications and losses within the cyclooxygenase family of teleosts and other chordates Mol Biol Evol 25 2008 2349 2359 10.1093/molbev/msn183 http://www.ncbi.nlm.nih.gov/ pubmed/18718920 http://mbe.oxfordjournals.org/content/25/11/2349.full.pdf
    • (2008) Mol Biol Evol , vol.25 , pp. 2349-2359
    • Havird, J.C.1    Miyamoto, M.M.2    Choe, K.P.3    Evans, D.H.4
  • 46
    • 0032540344 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy
    • DOI 10.1074/jbc.273.16.9886
    • A.G. Spencer, J.W. Woods, T. Arakawa, I.I. Singer, and W.L. Smith Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy J Biol Chem 273 1998 9886 9893 http://www.ncbi.nlm. nih.gov/pubmed/9545330 http://www.jbc.org/content/273/16/9886.full.pdf (Pubitemid 28183086)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9886-9893
    • Spencer, A.G.1    Woods, J.W.2    Arakawa, T.3    Singer, I.I.4    Smith, W.L.5
  • 47
    • 0033613852 scopus 로고    scopus 로고
    • 2s and cyclooxygenases in immediate and delayed prostanoid biosynthetic pathways
    • DOI 10.1074/jbc.274.5.3103
    • 2s and cyclooxygenases in immediate and delayed prostanoid biosynthetic pathways J Biol Chem 274 1999 3103 3115 http://www.ncbi.nlm.nih.gov/pubmed/9915849 http://www.jbc.org/content/274/5/ 3103.full.pdf (Pubitemid 29075398)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 3103-3115
    • Murakami, M.1    Kambe, T.2    Shimbara, S.3    Kudo, I.4
  • 48
    • 0034693050 scopus 로고    scopus 로고
    • 2 biosynthesis
    • 10.1074/jbc.M003504200 http://www.jbc.org/content/275/42/32775.full.pdf
    • 2 biosynthesis J Biol Chem 275 2000 32775 32782 10.1074/jbc. M003504200 http://www.ncbi.nlm.nih.gov/pubmed/10922363 http://www.jbc.org/ content/275/42/32775.full.pdf
    • (2000) J Biol Chem , vol.275 , pp. 32775-32782
    • Tanioka, T.1    Nakatani, Y.2    Semmyo, N.3    Murakami, M.4    Kudo, I.5
  • 49
    • 0034692689 scopus 로고    scopus 로고
    • 2 synthase that acts in concert with cyclooxygenase-2
    • 10.1074/jbc.M003505200 http://www.jbc.org/content/275/42/32783.full.pdf
    • 2 synthase that acts in concert with cyclooxygenase-2 J Biol Chem 275 2000 32783 32792 10.1074/jbc.M003505200 http://www.ncbi.nlm.nih.gov/pubmed/ 10869354 http://www.jbc.org/content/275/42/32783.full.pdf
    • (2000) J Biol Chem , vol.275 , pp. 32783-32792
    • Murakami, M.1    Naraba, H.2    Tanioka, T.3
  • 50
    • 0029919697 scopus 로고    scopus 로고
    • 2 formation in rat carrageenin-induced pleurisy
    • http://ac.els-cdn.com/0090698095001689/1-s2.0-0090698095001689-main.pdf? -tid=d4d3fae2-3d3e-11e3-a6e1-00000aab0f6b&acdnat=1382682762- d26be353f506a6e2a4acd01f064434ec
    • 2 formation in rat carrageenin-induced pleurisy Prostaglandins 51 1996 19 33 http://www.ncbi.nlm.nih.gov/pubmed/8900441 http://ac.els-cdn.com/0090698095001689/1-s2.0-0090698095001689-main.pdf?-tid= d4d3fae2-3d3e-11e3-a6e1-00000aab0f6b&acdnat=1382682762- d26be353f506a6e2a4acd01f064434ec
    • (1996) Prostaglandins , vol.51 , pp. 19-33
    • Harada, Y.1    Hatanaka, K.2    Kawamura, M.3
  • 52
    • 0029149067 scopus 로고
    • Fatty acid substrate specificities of human prostaglandin-endoperoxide H synthase-1 and -2. Formation of 12-hydroxy-(9Z,13E/Z,15Z)-octadecatrienoic acids from α-linolenic acid
    • O. Laneuville, D.K. Breuer, and N. Xu et al. Fatty acid substrate specificities of human prostaglandin-endoperoxide H synthase-1 and -2. Formation of 12-hydroxy-(9Z,13E/Z,15Z)-octadecatrienoic acids from α-linolenic acid J Biol Chem 270 1995 19330 19336 http://www.ncbi.nlm.nih.gov/pubmed/7642610
    • (1995) J Biol Chem , vol.270 , pp. 19330-19336
    • Laneuville, O.1    Breuer, D.K.2    Xu, N.3
  • 53
    • 0032484672 scopus 로고    scopus 로고
    • Different substrate utilization between prostaglandin endoperoxide H synthase-1 and -2 in NIH3T3 fibroblasts
    • DOI 10.1016/S0005-2760(97)00129-X, PII S000527609700129X
    • M. Shitashige, I. Morita, and S. Murota Different substrate utilization between prostaglandin endoperoxide H synthase-1 and -2 in NIH3T3 fibroblasts Biochim Biophys Acta 1389 1998 57 66 http://www.ncbi.nlm.nih.gov/pubmed/9443604 (Pubitemid 28015060)
    • (1998) Biochimica et Biophysica Acta - Lipids and Lipid Metabolism , vol.1389 , Issue.1 , pp. 57-66
    • Shitashige, M.1    Morita, I.2    Murota, S.-I.3
  • 54
    • 0028810964 scopus 로고
    • Comparison of hydroperoxide initiator requirements for the cyclooxygenase activities of prostaglandin H synthase-1 and -2
    • http://www.jbc.org/content/270/41/24019.full.pdf
    • R.J. Kulmacz, and L.H. Wang Comparison of hydroperoxide initiator requirements for the cyclooxygenase activities of prostaglandin H synthase-1 and -2 J Biol Chem 270 1995 24019 24023 http://www.ncbi.nlm.nih.gov/pubmed/7592599 http://www.jbc.org/content/270/41/24019.full.pdf
    • (1995) J Biol Chem , vol.270 , pp. 24019-24023
    • Kulmacz, R.J.1    Wang, L.H.2
  • 55
    • 37749018414 scopus 로고    scopus 로고
    • Nutritionally essential fatty acids and biologically indispensable cyclooxygenases
    • 10.1016/j.tibs.2007.09.013 http://ac.els-cdn.com/S0968000407002897/1-s2. 0-S0968000407002897-main.pdf?-tid=f78e2508-9923-11e3-9cbd- 00000aacb35f&acdnat=1392786730-bf48425c9bbbbec464e2ac5e00ec9aa4
    • W.L. Smith Nutritionally essential fatty acids and biologically indispensable cyclooxygenases Trends Biochem Sci 33 2008 27 37 10.1016/j.tibs.2007.09.013 http://www.ncbi.nlm.nih.gov/pubmed/18155912 http://ac.els-cdn.com/S0968000407002897/1-s2.0-S0968000407002897-main.pdf?-tid= f78e2508-9923-11e3-9cbd-00000aacb35f&acdnat=1392786730- bf48425c9bbbbec464e2ac5e00ec9aa4
    • (2008) Trends Biochem Sci , vol.33 , pp. 27-37
    • Smith, W.L.1
  • 56
    • 0029924110 scopus 로고    scopus 로고
    • Prostaglandin endoperoxide synthase: Why two isoforms?
    • G393-400
    • C.S. Williams, and R.N. DuBois Prostaglandin endoperoxide synthase: why two isoforms? Am J Physiol 270 1996 G393-400 http://www.ncbi.nlm.nih.gov/pubmed/ 8638704
    • (1996) Am J Physiol , vol.270
    • Williams, C.S.1    Dubois, R.N.2
  • 58
    • 34248576291 scopus 로고    scopus 로고
    • Genome of the marsupial Monodelphis domestica reveals innovation in non-coding sequences
    • DOI 10.1038/nature05805, PII NATURE05805
    • T.S. Mikkelsen, M.J. Wakefield, and B. Aken et al. Genome of the marsupial Monodelphis domestica reveals innovation in non-coding sequences Nature 447 2007 167 177 10.1038/nature05805 http://www.ncbi.nlm.nih.gov/pubmed/ 17495919 http://www.nature.com/nature/journal/v447/n7141/pdf/nature05805.pdf (Pubitemid 46763085)
    • (2007) Nature , vol.447 , Issue.7141 , pp. 167-177
    • Mikkelsen, T.S.1    Wakefield, M.J.2    Aken, B.3    Amemiya, C.T.4    Chang, J.L.5    Duke, S.6    Garber, M.7    Gentles, A.J.8    Goodstadt, L.9
  • 59
    • 34248596154 scopus 로고    scopus 로고
    • An analysis of the gene complement of a marsupial, Monodelphis domestica: Evolution of lineage-specific genes and giant chromosomes
    • DOI 10.1101/gr.6093907
    • L. Goodstadt, A. Heger, C. Webber, and C.P. Ponting An analysis of the gene complement of a marsupial. Monodelphis domestica: evolution of lineage-specific genes and giant chromosomes Genome Res 17 2007 969 981 10.1101/gr.6093907 http://www.ncbi.nlm.nih.gov/pubmed/17495010 http://genome.cshlp.org/content/17/7/969.full.pdf (Pubitemid 47026344)
    • (2007) Genome Research , vol.17 , Issue.7 , pp. 969-981
    • Goodstadt, L.1    Heger, A.2    Webber, C.3    Ponting, C.P.4
  • 60
    • 0036896487 scopus 로고    scopus 로고
    • Genetic and genomic tools for Xenopus research: The NIH Xenopus initiative
    • DOI 10.1002/dvdy.10174
    • S.L. Klein, R.L. Strausberg, L. Wagner, J. Pontius, S.W. Clifton, and P. Richardson Genetic and genomic tools for Xenopus research: the NIH Xenopus initiative Dev Dyn 225 2002 384 391 10.1002/dvdy.10174 http://www.ncbi.nlm.nih. gov/pubmed/12454917 http://onlinelibrary.wiley.com/store/10.1002/dvdy.10174/ asset/10174-ftp.pdf?v=1&t=hn71je73&s= 67acb2914ec627ee1407f2bd98a4eb261b5a1e6a (Pubitemid 35429723)
    • (2002) Developmental Dynamics , vol.225 , Issue.4 , pp. 384-391
    • Klein, S.L.1    Strausberg, R.L.2    Wagner, L.3    Pontius, J.4    Clifton, S.W.5    Richardson, P.6
  • 61
    • 33750190150 scopus 로고    scopus 로고
    • Cyclooxygenase 1 and 2 mRNA and protein expression in the Gallus domesticus model of ovarian cancer
    • DOI 10.1016/j.ygyno.2006.05.012, PII S0090825806003787
    • M.E. Urick, and P.A. Johnson Cyclooxygenase 1 and 2 mRNA and protein expression in the Gallus domesticus model of ovarian cancer Gynecol Oncol 103 2006 673 678 10.1016/j.ygyno.2006.05.012 http://www.ncbi.nlm.nih.gov/pubmed/ 16797680 (Pubitemid 44602185)
    • (2006) Gynecologic Oncology , vol.103 , Issue.2 , pp. 673-678
    • Urick, M.E.1    Johnson, P.A.2
  • 62
    • 2442707716 scopus 로고    scopus 로고
    • Fugu genome analysis provides evidence for a whole-genome duplication early during the evolution of ray-finned fishes
    • DOI 10.1093/molbev/msh114
    • A. Christoffels, E.G. Koh, J.M. Chia, S. Brenner, S. Aparicio, and B. Venkatesh Fugu genome analysis provides evidence for a whole-genome duplication early during the evolution of ray-finned fishes Mol Biol Evol 21 2004 1146 1151 10.1093/molbev/msh114 http://www.ncbi.nlm.nih.gov/pubmed/15014147 http://mbe.oxfordjournals.org/content/21/6/1146.full.pdf (Pubitemid 38658222)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.6 , pp. 1146-1151
    • Christoffels, A.1    Koh, E.G.L.2    Chia, J.-M.3    Brenner, S.4    Aparicio, S.5    Venkatesh, B.6
  • 63
    • 28944450051 scopus 로고    scopus 로고
    • The "fish-specific" Hox cluster duplication is coincident with the origin of teleosts
    • DOI 10.1093/molbev/msj020
    • K.D. Crow, P.F. Stadler, V.J. Lynch, C. Amemiya, and G.P. Wagner The "fish-specific" Hox cluster duplication is coincident with the origin of teleosts Mol Biol Evol 23 2006 121 136 10.1093/molbev/msj020 http://www.ncbi.nlm.nih.gov/pubmed/16162861 http://mbe.oxfordjournals.org/ content/23/1/121.full.pdf (Pubitemid 41785959)
    • (2006) Molecular Biology and Evolution , vol.23 , Issue.1 , pp. 121-136
    • Crow, K.D.1    Stadler, P.F.2    Lynch, V.J.3    Amemiya, C.4    Wagner, G.P.5
  • 64
    • 4143134848 scopus 로고    scopus 로고
    • Phylogenetic timing of the fish-specific genome duplication correlates with the diversification of teleost fish
    • DOI 10.1007/s00239-004-2613-z
    • S. Hoegg, H. Brinkmann, J.S. Taylor, and A. Meyer Phylogenetic timing of the fish-specific genome duplication correlates with the diversification of teleost fish J Mol Evol 59 2004 190 203 10.1007/s00239-004-2613-z http://www.ncbi.nlm.nih.gov/pubmed/15486693 (Pubitemid 39128342)
    • (2004) Journal of Molecular Evolution , vol.59 , Issue.2 , pp. 190-203
    • Hoegg, S.1    Brinkmann, H.2    Taylor, J.S.3    Meyer, A.4
  • 65
    • 58649118651 scopus 로고    scopus 로고
    • Rapidly evolving fish genomes and teleost diversity
    • 10.1016/j.gde.2008.11.001 http://ac.els-cdn.com/S0959437X08001512/1-s2.0- S0959437X08001512-main.pdf?-tid=4ad222c8-3d3f-11e3-813f-00000aab0f6c&acdnat= 1382682959-88eee12b2827a1a131fa1f295de1c3f0
    • V. Ravi, and B. Venkatesh Rapidly evolving fish genomes and teleost diversity Curr Opin Genet Dev 18 2008 544 550 10.1016/j.gde.2008.11.001 http://www.ncbi.nlm.nih.gov/pubmed/19095434 http://ac.els-cdn.com/ S0959437X08001512/1-s2.0-S0959437X08001512-main.pdf?-tid=4ad222c8-3d3f-11e3- 813f-00000aab0f6c&acdnat=1382682959-88eee12b2827a1a131fa1f295de1c3f0
    • (2008) Curr Opin Genet Dev , vol.18 , pp. 544-550
    • Ravi, V.1    Venkatesh, B.2
  • 66
    • 1242274629 scopus 로고    scopus 로고
    • Major events in the genome evolution of vertebrates: Paranome age and size differ considerably between ray-finned fishes and land vertebrates
    • DOI 10.1073/pnas.0307968100
    • K. Vandepoele, W. De Vos, J.S. Taylor, A. Meyer, and Y. Van de Peer Major events in the genome evolution of vertebrates: paranome age and size differ considerably between ray-finned fishes and land vertebrates Proc Natl Acad Sci U S A 101 2004 1638 1643 http://www.ncbi.nlm.nih.gov/pubmed/14757817 http://www.pnas.org/content/101/6/1638.full.pdf 10.1073/pnas.0307968100 (Pubitemid 38234207)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.6 , pp. 1638-1643
    • Vandepoele, K.1    De Vos, W.2    Taylor, J.S.3    Meyer, A.4    Van De Peer, Y.5
  • 67
    • 1842690846 scopus 로고    scopus 로고
    • On the evolutionary origin of cyclooxygenase (COX) isozymes: Characterization of marine invertebrate COX genes points to independent duplication events in vertebrate and invertebrate lineages
    • DOI 10.1074/jbc.M313258200
    • R. Järving, I. Järving, R. Kurg, A.R. Brash, and N. Samel On the evolutionary origin of cyclooxygenase (COX) isozymes: characterization of marine invertebrate COX genes points to independent duplication events in vertebrate and invertebrate lineages J Biol Chem 279 2004 13624 13633 10.1074/jbc.M313258200 http://www.ncbi.nlm.nih.gov/pubmed/14732711 http://www.jbc.org/content/279/14/13624.full.pdf (Pubitemid 38468889)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13624-13633
    • Jarving, R.1    Jarving, I.2    Kurg, R.3    Brash, A.R.4    Samel, N.5
  • 68
    • 33751435161 scopus 로고    scopus 로고
    • The zebrafish genome contains two inducible, functional cyclooxygenase-2 genes
    • DOI 10.1016/j.bbrc.2006.11.007, PII S0006291X06024533
    • T.O. Ishikawa, K.J. Griffin, U. Banerjee, and H.R. Herschman The zebrafish genome contains two inducible, functional cyclooxygenase-2 genes Biochem Biophys Res Commun 352 2007 181 187 10.1016/j.bbrc.2006.11.007 http://www.ncbi.nlm.nih.gov/pubmed/17112475 http://ac.els-cdn.com/ S0006291X06024533/1-s2.0-S0006291X06024533-main.pdf?-tid=e0bee5d8-3d3e-11e3- a10f-00000aab0f01&acdnat=1382682782-c977181cb3ad5dc3d6ca5fbf409479e0 (Pubitemid 44821111)
    • (2007) Biochemical and Biophysical Research Communications , vol.352 , Issue.1 , pp. 181-187
    • Ishikawa, T.-o.1    Griffin, K.J.P.2    Banerjee, U.3    Herschman, H.R.4
  • 69
    • 36849023824 scopus 로고    scopus 로고
    • Two inducible, functional cyclooxygenase-2 genes are present in the rainbow trout genome
    • DOI 10.1002/jcb.21368
    • T.O. Ishikawa, and H.R. Herschman Two inducible, functional cyclooxygenase-2 genes are present in the rainbow trout genome J Cell Biochem 102 2007 1486 1492 10.1002/jcb.21368 http://www.ncbi.nlm.nih.gov/pubmed/17471498 (Pubitemid 350223950)
    • (2007) Journal of Cellular Biochemistry , vol.102 , Issue.6 , pp. 1486-1492
    • Ishikawa, T.-O.1    Herschman, H.R.2
  • 70
    • 0003728605 scopus 로고
    • 3rd ed. John Wiley & Sons Hoboken, NJ
    • J.S. Nelson Fishes of the world 3rd ed. 1994 John Wiley & Sons Hoboken, NJ
    • (1994) Fishes of the world
    • Nelson, J.S.1
  • 71
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • http://www.sciencemag.org/content/290/5494/1151.full.pdf
    • M. Lynch, and J.S. Conery The evolutionary fate and consequences of duplicate genes Science 290 2000 1151 1155 http://www.ncbi.nlm.nih.gov/pubmed/ 11073452 http://www.sciencemag.org/content/290/5494/1151.full.pdf
    • (2000) Science , vol.290 , pp. 1151-1155
    • Lynch, M.1    Conery, J.S.2
  • 72
    • 78650523554 scopus 로고    scopus 로고
    • Expression of cyclooxygenase-2 and prostaglandin receptor EP4b mRNA in the ovary of the medaka fish, Oryzias latipes: Possible involvement in ovulation
    • 10.1016/j.mce.2010.09.015 http://ac.els-cdn.com/S0303720710004764/1-s2.0- S0303720710004764-main.pdf?-tid=ca1bd05c-3d3e-11e3-a9ae-00000aab0f26&acdnat= 1382682744-a416428d7eb63450440514b7136a8e3c
    • C. Fujimori, K. Ogiwara, A. Hagiwara, S. Rajapakse, A. Kimura, and T. Takahashi Expression of cyclooxygenase-2 and prostaglandin receptor EP4b mRNA in the ovary of the medaka fish, Oryzias latipes: Possible involvement in ovulation Mol Cell Endocrinol 332 2011 67 77 10.1016/j.mce.2010.09.015 http://www.ncbi.nlm.nih.gov/pubmed/20932877 http://ac.els-cdn.com/ S0303720710004764/1-s2.0-S0303720710004764-main.pdf?-tid=ca1bd05c-3d3e-11e3- a9ae-00000aab0f26&acdnat=1382682744-a416428d7eb63450440514b7136a8e3c
    • (2011) Mol Cell Endocrinol , vol.332 , pp. 67-77
    • Fujimori, C.1    Ogiwara, K.2    Hagiwara, A.3    Rajapakse, S.4    Kimura, A.5    Takahashi, T.6
  • 73
    • 34648816680 scopus 로고    scopus 로고
    • The 2R hypothesis: An update
    • DOI 10.1016/j.coi.2007.07.009, PII S0952791507001239, Hematopoietic cell death/Immunogenetics/Transplantation
    • M. Kasahara The 2R hypothesis: an update Curr Opin Immunol 19 2007 547 552 10.1016/j.coi.2007.07.009 http://www.ncbi.nlm.nih.gov/pubmed/17707623 http://ac.els-cdn.com/S0952791507001239/1-s2.0-S0952791507001239-main.pdf?-tid= ecabe1d4-3d3e-11e3-9fcc-00000aab0f01&acdnat=1382682802- 4091020ddef76f472e3cfb23d5cd7951 (Pubitemid 47464919)
    • (2007) Current Opinion in Immunology , vol.19 , Issue.5 , pp. 547-552
    • Kasahara, M.1
  • 74
    • 33644536713 scopus 로고    scopus 로고
    • Tunicates and not cephalochordates are the closest living relatives of vertebrates
    • DOI 10.1038/nature04336, PII N04336
    • F. Delsuc, H. Brinkmann, D. Chourrout, and H. Philippe Tunicates and not cephalochordates are the closest living relatives of vertebrates Nature 439 2006 965 968 10.1038/nature04336 http://www.ncbi.nlm.nih.gov/pubmed/16495997 http://www.nature.com/nature/journal/v439/n7079/pdf/nature04336.pdf (Pubitemid 43292413)
    • (2006) Nature , vol.439 , Issue.7079 , pp. 965-968
    • Delsuc, F.1    Brinkmann, H.2    Chourrout, D.3    Philippe, H.4
  • 76
    • 73449096708 scopus 로고    scopus 로고
    • Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: Genetic and biochemical characterization of two crustacean cyclooxygenases
    • 10.1016/j.ibmb.2009.10.002 http://ac.els-cdn.com/S0965174809001490/1-s2. 0-S0965174809001490-main.pdf?-tid=84ae887e-3d3f-11e3-a7d5- 00000aacb35e&acdnat=1382683057-970a2bf3e389c28e64781d5fa64f3dd3
    • K. Varvas, R. Kurg, and K. Hansen et al. Direct evidence of the cyclooxygenase pathway of prostaglandin synthesis in arthropods: genetic and biochemical characterization of two crustacean cyclooxygenases Insect Biochem Mol Biol 39 2009 851 860 10.1016/j.ibmb.2009.10.002 http://www.ncbi.nlm.nih.gov/ pubmed/19854273 http://ac.els-cdn.com/S0965174809001490/1-s2.0- S0965174809001490-main.pdf?-tid=84ae887e-3d3f-11e3-a7d5-00000aacb35e&acdnat= 1382683057-970a2bf3e389c28e64781d5fa64f3dd3
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 851-860
    • Varvas, K.1    Kurg, R.2    Hansen, K.3
  • 77
    • 30844448127 scopus 로고    scopus 로고
    • Prostaglandins and other eicosanoids in insects: Biological significance
    • DOI 10.1146/annurev.ento.51.110104.151021
    • D. Stanley Prostaglandins and other eicosanoids in insects: biological significance Annu Rev Entomol 51 2006 25 44 10.1146/annurev.ento.51.110104. 151021 http://www.ncbi.nlm.nih.gov/pubmed/16332202 (Pubitemid 43107813)
    • (2006) Annual Review of Entomology , vol.51 , pp. 25-44
    • Stanley, D.1
  • 79
    • 4544365241 scopus 로고    scopus 로고
    • Structural and functional comparison of 15S- and 15R-specific cyclooxygenases from the coral Plexaura homomalla
    • DOI 10.1111/j.0014-2956.2004.04289.x
    • K. Valmsen, W.E. Boeglin, and I. Jarving et al. Structural and functional comparison of 15S- and 15R-specific cyclooxygenases from the coral Plexaura homomalla Eur J Biochem 271 2004 3533 3538 10.1111/j.0014-2956.2004.04289.x http://www.ncbi.nlm.nih.gov/pubmed/15317588 (Pubitemid 39215342)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.17 , pp. 3533-3538
    • Valmsen, K.1    Boeglin, W.E.2    Jarving, I.3    Schneider, C.4    Varvas, K.5    Brash, A.R.6    Samel, N.7
  • 80
    • 0035831484 scopus 로고    scopus 로고
    • The basis of prostaglandin synthesis in coral: Molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa
    • 10.1074/jbc.M009803200 http://www.jbc.org/content/276/10/7033.full.pdf
    • R. Koljak, I. Järving, and R. Kurg et al. The basis of prostaglandin synthesis in coral: molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa J Biol Chem 276 2001 7033 7040 10.1074/jbc.M009803200 http://www.ncbi.nlm.nih.gov/pubmed/11085996 http://www.jbc.org/content/276/10/7033.full.pdf
    • (2001) J Biol Chem , vol.276 , pp. 7033-7040
    • Koljak, R.1    Järving, I.2    Kurg, R.3
  • 81
    • 19544394243 scopus 로고    scopus 로고
    • The cyclooxygenases
    • DOI 10.1186/gb-2004-5-9-241
    • N.V. Chandrasekharan, and D.L. Simmons The cyclooxygenases Genome Biol 5 2004 241 10.1186/gb-2004-5-9-241 http://www.ncbi.nlm.nih.gov/pubmed/15345041 (Pubitemid 39335025)
    • (2004) Genome Biology , vol.5 , Issue.9 , pp. 241
    • Chandrasekharan, N.V.1    Simmons, D.L.2
  • 82
    • 0033972072 scopus 로고    scopus 로고
    • The probability of duplicate gene preservation by subfunctionalization
    • M. Lynch, and A. Force The probability of duplicate gene preservation by subfunctionalization Genetics 154 2000 459 473 http://www.ncbi.nlm.nih.gov/ pubmed/10629003 http://www.genetics.org/content/154/1/459.full.pdf (Pubitemid 30045935)
    • (2000) Genetics , vol.154 , Issue.1 , pp. 459-473
    • Lynch, M.1    Force, A.2
  • 84
    • 1842838629 scopus 로고    scopus 로고
    • Evidence for independent Hox gene duplications in the hagfish lineage: A PCR-based gene inventory of Eptatretus stoutii
    • DOI 10.1016/j.ympev.2004.03.015, PII S1055790304001083
    • P.F. Stadler, C. Fried, and S.J. Prohaska et al. Evidence for independent Hox gene duplications in the hagfish lineage: a PCR-based gene inventory of Eptatretus stoutii Mol Phylogenet Evol 32 2004 686 694 10.1016/j.ympev.2004.03. 015 http://www.ncbi.nlm.nih.gov/pubmed/15288047 http://ac.els-cdn.com/ S1055790304001083/1-s2.0-S1055790304001083-main.pdf?-tid=62abbc42-3d3f-11e3- a0a2-00000aacb35e&acdnat=1382683000-bbf9f2cee466614aae179bf5e12a7fd2 (Pubitemid 39039944)
    • (2004) Molecular Phylogenetics and Evolution , vol.32 , Issue.3 , pp. 686-694
    • Stadler, P.F.1    Fried, C.2    Prohaska, S.J.3    Bailey, W.J.4    Misof, B.Y.5    Ruddle, F.H.6    Wagner, G.P.7
  • 85
    • 0032733930 scopus 로고    scopus 로고
    • Gene and genome duplications in vertebrates: The one-to-four (-To-Eight in fish) rule and the evolution of novel gene functions
    • A. Meyer, and M. Schartl Gene and genome duplications in vertebrates: the one-to-four (-to-eight in fish) rule and the evolution of novel gene functions Curr Opin Cell Biol 11 1999 699 704 http://www.ncbi.nlm.nih.gov/pubmed/10600714
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 699-704
    • Meyer, A.1    Schartl, M.2
  • 86
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 22 1994 4673 4680 http://www.ncbi.nlm.nih.gov/pubmed/7984417 http://nar.oxfordjournals.org/content/22/22/4673 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.