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Volumn 43, Issue 3, 2011, Pages 374-386

Increasing recognition of the importance of aldehyde oxidase in drug development and discovery

Author keywords

AOX1; Cancer; Drug metabolism; Molybdenum; Obesity; Prodrugs; Xanthine oxidase

Indexed keywords

5 FLUORO 2 PYRIMIDINONE; 5 IODO 2 PYRIMIDINONE 2 DEOXYRIBOSE; ADIPONECTIN; ALDEHYDE OXIDASE; ALDEHYDE OXIDASE 1; ALDEHYDE OXIDASE 3; ALDEHYDE OXIDASE 3L1; ALDEHYDE OXIDASE 4; BETA CARBOLINE; CHLORPROMAZINE; FENOFIBRATE; HETEROCYCLIC COMPOUND; ISOENZYME; MENADIONE; MESSENGER RNA; N(1) METHYL 2 PYRIDINE 5 CARBOXAMIDE; PYRIMIDINE ANTAGONIST; RALOXIFENE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG; XANTHINE OXIDASE; XENOBIOTIC AGENT; ZEBULARINE;

EID: 79960719085     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.3109/03602532.2011.560606     Document Type: Article
Times cited : (101)

References (134)
  • 3
    • 0019487878 scopus 로고
    • Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. Characterization and cytochemical localization
    • Badwey, J. A., Robinson, J. M., Karnovsky, M. J., Karnovsky, M. L. (1981). Superoxide production by an unusual aldehyde oxidase in guinea pig granulocytes. Characterization and cytochemical localization. J Biol Chem 256:3479-3486. (Pubitemid 11082515)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.7 , pp. 3479-3486
    • Badwey, J.A.1    Robinson, J.M.2    Karnovsky, M.J.3    Karnovsky, M.L.4
  • 4
    • 3543056459 scopus 로고    scopus 로고
    • Purification and biochemical characterization of simplified eukaryotic nitrate reductase expressed in Pichia pastoris
    • DOI 10.1016/j.pep.2004.05.021, PII S1046592804001895
    • Barbier, G. G., Joshi, R. C., Campbell, E. R., Campbell, W. H. (2004). Purifcation and biochemical characterization of simplifed eukaryotic nitrate reductase expressed in Pichia pastoris. Protein Expr Purif 37:61-71. (Pubitemid 39027244)
    • (2004) Protein Expression and Purification , vol.37 , Issue.1 , pp. 61-71
    • Barbier, G.G.1    Joshi, R.C.2    Campbell, E.R.3    Campbell, W.H.4
  • 5
    • 0023528062 scopus 로고
    • Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specifcity
    • Beedham, C (1987). Molybdenum hydroxylases: biological distribution and substrate-inhibitor specifcity. Prog Med Chem 24:85-127.
    • (1987) Prog Med Chem , vol.24 , pp. 85-127
    • Beedham, C.1
  • 6
    • 0030772328 scopus 로고    scopus 로고
    • The role of non-P450 enzymes in drug oxidation
    • DOI 10.1023/A:1008668913093
    • Beedham, C. (1997). Te role of non-P450 enzymes in drug oxidation. Pharm World Sci 19:255-263. (Pubitemid 27511692)
    • (1997) Pharmacy World and Science , vol.19 , Issue.6 , pp. 255-263
    • Beedham, C.1
  • 7
    • 18544365698 scopus 로고    scopus 로고
    • Gene-expression profles predict survival of patients with lung adenocarcinoma
    • Beer, D. G., Kardia, S. L., Huang, C. C., Giordano, T. J., Levin, A. M., Misek, D. E., et al. (2002). Gene-expression profles predict survival of patients with lung adenocarcinoma. Nat Med 8:816-824.
    • (2002) Nat Med , vol.8 , pp. 816-824
    • Beer, D.G.1    Kardia, S.L.2    Huang, C.C.3    Giordano, T.J.4    Levin, A.M.5    Misek, D.E.6
  • 8
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von-Hippel Lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • Beroukhim, R., Brunet, J. P., Di Napoli, A., Mertz, K. D., Seeley, A., Pires, M. M., et al. (2009). Patterns of gene expression and copy-number alterations in von-Hippel Lindau disease-associated and sporadic clear cell carcinoma of the kidney. Cancer Res 69:4674-4681.
    • (2009) Cancer Res , vol.69 , pp. 4674-4681
    • Beroukhim, R.1    Brunet, J.P.2    Di Napoli, A.3    Mertz, K.D.4    Seeley, A.5    Pires, M.M.6
  • 9
    • 38049100456 scopus 로고    scopus 로고
    • Assessing the signifcance of chromosomal aberrations in cancer: Methodology and application to glioma
    • Beroukhim, R., Getz, G., Nghiemphu, L., Barretina, J., Hsueh, T., Linhart, D., et al. (2007). Assessing the signifcance of chromosomal aberrations in cancer: methodology and application to glioma. Proc Natl Acad Sci USA 104:20007-20012.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20007-20012
    • Beroukhim, R.1    Getz, G.2    Nghiemphu, L.3    Barretina, J.4    Hsueh, T.5    Linhart, D.6
  • 11
    • 20144368274 scopus 로고    scopus 로고
    • High-resolution genome-wide mapping of genetic alterations in human glial brain tumors
    • DOI 10.1158/0008-5472.CAN-04-4229
    • Bredel, M., Bredel, C., Juric, D., Harsh, G. R., Vogel, H., Recht, L. D., et al. (2005). High-resolution genome-wide mapping of genetic alterations in human glial brain tumors. Cancer Res 65:4088-4096. (Pubitemid 40775645)
    • (2005) Cancer Research , vol.65 , Issue.10 , pp. 4088-4096
    • Bredel, M.1    Bredel, C.2    Juric, D.3    Harsh, G.R.4    Vogel, H.5    Recht, L.D.6    Sikic, B.I.7
  • 13
    • 0018857782 scopus 로고
    • Cyclophosphamide potentiation and aldehyde oxidase inhibition by phosphorylated aldehydes and acetals
    • Cates, L. A., Jones, G. S., Jr., Good, D. J., Tsai, H. Y., Li, V. S., Caron, N., et al. (1980). Cyclophosphamide potentiation and aldehyde oxidase inhibition by phosphorylated aldehydes and acetals. J Med Chem 23:300-304. (Pubitemid 10129974)
    • (1980) Journal of Medicinal Chemistry , vol.23 , Issue.3 , pp. 300-304
    • Cates, L.A.1    Jones Jr., G.S.2    Good, D.J.3
  • 14
    • 0026762436 scopus 로고
    • Conversion of 5-iodo-2-pyrimidinone-2'-deoxyribose to 5-iodo-deoxyuridine by aldehyde oxidase. Implication in hepatotropic drug design
    • Chang, C. N., Doong, S. L., Cheng, Y. C. (1992). Conversion of 5-iodo-2-pyrimidinone-2'-deoxyribose to 5-iodo-deoxyuridine by aldehyde oxidase. Implication in hepatotropic drug design. Biochem Pharmacol 43:2269-2273.
    • (1992) Biochem Pharmacol , vol.43 , pp. 2269-2273
    • Chang, C.N.1    Doong, S.L.2    Cheng, Y.C.3
  • 19
    • 0021836751 scopus 로고
    • In vitro pigment formation from tryptamine. Role of indole-3-acetaldehyde
    • DOI 10.1016/0006-2952(85)90564-7
    • Das, P. K., Guha, S. R. (1985). In vitro pigment formation from tryptamine. Role of indole-3-acetaldehyde. Biochem Pharmacol 34:2663-2667. (Pubitemid 15041749)
    • (1985) Biochemical Pharmacology , vol.34 , Issue.15 , pp. 2663-2667
    • Das, P.K.1    Guha, S.R.2
  • 20
    • 0032711085 scopus 로고    scopus 로고
    • Te mouse aldehyde oxidase gene: Molecular cloning, chromosomal mapping, and functional characterization of the 5'-fanking region
    • Demontis, S., Kurosaki, M., Saccone, S., Motta, S., Garattini, E., Terao, M. (1999). Te mouse aldehyde oxidase gene: molecular cloning, chromosomal mapping, and functional characterization of the 5'-fanking region. Biochim Biophys Acta 1489:207-222.
    • (1999) Biochim Biophys Acta , vol.1489 , pp. 207-222
    • Demontis, S.1    Kurosaki, M.2    Saccone, S.3    Motta, S.4    Garattini, E.5    Terao, M.6
  • 21
    • 21344445924 scopus 로고    scopus 로고
    • Analysis of hypoxia-related gene expression in sarcomas and effect of hypoxia on RNA interference of vascular endothelial cell growth factor A
    • DOI 10.1158/0008-5472.CAN-04-4078
    • Detwiller, K. Y., Fernando, N. T., Segal, N. H., Ryeom, S. W., D'Amore, P. A., Yoon, S. S. (2005). Analysis of hypoxia-related gene expression in sarcomas and efect of hypoxia on RNA interference of vascular endothelial cell growth factor A. Cancer Res 65:5881-5889. (Pubitemid 40911194)
    • (2005) Cancer Research , vol.65 , Issue.13 , pp. 5881-5889
    • Detwiller, K.Y.1    Fernando, N.T.2    Segal, N.H.3    Ryeom, S.W.4    D'Amore, P.A.5    Yoon, S.S.6
  • 22
    • 2542565666 scopus 로고    scopus 로고
    • Gene expression in the urinary bladder: A common carcinoma in situ gene expression signature exists disregarding histopathological classification
    • DOI 10.1158/0008-5472.CAN-03-3620
    • Dyrskjot, L., Kruhofer, M., Tykjaer, T., Marcussen, N., Jensen, J. L., Moller, K., et al. (2004). Gene expression in the urinary bladder: a common carcinoma in situ gene expression signature exists disregarding histopathological classifcation. Cancer Res 64:4040-4048. (Pubitemid 38697320)
    • (2004) Cancer Research , vol.64 , Issue.11 , pp. 4040-4048
    • Dyrskjot, L.1    Kruhoffer, M.2    Thykjaer, T.3    Marcussen, N.4    Jensen, J.L.5    Moller, K.6    Orntoft, T.F.7
  • 23
    • 0034525032 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray diffraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk
    • DOI 10.1107/S0907444900012890
    • Eger, B. T., Okamoto, K., Enroth, C., Sato, M., Nishino, T., Pai, E. F. (2000). Purifcation, crystallization, and preliminary X-ray difraction studies of xanthine dehydrogenase and xanthine oxidase isolated from bovine milk. Acta Crystallogr D Biol Crystallogr 56:1656-1658. (Pubitemid 32040029)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.12 , pp. 1656-1658
    • Eger, B.T.1    Okamoto, K.2    Enroth, C.3    Sato, M.4    Nishino, T.5    Pai, E.F.6    Nishino, T.7
  • 24
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • Enroth, C., Eger, B. T., Okamoto, K., Nishino, T., Pai, E. F. (2000). Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc Natl Acad Sci USA 97:10723-10728.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Pai, E.F.5
  • 26
    • 22544435739 scopus 로고    scopus 로고
    • Structural basis of eukaryotic nitrate reduction: Crystal structures of the nitrate reductase active site
    • DOI 10.1105/tpc.104.029694
    • Fischer, K., Barbier, G. G., Hecht, H. J., Mendel, R. R., Campbell, W. H., Schwarz, G. (2005). Structural basis of eukaryotic nitrate reduction: crystal structures of the nitrate reductase active site. Plant Cell 17:1167-1179. (Pubitemid 43142134)
    • (2005) Plant Cell , vol.17 , Issue.4 , pp. 1167-1179
    • Fischer, K.1    Barbier, G.G.2    Hecht, H.-J.3    Mendel, R.R.4    Campbell, W.H.5    Schwarz, G.6
  • 27
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: Genetics, evolution, and biochemistry
    • Garattini, E., Fratelli, M., Terao, M. (2008). Mammalian aldehyde oxidases: genetics, evolution, and biochemistry. Cell Mol Life Sci 65:1019-1048.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 28
    • 76249096555 scopus 로고    scopus 로고
    • Te mammalian aldehyde oxidase gene family
    • Garattini, E., Fratelli, M., Terao, M. (2009). Te mammalian aldehyde oxidase gene family. Hum Genomics 4:119-130.
    • (2009) Hum Genomics , vol.4 , pp. 119-130
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 29
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • DOI 10.1042/BJ20030121
    • Garattini, E., Mendel, R., Romao, M. J., Wright, R., Terao, M. (2003). Mammalian molybdo-favoenzymes, an expanding family of proteins: structure, genetics, regulation, function, and pathophysiology. Biochem J 372:15-32. (Pubitemid 36609603)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 30
    • 0242383272 scopus 로고    scopus 로고
    • Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria
    • DOI 10.1093/ndt/gfg385
    • Gok, F. , Ichida, K., Topaloglu, R. (2003). Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria. Nephrol Dial Transpl 18:2278-2283. (Pubitemid 37336814)
    • (2003) Nephrology Dialysis Transplantation , vol.18 , Issue.11 , pp. 2278-2283
    • Gok, F.1    Ichida, K.2    Topaloglu, R.3
  • 31
    • 36749103200 scopus 로고    scopus 로고
    • The dual substrate specificity of aldehyde oxidase 1 for retinal and acetaldehyde and its role in ABCA1 mediated efflux
    • DOI 10.1055/s-2007-992126
    • Graessler, J., Fischer, S. (2007). Te dual substrate specifcity of aldehyde oxidase 1 for retinal and acetaldehyde and its role in ABCA1 mediated efux. Horm Metab Res 39:775-776. (Pubitemid 350206896)
    • (2007) Hormone and Metabolic Research , vol.39 , Issue.11 , pp. 775-776
    • Graessler, J.1    Fischer, S.2
  • 33
    • 0028987176 scopus 로고
    • 5-fuoro-2-pyrimidinone, a liver aldehyde oxidase-activated prodrug of 5-fuorouracil
    • Guo, X., Lerner-Tung, M., Chen, H. X., Chang, C. N., Zhu, J. L., Chang, C. P., et al. (1995). 5-fuoro-2-pyrimidinone, a liver aldehyde oxidase-activated prodrug of 5-fuorouracil. Biochem Pharmacol 49:1111-1116.
    • (1995) Biochem Pharmacol , vol.49 , pp. 1111-1116
    • Guo, X.1    Lerner-Tung, M.2    Chen, H.X.3    Chang, C.N.4    Zhu, J.L.5    Chang, C.P.6
  • 35
    • 0023037533 scopus 로고
    • Aldehyde oxidase from rabbit liver: Specificity toward purines and their analogs
    • DOI 10.1016/0003-9861(86)90048-2
    • Hall, W. W., Krenitsky, T. A. (1986). Aldehyde oxidase from rabbit liver: specifcity toward purines and their analogs. Arch Biochem Biophys 251:36-46. (Pubitemid 17192981)
    • (1986) Archives of Biochemistry and Biophysics , vol.251 , Issue.1 , pp. 36-46
    • Hall, W.W.1    Krenitsky, T.A.2
  • 36
    • 33748117784 scopus 로고    scopus 로고
    • Gene Expression Profiling Reveals Stromal Genes Expressed in Common Between Barrett's Esophagus and Adenocarcinoma
    • DOI 10.1053/j.gastro.2006.04.026, PII S0016508506008158
    • Hao, Y., Triadaflopoulos, G., Sahbaie, P., Young, H. S., Omary, M. B., Lowe, A. W. (2006). Gene expression profling reveals stromal genes expressed in common between Barrett's esophagus and adenocarcinoma. Gastroenterology 131:925-933. (Pubitemid 44307058)
    • (2006) Gastroenterology , vol.131 , Issue.3 , pp. 925-933
    • Hao, Y.1    Triadafilopoulos, G.2    Sahbaie, P.3    Young, H.S.4    Omary, M.B.5    Lowe, A.W.6
  • 37
    • 32944462571 scopus 로고    scopus 로고
    • Fibroblast growth factor 9 has oncogenic activity and is a downstream target of Wnt signaling in ovarian endometrioid adenocarcinomas
    • DOI 10.1158/0008-5472.CAN-05-3694
    • Hendrix, N. D., Wu, R., Kuick, R., Schwartz, D. R., Fearon, E. R., Cho, K. R. (2006). Fibroblast growth factor 9 has oncogenic activity and is a downstream target of Wnt signaling in ovarian endometrioid adenocarcinomas. Cancer Res 66:1354-1362. (Pubitemid 43259914)
    • (2006) Cancer Research , vol.66 , Issue.3 , pp. 1354-1362
    • Hendrix, N.D.1    Wu, R.2    Kuick, R.3    Schwartz, D.R.4    Fearon, E.R.5    Cho, K.R.6
  • 38
    • 1842741259 scopus 로고    scopus 로고
    • Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: Differential gene expression and enzyme activities
    • DOI 10.1074/jbc.M312929200
    • Hesberg, C., Hansch, R., Mendel, R. R., Bittner, F. (2004). Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: diferential gene expression and enzyme activities. J Biol Chem 279:13547-13554. (Pubitemid 38468880)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 13547-13554
    • Hesberg, C.1    Hansch, R.2    Mendel, R.R.3    Bittner, F.4
  • 39
    • 0029347181 scopus 로고
    • Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase
    • Hille, R., Nishino, T. (1995). Flavoprotein structure and mechanism. 4. Xanthine oxidase and xanthine dehydrogenase. FASEB J 9:995-1003.
    • (1995) FASEB J , vol.9 , pp. 995-1003
    • Hille, R.1    Nishino, T.2
  • 40
    • 0017154664 scopus 로고
    • Oxidation of selected pteridine derivatives by mamalian liver xanthine oxidase and aldehyde oxidase
    • Hodnett, C. N., McCormack, J. J., Sabean, J. A. (1976). Oxidation of selected pteridine derivatives by mamalian liver xanthine oxidase and aldehyde oxidase. J Pharm Sci 65:1150-1154.
    • (1976) J Pharm Sci , vol.65 , pp. 1150-1154
    • Hodnett, C.N.1    McCormack, J.J.2    Sabean, J.A.3
  • 43
    • 33749263503 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray
    • DOI 10.1016/j.lfs.2006.06.019, PII S0024320506004826
    • Hu, R., Xu, C., Shen, G., Jain, M. R., Khor, T. O., Gopalkrishnan, A., et al. (2006). Identifcation of Nrf2-regulated genes induced by chemopreventive isothiocyanate PEITC by oligonucleotide microarray. Life Sci 79:1944-1955. (Pubitemid 44485118)
    • (2006) Life Sciences , vol.79 , Issue.20 , pp. 1944-1955
    • Hu, R.1    Xu, C.2    Shen, G.3    Jain, M.R.4    Khor, T.Oo.5    Gopalkrishnan, A.6    Lin, W.7    Reddy, B.8    Chan, J.Y.9    Kong, A.-N.T.10
  • 44
    • 0033560621 scopus 로고    scopus 로고
    • Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli
    • DOI 10.1006/abbi.1999.1129
    • Huang, D. Y., Furukawa, A., Ichikawa, Y. (1999). Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch Biochem Biophys 364:264-272. (Pubitemid 29394280)
    • (1999) Archives of Biochemistry and Biophysics , vol.364 , Issue.2 , pp. 264-272
    • Huang, D.-Y.1    Furukawa, A.2    Ichikawa, Y.3
  • 46
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • Ignarro, L. J., Buga, G. M., Wood, K. S., Byrns, R. E., Chaudhuri, G. (1987). Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc Natl Acad Sci USA 84:9265-9269.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 48
    • 0014124340 scopus 로고
    • Human liver aldehyde oxidase: Diferential inhibition of oxidation of charged and uncharged substrates
    • Johns, D. G. (1967). Human liver aldehyde oxidase: diferential inhibition of oxidation of charged and uncharged substrates. J Clin Invest 46:1492-1505.
    • (1967) J Clin Invest , vol.46 , pp. 1492-1505
    • Johns, D.G.1
  • 49
    • 0015627462 scopus 로고
    • Dialkyl esters of methotrexate and 3′,5′- dichloromethotrexate: Synthesis and interaction with aldehyde oxidase and dihydrofolate reductase
    • Johns, D. G., Farquhar, D., Wolpert, M. K., Chabner, B. A., Loo, T. L. (1973). Dialkyl esters of methotrexate and 3′,5′- dichloromethotrexate: synthesis and interaction with aldehyde oxidase and dihydrofolate reductase. Drug Metab Dispos 1:580-589.
    • (1973) Drug Metab Dispos , vol.1 , pp. 580-589
    • Johns, D.G.1    Farquhar, D.2    Wolpert, M.K.3    Chabner, B.A.4    Loo, T.L.5
  • 50
    • 39749137048 scopus 로고    scopus 로고
    • Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer
    • Kaiser, S., Park, Y. K., Franklin, J. L., Halberg, R. B., Yu, M., Jessen, W. J., et al. (2007). Transcriptional recapitulation and subversion of embryonic colon development by mouse colon tumor models and human colon cancer. Genome Biol 8:R131.
    • (2007) Genome Biol , vol.8
    • Kaiser, S.1    Park, Y.K.2    Franklin, J.L.3    Halberg, R.B.4    Yu, M.5    Jessen, W.J.6
  • 52
    • 33846264538 scopus 로고    scopus 로고
    • Nrf2-deficient mice have an increased susceptibility to dextran sulfate sodium-induced colitis
    • DOI 10.1158/0008-5472.CAN-06-3562
    • Khor, T. O., Huang, M. T., Kwon, K. H., Chan, J. Y., Reddy, B. S., Kong, A. N. (2006). Nrf2-defcient mice have an increased susceptibility to dextran sulfate sodium-induced colitis. Cancer Res 66:11580-11584. (Pubitemid 46094166)
    • (2006) Cancer Research , vol.66 , Issue.24 , pp. 11580-11584
    • Khor, T.O.1    Huang, M.-T.2    Kwon, K.H.3    Chan, J.Y.4    Reddy, B.S.5    Kong, A.-N.6
  • 53
    • 34648831071 scopus 로고    scopus 로고
    • Whole genome analysis for liver metastasis gene signatures in colorectal cancer
    • Ki, D. H., Jeung, H. C., Park, C. H., Kang, S. H., Lee, G. Y., Lee, W. S., et al. (2007). Whole genome analysis for liver metastasis gene signatures in colorectal cancer. Int J Cancer 121:2005-2012.
    • (2007) Int J Cancer , vol.121 , pp. 2005-2012
    • Ki, D.H.1    Jeung, H.C.2    Park, C.H.3    Kang, S.H.4    Lee, G.Y.5    Lee, W.S.6
  • 54
    • 0028337391 scopus 로고
    • An in vivo comparison of oral 5-iodo-2'-deoxyuridine and 5-iodo-2-pyrimidinone-2'-deoxyribose toxicity, pharmacokinetics, and DNA incorporation in athymic mouse tissues and the human colon cancer xenograft, HCT-116
    • Kinsella, T. J., Kunugi, K. A., Vielhuber, K. A., McCulloch, W., Liu, S. H., Cheng, Y. C. (1994). An in vivo comparison of oral 5-iodo-2'-deoxyuridine and 5-iodo-2-pyrimidinone-2'-deoxyribose toxicity, pharmacokinetics, and DNA incorporation in athymic mouse tissues and the human colon cancer xenograft, HCT-116. Cancer Res 54:2695-2700.
    • (1994) Cancer Res , vol.54 , pp. 2695-2700
    • Kinsella, T.J.1    Kunugi, K.A.2    Vielhuber, K.A.3    McCulloch, W.4    Liu, S.H.5    Cheng, Y.C.6
  • 55
    • 0031931512 scopus 로고    scopus 로고
    • Preclinical evaluation of 5-iodo-2-pyrimidinone-2'-deoxyribose as a prodrug for 5-iodo-2'-deoxyuridine-mediated radiosensitization in mouse and human tissues
    • Kinsella, T. J., Kunugi, K. A., Vielhuber, K. A., Potter, D. M., Fitzsimmons, M. E., Collins, J. M. (1998). Preclinical evaluation of 5-iodo-2-pyrimidinone-2′-deoxyribose as a prodrug for 5-iodo-2′- deoxyuridine-mediated radiosensitization in mouse and human tissues. Clin Cancer Res 4:99-109. (Pubitemid 28062883)
    • (1998) Clinical Cancer Research , vol.4 , Issue.1 , pp. 99-109
    • Kinsella, T.J.1    Kunugi, K.A.2    Vielhuber, K.A.3    Potter, D.M.4    Fitzsimmons, M.E.5    Collins, J.M.6
  • 56
    • 0033813259 scopus 로고    scopus 로고
    • Preclinical study of the systemic toxicity and pharmacokinetics of 5-iodo-2-deoxypyrimidinone-2′;-deoxyribose as a radiosensitizing prodrug in two, non-rodent animal species: Implications for phase i study design
    • Kinsella, T. J., Schupp, J. E., Davis, T. W., Berry, S. E., Hwang, H. S., Warren, K., et al (2000). Preclinical study of the systemic toxicity and pharmacokinetics of 5-iodo-2-deoxypyrimidinone-2′;-deoxyribose as a radiosensitizing prodrug in two, non-rodent animal species: implications for phase I study design. Clin Cancer Res 6:3670-3679.
    • (2000) Clin Cancer Res , vol.6 , pp. 3670-3679
    • Kinsella, T.J.1    Schupp, J.E.2    Davis, T.W.3    Berry, S.E.4    Hwang, H.S.5    Warren, K.6
  • 59
    • 33947723940 scopus 로고    scopus 로고
    • Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues
    • DOI 10.1016/j.abb.2006.12.032, PII S0003986107000094
    • Kundu, T. K., Hille, R., Velayutham, M., Zweier, J. L. (2007). Characterization of superoxide production from aldehyde oxidase: an important source of oxidants in biological tissues. Arch Biochem Biophys 460:113-121. (Pubitemid 46505003)
    • (2007) Archives of Biochemistry and Biophysics , vol.460 , Issue.1 , pp. 113-121
    • Kundu, T.K.1    Hille, R.2    Velayutham, M.3    Zweier, J.L.4
  • 60
    • 0033166759 scopus 로고    scopus 로고
    • Molecular cloning of the cDNA coding for mouse aldehyde oxidase: Tissue distribution and regulation in vivo by testosterone
    • DOI 10.1042/0264-6021:3410071
    • Kurosaki, M., Demontis, S., Barzago, M. M., Garattini, E., Terao, M. (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. (Pubitemid 29359049)
    • (1999) Biochemical Journal , vol.341 , Issue.1 , pp. 71-80
    • Kurosaki, M.1    Demontis, S.2    Barzago, M.M.3    Garattini, E.4    Terao, M.5
  • 61
    • 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
    • DOI 10.1074/jbc.M408734200
    • Kurosaki, M., Terao, M., Barzago, M. M., Bastone, A., Bernardinello, D., Salmona, M., et al. (2004). Te aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdo-favoenzyme family with selective expression in the olfactory mucosa. J Biol Chem 279:50482-50498. (Pubitemid 39577867)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 50482-50498
    • Kurosaki, M.1    Terao, M.2    Barzago, M.M.3    Bastone, A.4    Bernardinello, D.5    Salmona, M.6    Garattini, E.7
  • 62
    • 45749140422 scopus 로고    scopus 로고
    • Gene expression signature of cigarette smoking and its role in lung adenocarcinoma development and survival
    • Landi, M. T., Dracheva, T., Rotunno, M., Figueroa, J. D., Liu, H., Dasgupta, A., et al. (2008). Gene expression signature of cigarette smoking and its role in lung adenocarcinoma development and survival. PLoS One 3:e1651.
    • (2008) PLoS One , vol.3
    • Landi, M.T.1    Dracheva, T.2    Rotunno, M.3    Figueroa, J.D.4    Liu, H.5    Dasgupta, A.6
  • 64
    • 33646358694 scopus 로고    scopus 로고
    • Tumor stem cells derived from glioblastomas cultured in bFGF and EGF more closely mirror the phenotype and genotype of primary tumors than do serum-cultured cell lines
    • DOI 10.1016/j.ccr.2006.03.030, PII S1535610806001176
    • Lee, J., Kotliarova, S., Kotliarov, Y., Li, A., Su, Q., Donin, N. M., et al. (2006). Tumor stem cells derived from glioblastomas cultured in bFGF and EGF more closely mirror the phenotype and genotype of primary tumors than do serum-cultured cell lines. Cancer Cell 9:391-403. (Pubitemid 43668737)
    • (2006) Cancer Cell , vol.9 , Issue.5 , pp. 391-403
    • Lee, J.1    Kotliarova, S.2    Kotliarov, Y.3    Li, A.4    Su, Q.5    Donin, N.M.6    Pastorino, S.7    Purow, B.W.8    Christopher, N.9    Zhang, W.10    Park, J.K.11    Fine, H.A.12
  • 65
    • 3042752912 scopus 로고    scopus 로고
    • Previously unidentifed changes in renal cell carcinoma gene expression identifed by parametric analysis of microarray data
    • Lenburg, M. E., Liou, L. S., Gerry, N. P., Frampton, G. M., Cohen, H. T., Christman, M. F. (2003). Previously unidentifed changes in renal cell carcinoma gene expression identifed by parametric analysis of microarray data. BMC Cancer 3:31.
    • (2003) BMC Cancer , vol.3 , pp. 31
    • Lenburg, M.E.1    Liou, L.S.2    Gerry, N.P.3    Frampton, G.M.4    Cohen, H.T.5    Christman, M.F.6
  • 66
    • 49649118849 scopus 로고    scopus 로고
    • Nitric oxide production from nitrite occurs primarily in tissues not in the blood: Critical role of xanthine oxidase and aldehyde oxidase
    • Li, H., Cui, H., Kundu, T. K., Alzawahra, W., Zweier, J. L. (2008). Nitric oxide production from nitrite occurs primarily in tissues not in the blood: critical role of xanthine oxidase and aldehyde oxidase. J Biol Chem 283:17855-17863.
    • (2008) J Biol Chem , vol.283 , pp. 17855-17863
    • Li, H.1    Cui, H.2    Kundu, T.K.3    Alzawahra, W.4    Zweier, J.L.5
  • 67
    • 71749090061 scopus 로고    scopus 로고
    • Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite
    • Li, H., Kundu, T. K., Zweier, J. L. (2009). Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite. J Biol Chem 284:33850-33858.
    • (2009) J Biol Chem , vol.284 , pp. 33850-33858
    • Li, H.1    Kundu, T.K.2    Zweier, J.L.3
  • 68
    • 33646256321 scopus 로고    scopus 로고
    • Sex-determining region y box 4 is a transforming oncogene in human prostate cancer cells
    • Liu, P., Ramachandran, S., Ali Seyed, M., Scharer, C. D., Laycock, N., Dalton, W. B., et al (2006). Sex-determining region Y box 4 is a transforming oncogene in human prostate cancer cells. Cancer Res 66:4011-4019.
    • (2006) Cancer Res , vol.66 , pp. 4011-4019
    • Liu, P.1    Ramachandran, S.2    Ali Seyed, M.3    Scharer, C.D.4    Laycock, N.5    Dalton, W.B.6
  • 69
    • 0038179900 scopus 로고    scopus 로고
    • Molecular profiling of pancreatic adenocarcinoma and chronic pancreatitis identifies multiple genes differentially regulated in pancreatic cancer
    • Logsdon, C. D., Simeone, D. M., Binkley, C., Arumugam, T., Greenson, J. K., Giordano, T. J., et al. (2003). Molecular profling of pancreatic adenocarcinoma and chronic pancreatitis identifes multiple genes diferentially regulated in pancreatic cancer. Cancer Res 63:2649-2657. (Pubitemid 36605209)
    • (2003) Cancer Research , vol.63 , Issue.10 , pp. 2649-2657
    • Logsdon, C.D.1    Simeone, D.M.2    Binkley, C.3    Arumugam, T.4    Greenson, J.K.5    Giordano, T.J.6    Misek, D.E.7    Hanash, S.8
  • 73
    • 0034097952 scopus 로고    scopus 로고
    • Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris
    • Mertens, J. A., Shiraishi, N., Campbell, W. H. (2000). Recombinant expression of molybdenum reductase fragments of plant nitrate reductase at high levels in Pichia pastoris. Plant Physiol 123:743-756. (Pubitemid 30411159)
    • (2000) Plant Physiology , vol.123 , Issue.2 , pp. 743-756
    • Mertens, J.A.1    Shiraishi, N.2    Campbell, W.H.3
  • 74
    • 0028903713 scopus 로고
    • Evidence for free radical generation due to NADH oxidation by aldehyde oxidase during ethanol metabolism
    • Mira, L., Maia, L., Barreira, L., Manso, C. F. (1995). Evidence for free radical generation due to NADH oxidation by aldehyde oxidase during ethanol metabolism. Arch Biochem Biophys 318:53-58.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 53-58
    • Mira, L.1    Maia, L.2    Barreira, L.3    Manso, C.F.4
  • 75
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada, S., Palmer, R. M., Higgs, E. A. (1991). Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 43:109-142.
    • (1991) Pharmacol Rev , vol.43 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 77
    • 34147141506 scopus 로고    scopus 로고
    • Tissue-specifc mRNA expression profles of human phase i metabolizing enzymes except for cytochrome P450 and phase II metabolizing enzymes
    • Nishimura, M., Naito, S. (2006). Tissue-specifc mRNA expression profles of human phase I metabolizing enzymes except for cytochrome P450 and phase II metabolizing enzymes. Drug Metab Pharmacokinet 21:357-374.
    • (2006) Drug Metab Pharmacokinet , vol.21 , pp. 357-374
    • Nishimura, M.1    Naito, S.2
  • 78
    • 0028069815 scopus 로고
    • The conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury
    • Nishino, T. (1994). Te conversion of xanthine dehydrogenase to xanthine oxidase and the role of the enzyme in reperfusion injury. J Biochem 116:1-6. (Pubitemid 24230774)
    • (1994) Journal of Biochemistry , vol.116 , Issue.1 , pp. 1-6
    • Nishino, T.1
  • 79
    • 1842855681 scopus 로고    scopus 로고
    • Purification and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system
    • Nishino, T., Amaya, Y., Kawamoto, S., Kashima, Y., Okamoto, K. (2002). Purifcation and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system. J Biochem 132:597-606. (Pubitemid 35238914)
    • (2002) Journal of Biochemistry , vol.132 , Issue.4 , pp. 597-606
    • Nishino, T.1    Amaya, Y.2    Kawamoto, S.3    Kashima, Y.4    Okamoto, K.5    Nishino, T.6
  • 80
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase - Mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • DOI 10.1111/j.1742-4658.2008.06489.x
    • Nishino, T., Okamoto, K., Eger, B. T., Pai, E. F. (2008). Mammalian xanthine oxidoreductase-mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J 275:3278-3289. (Pubitemid 351813552)
    • (2008) FEBS Journal , vol.275 , Issue.13 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 81
    • 0035300437 scopus 로고    scopus 로고
    • Transcriptional gene expression profiles of colorectal adenoma, adenocarcinoma, and normal tissue examined by oligonucleotide arrays
    • Notterman, D. A., Alon, U., Sierk, A. J., Levine, A. J. (2001). Transcriptional gene expression profles of colorectal adenoma, adenocarcinoma, and normal tissue examined by oligonucleotide arrays. Cancer Res 61:3124-3130. (Pubitemid 32691964)
    • (2001) Cancer Research , vol.61 , Issue.7 , pp. 3124-3130
    • Notterman, D.A.1    Alon, U.2    Sierk, A.J.3    Levine, A.J.4
  • 82
    • 1642539111 scopus 로고    scopus 로고
    • Potent inhibition of human liver aldehyde oxidase by raloxifene
    • DOI 10.1124/dmd.32.1.89
    • Obach, R. S. (2004). Potent inhibition of human liver aldehyde oxidase by raloxifene. Drug Metab Dispos 32:89-97. (Pubitemid 38112540)
    • (2004) Drug Metabolism and Disposition , vol.32 , Issue.1 , pp. 89-97
    • Obach, R.S.1
  • 83
  • 84
    • 0021090704 scopus 로고
    • 1- methylnicotinamide oxidase activities in the livers of the rats administered alkylating agents
    • Ohkubo, M., Sakiyama, S., Fujimura, S. (1983). Increase of nicotinamide methyltransferase and N1-methyl-nicotinamide oxidase activities in the livers of the rats administered alkylating agents. Cancer Lett 21:175-181. (Pubitemid 14217348)
    • (1983) Cancer Letters , vol.21 , Issue.2 , pp. 175-181
    • Ohkubo, M.1    Sakiyama, S.2    Fujimura, S.3
  • 86
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • DOI 10.1038/327524a0
    • Palmer, R. M., Ferrige, A. G., Moncada, S. (1987). Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 327:524-526. (Pubitemid 17085822)
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 87
    • 48349108505 scopus 로고    scopus 로고
    • Early anti-oxidative and anti-proliferative curcumin efects on neuroglioma cells suggest therapeutic targets
    • Panchal, H. D., Vranizan, K., Lee, C. Y., Ho, J., Ngai, J., Timiras, P. S. (2008). Early anti-oxidative and anti-proliferative curcumin efects on neuroglioma cells suggest therapeutic targets. Neurochem Res 33:1701-1710.
    • (2008) Neurochem Res , vol.33 , pp. 1701-1710
    • Panchal, H.D.1    Vranizan, K.2    Lee, C.Y.3    Ho, J.4    Ngai, J.5    Timiras, P.S.6
  • 88
    • 11144280578 scopus 로고    scopus 로고
    • Identification and validation of commonly overexpressed genes in solid tumors by comparison of microarray data
    • DOI 10.1593/neo.04277
    • Pilarsky, C., Wenzig, M., Specht, T., Saeger, H. D., Grutzmann, R (2004). Identifcation and validation of commonly overexpressed genes in solid tumors by comparison of microarray data. Neoplasia 6:744-750. (Pubitemid 40041492)
    • (2004) Neoplasia , vol.6 , Issue.6 , pp. 744-750
    • Pilarsky, C.1    Wenzig, M.2    Specht, T.3    Saeger, H.D.4    Grutzmann, R.5
  • 92
    • 12344251988 scopus 로고    scopus 로고
    • Identification of aldehyde oxidase 1 and aldehyde oxidase homologue 1 as dioxin-inducible genes
    • DOI 10.1016/j.tox.2004.10.009, PII S0300483X04005906
    • Rivera, S. P., Choi, H. H., Chapman, B., Whitekus, M. J., Terao, M., Garattini, E., et al. (2005). Identifcation of aldehyde oxidase 1 and aldehyde oxidase homologue 1 as dioxin-inducible genes. Toxicology 207:401-409. (Pubitemid 40138937)
    • (2005) Toxicology , vol.207 , Issue.3 , pp. 401-409
    • Rivera, S.P.1    Choi, H.H.2    Chapman, B.3    Whitekus, M.J.4    Terao, M.5    Garattini, E.6    Hankinson, O.7
  • 96
    • 0025032060 scopus 로고
    • Influence of lipophilicity and carboxyl group content on the rate of hydroxylation of methotrexate derivatives by aldehyde oxidase
    • DOI 10.1016/0006-2952(90)90326-G
    • Rosowsky, A., Wright, J. E., Holden, S. A., Waxman, D. J. (1990). Infuence of lipophilicity and carboxyl group content on the rate of hydroxylation of methotrexate derivatives by aldehyde oxidase. Biochem Pharmacol 40:851-857. (Pubitemid 20246595)
    • (1990) Biochemical Pharmacology , vol.40 , Issue.4 , pp. 851-857
    • Rosowsky, A.1    Wright, J.E.2    Holden, S.A.3    Waxman, D.J.4
  • 97
    • 33646429798 scopus 로고    scopus 로고
    • Gene expression analyses reveal molecular relationships among 20 regions of the human CNS
    • Roth, R. B., Hevezi, P., Lee, J., Willhite, D., Lechner, S. M., Foster, A. C., et al. (2006). Gene expression analyses reveal molecular relationships among 20 regions of the human CNS. Neurogenetics 7:67-80.
    • (2006) Neurogenetics , vol.7 , pp. 67-80
    • Roth, R.B.1    Hevezi, P.2    Lee, J.3    Willhite, D.4    Lechner, S.M.5    Foster, A.C.6
  • 98
    • 53749108330 scopus 로고    scopus 로고
    • Aldehyde oxidase activity and inhibition in hepatocytes and cytosolic fractions from mouse, rat, monkey, and human
    • Sahi, J., Khan, K. K., Black, C. B. (2008). Aldehyde oxidase activity and inhibition in hepatocytes and cytosolic fractions from mouse, rat, monkey, and human. Drug Metab Lett 2:176-183.
    • (2008) Drug Metab Lett , vol.2 , pp. 176-183
    • Sahi, J.1    Khan, K.K.2    Black, C.B.3
  • 100
    • 33644867290 scopus 로고    scopus 로고
    • Defining molecular profiles of poor outcome in patients with invasive bladder cancer using oligonucleotide microarrays
    • DOI 10.1200/JCO.2005.03.2375
    • Sanchez-Carbayo, M., Socci, N. D., Lozano, J., Saint, F. , Cordon-Cardo, C. (2006). Defning molecular profles of poor outcome in patients with invasive bladder cancer using oligonucleotide microarrays. J Clin Oncol 24:778-789. (Pubitemid 46622045)
    • (2006) Journal of Clinical Oncology , vol.24 , Issue.5 , pp. 778-789
    • Sanchez-Carbayo, M.1    Socci, N.D.2    Lozano, J.3    Saint, F.4    Cordon-Cardo, C.5
  • 101
    • 65549121564 scopus 로고    scopus 로고
    • Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1
    • Schumann, S., Terao, M., Garattini, E., Saggu, M., Lendzian, F., Hildebrandt, P., et al. (2009). Site directed mutagenesis of amino acid residues at the active site of mouse aldehyde oxidase AOX1. PLoS One 4:e5348.
    • (2009) PLoS One , vol.4
    • Schumann, S.1    Terao, M.2    Garattini, E.3    Saggu, M.4    Lendzian, F.5    Hildebrandt, P.6
  • 105
    • 1442335997 scopus 로고    scopus 로고
    • Gene expression-based high-throughput screening (GE-HTS) and application to leukemia differentiation
    • DOI 10.1038/ng1305
    • Stegmaier, K., Ross, K. N., Colavito, S. A., O'Malley, S., Stockwell, B. R., Golub, T. R. (2004). Gene expression-based high-throughput screening(GE-HTS) and application to leukemia diferentiation. Nat Genet 36: 257-263. (Pubitemid 38282750)
    • (2004) Nature Genetics , vol.36 , Issue.3 , pp. 257-263
    • Stegmaier, K.1    Ross, K.N.2    Colavito, S.A.3    O'Malley, S.4    Stockwell, B.R.5    Golub, T.R.6
  • 107
    • 34347209095 scopus 로고    scopus 로고
    • Selection of DDX5 as a novel internal control for Q-RT-PCR from microarray data using a block bootstrap re-sampling scheme
    • Su, L. J., Chang, C. W., Wu, Y. C., Chen, K. C., Lin, C. J., Liang, S. C., et al (2007). Selection of DDX5 as a novel internal control for Q-RT-PCR from microarray data using a block bootstrap re-sampling scheme. BMC Genomics 8:140.
    • (2007) BMC Genomics , vol.8 , pp. 140
    • Su, L.J.1    Chang, C.W.2    Wu, Y.C.3    Chen, K.C.4    Lin, C.J.5    Liang, S.C.6
  • 108
    • 31344433975 scopus 로고    scopus 로고
    • 1-methylnicotinamide to pyridones, and intraspecies variation of the enzyme activity in rats
    • DOI 10.1124/dmd.105.006544
    • Sugihara, K., Tayama, Y., Shimomiya, K., Yoshimoto, D., Ohta, S., Kitamura, S. (2006). Estimation of aldehyde oxidase activity in vivo from conversion ratio of N1-methylnicotinamide to pyridones, and intraspecies variation of the enzyme activity in rats. Drug Metab Dispos 34:208-212. (Pubitemid 43145022)
    • (2006) Drug Metabolism and Disposition , vol.34 , Issue.2 , pp. 208-212
    • Sugihara, K.1    Tayama, Y.2    Shimomiya, K.3    Yoshimoto, D.4    Ohta, S.5    Kitamura, S.6
  • 110
    • 58249104034 scopus 로고    scopus 로고
    • Role of the molybdofavoenzyme aldehyde oxidase homolog 2 in the biosynthesis of retinoic acid: Generation and characterization of a knockout mouse
    • Terao, M., Kurosaki, M., Barzago, M. M., Fratelli, M., Bagnati, R., Bastone, A., et al. (2009). Role of the molybdofavoenzyme aldehyde oxidase homolog 2 in the biosynthesis of retinoic acid: generation and characterization of a knockout mouse. Mol Cell Biol 29:357-377.
    • (2009) Mol Cell Biol , vol.29 , pp. 357-377
    • Terao, M.1    Kurosaki, M.2    Barzago, M.M.3    Fratelli, M.4    Bagnati, R.5    Bastone, A.6
  • 112
    • 0032104270 scopus 로고    scopus 로고
    • Isolation and characterization of the human aldehyde oxidase gene: Conservation of intron/exon boundaries with the xanthine oxidoreductase gene indicates a common origin
    • Terao, M., Kurosaki, M., Demontis, S., Zanotta, S., Garattini, E. (1998). Isolation and characterization of the human aldehyde oxidase gene: conservation of intron/exon boundaries with the xanthine oxidoreductase gene indicates a common origin. Biochem J 332(Pt 2):383-393. (Pubitemid 28271870)
    • (1998) Biochemical Journal , vol.332 , Issue.2 , pp. 383-393
    • Terao, M.1    Kurosaki, M.2    Demontis, S.3    Zanotta, S.4    Garattini, E.5
  • 113
    • 0035824605 scopus 로고    scopus 로고
    • Purifcation of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identifcation of a novel molybdo-favoprotein gene cluster on mouse chromosome 1
    • Terao, M., Kurosaki, M., Marini, M., Vanoni, M. A., Saltini, G., Bonetto, V., et al. (2001). Purifcation of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identifcation of a novel molybdo-favoprotein gene cluster on mouse chromosome 1. J Biol Chem 276:46347-46363.
    • (2001) J Biol Chem , vol.276 , pp. 46347-46363
    • Terao, M.1    Kurosaki, M.2    Marini, M.3    Vanoni, M.A.4    Saltini, G.5    Bonetto, V.6
  • 114
    • 0034730637 scopus 로고    scopus 로고
    • Cloning of the cDNAs coding for two novel molybdo-favoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase
    • Terao, M., Kurosaki, M., Saltini, G., Demontis, S., Marini, M., Salmona, M., et al. (2000). Cloning of the cDNAs coding for two novel molybdo-favoproteins showing high similarity with aldehyde oxidase and xanthine oxidoreductase. J Biol Chem 275:30690-30700.
    • (2000) J Biol Chem , vol.275 , pp. 30690-30700
    • Terao, M.1    Kurosaki, M.2    Saltini, G.3    Demontis, S.4    Marini, M.5    Salmona, M.6
  • 116
    • 0043244946 scopus 로고    scopus 로고
    • Transcriptional silencing of zinc finger protein 185 identified by expression profiling is associated with prostate cancer progression
    • Vanaja, D. K., Cheville, J. C., Iturria, S. J., Young, C. Y. (2003). Transcriptional silencing of zinc fnger protein 185 identifed by expression profling is associated with prostate cancer progression. Cancer Res 63:3877-3882. (Pubitemid 36917897)
    • (2003) Cancer Research , vol.63 , Issue.14 , pp. 3877-3882
    • Vanaja, D.K.1    Cheville, J.C.2    Iturria, S.J.3    Young, C.Y.F.4
  • 118
    • 0019144787 scopus 로고
    • Development and maturation of aldehyde oxidase levels in fetal hepatic tissue of C57BL/6J mice
    • Ventura, S. M., Dachtler, S. L. (1980). Development and maturation of aldehyde oxidase levels in fetal hepatic tissue of C57BL/6J mice. Enzyme 25:213-219. (Pubitemid 11252524)
    • (1980) Enzyme , vol.25 , Issue.4 , pp. 213-219
    • Ventura, S.M.1    Dachtler, S.L.2
  • 119
    • 0019441864 scopus 로고
    • Effects of sex hormones on hepatic aldehyde oxidase activity in C57BL/6J mice
    • Ventura, S. M., Dachtler, S. L. (1981). Efects of sex hormones on hepatic aldehyde oxidase activity in C57BL/6J mice. Horm Res 14:250-259. (Pubitemid 11029209)
    • (1981) Hormone Research , vol.14 , Issue.4 , pp. 250-259
    • Ventura, S.M.1    Dachtler, S.L.2
  • 120
    • 1542365400 scopus 로고    scopus 로고
    • Regulation and biochemistry of mouse molybdo-flavoenzymes: The DBA/2 mouse is selectively deficient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purification and characterization of aldehyde oxidase
    • DOI 10.1074/jbc.M308137200
    • Vila, R., Kurosaki, M., Barzago, M. M., Kolek, M., Bastone, A., Colombo, L., et al. (2004). Regulation and biochemistry of mouse molybdo-favoenzymes. Te DBA/2 mouse is selectively defcient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purifcation and characterization of aldehyde oxidase. J Biol Chem 279:8668-8683. (Pubitemid 38295922)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8668-8683
    • Vila, R.1    Kurosaki, M.2    Barzago, M.M.3    Kolek, M.4    Bastone, A.5    Colombo, L.6    Salmona, M.7    Terao, M.8    Garattini, E.9
  • 121
    • 28444448000 scopus 로고    scopus 로고
    • Interactome-transcriptome analysis reveals the high centrality of genes differentially expressed in lung cancer tissues
    • DOI 10.1093/bioinformatics/bti688
    • Wachi, S., Yoneda, K., Wu, R. (2005). Interactome-transcriptome analysis reveals the high centrality of genes diferentially expressed in lung cancer tissues. Bioinformatics 21:4205-4208. (Pubitemid 41724298)
    • (2005) Bioinformatics , vol.21 , Issue.23 , pp. 4205-4208
    • Wachi, S.1    Yoneda, K.2    Wu, R.3
  • 123
    • 0029841018 scopus 로고    scopus 로고
    • Measurement of nitric oxide and peroxynitrite generation in the postischemic heart: Evidence for peroxynitrite-mediated reperfusion injury
    • DOI 10.1074/jbc.271.46.29223
    • Wang, P. , Zweier, J. L. (1996). Measurement of nitric oxide and peroxynitrite generation in the postischemic heart. Evidence for peroxynitrite-mediated reperfusion injury. J Biol Chem 271:29223-29230. (Pubitemid 26382634)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 29223-29230
    • Wang, P.1    Zweier, J.L.2
  • 124
    • 48749121995 scopus 로고    scopus 로고
    • Small-interference RNA-mediated knockdown of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release
    • Weigert, J., Neumeier, M., Bauer, S., Mages, W., Schnitzbauer, A. A., Obed, A., et al. (2008). Small-interference RNA-mediated knockdown of aldehyde oxidase 1 in 3T3-L1 cells impairs adipogenesis and adiponectin release. FEBS Lett 582:2965-2972.
    • (2008) FEBS Lett , vol.582 , pp. 2965-2972
    • Weigert, J.1    Neumeier, M.2    Bauer, S.3    Mages, W.4    Schnitzbauer, A.A.5    Obed, A.6
  • 126
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum, and possible cofactor-binding domains
    • Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A., et al. (1991). Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum, and possible cofactor-binding domains. Biochim Biophys Acta 1057:157-185.
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6
  • 127
    • 0023257268 scopus 로고
    • Metabolism of methotrexate and γ-tert-butyl methotrexate by human leukemic cells in culture and by hepatic aldehyde oxidase in vitro
    • DOI 10.1016/0006-2952(87)90152-3
    • Wright, J. E., Rosowsky, A., Waxman, D. J., Trites, D., Cucchi, C. A., Flatow, J., et al. (1987). Metabolism of methotrexate and gamma-tert-butyl methotrexate by human leukemic cells in culture and by hepatic aldehyde oxidase in vitro. Biochem Pharmacol 36:2209-2214. (Pubitemid 17101736)
    • (1987) Biochemical Pharmacology , vol.36 , Issue.13 , pp. 2209-2214
    • Wright, J.E.1    Rosowsky, A.2    Waxman, D.J.3
  • 128
    • 0032900113 scopus 로고    scopus 로고
    • Alcohol-induced breast cancer: A proposed mechanism
    • DOI 10.1016/S0891-5849(98)00204-4, PII S0891584998002044
    • Wright, R. M., McManaman, J. L., Repine, J. E. (1999). Alcohol-induced breast cancer: a proposed mechanism. Free Radic Biol Med 26:348-354. (Pubitemid 29013466)
    • (1999) Free Radical Biology and Medicine , vol.26 , Issue.3-4 , pp. 348-354
    • Wright, R.M.1    McManaman, J.L.2    Repine, J.E.3
  • 129
    • 0034472034 scopus 로고    scopus 로고
    • 1) promoter by tandem cooperative Sp1/Sp3 binding sites: Identification of complex architecture in the hAOX upstream DNA that includes a proximal promoter, distal activation sites, and a silencer element
    • DOI 10.1089/10445490050128395
    • Wright, R. M., Riley, M. G., Weigel, L. K., Ginger, L. A., Costantino, D. A., McManaman, J. L. (2000). Activation of the human aldehyde oxidase (hAOX1) promoter by tandem cooperative Sp1/Sp3 binding sites: identifcation of complex architecture in the hAOX upstream DNA that includes a proximal promoter, distal activation sites, and a silencer element. DNA Cell Biol 19:459-474. (Pubitemid 32186441)
    • (2000) DNA and Cell Biology , vol.19 , Issue.8 , pp. 459-474
    • Wright, R.M.1    Riley, M.G.2    Weigel, L.K.3    Ginger, L.A.4    Costantino, D.A.5    McManaman, J.L.6
  • 131
    • 61549106628 scopus 로고    scopus 로고
    • Long-term epigenetic therapy with oral zebularine has minimal side efects and prevents intestinal tumors in mice
    • Yoo, C. B., Chuang, J. C., Byun, H. M., Egger, G., Yang, A. S., Dubeau, L., et al. (2008). Long-term epigenetic therapy with oral zebularine has minimal side efects and prevents intestinal tumors in mice. Cancer Prev Res (Phila Pa) 1:233-240.
    • (2008) Cancer Prev Res (Phila Pa) , vol.1 , pp. 233-240
    • Yoo, C.B.1    Chuang, J.C.2    Byun, H.M.3    Egger, G.4    Yang, A.S.5    Dubeau, L.6
  • 132
    • 66749104378 scopus 로고    scopus 로고
    • High-resolution DNA copy number and gene expression analyses distinguish
    • Yusenko, M. V., Kuiper, R. P., Boethe, T., Ljungberg, B., van Kessel, A. G., Kovacs, G. (2009). High-resolution DNA copy number and gene expression analyses distinguish chromophobe renal cell carcinomas and renal oncocytomas. BMC Cancer 9:152.
    • (2009) BMC Cancer , vol.9 , pp. 152
    • Yusenko, M.V.1    Kuiper, R.P.2    Boethe, T.3    Ljungberg, B.4    Van Kessel, A.G.5    Kovacs, G.6
  • 133
    • 1542543326 scopus 로고    scopus 로고
    • Hereditary xanthinuria type II associated with mental delay, autism, cortical renal cysts, nephrocalcinosis, osteopenia, and hair and teeth defects
    • Zannolli, R., Micheli, V. , Mazzei, M. A., Sacco, P., Piomboni, P., Bruni, E., et al. (2003). Hereditary xanthinuria type II associated with mental delay, autism, cortical renal cysts, nephrocalcinosis, osteopenia, and hair and teeth defects. J Med Genet 40:e121.
    • (2003) J Med Genet , vol.40
    • Zannolli, R.1    Micheli, V.2    Mazzei, M.A.3    Sacco, P.4    Piomboni, P.5    Bruni, E.6
  • 134
    • 78650303504 scopus 로고    scopus 로고
    • In silico and in vitro pharmacogenetics: Aldehyde oxidase rapidly metabolizes a p38 kinase inhibitor
    • Zhang, X., Liu, H. H., Weller, P., Zheng, M., Tao, W., Wang, J., et al. (2011). In silico and in vitro pharmacogenetics: aldehyde oxidase rapidly metabolizes a p38 kinase inhibitor. Pharmacogenomics J 11:15-24.
    • (2011) Pharmacogenomics J , vol.11 , pp. 15-24
    • Zhang, X.1    Liu, H.H.2    Weller, P.3    Zheng, M.4    Tao, W.5    Wang, J.6


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