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Volumn 425, Issue 21, 2013, Pages 3978-3992

Advances in molecular modeling of human cytochrome P450 polymorphism

Author keywords

cytochrome P450; metabolizing enzymes; molecular modeling; polymorphism

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 2A6; CYTOCHROME P450 2B6; CYTOCHROME P450 2C19; CYTOCHROME P450 2C9; CYTOCHROME P450 2D6;

EID: 84885179307     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.07.010     Document Type: Review
Times cited : (37)

References (145)
  • 1
    • 24644445302 scopus 로고    scopus 로고
    • The human genome project and novel aspects of cytochrome P450 research
    • M. Ingelman-Sundberg The human genome project and novel aspects of cytochrome P450 research Toxicol Appl Pharmacol 207 2005 52 56
    • (2005) Toxicol Appl Pharmacol , vol.207 , pp. 52-56
    • Ingelman-Sundberg, M.1
  • 3
    • 79952083050 scopus 로고    scopus 로고
    • Genetic polymorphism and toxicology - With emphasis on cytochrome p450
    • I. Johansson, and M. Ingelman-Sundberg Genetic polymorphism and toxicology - with emphasis on cytochrome p450 Toxicol Sci 120 2011 1 13
    • (2011) Toxicol Sci , vol.120 , pp. 1-13
    • Johansson, I.1    Ingelman-Sundberg, M.2
  • 4
    • 34047243800 scopus 로고    scopus 로고
    • Xenobiotic-metabolizing enzymes involved in activation and detoxification of carcinogenic polycyclic aromatic hydrocarbons
    • T. Shimada Xenobiotic-metabolizing enzymes involved in activation and detoxification of carcinogenic polycyclic aromatic hydrocarbons Drug Metab Pharmacokinet 21 2006 257 276
    • (2006) Drug Metab Pharmacokinet , vol.21 , pp. 257-276
    • Shimada, T.1
  • 5
    • 33645116164 scopus 로고    scopus 로고
    • Cytochrome P450 pharmacogenetics and cancer
    • C. Rodriguez-Antona, and M. Ingelman-Sundberg Cytochrome P450 pharmacogenetics and cancer Oncogene 25 2006 1679 1691
    • (2006) Oncogene , vol.25 , pp. 1679-1691
    • Rodriguez-Antona, C.1    Ingelman-Sundberg, M.2
  • 6
    • 0037184794 scopus 로고    scopus 로고
    • Polymorphism of cytochrome P450 and xenobiotic toxicity
    • M. Ingelman-Sundberg Polymorphism of cytochrome P450 and xenobiotic toxicity Toxicology 181-182 2002 447 452
    • (2002) Toxicology , vol.181-182 , pp. 447-452
    • Ingelman-Sundberg, M.1
  • 7
    • 77952541257 scopus 로고    scopus 로고
    • The nasty surprise of a complex drug-drug interaction
    • C. Bode The nasty surprise of a complex drug-drug interaction Drug Discov Today 15 2010 391 395
    • (2010) Drug Discov Today , vol.15 , pp. 391-395
    • Bode, C.1
  • 8
    • 81055125444 scopus 로고    scopus 로고
    • The importance of HT-ADME in drug discovery
    • D. Morgan The importance of HT-ADME in drug discovery Bioanalysis 3 2011 2385 2387
    • (2011) Bioanalysis , vol.3 , pp. 2385-2387
    • Morgan, D.1
  • 9
    • 0033997634 scopus 로고    scopus 로고
    • Automated high throughput human CYP isoform activity assay using SPE-LC/MS method: Application in CYP inhibition evaluation
    • H. Yin, J. Racha, S.Y. Li, N. Olejnik, H. Satoh, and D. Moore Automated high throughput human CYP isoform activity assay using SPE-LC/MS method: application in CYP inhibition evaluation Xenobiotica 30 2000 141 154
    • (2000) Xenobiotica , vol.30 , pp. 141-154
    • Yin, H.1    Racha, J.2    Li, S.Y.3    Olejnik, N.4    Satoh, H.5    Moore, D.6
  • 10
    • 0035031472 scopus 로고    scopus 로고
    • In vitro high throughput screening of compounds for favorable metabolic properties in drug discovery
    • C.M. Masimirembwa, R. Thompson, and T.B. Andersson In vitro high throughput screening of compounds for favorable metabolic properties in drug discovery Comb Chem High Throughput Screening 4 2001 245 263
    • (2001) Comb Chem High Throughput Screening , vol.4 , pp. 245-263
    • Masimirembwa, C.M.1    Thompson, R.2    Andersson, T.B.3
  • 11
    • 0035032365 scopus 로고    scopus 로고
    • Development of a miniaturized 384-well high throughput screen for the detection of substrates of cytochrome P450 2D6 and 3A4 metabolism
    • I. Kariv, M.P. Fereshteh, and K.R. Oldenburg Development of a miniaturized 384-well high throughput screen for the detection of substrates of cytochrome P450 2D6 and 3A4 metabolism J Biomol Screening 6 2001 91 99
    • (2001) J Biomol Screening , vol.6 , pp. 91-99
    • Kariv, I.1    Fereshteh, M.P.2    Oldenburg, K.R.3
  • 12
    • 71449103290 scopus 로고    scopus 로고
    • Structure-based drug metabolism predictions for drug design
    • H. Sun, and D.O. Scott Structure-based drug metabolism predictions for drug design Chem Biol Drug Des 75 2010 3 17
    • (2010) Chem Biol Drug des , vol.75 , pp. 3-17
    • Sun, H.1    Scott, D.O.2
  • 13
    • 27444434892 scopus 로고    scopus 로고
    • MetaSite: Understanding metabolism in human cytochromes from the perspective of the chemist
    • G. Cruciani, E. Carosati, B. De Boeck, K. Ethirajulu, C. Mackie, and T. Howe MetaSite: understanding metabolism in human cytochromes from the perspective of the chemist J Med Chem 48 2005 6970 6979
    • (2005) J Med Chem , vol.48 , pp. 6970-6979
    • Cruciani, G.1    Carosati, E.2    De Boeck, B.3    Ethirajulu, K.4    Mackie, C.5    Howe, T.6
  • 14
    • 79551667504 scopus 로고    scopus 로고
    • In-silico ADME models: A general assessment of their utility in drug discovery applications
    • M.P. Gleeson, A. Hersey, and S. Hannongbua In-silico ADME models: a general assessment of their utility in drug discovery applications Curr Top Med Chem 11 2011 358 381
    • (2011) Curr Top Med Chem , vol.11 , pp. 358-381
    • Gleeson, M.P.1    Hersey, A.2    Hannongbua, S.3
  • 15
    • 73749087528 scopus 로고    scopus 로고
    • Computational toxicology - A tool for early safety evaluation
    • C. Merlot Computational toxicology - a tool for early safety evaluation Drug Discov Today 15 2010 16 22
    • (2010) Drug Discov Today , vol.15 , pp. 16-22
    • Merlot, C.1
  • 17
    • 0035861049 scopus 로고    scopus 로고
    • Potential role of pharmacogenomics in reducing adverse drug reactions: A systematic review
    • K.A. Phillips, D.L. Veenstra, E. Oren, J.K. Lee, and W. Sadee Potential role of pharmacogenomics in reducing adverse drug reactions: a systematic review JAMA 286 2001 2270 2279
    • (2001) JAMA , vol.286 , pp. 2270-2279
    • Phillips, K.A.1    Veenstra, D.L.2    Oren, E.3    Lee, J.K.4    Sadee, W.5
  • 18
    • 44349094918 scopus 로고    scopus 로고
    • P450 oxidoreductase: Genetic polymorphisms and implications for drug metabolism and toxicity
    • S.N. Hart, and X.B. Zhong P450 oxidoreductase: genetic polymorphisms and implications for drug metabolism and toxicity Expert Opin Drug Metab Toxicol 4 2008 439 452
    • (2008) Expert Opin Drug Metab Toxicol , vol.4 , pp. 439-452
    • Hart, S.N.1    Zhong, X.B.2
  • 19
    • 84857273073 scopus 로고    scopus 로고
    • Cytochrome P450 variations in different ethnic populations
    • J. McGraw, and D. Waller Cytochrome P450 variations in different ethnic populations Expert Opin Drug Metab Toxicol 8 2012 371 382
    • (2012) Expert Opin Drug Metab Toxicol , vol.8 , pp. 371-382
    • McGraw, J.1    Waller, D.2
  • 21
    • 79955685734 scopus 로고    scopus 로고
    • Clinically relevant genetic variations in drug metabolizing enzymes
    • N. Pinto, and M.E. Dolan Clinically relevant genetic variations in drug metabolizing enzymes Curr Drug Metab 12 2011 487 497
    • (2011) Curr Drug Metab , vol.12 , pp. 487-497
    • Pinto, N.1    Dolan, M.E.2
  • 22
    • 79954537612 scopus 로고    scopus 로고
    • In silico identification of microRNAs predicted to regulate the drug metabolizing cytochrome P450 genes
    • A. Ramamoorthy, and T.C. Skaar In silico identification of microRNAs predicted to regulate the drug metabolizing cytochrome P450 genes Drug Metab Lett 5 2011 126 131
    • (2011) Drug Metab Lett , vol.5 , pp. 126-131
    • Ramamoorthy, A.1    Skaar, T.C.2
  • 23
    • 15344340688 scopus 로고    scopus 로고
    • Polymorphisms affecting gene regulation and mRNA processing: Broad implications for pharmacogenetics
    • A.D. Johnson, D. Wang, and W. Sadee Polymorphisms affecting gene regulation and mRNA processing: broad implications for pharmacogenetics Pharmacol Ther 106 2005 19 38
    • (2005) Pharmacol Ther , vol.106 , pp. 19-38
    • Johnson, A.D.1    Wang, D.2    Sadee, W.3
  • 24
    • 36248964215 scopus 로고    scopus 로고
    • Past and future applications of CYP450-genetic polymorphisms for biomonitoring of environmental toxicants
    • B. Yi, J.Y. Yang, and M. Yang Past and future applications of CYP450-genetic polymorphisms for biomonitoring of environmental toxicants J Environ Sci Health C Environ Carcinog Ecotoxicol Rev 25 2007 353 377
    • (2007) J Environ Sci Health C Environ Carcinog Ecotoxicol Rev , vol.25 , pp. 353-377
    • Yi, B.1    Yang, J.Y.2    Yang, M.3
  • 25
    • 0032698297 scopus 로고    scopus 로고
    • Identification and characterisation of novel polymorphisms in the CYP2A locus: Implications for nicotine metabolism
    • M. Oscarson, R.A. McLellan, H. Gullsten, J.A. Agundez, J. Benitez, and A. Rautio Identification and characterisation of novel polymorphisms in the CYP2A locus: implications for nicotine metabolism FEBS Lett 460 1999 321 327
    • (1999) FEBS Lett , vol.460 , pp. 321-327
    • Oscarson, M.1    McLellan, R.A.2    Gullsten, H.3    Agundez, J.A.4    Benitez, J.5    Rautio, A.6
  • 26
    • 0037291512 scopus 로고    scopus 로고
    • Nicotine metabolism, human drug metabolism polymorphisms, and smoking behaviour
    • A.R. Tricker Nicotine metabolism, human drug metabolism polymorphisms, and smoking behaviour Toxicology 183 2003 151 173
    • (2003) Toxicology , vol.183 , pp. 151-173
    • Tricker, A.R.1
  • 27
    • 0029591606 scopus 로고
    • Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19
    • S.M. Hoffman, P. Fernandez-Salguero, F.J. Gonzalez, and H.W. Mohrenweiser Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19 J Mol Evol 41 1995 894 900
    • (1995) J Mol Evol , vol.41 , pp. 894-900
    • Hoffman, S.M.1    Fernandez-Salguero, P.2    Gonzalez, F.J.3    Mohrenweiser, H.W.4
  • 29
    • 0030697098 scopus 로고    scopus 로고
    • A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin
    • H. Hadidi, K. Zahlsen, J.R. Idle, and S. Cholerton A single amino acid substitution (Leu160His) in cytochrome P450 CYP2A6 causes switching from 7-hydroxylation to 3-hydroxylation of coumarin Food Chem Toxicol 35 1997 903 907
    • (1997) Food Chem Toxicol , vol.35 , pp. 903-907
    • Hadidi, H.1    Zahlsen, K.2    Idle, J.R.3    Cholerton, S.4
  • 30
    • 0034805710 scopus 로고    scopus 로고
    • A novel single nucleotide polymorphism altering stability and activity of CYP2a6
    • N. Ariyoshi, Y. Sawamura, and T. Kamataki A novel single nucleotide polymorphism altering stability and activity of CYP2a6 Biochem Biophys Res Commun 281 2001 810 814
    • (2001) Biochem Biophys Res Commun , vol.281 , pp. 810-814
    • Ariyoshi, N.1    Sawamura, Y.2    Kamataki, T.3
  • 31
    • 42949141477 scopus 로고    scopus 로고
    • Novel and established CYP2A6 alleles impair in vivo nicotine metabolism in a population of Black African descent
    • J.C. Mwenifumbo, N. Al Koudsi, M.K. Ho, Q. Zhou, E.B. Hoffmann, and E.M. Sellers Novel and established CYP2A6 alleles impair in vivo nicotine metabolism in a population of Black African descent Hum Mutat 29 2008 679 688
    • (2008) Hum Mutat , vol.29 , pp. 679-688
    • Mwenifumbo, J.C.1    Al Koudsi, N.2    Ho, M.K.3    Zhou, Q.4    Hoffmann, E.B.5    Sellers, E.M.6
  • 32
    • 0035947589 scopus 로고    scopus 로고
    • CYP2A66, a novel polymorphism in cytochrome p450 2A6, has a single amino acid substitution (R128Q) that inactivates enzymatic activity
    • K. Kitagawa, N. Kunugita, M. Kitagawa, and T. Kawamoto CYP2A66, a novel polymorphism in cytochrome p450 2A6, has a single amino acid substitution (R128Q) that inactivates enzymatic activity J Biol Chem 276 2001 17830 17835
    • (2001) J Biol Chem , vol.276 , pp. 17830-17835
    • Kitagawa, K.1    Kunugita, N.2    Kitagawa, M.3    Kawamoto, T.4
  • 34
    • 0037757965 scopus 로고    scopus 로고
    • Effects of polymorphism in promoter region of human CYP2A6 gene (CYP2A69) on expression level of messenger ribonucleic acid and enzymatic activity in vivo and in vitro
    • R. Yoshida, M. Nakajima, K. Nishimura, S. Tokudome, J.T. Kwon, and T. Yokoi Effects of polymorphism in promoter region of human CYP2A6 gene (CYP2A69) on expression level of messenger ribonucleic acid and enzymatic activity in vivo and in vitro Clin Pharmacol Ther 74 2003 69 76
    • (2003) Clin Pharmacol Ther , vol.74 , pp. 69-76
    • Yoshida, R.1    Nakajima, M.2    Nishimura, K.3    Tokudome, S.4    Kwon, J.T.5    Yokoi, T.6
  • 36
    • 0036016314 scopus 로고    scopus 로고
    • A novel mutant allele of the CYP2A6 gene (CYP2A611) found in a cancer patient who showed poor metabolic phenotype towards tegafur
    • S. Daigo, Y. Takahashi, M. Fujieda, N. Ariyoshi, H. Yamazaki, and W. Koizumi A novel mutant allele of the CYP2A6 gene (CYP2A611) found in a cancer patient who showed poor metabolic phenotype towards tegafur Pharmacogenetics 12 2002 299 306
    • (2002) Pharmacogenetics , vol.12 , pp. 299-306
    • Daigo, S.1    Takahashi, Y.2    Fujieda, M.3    Ariyoshi, N.4    Yamazaki, H.5    Koizumi, W.6
  • 37
    • 0036389893 scopus 로고    scopus 로고
    • Characterization of a novel CYP2A7/CYP2A6 hybrid allele (CYP2A612) that causes reduced CYP2A6 activity
    • M. Oscarson, R.A. McLellan, V. Asp, M. Ledesma, M.L. Bernal Ruiz, and B. Sinues Characterization of a novel CYP2A7/CYP2A6 hybrid allele (CYP2A612) that causes reduced CYP2A6 activity Hum Mutat 20 2002 275 283
    • (2002) Hum Mutat , vol.20 , pp. 275-283
    • Oscarson, M.1    McLellan, R.A.2    Asp, V.3    Ledesma, M.4    Bernal Ruiz, M.L.5    Sinues, B.6
  • 38
    • 10044244648 scopus 로고    scopus 로고
    • A novel polymorphism of human CYP2A6 gene CYP2A617 has an amino acid substitution (V365M) that decreases enzymatic activity in vitro and in vivo
    • T. Fukami, M. Nakajima, R. Yoshida, Y. Tsuchiya, Y. Fujiki, and M. Katoh A novel polymorphism of human CYP2A6 gene CYP2A617 has an amino acid substitution (V365M) that decreases enzymatic activity in vitro and in vivo Clin Pharmacol Ther 76 2004 519 527
    • (2004) Clin Pharmacol Ther , vol.76 , pp. 519-527
    • Fukami, T.1    Nakajima, M.2    Yoshida, R.3    Tsuchiya, Y.4    Fujiki, Y.5    Katoh, M.6
  • 39
    • 22944465782 scopus 로고    scopus 로고
    • Characterization of novel CYP2A6 polymorphic alleles (CYP2A618 and CYP2A619) that affect enzymatic activity
    • T. Fukami, M. Nakajima, E. Higashi, H. Yamanaka, H. Sakai, and H.L. McLeod Characterization of novel CYP2A6 polymorphic alleles (CYP2A618 and CYP2A619) that affect enzymatic activity Drug Metab Dispos 33 2005 1202 1210
    • (2005) Drug Metab Dispos , vol.33 , pp. 1202-1210
    • Fukami, T.1    Nakajima, M.2    Higashi, E.3    Yamanaka, H.4    Sakai, H.5    McLeod, H.L.6
  • 40
    • 38549137889 scopus 로고    scopus 로고
    • A novel CYP2A6 allele, CYP2A623, impairs enzyme function in vitro and in vivo and decreases smoking in a population of Black-African descent
    • M.K. Ho, J.C. Mwenifumbo, B. Zhao, E.M. Gillam, and R.F. Tyndale A novel CYP2A6 allele, CYP2A623, impairs enzyme function in vitro and in vivo and decreases smoking in a population of Black-African descent Pharmacogenet Genomics 18 2008 67 75
    • (2008) Pharmacogenet Genomics , vol.18 , pp. 67-75
    • Ho, M.K.1    Mwenifumbo, J.C.2    Zhao, B.3    Gillam, E.M.4    Tyndale, R.F.5
  • 41
    • 67849090529 scopus 로고    scopus 로고
    • A novel CYP2A6 allele (CYP2A635) resulting in an amino-acid substitution (Asn438Tyr) is associated with lower CYP2A6 activity in vivo
    • N. Al Koudsi, J.S. Ahluwalia, S.K. Lin, E.M. Sellers, and R.F. Tyndale A novel CYP2A6 allele (CYP2A635) resulting in an amino-acid substitution (Asn438Tyr) is associated with lower CYP2A6 activity in vivo Pharmacogenomics J 9 2009 274 282
    • (2009) Pharmacogenomics J , vol.9 , pp. 274-282
    • Al Koudsi, N.1    Ahluwalia, J.S.2    Lin, S.K.3    Sellers, E.M.4    Tyndale, R.F.5
  • 42
    • 4644255903 scopus 로고    scopus 로고
    • Ethnic variation in CYP2A6 and association of genetically slow nicotine metabolism and smoking in adult Caucasians
    • K.A. Schoedel, E.B. Hoffmann, Y. Rao, E.M. Sellers, and R.F. Tyndale Ethnic variation in CYP2A6 and association of genetically slow nicotine metabolism and smoking in adult Caucasians Pharmacogenetics 14 2004 615 626
    • (2004) Pharmacogenetics , vol.14 , pp. 615-626
    • Schoedel, K.A.1    Hoffmann, E.B.2    Rao, Y.3    Sellers, E.M.4    Tyndale, R.F.5
  • 43
    • 70349386728 scopus 로고    scopus 로고
    • Polymorphism of human cytochrome P450 2D6 and its clinical significance: Part i
    • S.F. Zhou Polymorphism of human cytochrome P450 2D6 and its clinical significance: part I Clin Pharmacokinet 48 2009 689 723
    • (2009) Clin Pharmacokinet , vol.48 , pp. 689-723
    • Zhou, S.F.1
  • 45
    • 33645056468 scopus 로고    scopus 로고
    • CYP2A6 polymorphisms are associated with nicotine dependence and influence withdrawal symptoms in smoking cessation
    • T. Kubota, C. Nakajima-Taniguchi, T. Fukuda, M. Funamoto, M. Maeda, and E. Tange CYP2A6 polymorphisms are associated with nicotine dependence and influence withdrawal symptoms in smoking cessation Pharmacogenomics J 6 2006 115 119
    • (2006) Pharmacogenomics J , vol.6 , pp. 115-119
    • Kubota, T.1    Nakajima-Taniguchi, C.2    Fukuda, T.3    Funamoto, M.4    Maeda, M.5    Tange, E.6
  • 47
    • 0032926621 scopus 로고    scopus 로고
    • Monospecific antipeptide antibody to cytochrome P-450 2B6
    • D.M. Stresser, and D. Kupfer Monospecific antipeptide antibody to cytochrome P-450 2B6 Drug Metab Dispos 27 1999 517 525
    • (1999) Drug Metab Dispos , vol.27 , pp. 517-525
    • Stresser, D.M.1    Kupfer, D.2
  • 48
    • 4644349582 scopus 로고    scopus 로고
    • Multiple novel nonsynonymous CYP2B6 gene polymorphisms in Caucasians: Demonstration of phenotypic null alleles
    • T. Lang, K. Klein, T. Richter, A. Zibat, R. Kerb, and M. Eichelbaum Multiple novel nonsynonymous CYP2B6 gene polymorphisms in Caucasians: demonstration of phenotypic null alleles J Pharmacol Exp Ther 311 2004 34 43
    • (2004) J Pharmacol Exp Ther , vol.311 , pp. 34-43
    • Lang, T.1    Klein, K.2    Richter, T.3    Zibat, A.4    Kerb, R.5    Eichelbaum, M.6
  • 49
    • 0034092057 scopus 로고    scopus 로고
    • Identification of the human cytochromes P450 involved in the oxidative metabolism of "ecstasy"-related designer drugs
    • K. Kreth, K. Kovar, M. Schwab, and U.M. Zanger Identification of the human cytochromes P450 involved in the oxidative metabolism of "Ecstasy"-related designer drugs Biochem Pharmacol 59 2000 1563 1571
    • (2000) Biochem Pharmacol , vol.59 , pp. 1563-1571
    • Kreth, K.1    Kovar, K.2    Schwab, M.3    Zanger, U.M.4
  • 50
    • 0032931833 scopus 로고    scopus 로고
    • Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes
    • H. Yamazaki, K. Inoue, M. Hashimoto, and T. Shimada Roles of CYP2A6 and CYP2B6 in nicotine C-oxidation by human liver microsomes Arch Toxicol 73 1999 65 70
    • (1999) Arch Toxicol , vol.73 , pp. 65-70
    • Yamazaki, H.1    Inoue, K.2    Hashimoto, M.3    Shimada, T.4
  • 51
    • 0030739223 scopus 로고    scopus 로고
    • Human cytochrome P4502B6: Interindividual hepatic expression, substrate specificity, and role in procarcinogen activation
    • E.L. Code, C.L. Crespi, B.W. Penman, F.J. Gonzalez, T.K. Chang, and D.J. Waxman Human cytochrome P4502B6: interindividual hepatic expression, substrate specificity, and role in procarcinogen activation Drug Metab Dispos 25 1997 985 993
    • (1997) Drug Metab Dispos , vol.25 , pp. 985-993
    • Code, E.L.1    Crespi, C.L.2    Penman, B.W.3    Gonzalez, F.J.4    Chang, T.K.5    Waxman, D.J.6
  • 53
    • 16544373587 scopus 로고    scopus 로고
    • Three novel single nucleotide polymorphisms (SNPs) of the CYP2B6 gene in Japanese individuals
    • M. Hiratsuka, Y. Hinai, Y. Konno, H. Nozawa, S. Konno, and M. Mizugaki Three novel single nucleotide polymorphisms (SNPs) of the CYP2B6 gene in Japanese individuals Drug Metab Pharmacokinet 19 2004 155 158
    • (2004) Drug Metab Pharmacokinet , vol.19 , pp. 155-158
    • Hiratsuka, M.1    Hinai, Y.2    Konno, Y.3    Nozawa, H.4    Konno, S.5    Mizugaki, M.6
  • 54
    • 0034948077 scopus 로고    scopus 로고
    • Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver
    • T. Lang, K. Klein, J. Fischer, A.K. Nussler, P. Neuhaus, and U. Hofmann Extensive genetic polymorphism in the human CYP2B6 gene with impact on expression and function in human liver Pharmacogenetics 11 2001 399 415
    • (2001) Pharmacogenetics , vol.11 , pp. 399-415
    • Lang, T.1    Klein, K.2    Fischer, J.3    Nussler, A.K.4    Neuhaus, P.5    Hofmann, U.6
  • 55
    • 17844375918 scopus 로고    scopus 로고
    • A natural CYP2B6 TATA box polymorphism (- 82T → C) leading to enhanced transcription and relocation of the transcriptional start site
    • J. Zukunft, T. Lang, T. Richter, K.I. Hirsch-Ernst, A.K. Nussler, and K. Klein A natural CYP2B6 TATA box polymorphism (- 82T → C) leading to enhanced transcription and relocation of the transcriptional start site Mol Pharmacol 67 2005 1772 1782
    • (2005) Mol Pharmacol , vol.67 , pp. 1772-1782
    • Zukunft, J.1    Lang, T.2    Richter, T.3    Hirsch-Ernst, K.I.4    Nussler, A.K.5    Klein, K.6
  • 56
    • 10744221053 scopus 로고    scopus 로고
    • Hepatic CYP2B6 expression: Gender and ethnic differences and relationship to CYP2B6 genotype and CAR (constitutive androstane receptor) expression
    • V. Lamba, J. Lamba, K. Yasuda, S. Strom, J. Davila, and M.L. Hancock Hepatic CYP2B6 expression: gender and ethnic differences and relationship to CYP2B6 genotype and CAR (constitutive androstane receptor) expression J Pharmacol Exp Ther 307 2003 906 922
    • (2003) J Pharmacol Exp Ther , vol.307 , pp. 906-922
    • Lamba, V.1    Lamba, J.2    Yasuda, K.3    Strom, S.4    Davila, J.5    Hancock, M.L.6
  • 58
    • 27944492382 scopus 로고    scopus 로고
    • Genetic variability of CYP2B6 in populations of African and Asian origin: Allele frequencies, novel functional variants, and possible implications for anti-HIV therapy with efavirenz
    • K. Klein, T. Lang, T. Saussele, E. Barbosa-Sicard, W.H. Schunck, and M. Eichelbaum Genetic variability of CYP2B6 in populations of African and Asian origin: allele frequencies, novel functional variants, and possible implications for anti-HIV therapy with efavirenz Pharmacogenet Genomics 15 2005 861 873
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 861-873
    • Klein, K.1    Lang, T.2    Saussele, T.3    Barbosa-Sicard, E.4    Schunck, W.H.5    Eichelbaum, M.6
  • 59
    • 33947382259 scopus 로고    scopus 로고
    • Predictive value of known and novel alleles of CYP2B6 for efavirenz plasma concentrations in HIV-infected individuals
    • M. Rotger, H. Tegude, S. Colombo, M. Cavassini, H. Furrer, and L. Decosterd Predictive value of known and novel alleles of CYP2B6 for efavirenz plasma concentrations in HIV-infected individuals Clin Pharmacol Ther 81 2007 557 566
    • (2007) Clin Pharmacol Ther , vol.81 , pp. 557-566
    • Rotger, M.1    Tegude, H.2    Colombo, S.3    Cavassini, M.4    Furrer, H.5    Decosterd, L.6
  • 61
    • 2942551228 scopus 로고    scopus 로고
    • Homozygous CYP2B66 (Q172H and K262R) correlates with high plasma efavirenz concentrations in HIV-1 patients treated with standard efavirenz-containing regimens
    • K. Tsuchiya, H. Gatanaga, N. Tachikawa, K. Teruya, Y. Kikuchi, and M. Yoshino Homozygous CYP2B66 (Q172H and K262R) correlates with high plasma efavirenz concentrations in HIV-1 patients treated with standard efavirenz-containing regimens Biochem Biophys Res Commun 319 2004 1322 1326
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 1322-1326
    • Tsuchiya, K.1    Gatanaga, H.2    Tachikawa, N.3    Teruya, K.4    Kikuchi, Y.5    Yoshino, M.6
  • 62
    • 20244364148 scopus 로고    scopus 로고
    • Influence of CYP2B6 polymorphism on plasma and intracellular concentrations and toxicity of efavirenz and nevirapine in HIV-infected patients
    • M. Rotger, S. Colombo, H. Furrer, G. Bleiber, T. Buclin, and B.L. Lee Influence of CYP2B6 polymorphism on plasma and intracellular concentrations and toxicity of efavirenz and nevirapine in HIV-infected patients Pharmacogenet Genomics 15 2005 1 5
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 1-5
    • Rotger, M.1    Colombo, S.2    Furrer, H.3    Bleiber, G.4    Buclin, T.5    Lee, B.L.6
  • 63
    • 19944428456 scopus 로고    scopus 로고
    • Pharmacogenetics of efavirenz and central nervous system side effects: An adult AIDS clinical trials group study
    • D.W. Haas, H.J. Ribaudo, R.B. Kim, C. Tierney, G.R. Wilkinson, and R.M. Gulick Pharmacogenetics of efavirenz and central nervous system side effects: an adult AIDS clinical trials group study AIDS 18 2004 2391 2400
    • (2004) AIDS , vol.18 , pp. 2391-2400
    • Haas, D.W.1    Ribaudo, H.J.2    Kim, R.B.3    Tierney, C.4    Wilkinson, G.R.5    Gulick, R.M.6
  • 64
    • 77950284730 scopus 로고    scopus 로고
    • Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-Å resolution
    • S.C. Gay, M.B. Shah, J.C. Talakad, K. Maekawa, A.G. Roberts, and P.R. Wilderman Crystal structure of a cytochrome P450 2B6 genetic variant in complex with the inhibitor 4-(4-chlorophenyl)imidazole at 2.0-Å resolution Mol Pharmacol 77 2010 529 538
    • (2010) Mol Pharmacol , vol.77 , pp. 529-538
    • Gay, S.C.1    Shah, M.B.2    Talakad, J.C.3    Maekawa, K.4    Roberts, A.G.5    Wilderman, P.R.6
  • 65
    • 84874602232 scopus 로고    scopus 로고
    • Impact of genetic polymorphisms in CYP2C9 and CYP2C19 on the pharmacokinetics of clinically used drugs
    • T. Hirota, S. Eguchi, and I. Ieiri Impact of genetic polymorphisms in CYP2C9 and CYP2C19 on the pharmacokinetics of clinically used drugs Drug Metab Pharmacokinet 28 2013 28 37
    • (2013) Drug Metab Pharmacokinet , vol.28 , pp. 28-37
    • Hirota, T.1    Eguchi, S.2    Ieiri, I.3
  • 66
    • 84860636608 scopus 로고    scopus 로고
    • Drug metabolizing enzyme activities versus genetic variances for drug of clinical pharmacogenomic relevance
    • A.H. Wu Drug metabolizing enzyme activities versus genetic variances for drug of clinical pharmacogenomic relevance Clin Proteomics 8 2011 12
    • (2011) Clin Proteomics , vol.8 , pp. 12
    • Wu, A.H.1
  • 67
    • 0031260323 scopus 로고    scopus 로고
    • Progesterone and testosterone hydroxylation by cytochromes P450 2C19, 2C9, and 3A4 in human liver microsomes
    • H. Yamazaki, and T. Shimada Progesterone and testosterone hydroxylation by cytochromes P450 2C19, 2C9, and 3A4 in human liver microsomes Arch Biochem Biophys 346 1997 161 169
    • (1997) Arch Biochem Biophys , vol.346 , pp. 161-169
    • Yamazaki, H.1    Shimada, T.2
  • 68
    • 79961092809 scopus 로고    scopus 로고
    • Pharmacogenetics of cytochrome P450 (CYP) in the elderly
    • D. Seripa, A. Pilotto, F. Panza, and M.G. Matera Pharmacogenetics of cytochrome P450 (CYP) in the elderly Ageing Res Rev 9 2010 457 474
    • (2010) Ageing Res Rev , vol.9 , pp. 457-474
    • Seripa, D.1    Pilotto, A.2    Panza, F.3    Matera, M.G.4
  • 69
    • 11244284872 scopus 로고    scopus 로고
    • Upstream and coding region CYP2C9 polymorphisms: Correlation with warfarin dose and metabolism
    • B.P. King, T.I. Khan, G.P. Aithal, F. Kamali, and A.K. Daly Upstream and coding region CYP2C9 polymorphisms: correlation with warfarin dose and metabolism Pharmacogenetics 14 2004 813 822
    • (2004) Pharmacogenetics , vol.14 , pp. 813-822
    • King, B.P.1    Khan, T.I.2    Aithal, G.P.3    Kamali, F.4    Daly, A.K.5
  • 70
    • 27444433157 scopus 로고    scopus 로고
    • CYP2C9, CYP2C19, ABCB1 (MDR1) genetic polymorphisms and phenytoin metabolism in a Black Beninese population
    • A.C. Allabi, J.L. Gala, and Y. Horsmans CYP2C9, CYP2C19, ABCB1 (MDR1) genetic polymorphisms and phenytoin metabolism in a Black Beninese population Pharmacogenet Genomics 15 2005 779 786
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 779-786
    • Allabi, A.C.1    Gala, J.L.2    Horsmans, Y.3
  • 72
    • 3242760534 scopus 로고    scopus 로고
    • Identification of a novel variant CYP2C9 allele in Chinese
    • D. Si, Y. Guo, Y. Zhang, L. Yang, H. Zhou, and D. Zhong Identification of a novel variant CYP2C9 allele in Chinese Pharmacogenetics 14 2004 465 469
    • (2004) Pharmacogenetics , vol.14 , pp. 465-469
    • Si, D.1    Guo, Y.2    Zhang, Y.3    Yang, L.4    Zhou, H.5    Zhong, D.6
  • 73
    • 18844392062 scopus 로고    scopus 로고
    • Role of CYP2C9 and its variants (CYP2C93 and CYP2C913) in the metabolism of lornoxicam in humans
    • Y. Guo, Y. Zhang, Y. Wang, X. Chen, D. Si, and D. Zhong Role of CYP2C9 and its variants (CYP2C93 and CYP2C913) in the metabolism of lornoxicam in humans Drug Metab Dispos 33 2005 749 753
    • (2005) Drug Metab Dispos , vol.33 , pp. 749-753
    • Guo, Y.1    Zhang, Y.2    Wang, Y.3    Chen, X.4    Si, D.5    Zhong, D.6
  • 74
    • 4544288090 scopus 로고    scopus 로고
    • Novel CYP2C9 genetic variants in Asian subjects and their influence on maintenance warfarin dose
    • F. Zhao, C. Loke, S.C. Rankin, J.Y. Guo, H.S. Lee, and T.S. Wu Novel CYP2C9 genetic variants in Asian subjects and their influence on maintenance warfarin dose Clin Pharmacol Ther 76 2004 210 219
    • (2004) Clin Pharmacol Ther , vol.76 , pp. 210-219
    • Zhao, F.1    Loke, C.2    Rankin, S.C.3    Guo, J.Y.4    Lee, H.S.5    Wu, T.S.6
  • 75
    • 27744575173 scopus 로고    scopus 로고
    • Functional characterization of novel allelic variants of CYP2C9 recently discovered in southeast Asians
    • T.C. DeLozier, S.C. Lee, S.J. Coulter, B.C. Goh, and J.A. Goldstein Functional characterization of novel allelic variants of CYP2C9 recently discovered in southeast Asians J Pharmacol Exp Ther 315 2005 1085 1090
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 1085-1090
    • Delozier, T.C.1    Lee, S.C.2    Coulter, S.J.3    Goh, B.C.4    Goldstein, J.A.5
  • 77
    • 55449103747 scopus 로고    scopus 로고
    • Genetic variations of CYP2C9 in 724 Japanese individuals and their impact on the antihypertensive effects of losartan
    • T. Yin, K. Maekawa, K. Kamide, Y. Saito, H. Hanada, and K. Miyashita Genetic variations of CYP2C9 in 724 Japanese individuals and their impact on the antihypertensive effects of losartan Hypertens Res 31 2008 1549 1557
    • (2008) Hypertens Res , vol.31 , pp. 1549-1557
    • Yin, T.1    Maekawa, K.2    Kamide, K.3    Saito, Y.4    Hanada, H.5    Miyashita, K.6
  • 78
    • 0035217171 scopus 로고    scopus 로고
    • Identification of a null allele of CYP2C9 in an African-American exhibiting toxicity to phenytoin
    • R.S. Kidd, T.B. Curry, S. Gallagher, T. Edeki, J. Blaisdell, and J.A. Goldstein Identification of a null allele of CYP2C9 in an African-American exhibiting toxicity to phenytoin Pharmacogenetics 11 2001 803 808
    • (2001) Pharmacogenetics , vol.11 , pp. 803-808
    • Kidd, R.S.1    Curry, T.B.2    Gallagher, S.3    Edeki, T.4    Blaisdell, J.5    Goldstein, J.A.6
  • 79
    • 0034978572 scopus 로고    scopus 로고
    • The effect of genetic polymorphism of cytochrome P450 CYP2C9 on phenytoin dose requirement
    • J. van der Weide, L.S. Steijns, M.J. van Weelden, and K. de Haan The effect of genetic polymorphism of cytochrome P450 CYP2C9 on phenytoin dose requirement Pharmacogenetics 11 2001 287 291
    • (2001) Pharmacogenetics , vol.11 , pp. 287-291
    • Van Der Weide, J.1    Steijns, L.S.2    Van Weelden, M.J.3    De Haan, K.4
  • 81
    • 0037012465 scopus 로고    scopus 로고
    • Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy
    • M.K. Higashi, D.L. Veenstra, L.M. Kondo, A.K. Wittkowsky, S.L. Srinouanprachanh, and F.M. Farin Association between CYP2C9 genetic variants and anticoagulation-related outcomes during warfarin therapy JAMA 287 2002 1690 1698
    • (2002) JAMA , vol.287 , pp. 1690-1698
    • Higashi, M.K.1    Veenstra, D.L.2    Kondo, L.M.3    Wittkowsky, A.K.4    Srinouanprachanh, S.L.5    Farin, F.M.6
  • 82
    • 77953304931 scopus 로고    scopus 로고
    • Warfarin genotyping reduces hospitalization rates results from the MM-WES (Medco-Mayo Warfarin Effectiveness study)
    • R.S. Epstein, T.P. Moyer, R.E. Aubert, O.K. DJ, F. Xia, and R.R. Verbrugge Warfarin genotyping reduces hospitalization rates results from the MM-WES (Medco-Mayo Warfarin Effectiveness study) J Am Coll Cardiol 55 2010 2804 2812
    • (2010) J Am Coll Cardiol , vol.55 , pp. 2804-2812
    • Epstein, R.S.1    Moyer, T.P.2    Aubert, R.E.3    Dj, O.K.4    Xia, F.5    Verbrugge, R.R.6
  • 83
    • 84856072430 scopus 로고    scopus 로고
    • Vitamin K antagonists in children with heart disease: Height and VKORC1 genotype are the main determinants of the warfarin dose requirement
    • C. Moreau, F. Bajolle, V. Siguret, D. Lasne, J.L. Golmard, and C. Elie Vitamin K antagonists in children with heart disease: height and VKORC1 genotype are the main determinants of the warfarin dose requirement Blood 119 2012 861 867
    • (2012) Blood , vol.119 , pp. 861-867
    • Moreau, C.1    Bajolle, F.2    Siguret, V.3    Lasne, D.4    Golmard, J.L.5    Elie, C.6
  • 84
    • 78149450633 scopus 로고    scopus 로고
    • Mechanism of the decrease in catalytic activity of human cytochrome P450 2C9 polymorphic variants investigated by computational analysis
    • E. Sano, W. Li, H. Yuki, X. Liu, T. Furihata, and K. Kobayashi Mechanism of the decrease in catalytic activity of human cytochrome P450 2C9 polymorphic variants investigated by computational analysis J Comput Chem 31 2010 2746 2758
    • (2010) J Comput Chem , vol.31 , pp. 2746-2758
    • Sano, E.1    Li, W.2    Yuki, H.3    Liu, X.4    Furihata, T.5    Kobayashi, K.6
  • 85
    • 0031856787 scopus 로고    scopus 로고
    • Characterization of CYP2C19 and CYP2C9 from human liver: Respective roles in microsomal tolbutamide, S-mephenytoin, and omeprazole hydroxylations
    • J.M. Lasker, M.R. Wester, E. Aramsombatdee, and J.L. Raucy Characterization of CYP2C19 and CYP2C9 from human liver: respective roles in microsomal tolbutamide, S-mephenytoin, and omeprazole hydroxylations Arch Biochem Biophys 353 1998 16 28
    • (1998) Arch Biochem Biophys , vol.353 , pp. 16-28
    • Lasker, J.M.1    Wester, M.R.2    Aramsombatdee, E.3    Raucy, J.L.4
  • 86
    • 12244261584 scopus 로고    scopus 로고
    • Identification and functional characterization of new potentially defective alleles of human CYP2C19
    • J. Blaisdell, H. Mohrenweiser, J. Jackson, S. Ferguson, S. Coulter, and B. Chanas Identification and functional characterization of new potentially defective alleles of human CYP2C19 Pharmacogenetics 12 2002 703 711
    • (2002) Pharmacogenetics , vol.12 , pp. 703-711
    • Blaisdell, J.1    Mohrenweiser, H.2    Jackson, J.3    Ferguson, S.4    Coulter, S.5    Chanas, B.6
  • 87
    • 30344457586 scopus 로고    scopus 로고
    • A common novel CYP2C19 gene variant causes ultrarapid drug metabolism relevant for the drug response to proton pump inhibitors and antidepressants
    • S.C. Sim, C. Risinger, M.L. Dahl, E. Aklillu, M. Christensen, and L. Bertilsson A common novel CYP2C19 gene variant causes ultrarapid drug metabolism relevant for the drug response to proton pump inhibitors and antidepressants Clin Pharmacol Ther 79 2006 103 113
    • (2006) Clin Pharmacol Ther , vol.79 , pp. 103-113
    • Sim, S.C.1    Risinger, C.2    Dahl, M.L.3    Aklillu, E.4    Christensen, M.5    Bertilsson, L.6
  • 89
    • 84859747728 scopus 로고    scopus 로고
    • Cytochromes P450 catalyze both steps of the major pathway of clopidogrel bioactivation, whereas paraoxonase catalyzes the formation of a minor thiol metabolite isomer
    • P.M. Dansette, J. Rosi, G. Bertho, and D. Mansuy Cytochromes P450 catalyze both steps of the major pathway of clopidogrel bioactivation, whereas paraoxonase catalyzes the formation of a minor thiol metabolite isomer Chem Res Toxicol 25 2012 348 356
    • (2012) Chem Res Toxicol , vol.25 , pp. 348-356
    • Dansette, P.M.1    Rosi, J.2    Bertho, G.3    Mansuy, D.4
  • 90
    • 77955416969 scopus 로고    scopus 로고
    • Isolated and interactive impact of common CYP2C19 genetic variants on the antiplatelet effect of chronic clopidogrel therapy
    • D. Sibbing, D. Gebhard, W. Koch, S. Braun, J. Stegherr, and T. Morath Isolated and interactive impact of common CYP2C19 genetic variants on the antiplatelet effect of chronic clopidogrel therapy J Thromb Haemostasis 8 2010 1685 1693
    • (2010) J Thromb Haemostasis , vol.8 , pp. 1685-1693
    • Sibbing, D.1    Gebhard, D.2    Koch, W.3    Braun, S.4    Stegherr, J.5    Morath, T.6
  • 91
    • 0742286803 scopus 로고    scopus 로고
    • Cytochrome P450 2D6: Overview and update on pharmacology, genetics, biochemistry
    • U.M. Zanger, S. Raimundo, and M. Eichelbaum Cytochrome P450 2D6: overview and update on pharmacology, genetics, biochemistry Naunyn Schmiedebergs Arch Pharmacol 369 2004 23 37
    • (2004) Naunyn Schmiedebergs Arch Pharmacol , vol.369 , pp. 23-37
    • Zanger, U.M.1    Raimundo, S.2    Eichelbaum, M.3
  • 92
    • 85027954420 scopus 로고    scopus 로고
    • The Human Cytochrome P450 (CYP) Allele Nomenclature website: A peer-reviewed database of CYP variants and their associated effects
    • S.C. Sim, and M. Ingelman-Sundberg The Human Cytochrome P450 (CYP) Allele Nomenclature website: a peer-reviewed database of CYP variants and their associated effects Hum Genomics 4 2010 278 281
    • (2010) Hum Genomics , vol.4 , pp. 278-281
    • Sim, S.C.1    Ingelman-Sundberg, M.2
  • 93
    • 2042512985 scopus 로고    scopus 로고
    • CYP2D6 genotype: Impact on adverse effects and nonresponse during treatment with antidepressants - A pilot study
    • T. Rau, G. Wohlleben, H. Wuttke, N. Thuerauf, J. Lunkenheimer, and M. Lanczik CYP2D6 genotype: impact on adverse effects and nonresponse during treatment with antidepressants - a pilot study Clin Pharmacol Ther 75 2004 386 393
    • (2004) Clin Pharmacol Ther , vol.75 , pp. 386-393
    • Rau, T.1    Wohlleben, G.2    Wuttke, H.3    Thuerauf, N.4    Lunkenheimer, J.5    Lanczik, M.6
  • 94
    • 33846465345 scopus 로고    scopus 로고
    • Safety of codeine during breastfeeding: Fatal morphine poisoning in the breastfed neonate of a mother prescribed codeine
    • P. Madadi, G. Koren, J. Cairns, D. Chitayat, A. Gaedigk, and J.S. Leeder Safety of codeine during breastfeeding: fatal morphine poisoning in the breastfed neonate of a mother prescribed codeine Can Fam Physician 53 2007 33 35
    • (2007) Can Fam Physician , vol.53 , pp. 33-35
    • Madadi, P.1    Koren, G.2    Cairns, J.3    Chitayat, D.4    Gaedigk, A.5    Leeder, J.S.6
  • 96
    • 80052340721 scopus 로고    scopus 로고
    • Structure and dynamics of the membrane-bound cytochrome P450 2C9
    • V. Cojocaru, K. Balali-Mood, M.S. Sansom, and R.C. Wade Structure and dynamics of the membrane-bound cytochrome P450 2C9 PLoS Comput Biol 7 2011 e1002152
    • (2011) PLoS Comput Biol , vol.7 , pp. 1002152
    • Cojocaru, V.1    Balali-Mood, K.2    Sansom, M.S.3    Wade, R.C.4
  • 97
    • 0031884233 scopus 로고    scopus 로고
    • Assessment of the predictive power of genotypes for the in-vivo catalytic function of CYP2D6 in a German population
    • E.U. Griese, U.M. Zanger, U. Brudermanns, A. Gaedigk, G. Mikus, and K. Morike Assessment of the predictive power of genotypes for the in-vivo catalytic function of CYP2D6 in a German population Pharmacogenetics 8 1998 15 26
    • (1998) Pharmacogenetics , vol.8 , pp. 15-26
    • Griese, E.U.1    Zanger, U.M.2    Brudermanns, U.3    Gaedigk, A.4    Mikus, G.5    Morike, K.6
  • 98
    • 0031038038 scopus 로고    scopus 로고
    • Cytochrome P450 2D6 variants in a Caucasian population: Allele frequencies and phenotypic consequences
    • C. Sachse, J. Brockmoller, S. Bauer, and I. Roots Cytochrome P450 2D6 variants in a Caucasian population: allele frequencies and phenotypic consequences Am J Hum Genet 60 1997 284 295
    • (1997) Am J Hum Genet , vol.60 , pp. 284-295
    • Sachse, C.1    Brockmoller, J.2    Bauer, S.3    Roots, I.4
  • 99
    • 0029846193 scopus 로고    scopus 로고
    • Rapid detection of CYP2D6 null alleles by long distance- and multiplex-polymerase chain reaction
    • T. Stuven, E.U. Griese, H.K. Kroemer, M. Eichelbaum, and U.M. Zanger Rapid detection of CYP2D6 null alleles by long distance- and multiplex-polymerase chain reaction Pharmacogenetics 6 1996 417 421
    • (1996) Pharmacogenetics , vol.6 , pp. 417-421
    • Stuven, T.1    Griese, E.U.2    Kroemer, H.K.3    Eichelbaum, M.4    Zanger, U.M.5
  • 100
    • 0029622336 scopus 로고
    • An efficient strategy for detection of known and new mutations of the CYP2D6 gene using single strand conformation polymorphism analysis
    • F. Broly, D. Marez, N. Sabbagh, M. Legrand, S. Millecamps, and J.M. Lo Guidice An efficient strategy for detection of known and new mutations of the CYP2D6 gene using single strand conformation polymorphism analysis Pharmacogenetics 5 1995 373 384
    • (1995) Pharmacogenetics , vol.5 , pp. 373-384
    • Broly, F.1    Marez, D.2    Sabbagh, N.3    Legrand, M.4    Millecamps, S.5    Lo Guidice, J.M.6
  • 101
    • 57149135263 scopus 로고    scopus 로고
    • Pharmacogenetic testing in psychiatry: A review of features and clinical realities
    • J. de Leon, M.J. Arranz, and G. Ruano Pharmacogenetic testing in psychiatry: a review of features and clinical realities Clin Lab Med 28 2008 599 617
    • (2008) Clin Lab Med , vol.28 , pp. 599-617
    • De Leon, J.1    Arranz, M.J.2    Ruano, G.3
  • 102
    • 84882989719 scopus 로고    scopus 로고
    • Update on allele nomenclature for human cytochromes P450 and the Human Cytochrome P450 Allele (CYP-allele) Nomenclature Database
    • S.C. Sim, and M. Ingelman-Sundberg Update on allele nomenclature for human cytochromes P450 and the Human Cytochrome P450 Allele (CYP-allele) Nomenclature Database Methods Mol Biol 987 2013 251 259
    • (2013) Methods Mol Biol , vol.987 , pp. 251-259
    • Sim, S.C.1    Ingelman-Sundberg, M.2
  • 103
    • 75549086408 scopus 로고    scopus 로고
    • SuperCYP: A comprehensive database on cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions
    • S. Preissner, K. Kroll, M. Dunkel, C. Senger, G. Goldsobel, and D. Kuzman SuperCYP: a comprehensive database on cytochrome P450 enzymes including a tool for analysis of CYP-drug interactions Nucleic Acids Res 38 2010 D237 D243
    • (2010) Nucleic Acids Res , vol.38
    • Preissner, S.1    Kroll, K.2    Dunkel, M.3    Senger, C.4    Goldsobel, G.5    Kuzman, D.6
  • 104
    • 84861052952 scopus 로고    scopus 로고
    • Analyzing effects of naturally occurring missense mutations
    • Z. Zhang, M.A. Miteva, L. Wang, and E. Alexov Analyzing effects of naturally occurring missense mutations Comput Math Methods Med 2012 2012 805827
    • (2012) Comput Math Methods Med , vol.2012 , pp. 805827
    • Zhang, Z.1    Miteva, M.A.2    Wang, L.3    Alexov, E.4
  • 105
    • 84882771490 scopus 로고    scopus 로고
    • A rational free energy-based approach to understanding and targeting disease-causing missense mutations
    • Z. Zhang, S. Witham, M. Petukh, G. Moroy, M. Miteva, and Y. Ikeguchi A rational free energy-based approach to understanding and targeting disease-causing missense mutations J Am Med Inform Assoc 20 2013 643 651
    • (2013) J Am Med Inform Assoc , vol.20 , pp. 643-651
    • Zhang, Z.1    Witham, S.2    Petukh, M.3    Moroy, G.4    Miteva, M.5    Ikeguchi, Y.6
  • 106
    • 17444419765 scopus 로고    scopus 로고
    • Mapping SNPs to protein sequence and structure data
    • A. Cavallo, and A.C. Martin Mapping SNPs to protein sequence and structure data Bioinformatics 21 2005 1443 1450
    • (2005) Bioinformatics , vol.21 , pp. 1443-1450
    • Cavallo, A.1    Martin, A.C.2
  • 107
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 108
    • 0036879348 scopus 로고    scopus 로고
    • Genomics of steroid hormones: In silico analysis of nucleotide sequence variants (polymorphisms) of the enzymes involved in the biosynthesis and metabolism of steroid hormones
    • P. Igaz, E. Pap, A. Patocs, A. Falus, Z. Tulassay, and K. Racz Genomics of steroid hormones: in silico analysis of nucleotide sequence variants (polymorphisms) of the enzymes involved in the biosynthesis and metabolism of steroid hormones J Steroid Biochem Mol Biol 82 2002 359 367
    • (2002) J Steroid Biochem Mol Biol , vol.82 , pp. 359-367
    • Igaz, P.1    Pap, E.2    Patocs, A.3    Falus, A.4    Tulassay, Z.5    Racz, K.6
  • 110
    • 77953602809 scopus 로고    scopus 로고
    • Testing computational prediction of missense mutation phenotypes: Functional characterization of 204 mutations of human cystathionine beta synthase
    • Q. Wei, L. Wang, Q. Wang, W.D. Kruger, and R.L. Dunbrack Testing computational prediction of missense mutation phenotypes: functional characterization of 204 mutations of human cystathionine beta synthase Proteins 78 2010 2058 2074
    • (2010) Proteins , vol.78 , pp. 2058-2074
    • Wei, Q.1    Wang, L.2    Wang, Q.3    Kruger, W.D.4    Dunbrack, R.L.5
  • 111
    • 33645764714 scopus 로고    scopus 로고
    • SNPs3D: Candidate gene and SNP selection for association studies
    • P. Yue, E. Melamud, and J. Moult SNPs3D: candidate gene and SNP selection for association studies BMC Bioinformatics 7 2006 166
    • (2006) BMC Bioinformatics , vol.7 , pp. 166
    • Yue, P.1    Melamud, E.2    Moult, J.3
  • 112
    • 0043122919 scopus 로고    scopus 로고
    • SIFT: Predicting amino acid changes that affect protein function
    • P.C. Ng, and S. Henikoff SIFT: predicting amino acid changes that affect protein function Nucleic Acids Res 31 2003 3812 3814
    • (2003) Nucleic Acids Res , vol.31 , pp. 3812-3814
    • Ng, P.C.1    Henikoff, S.2
  • 114
    • 66449133554 scopus 로고    scopus 로고
    • A bioinformatics approach for the phenotype prediction of nonsynonymous single nucleotide polymorphisms in human cytochromes P450
    • L.L. Wang, Y. Li, and S.F. Zhou A bioinformatics approach for the phenotype prediction of nonsynonymous single nucleotide polymorphisms in human cytochromes P450 Drug Metab Dispos 37 2009 977 991
    • (2009) Drug Metab Dispos , vol.37 , pp. 977-991
    • Wang, L.L.1    Li, Y.2    Zhou, S.F.3
  • 115
    • 37648998629 scopus 로고    scopus 로고
    • Getting to the root of miRNA-mediated gene silencing
    • A. Eulalio, E. Huntzinger, and E. Izaurralde Getting to the root of miRNA-mediated gene silencing Cell 132 2008 9 14
    • (2008) Cell , vol.132 , pp. 9-14
    • Eulalio, A.1    Huntzinger, E.2    Izaurralde, E.3
  • 116
    • 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
    • N.R. Smalheiser EST analyses predict the existence of a population of chimeric microRNA precursor-mRNA transcripts expressed in normal human and mouse tissues Genome Biol 4 2003 403
    • (2003) Genome Biol , vol.4 , pp. 403
    • Smalheiser, N.R.1
  • 120
    • 34748821761 scopus 로고    scopus 로고
    • The role of site accessibility in microRNA target recognition
    • M. Kertesz, N. Iovino, U. Unnerstall, U. Gaul, and E. Segal The role of site accessibility in microRNA target recognition Nat Genet 39 2007 1278 1284
    • (2007) Nat Genet , vol.39 , pp. 1278-1284
    • Kertesz, M.1    Iovino, N.2    Unnerstall, U.3    Gaul, U.4    Segal, E.5
  • 121
    • 0029995711 scopus 로고    scopus 로고
    • A three-dimensional protein model for human cytochrome P450 2D6 based on the crystal structures of P450 101, P450 102, and P450 108
    • M.J. de Groot, N.P. Vermeulen, J.D. Kramer, F.A. van Acker, and G.M. Donne-Op den Kelder A three-dimensional protein model for human cytochrome P450 2D6 based on the crystal structures of P450 101, P450 102, and P450 108 Chem Res Toxicol 9 1996 1079 1091
    • (1996) Chem Res Toxicol , vol.9 , pp. 1079-1091
    • De Groot, M.J.1    Vermeulen, N.P.2    Kramer, J.D.3    Van Acker, F.A.4    Donne-Op Den Kelder, G.M.5
  • 122
    • 0034962557 scopus 로고    scopus 로고
    • Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome p450 active sites
    • S. Ekins, M.J. de Groot, and J.P. Jones Pharmacophore and three-dimensional quantitative structure activity relationship methods for modeling cytochrome p450 active sites Drug Metab Dispos 29 2001 936 944
    • (2001) Drug Metab Dispos , vol.29 , pp. 936-944
    • Ekins, S.1    De Groot, M.J.2    Jones, J.P.3
  • 123
    • 33847129220 scopus 로고    scopus 로고
    • 3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design
    • J.F. Wang, D.Q. Wei, L. Li, S.Y. Zheng, Y.X. Li, and K.C. Chou 3D structure modeling of cytochrome P450 2C19 and its implication for personalized drug design Biochem Biophys Res Commun 355 2007 513 519
    • (2007) Biochem Biophys Res Commun , vol.355 , pp. 513-519
    • Wang, J.F.1    Wei, D.Q.2    Li, L.3    Zheng, S.Y.4    Li, Y.X.5    Chou, K.C.6
  • 125
    • 77949904078 scopus 로고    scopus 로고
    • In silico toxicology in drug discovery - Concepts based on three-dimensional models
    • A. Vedani, and M. Smiesko In silico toxicology in drug discovery - concepts based on three-dimensional models Altern Lab Anim 37 2009 477 496
    • (2009) Altern Lab Anim , vol.37 , pp. 477-496
    • Vedani, A.1    Smiesko, M.2
  • 126
    • 79958186689 scopus 로고    scopus 로고
    • Utility of protein structures in overcoming ADMET-related issues of drug-like compounds
    • F. Stoll, A.H. Goller, and A. Hillisch Utility of protein structures in overcoming ADMET-related issues of drug-like compounds Drug Discov Today 16 2011 530 538
    • (2011) Drug Discov Today , vol.16 , pp. 530-538
    • Stoll, F.1    Goller, A.H.2    Hillisch, A.3
  • 127
    • 84859178050 scopus 로고    scopus 로고
    • Computational prediction of metabolism: Sites, products, SAR, P450 enzyme dynamics, and mechanisms
    • J. Kirchmair, M.J. Williamson, J.D. Tyzack, L. Tan, P.J. Bond, and A. Bender Computational prediction of metabolism: sites, products, SAR, P450 enzyme dynamics, and mechanisms J Chem Inf Model 52 2012 617 648
    • (2012) J Chem Inf Model , vol.52 , pp. 617-648
    • Kirchmair, J.1    Williamson, M.J.2    Tyzack, J.D.3    Tan, L.4    Bond, P.J.5    Bender, A.6
  • 128
    • 77952985827 scopus 로고    scopus 로고
    • Improved ligand-protein binding affinity predictions using multiple binding modes
    • E. Stjernschantz, and C. Oostenbrink Improved ligand-protein binding affinity predictions using multiple binding modes Biophys J 98 2010 2682 2691
    • (2010) Biophys J , vol.98 , pp. 2682-2691
    • Stjernschantz, E.1    Oostenbrink, C.2
  • 129
    • 84879596752 scopus 로고    scopus 로고
    • Prediction of cytochrome P450 xenobiotic metabolism: Tethered docking and reactivity derived from ligand molecular orbital analysis
    • J.D. Tyzack, M.J. Williamson, R. Torella, and R.C. Glen Prediction of cytochrome P450 xenobiotic metabolism: tethered docking and reactivity derived from ligand molecular orbital analysis J Chem Inf Model 53 2013 1294 1305
    • (2013) J Chem Inf Model , vol.53 , pp. 1294-1305
    • Tyzack, J.D.1    Williamson, M.J.2    Torella, R.3    Glen, R.C.4
  • 131
    • 78651478620 scopus 로고    scopus 로고
    • Probing small-molecule binding to cytochrome P450 2D6 and 2C9: An in silico protocol for generating toxicity alerts
    • G. Rossato, B. Ernst, M. Smiesko, M. Spreafico, and A. Vedani Probing small-molecule binding to cytochrome P450 2D6 and 2C9: an in silico protocol for generating toxicity alerts ChemMedChem 5 2010 2088 2101
    • (2010) ChemMedChem , vol.5 , pp. 2088-2101
    • Rossato, G.1    Ernst, B.2    Smiesko, M.3    Spreafico, M.4    Vedani, A.5
  • 132
    • 79251568943 scopus 로고    scopus 로고
    • Structure-based analysis of five novel disease-causing mutations in 21-hydroxylase-deficient patients
    • C. Minutolo, A.D. Nadra, C. Fernandez, M. Taboas, N. Buzzalino, and B. Casali Structure-based analysis of five novel disease-causing mutations in 21-hydroxylase-deficient patients PLoS One 6 2011 e15899
    • (2011) PLoS One , vol.6 , pp. 15899
    • Minutolo, C.1    Nadra, A.D.2    Fernandez, C.3    Taboas, M.4    Buzzalino, N.5    Casali, B.6
  • 133
    • 66149102833 scopus 로고    scopus 로고
    • Modeling effects of human single nucleotide polymorphisms on protein-protein interactions
    • S. Teng, T. Madej, A. Panchenko, and E. Alexov Modeling effects of human single nucleotide polymorphisms on protein-protein interactions Biophys J 96 2009 2178 2188
    • (2009) Biophys J , vol.96 , pp. 2178-2188
    • Teng, S.1    Madej, T.2    Panchenko, A.3    Alexov, E.4
  • 135
    • 40349087133 scopus 로고    scopus 로고
    • Towards the development of universal, fast and highly accurate docking/scoring methods: A long way to go
    • N. Moitessier, P. Englebienne, D. Lee, J. Lawandi, and C.R. Corbeil Towards the development of universal, fast and highly accurate docking/scoring methods: a long way to go Br J Pharmacol 153 2008 S7 S26
    • (2008) Br J Pharmacol , vol.153
    • Moitessier, N.1    Englebienne, P.2    Lee, D.3    Lawandi, J.4    Corbeil, C.R.5
  • 136
    • 84875480305 scopus 로고    scopus 로고
    • Latest developments in molecular docking
    • E. Yuriev, and P.A. Ramsland Latest developments in molecular docking J Mol Recognit 26 2013 215 239
    • (2013) J Mol Recognit , vol.26 , pp. 215-239
    • Yuriev, E.1    Ramsland, P.A.2
  • 137
    • 79959224583 scopus 로고    scopus 로고
    • Molecular docking: A powerful approach for structure-based drug discovery
    • X.Y. Meng, H.X. Zhang, M. Mezei, and M. Cui Molecular docking: a powerful approach for structure-based drug discovery Curr Comput Aided Drug Des 7 2011 146 157
    • (2011) Curr Comput Aided Drug des , vol.7 , pp. 146-157
    • Meng, X.Y.1    Zhang, H.X.2    Mezei, M.3    Cui, M.4
  • 138
  • 139
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • S.J. Teague Implications of protein flexibility for drug discovery Nat Rev Drug Discov 2 2003 527 541
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 140
    • 84879596358 scopus 로고    scopus 로고
    • Structural basis for the mutation-induced dysfunction of human CYP2J2: A computational study
    • S. Cong, X.T. Ma, Y.X. Li, and J.F. Wang Structural basis for the mutation-induced dysfunction of human CYP2J2: a computational study J Chem Inf Model 53 2013 1350 1357
    • (2013) J Chem Inf Model , vol.53 , pp. 1350-1357
    • Cong, S.1    Ma, X.T.2    Li, Y.X.3    Wang, J.F.4
  • 142
    • 20844452556 scopus 로고    scopus 로고
    • Risk of coronary artery disease associated with polymorphism of the cytochrome P450 epoxygenase CYP2J2
    • M. Spiecker, H. Darius, T. Hankeln, M. Soufi, A.M. Sattler, and J.R. Schaefer Risk of coronary artery disease associated with polymorphism of the cytochrome P450 epoxygenase CYP2J2 Circulation 110 2004 2132 2136
    • (2004) Circulation , vol.110 , pp. 2132-2136
    • Spiecker, M.1    Darius, H.2    Hankeln, T.3    Soufi, M.4    Sattler, A.M.5    Schaefer, J.R.6
  • 143
    • 17644385223 scopus 로고    scopus 로고
    • Identification and functional characterization of novel CYP2J2 variants: G312R variant causes loss of enzyme catalytic activity
    • S.S. Lee, H.E. Jeong, K.H. Liu, J.Y. Ryu, T. Moon, and C.N. Yoon Identification and functional characterization of novel CYP2J2 variants: G312R variant causes loss of enzyme catalytic activity Pharmacogenet Genomics 15 2005 105 113
    • (2005) Pharmacogenet Genomics , vol.15 , pp. 105-113
    • Lee, S.S.1    Jeong, H.E.2    Liu, K.H.3    Ryu, J.Y.4    Moon, T.5    Yoon, C.N.6
  • 144
    • 80053426513 scopus 로고    scopus 로고
    • Role of a mutated residue at the entrance of the substrate access channel in cytochrome p450 engineered for vitamin D(3) hydroxylation activity
    • H. Fukunishi, H. Yagi, K. Kamijo, and J. Shimada Role of a mutated residue at the entrance of the substrate access channel in cytochrome p450 engineered for vitamin D(3) hydroxylation activity Biochemistry 50 2011 8302 8310
    • (2011) Biochemistry , vol.50 , pp. 8302-8310
    • Fukunishi, H.1    Yagi, H.2    Kamijo, K.3    Shimada, J.4
  • 145
    • 70350028665 scopus 로고    scopus 로고
    • Effect of conformational dynamics on substrate recognition and specificity as probed by the introduction of a de novo disulfide bond into cytochrome P450 2B1
    • H. Zhang, C. Kenaan, D. Hamdane, G.H. Hoa, and P.F. Hollenberg Effect of conformational dynamics on substrate recognition and specificity as probed by the introduction of a de novo disulfide bond into cytochrome P450 2B1 J Biol Chem 284 2009 25678 25686
    • (2009) J Biol Chem , vol.284 , pp. 25678-25686
    • Zhang, H.1    Kenaan, C.2    Hamdane, D.3    Hoa, G.H.4    Hollenberg, P.F.5


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