메뉴 건너뛰기




Volumn 70, Issue 10, 2013, Pages 1807-1830

Structure and evolution of vertebrate aldehyde oxidases: From gene duplication to gene suppression

Author keywords

Aldehyde oxidase; Drug metabolism; Molybdenum cofactor; Molybdo flavoenzyme

Indexed keywords

ALDEHYDE OXIDASE; COMPLEMENTARY DNA; MICRORNA;

EID: 84876947486     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-012-1229-5     Document Type: Article
Times cited : (55)

References (54)
  • 1
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: Genetics, evolution and biochemistry
    • 18066686 10.1007/s00018-007-7398-y 1:CAS:528:DC%2BD1cXkvFynt70%3D
    • Garattini E, Fratelli M, Terao M (2008) Mammalian aldehyde oxidases: genetics, evolution and biochemistry. Cell Mol Life Sci 65(7-8):1019-1048
    • (2008) Cell Mol Life Sci , vol.65 , Issue.7-8 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 2
    • 76249096555 scopus 로고    scopus 로고
    • The mammalian aldehyde oxidase gene family
    • 20038499 1:CAS:528:DC%2BC3cXpt1yrur0%3D
    • Garattini E, Fratelli M, Terao M (2009) The mammalian aldehyde oxidase gene family. Hum Genomics 4(2):119-130
    • (2009) Hum Genomics , vol.4 , Issue.2 , pp. 119-130
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 3
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • 12578558 10.1042/BJ20030121 1:CAS:528:DC%2BD3sXjsFeitbg%3D
    • Garattini E et al (2003) Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372(Pt 1):15-32
    • (2003) Biochem J , vol.372 , Issue.PART 1 , pp. 15-32
    • Garattini, E.1
  • 4
    • 79960719085 scopus 로고    scopus 로고
    • Increasing recognition of the importance of aldehyde oxidase in drug development and discovery
    • 21428696 10.3109/03602532.2011.560606 1:CAS:528:DC%2BC3MXpt1ajtLo%3D
    • Garattini E, Terao M (2011) Increasing recognition of the importance of aldehyde oxidase in drug development and discovery. Drug Metab Rev 43(3):374-386
    • (2011) Drug Metab Rev , vol.43 , Issue.3 , pp. 374-386
    • Garattini, E.1    Terao, M.2
  • 5
    • 84870012251 scopus 로고    scopus 로고
    • The first mammalian aldehyde oxidase crystal structure: Insights into substrate specificity
    • 23019336 10.1074/jbc.M112.390419 1:CAS:528:DC%2BC38Xhslantr7L
    • Coelho C et al (2012) The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity. J Biol Chem 287(48):40690-40702
    • (2012) J Biol Chem , vol.287 , Issue.48 , pp. 40690-40702
    • Coelho, C.1
  • 6
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • 11005854 10.1073/pnas.97.20.10723 1:CAS:528:DC%2BD3cXnt1aiurY%3D
    • Enroth C et al (2000) Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc Natl Acad Sci USA 97(20):10723-10728
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.20 , pp. 10723-10728
    • Enroth, C.1
  • 7
    • 84858848617 scopus 로고    scopus 로고
    • The role of aldehyde oxidase in drug metabolism
    • 22335465 10.1517/17425255.2012.663352 1:CAS:528:DC%2BC38XksVOrsLg%3D
    • Garattini E, Terao M (2012) The role of aldehyde oxidase in drug metabolism. Expert Opin Drug Metab Toxicol 8(4):487-503
    • (2012) Expert Opin Drug Metab Toxicol , vol.8 , Issue.4 , pp. 487-503
    • Garattini, E.1    Terao, M.2
  • 8
    • 0030920524 scopus 로고    scopus 로고
    • Cloning and molecular characterization of plant aldehyde oxidase
    • 9182554 10.1074/jbc.272.24.15280 1:CAS:528:DyaK2sXjvFOmtb0%3D
    • Sekimoto H et al (1997) Cloning and molecular characterization of plant aldehyde oxidase. J Biol Chem 272(24):15280-15285
    • (1997) J Biol Chem , vol.272 , Issue.24 , pp. 15280-15285
    • Sekimoto, H.1
  • 9
    • 11144345842 scopus 로고    scopus 로고
    • Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds
    • 15574845 10.1093/pcp/pch198 1:CAS:528:DC%2BD2cXhtVGis7nO
    • Seo M et al (2004) Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds. Plant Cell Physiol 45(11):1694-1703
    • (2004) Plant Cell Physiol , vol.45 , Issue.11 , pp. 1694-1703
    • Seo, M.1
  • 10
    • 0033749385 scopus 로고    scopus 로고
    • The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves
    • 11050171 10.1073/pnas.220426197 1:CAS:528:DC%2BD3cXotFykt7w%3D
    • Seo M et al (2000) The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves. Proc Natl Acad Sci USA 97(23):12908-12913
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.23 , pp. 12908-12913
    • Seo, M.1
  • 11
    • 59349113182 scopus 로고    scopus 로고
    • Cloning and expression analysis of an aldehyde oxidase gene in Arachis hygogaea L
    • 20112869 1:CAS:528:DC%2BD1MXisV2ks7w%3D
    • Yang L et al (2009) Cloning and expression analysis of an aldehyde oxidase gene in Arachis hygogaea L. J Environ Biol 30(1):93-98
    • (2009) J Environ Biol , vol.30 , Issue.1 , pp. 93-98
    • Yang, L.1
  • 12
    • 2442626687 scopus 로고    scopus 로고
    • Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in 'Hass' avocado
    • 15015080 10.1007/s10265-003-0136-0 1:CAS:528:DC%2BD2cXjtlyjs7k%3D
    • Taylor NJ, Cowan AK (2004) Xanthine dehydrogenase and aldehyde oxidase impact plant hormone homeostasis and affect fruit size in 'Hass' avocado. J Plant Res 117(2):121-130
    • (2004) J Plant Res , vol.117 , Issue.2 , pp. 121-130
    • Taylor, N.J.1    Cowan, A.K.2
  • 13
    • 21244461224 scopus 로고    scopus 로고
    • The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid
    • 15941399 10.1111/j.1365-313X.2005.02422.x 1:CAS:528:DC%2BD2MXlslCgurs%3D
    • Yesbergenova Z et al (2005) The plant Mo-hydroxylases aldehyde oxidase and xanthine dehydrogenase have distinct reactive oxygen species signatures and are induced by drought and abscisic acid. Plant J 42(6):862-876
    • (2005) Plant J , vol.42 , Issue.6 , pp. 862-876
    • Yesbergenova, Z.1
  • 14
    • 84859917371 scopus 로고    scopus 로고
    • The impact of single nucleotide polymorphisms on human aldehyde oxidase
    • 22279051 10.1124/dmd.111.043828 1:CAS:528:DC%2BC38Xmt1Kgu7w%3D
    • Hartmann T et al (2012) The impact of single nucleotide polymorphisms on human aldehyde oxidase. Drug Metab Dispos 40(5):856-864
    • (2012) Drug Metab Dispos , vol.40 , Issue.5 , pp. 856-864
    • Hartmann, T.1
  • 15
    • 78650379608 scopus 로고    scopus 로고
    • Aldehyde oxidase: An enzyme of emerging importance in drug discovery
    • 20853847 10.1021/jm100888d 1:CAS:528:DC%2BC3cXhtFygt73N
    • Pryde DC et al (2010) Aldehyde oxidase: an enzyme of emerging importance in drug discovery. J Med Chem 53(24):8441-8460
    • (2010) J Med Chem , vol.53 , Issue.24 , pp. 8441-8460
    • Pryde, D.C.1
  • 16
    • 0028111509 scopus 로고
    • Chromosomal mapping, isolation, and characterization of the mouse xanthine dehydrogenase gene
    • 7835888 10.1006/geno.1994.1515 1:CAS:528:DyaK2MXhtFOqsrY%3D
    • Cazzaniga G et al (1994) Chromosomal mapping, isolation, and characterization of the mouse xanthine dehydrogenase gene. Genomics 23(2):390-402
    • (1994) Genomics , vol.23 , Issue.2 , pp. 390-402
    • Cazzaniga, G.1
  • 17
    • 0033166759 scopus 로고    scopus 로고
    • Molecular cloning of the cDNA coding for mouse aldehyde oxidase: Tissue distribution and regulation in vivo by testosterone
    • 10377246 10.1042/0264-6021:3410071 1:CAS:528:DyaK1MXkvVKisLY%3D
    • Kurosaki M et al (1999) Molecular cloning of the cDNA coding for mouse aldehyde oxidase: tissue distribution and regulation in vivo by testosterone. Biochem J 341(Pt 1):71-80
    • (1999) Biochem J , vol.341 , Issue.PART 1 , pp. 71-80
    • Kurosaki, M.1
  • 18
    • 9644262449 scopus 로고    scopus 로고
    • The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa
    • 15383531 10.1074/jbc.M408734200 1:CAS:528:DC%2BD2cXhtVWjsL7N
    • Kurosaki M et al (2004) The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-flavoenzyme family with selective expression in the olfactory mucosa. J Biol Chem 279(48):50482-50498
    • (2004) J Biol Chem , vol.279 , Issue.48 , pp. 50482-50498
    • Kurosaki, M.1
  • 19
    • 0035824605 scopus 로고    scopus 로고
    • Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1
    • 11562361 10.1074/jbc.M105744200 1:CAS:528:DC%2BD3MXptVymtbg%3D
    • Terao M et al (2001) Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1. J Biol Chem 276(49):46347-46363
    • (2001) J Biol Chem , vol.276 , Issue.49 , pp. 46347-46363
    • Terao, M.1
  • 20
    • 0034730637 scopus 로고    scopus 로고
    • Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase
    • 10893244 10.1074/jbc.M005355200 1:CAS:528:DC%2BD3cXnt1agtbw%3D
    • Terao M et al (2000) Cloning of the cDNAs coding for two novel molybdo-flavoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase. J Biol Chem 275(39):30690-30700
    • (2000) J Biol Chem , vol.275 , Issue.39 , pp. 30690-30700
    • Terao, M.1
  • 21
    • 0347364803 scopus 로고    scopus 로고
    • Human liver aldehyde oxidase: Inhibition by 239 drugs
    • 14681337 10.1177/0091270003260336 1:CAS:528:DC%2BD2cXls1Ojsg%3D%3D
    • Obach RS et al (2004) Human liver aldehyde oxidase: inhibition by 239 drugs. J Clin Pharmacol 44(1):7-19
    • (2004) J Clin Pharmacol , vol.44 , Issue.1 , pp. 7-19
    • Obach, R.S.1
  • 22
    • 58249104034 scopus 로고    scopus 로고
    • Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the biosynthesis of retinoic acid: Generation and characterization of a knockout mouse
    • 18981221 10.1128/MCB.01385-08 1:CAS:528:DC%2BD1MXhsVChurw%3D
    • Terao M et al (2009) Role of the molybdoflavoenzyme aldehyde oxidase homolog 2 in the biosynthesis of retinoic acid: generation and characterization of a knockout mouse. Mol Cell Biol 29(2):357-377
    • (2009) Mol Cell Biol , vol.29 , Issue.2 , pp. 357-377
    • Terao, M.1
  • 23
    • 0344824014 scopus 로고    scopus 로고
    • Convergent neofunctionalization by positive Darwinian selection after ancient recurrent duplications of the xanthine dehydrogenase gene
    • 14576276 10.1073/pnas.1835646100 1:CAS:528:DC%2BD3sXptFOisbo%3D
    • Rodriguez-Trelles F, Tarrio R, Ayala FJ (2003) Convergent neofunctionalization by positive Darwinian selection after ancient recurrent duplications of the xanthine dehydrogenase gene. Proc Natl Acad Sci USA 100(23):13413-13417
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.23 , pp. 13413-13417
    • Rodriguez-Trelles, F.1    Tarrio, R.2    Ayala, F.J.3
  • 24
    • 33745871580 scopus 로고    scopus 로고
    • Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes
    • 16672219 10.1074/jbc.M600850200 1:CAS:528:DC%2BD28Xms1Gqtrs%3D
    • Terao M et al (2006) Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes. J Biol Chem 281(28):19748-19761
    • (2006) J Biol Chem , vol.281 , Issue.28 , pp. 19748-19761
    • Terao, M.1
  • 25
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • 14530136 10.1080/10635150390235520
    • Guindon S, Gascuel O (2003) A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst Biol 52(5):696-704
    • (2003) Syst Biol , vol.52 , Issue.5 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 26
    • 0030807655 scopus 로고    scopus 로고
    • BIONJ: An improved version of the NJ algorithm based on a simple model of sequence data
    • 9254330 10.1093/oxfordjournals.molbev.a025808 1:CAS:528: DyaK2sXksVahs7o%3D
    • Gascuel O (1997) BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol Biol Evol 14(7):685-695
    • (1997) Mol Biol Evol , vol.14 , Issue.7 , pp. 685-695
    • Gascuel, O.1
  • 27
    • 84865022771 scopus 로고    scopus 로고
    • Sequencing three crocodilian genomes to illuminate the evolution of archosaurs and amniotes
    • St John JA et al (2012) Sequencing three crocodilian genomes to illuminate the evolution of archosaurs and amniotes. Genome Biol. 13(1):415
    • (2012) Genome Biol. , vol.13 , Issue.1 , pp. 415
    • St John, J.A.1
  • 28
    • 45449113138 scopus 로고    scopus 로고
    • CID-miRNA: A web server for prediction of novel miRNA precursors in human genome
    • 18522801 10.1016/j.bbrc.2008.05.134 1:CAS:528:DC%2BD1cXns1Sgt74%3D
    • Tyagi S et al (2008) CID-miRNA: a web server for prediction of novel miRNA precursors in human genome. Biochem Biophys Res Commun 372(4):831-834
    • (2008) Biochem Biophys Res Commun , vol.372 , Issue.4 , pp. 831-834
    • Tyagi, S.1
  • 29
    • 33750456225 scopus 로고    scopus 로고
    • A lamprey from the Devonian period of South Africa
    • 17066033 10.1038/nature05150 1:CAS:528:DC%2BD28XhtFaksrrE
    • Gess RW, Coates MI, Rubidge BS (2006) A lamprey from the Devonian period of South Africa. Nature 443(7114):981-984
    • (2006) Nature , vol.443 , Issue.7114 , pp. 981-984
    • Gess, R.W.1    Coates, M.I.2    Rubidge, B.S.3
  • 30
    • 77953135165 scopus 로고    scopus 로고
    • A multilocus timescale for the origin of extant amphibians
    • San Mauro D (2010) A multilocus timescale for the origin of extant amphibians. Mol Phylogenet Evol 56(2):554-561
    • (2010) Mol Phylogenet Evol , vol.56 , Issue.2 , pp. 554-561
    • San Mauro, D.1
  • 31
    • 34047108602 scopus 로고    scopus 로고
    • The delayed rise of present-day mammals
    • 17392779 10.1038/nature05634 1:CAS:528:DC%2BD2sXjsV2itb0%3D
    • Bininda-Emonds OR et al (2007) The delayed rise of present-day mammals. Nature 446(7135):507-512
    • (2007) Nature , vol.446 , Issue.7135 , pp. 507-512
    • Bininda-Emonds, O.R.1
  • 32
    • 84860827020 scopus 로고    scopus 로고
    • Tempo of trophic evolution and its impact on mammalian diversification
    • 22509033 10.1073/pnas.1117133109 1:CAS:528:DC%2BC38XntVWksbo%3D
    • Price SA et al (2012) Tempo of trophic evolution and its impact on mammalian diversification. Proc Natl Acad Sci USA 109(18):7008-7012
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.18 , pp. 7008-7012
    • Price, S.A.1
  • 33
    • 50049085521 scopus 로고    scopus 로고
    • Colloquium paper: Phylogenetic trees and the future of mammalian biodiversity
    • 18695230 10.1073/pnas.0801917105 1:CAS:528:DC%2BD1cXhtVSjtr3L
    • Davies TJ et al (2008) Colloquium paper: phylogenetic trees and the future of mammalian biodiversity. Proc Natl Acad Sci USA 105(Suppl 1):11556-11563
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.SUPPL. 1 , pp. 11556-11563
    • Davies, T.J.1
  • 34
    • 65749102640 scopus 로고    scopus 로고
    • Geographical variation in predictors of mammalian extinction risk: Big is bad, but only in the tropics
    • 19392714 10.1111/j.1461-0248.2009.01307.x
    • Fritz SA, Bininda-Emonds OR, Purvis A (2009) Geographical variation in predictors of mammalian extinction risk: big is bad, but only in the tropics. Ecol Lett 12(6):538-549
    • (2009) Ecol Lett , vol.12 , Issue.6 , pp. 538-549
    • Fritz, S.A.1    Bininda-Emonds, O.R.2    Purvis, A.3
  • 35
    • 77955131140 scopus 로고    scopus 로고
    • A primitive hyracoid (Mammalia, Paenungulata) from the early Priabonian (Late Eocene) of Egypt
    • Barrow EC, Seiffert ER, Simons EL (2010) A primitive hyracoid (Mammalia, Paenungulata) from the early Priabonian (Late Eocene) of Egypt. J Syst Palaeontol 8(2):213-244
    • (2010) J Syst Palaeontol , vol.8 , Issue.2 , pp. 213-244
    • Barrow, E.C.1    Seiffert, E.R.2    Simons, E.L.3
  • 36
    • 0032432842 scopus 로고    scopus 로고
    • Complete mitochondrial genome of a neotropical fruit bat, Artibeus jamaicensis, and a new hypothesis of the relationships of bats to other eutherian mammals
    • 9847413 10.1007/PL00006430 1:CAS:528:DyaK1cXotVGisLs%3D
    • Pumo DE et al (1998) Complete mitochondrial genome of a neotropical fruit bat, Artibeus jamaicensis, and a new hypothesis of the relationships of bats to other eutherian mammals. J Mol Evol 47(6):709-717
    • (1998) J Mol Evol , vol.47 , Issue.6 , pp. 709-717
    • Pumo, D.E.1
  • 37
    • 0035929321 scopus 로고    scopus 로고
    • Origin of whales from early artiodactyls: Hands and feet of Eocene Protocetidae from Pakistan
    • 11567134 10.1126/science.1063902 1:CAS:528:DC%2BD3MXntFCrtr4%3D
    • Gingerich PD et al (2001) Origin of whales from early artiodactyls: hands and feet of Eocene Protocetidae from Pakistan. Science 293(5538):2239-2242
    • (2001) Science , vol.293 , Issue.5538 , pp. 2239-2242
    • Gingerich, P.D.1
  • 38
    • 84857422378 scopus 로고    scopus 로고
    • Updating the evolutionary history of Carnivora (Mammalia): A new species-level supertree complete with divergence time estimates
    • 22369503 10.1186/1741-7007-10-12
    • Nyakatura K, Bininda-Emonds OR (2012) Updating the evolutionary history of Carnivora (Mammalia): a new species-level supertree complete with divergence time estimates. BMC Biol 10:12
    • (2012) BMC Biol , vol.10 , pp. 12
    • Nyakatura, K.1    Bininda-Emonds, O.R.2
  • 39
    • 0037417891 scopus 로고    scopus 로고
    • Placental mammal diversification and the Cretaceous-Tertiary boundary
    • 12552136 10.1073/pnas.0334222100 1:CAS:528:DC%2BD3sXhtF2gtrw%3D
    • Springer MS et al (2003) Placental mammal diversification and the Cretaceous-Tertiary boundary. Proc Natl Acad Sci USA 100(3):1056-1061
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.3 , pp. 1056-1061
    • Springer, M.S.1
  • 40
    • 77953128894 scopus 로고    scopus 로고
    • Pattern and timing of diversification of the mammalian order Carnivora inferred from multiple nuclear gene sequences
    • 20138220 10.1016/j.ympev.2010.01.033 1:CAS:528:DC%2BC3cXmvVWgtbs%3D
    • Eizirik E et al (2010) Pattern and timing of diversification of the mammalian order Carnivora inferred from multiple nuclear gene sequences. Mol Phylogenet Evol 56(1):49-63
    • (2010) Mol Phylogenet Evol , vol.56 , Issue.1 , pp. 49-63
    • Eizirik, E.1
  • 41
    • 0032558856 scopus 로고    scopus 로고
    • Primate evolution - In and out of Africa
    • (author reply 747-748)
    • Groves C (1998) Primate evolution - in and out of Africa. Curr Biol 8(21):R747 (author reply 747-748)
    • (1998) Curr Biol , vol.8 , Issue.21
    • Groves, C.1
  • 42
    • 3343008856 scopus 로고    scopus 로고
    • Timing the origin of New World monkeys
    • 12832653 10.1093/molbev/msg172 1:CAS:528:DC%2BD3sXotlWjs74%3D
    • Schrago CG, Russo CA (2003) Timing the origin of New World monkeys. Mol Biol Evol 20(10):1620-1625
    • (2003) Mol Biol Evol , vol.20 , Issue.10 , pp. 1620-1625
    • Schrago, C.G.1    Russo, C.A.2
  • 43
    • 74949130464 scopus 로고    scopus 로고
    • A fully resolved genus level phylogeny of neotropical primates (Platyrrhini)
    • 19632342 10.1016/j.ympev.2009.07.019 1:CAS:528:DC%2BD1MXhsVymsLzP
    • Wildman DE et al (2009) A fully resolved genus level phylogeny of neotropical primates (Platyrrhini). Mol Phylogenet Evol 53(3):694-702
    • (2009) Mol Phylogenet Evol , vol.53 , Issue.3 , pp. 694-702
    • Wildman, D.E.1
  • 44
    • 80051774778 scopus 로고    scopus 로고
    • In vivo safety and persistence of endoribonuclease gene-transduced CD4+ T cells in cynomolgus macaques for HIV-1 gene therapy model
    • 21858176 10.1371/journal.pone.0023585 1:CAS:528:DC%2BC3MXhtFKmsb%2FN
    • Chono H et al (2011) In vivo safety and persistence of endoribonuclease gene-transduced CD4+ T cells in cynomolgus macaques for HIV-1 gene therapy model. PLoS One 6(8):e23585
    • (2011) PLoS One , vol.6 , Issue.8 , pp. 23585
    • Chono, H.1
  • 45
    • 84855584286 scopus 로고    scopus 로고
    • The use of nonhuman primate models of HIV infection for the evaluation of antiviral strategies
    • 21902451 10.1089/aid.2011.0234
    • Van Rompay KK (2012) The use of nonhuman primate models of HIV infection for the evaluation of antiviral strategies. AIDS Res Hum Retroviruses 28(1):16-35
    • (2012) AIDS Res Hum Retroviruses , vol.28 , Issue.1 , pp. 16-35
    • Van Rompay, K.K.1
  • 46
    • 0042810677 scopus 로고    scopus 로고
    • EST analyses predict the existence of a population of chimeric microRNA precursor-mRNA transcripts expressed in normal human and mouse tissues
    • 12844357 10.1186/gb-2003-4-7-403
    • Smalheiser NR (2003) EST analyses predict the existence of a population of chimeric microRNA precursor-mRNA transcripts expressed in normal human and mouse tissues. Genome Biol 4(7):403
    • (2003) Genome Biol , vol.4 , Issue.7 , pp. 403
    • Smalheiser, N.R.1
  • 47
    • 33644919969 scopus 로고    scopus 로고
    • Primate microRNAs miR-220 and miR-492 lie within processed pseudogenes
    • 16489141 10.1093/jhered/esj022 1:CAS:528:DC%2BD28XitVOqsbo%3D
    • Devor EJ (2006) Primate microRNAs miR-220 and miR-492 lie within processed pseudogenes. J Hered 97(2):186-190
    • (2006) J Hered , vol.97 , Issue.2 , pp. 186-190
    • Devor, E.J.1
  • 48
    • 68249084505 scopus 로고    scopus 로고
    • Small RNAs originated from pseudogenes: Cis- or trans-acting?
    • 19649160 10.1371/journal.pcbi.1000449
    • Guo X et al (2009) Small RNAs originated from pseudogenes: cis- or trans-acting? PLoS Comput Biol 5(7):e1000449
    • (2009) PLoS Comput Biol , vol.5 , Issue.7 , pp. 1000449
    • Guo, X.1
  • 49
    • 4644309196 scopus 로고    scopus 로고
    • The functions of animal microRNAs
    • 15372042 10.1038/nature02871 1:CAS:528:DC%2BD2cXnsFaiu7g%3D
    • Ambros V (2004) The functions of animal microRNAs. Nature 431(7006):350-355
    • (2004) Nature , vol.431 , Issue.7006 , pp. 350-355
    • Ambros, V.1
  • 50
    • 0034525032 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk
    • 11092937 10.1107/S0907444900012890 1:STN:280:DC%2BD3M%2Fpt1Kisw%3D%3D
    • Eger BT et al (2000) Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallogr D Biol Crystallogr 56(Pt 12):1656-1658
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , Issue.PART 12 , pp. 1656-1658
    • Eger, B.T.1
  • 51
    • 0037816302 scopus 로고    scopus 로고
    • Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase
    • 12817083 10.1073/pnas.1431485100 1:CAS:528:DC%2BD3sXlsFGnsLo%3D
    • Kuwabara Y et al (2003) Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase. Proc Natl Acad Sci USA 100(14):8170-8175
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.14 , pp. 8170-8175
    • Kuwabara, Y.1
  • 52
    • 0033742183 scopus 로고    scopus 로고
    • The role of the [2Fe-2s] cluster centers in xanthine oxidoreductase
    • 11132637 10.1016/S0162-0134(00)00165-3 1:CAS:528:DC%2BD3cXotlCrtrc%3D
    • Nishino T, Okamoto K (2000) The role of the [2Fe-2s] cluster centers in xanthine oxidoreductase. J Inorg Biochem 82(1-4):43-49
    • (2000) J Inorg Biochem , vol.82 , Issue.1-4 , pp. 43-49
    • Nishino, T.1    Okamoto, K.2
  • 53
    • 0033735625 scopus 로고    scopus 로고
    • The structure of the nasal chemosensory system in squamate reptiles. 2. Lubricatory capacity of the vomeronasal organ
    • 10878859 1:STN:280:DC%2BD3cvpsVOltg%3D%3D
    • Rehorek SJ, Firth BT, Hutchinson MN (2000) The structure of the nasal chemosensory system in squamate reptiles. 2. Lubricatory capacity of the vomeronasal organ. J Biosci 25(2):181-190
    • (2000) J Biosci , vol.25 , Issue.2 , pp. 181-190
    • Rehorek, S.J.1    Firth, B.T.2    Hutchinson, M.N.3
  • 54
    • 0033745147 scopus 로고    scopus 로고
    • The structure of the nasal chemosensory system in squamate reptiles. 1. The olfactory organ, with special reference to olfaction in geckos
    • 10878858 1:STN:280:DC%2BD3cvpsVOlsQ%3D%3D
    • Rehorek SJ, Firth BT, Hutchinson MN (2000) The structure of the nasal chemosensory system in squamate reptiles. 1. The olfactory organ, with special reference to olfaction in geckos. J Biosci 25(2):173-179
    • (2000) J Biosci , vol.25 , Issue.2 , pp. 173-179
    • Rehorek, S.J.1    Firth, B.T.2    Hutchinson, M.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.