메뉴 건너뛰기




Volumn 573, Issue 1-2, 2005, Pages 180-194

Pharmacogenetic testing: Proofs of principle and pharmacoeconomic implications

Author keywords

Pharmacoeconomics; Pharmacogenetics

Indexed keywords

5,10 METHYLENETETRAHYDROFOLATE REDUCTASE (FADH2); 6 MERCAPTOPURINE DERIVATIVE; 7 ETHYL 10 HYDROXYCAMPTOTHECIN; ABACAVIR; ANTIRETROVIRUS AGENT; AZATHIOPRINE; CYTOCHROME P450 2C9; DIHYDROPYRIDINE DEHYDROGENASE; FLUOROURACIL; FOLIC ACID; GENERIC DRUG; IRINOTECAN; MERCAPTOPURINE; METHOTREXATE; OXIDOREDUCTASE; THIOPURINE METHYLTRANSFERASE; THYMIDYLATE SYNTHASE; TIOGUANINE; UNCLASSIFIED DRUG; WARFARIN;

EID: 17044418894     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2004.07.025     Document Type: Review
Times cited : (48)

References (110)
  • 2
    • 0000616920 scopus 로고
    • Enzymatic deficiency in primaquine-sensitive erythrocytes
    • A.S. Alving, P.E. Carson, C.L. Flanagan, and C.E. Ickes Enzymatic deficiency in primaquine-sensitive erythrocytes Science 124 1956 484 485
    • (1956) Science , vol.124 , pp. 484-485
    • Alving, A.S.1    Carson, P.E.2    Flanagan, C.L.3    Ickes, C.E.4
  • 3
    • 49749223413 scopus 로고
    • The familial incidence of low pseudocholinesterase level
    • W. Kalow The familial incidence of low pseudocholinesterase level Lancet 271 1956 124
    • (1956) Lancet , vol.271 , pp. 124
    • Kalow, W.1
  • 4
    • 26444539817 scopus 로고
    • Genetic control of isoniazid metabolism in man
    • D.A. Evans, K.A. Manley, and V.A. McKusick Genetic control of isoniazid metabolism in man Br. Med. 5197 1960 485 491
    • (1960) Br. Med. , vol.5197 , pp. 485-491
    • Evans, D.A.1    Manley, K.A.2    McKusick, V.A.3
  • 5
    • 0023854270 scopus 로고
    • Characterization of the common genetic defect in humans deficient in debrisoquine metabolism
    • F.J. Gonzalez, R.C. Skoda, S. Kimura, M. Umeno, U.M. Zanger, and D.W. Nebert Characterization of the common genetic defect in humans deficient in debrisoquine metabolism Nature 331 1988 442 446
    • (1988) Nature , vol.331 , pp. 442-446
    • Gonzalez, F.J.1    Skoda, R.C.2    Kimura, S.3    Umeno, M.4    Zanger, U.M.5    Nebert, D.W.6
  • 6
    • 0030995879 scopus 로고    scopus 로고
    • Molecular mechanisms of genetic polymorphisms of drug metabolism
    • U.A. Meyer, and U.M. Zanger Molecular mechanisms of genetic polymorphisms of drug metabolism Annu. Rev. Pharmacol. Toxicol. 37 1997 269 296
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 269-296
    • Meyer, U.A.1    Zanger, U.M.2
  • 7
    • 0027136288 scopus 로고
    • Inherited amplification of an active gene in the cytochrome P450 CYP2D locus as a cause of ultrarapid metabolism of debrisoquine
    • I. Johansson, E. Lundqvist, L. Bertilsson, M.L. Dahl, F. Sjoqvist, and M. Ingelman-Sundberg Inherited amplification of an active gene in the cytochrome P450 CYP2D locus as a cause of ultrarapid metabolism of debrisoquine Proc. Natl. Acad. Sci. U.S.A. 90 1993 11825 11829
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11825-11829
    • Johansson, I.1    Lundqvist, E.2    Bertilsson, L.3    Dahl, M.L.4    Sjoqvist, F.5    Ingelman-Sundberg, M.6
  • 8
    • 0035865322 scopus 로고    scopus 로고
    • A map of human genome sequence variation containing 1.42 million single nucleotide polymorphisms
    • R. Sachidanandam, D. Weissman, S.C. Schmidt, J.M. Kakol, L.D. Stein, and G. Marth A map of human genome sequence variation containing 1.42 million single nucleotide polymorphisms Nature 409 2001 928 933
    • (2001) Nature , vol.409 , pp. 928-933
    • Sachidanandam, R.1    Weissman, D.2    Schmidt, S.C.3    Kakol, J.M.4    Stein, L.D.5    Marth, G.6
  • 9
    • 0344035401 scopus 로고    scopus 로고
    • Monitoring of AZA/6-MP treatment in children with IBD is necessary
    • M.C. Dubinsky Monitoring of AZA/6-MP treatment in children with IBD is necessary Inflamm. Bowel Dis. 9 2003 386 388
    • (2003) Inflamm. Bowel Dis. , vol.9 , pp. 386-388
    • Dubinsky, M.C.1
  • 10
    • 0034067784 scopus 로고    scopus 로고
    • Pharmacogenomics and metabolite measurement for 6-mercaptopurine therapy in inflammatory bowel disease
    • M.C. Dubinsky, S. Lamothe, H.Y. Yang, S.R. Targan, D. Sinnett, and Y. Theoret Pharmacogenomics and metabolite measurement for 6-mercaptopurine therapy in inflammatory bowel disease Gastroenterology 118 2000 705 713
    • (2000) Gastroenterology , vol.118 , pp. 705-713
    • Dubinsky, M.C.1    Lamothe, S.2    Yang, H.Y.3    Targan, S.R.4    Sinnett, D.5    Theoret, Y.6
  • 11
    • 0025331198 scopus 로고
    • Genetic variation in response to 6-mercaptopurine for childhood acute lymphoblastic leukaemia
    • L. Lennard, J.S. Lilleyman, J. Van Loon, and R.M. Weinshilboum Genetic variation in response to 6-mercaptopurine for childhood acute lymphoblastic leukaemia Lancet 336 1990 225 229
    • (1990) Lancet , vol.336 , pp. 225-229
    • Lennard, L.1    Lilleyman, J.S.2    Van Loon, J.3    Weinshilboum, R.M.4
  • 13
    • 0026758498 scopus 로고
    • The clinical pharmacology of 6-mercaptopurine
    • L. Lennard The clinical pharmacology of 6-mercaptopurine Eur. J. Clin. Pharmacol. 43 1992 329 339
    • (1992) Eur. J. Clin. Pharmacol. , vol.43 , pp. 329-339
    • Lennard, L.1
  • 14
    • 0035423158 scopus 로고    scopus 로고
    • Differing contribution of thiopurine methyltransferase to mercaptopurine versus thioguanine effects in human leukemic cells
    • T. Dervieux, J.G. Blanco, E.Y. Krynetski, E.F. Vanin, M.F. Roussel, and M.V. Relling Differing contribution of thiopurine methyltransferase to mercaptopurine versus thioguanine effects in human leukemic cells Cancer Res. 61 2001 5810 5816
    • (2001) Cancer Res. , vol.61 , pp. 5810-5816
    • Dervieux, T.1    Blanco, J.G.2    Krynetski, E.Y.3    Vanin, E.F.4    Roussel, M.F.5    Relling, M.V.6
  • 15
    • 0242464926 scopus 로고    scopus 로고
    • CD28-dependent Rac1 activation is the molecular target of azathioprine in primary human CD4+ T lymphocytes
    • I. Tiede, G. Fritz, S. Strand, D. Poppe, R. Dvorsky, and D. Strand CD28-dependent Rac1 activation is the molecular target of azathioprine in primary human CD4+ T lymphocytes J. Clin. Invest. 111 2003 1133 1145
    • (2003) J. Clin. Invest. , vol.111 , pp. 1133-1145
    • Tiede, I.1    Fritz, G.2    Strand, S.3    Poppe, D.4    Dvorsky, R.5    Strand, D.6
  • 16
    • 0018822866 scopus 로고
    • Mercaptopurine pharmacogenetics: Monogenic inheritance of erythrocyte thiopurine methyltransferase activity
    • R.M. Weinshilboum, and S.L. Sladek Mercaptopurine pharmacogenetics: monogenic inheritance of erythrocyte thiopurine methyltransferase activity Am. J. Hum. Genet. 32 1980 651 662
    • (1980) Am. J. Hum. Genet. , vol.32 , pp. 651-662
    • Weinshilboum, R.M.1    Sladek, S.L.2
  • 17
    • 0029919807 scopus 로고    scopus 로고
    • Thiopurine S-methyltransferase deficiency: Two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians
    • H.L. Tai, E.Y. Krynetski, C.R. Yates, T. Loennechen, M.Y. Fessing, and N.F. Krynetskaia Thiopurine S-methyltransferase deficiency: two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians Am. J. Hum. Genet. 58 1996 694 702
    • (1996) Am. J. Hum. Genet. , vol.58 , pp. 694-702
    • Tai, H.L.1    Krynetski, E.Y.2    Yates, C.R.3    Loennechen, T.4    Fessing, M.Y.5    Krynetskaia, N.F.6
  • 18
    • 0030934850 scopus 로고    scopus 로고
    • Molecular diagnosis of thiopurine S-methyltransferase deficiency: Genetic basis for azathioprine and mercaptopurine intolerance
    • C.R. Yates, E.Y. Krynetski, T. Loennechen, M.Y. Fessing, H.L. Tai, and C.-H. Pui Molecular diagnosis of thiopurine S-methyltransferase deficiency: genetic basis for azathioprine and mercaptopurine intolerance Ann. Int. Med. 126 1997 608 614
    • (1997) Ann. Int. Med. , vol.126 , pp. 608-614
    • Yates, C.R.1    Krynetski, E.Y.2    Loennechen, T.3    Fessing, M.Y.4    Tai, H.L.5    Pui, C.-H.6
  • 20
    • 0030986251 scopus 로고    scopus 로고
    • Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): Mechanisms for the genetic polymorphism of TPMT activity
    • H.L. Tai, E.Y. Krynetski, E.G. Schuetz, Y. Yanishevski, and W.E. Evans Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2): mechanisms for the genetic polymorphism of TPMT activity Proc. Natl. Acad. Sci. U.S.A. 94 1997 6444 6449
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6444-6449
    • Tai, H.L.1    Krynetski, E.Y.2    Schuetz, E.G.3    Yanishevski, Y.4    Evans, W.E.5
  • 21
    • 0032693405 scopus 로고    scopus 로고
    • Enhanced proteosomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: Mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C
    • H.-L. Tai, M. Fessing, E.J. Bonten, Y. Yanishevski, A. d'Azzo, E. Krynetski, and W.E. Evans Enhanced proteosomal degradation of mutant human thiopurine S-methyltransferase (TPMT) in mammalian cells: mechanism for TPMT protein deficiency inherited by TPMT*2, TPMT*3A, TPMT*3B or TPMT*3C Pharmacogenetics 9 1999 641 650
    • (1999) Pharmacogenetics , vol.9 , pp. 641-650
    • Tai, H.-L.1    Fessing, M.2    Bonten, E.J.3    Yanishevski, Y.4    D'Azzo, A.5    Krynetski, E.6    Evans, W.E.7
  • 22
    • 0027524983 scopus 로고
    • Congenital thiopurine methyltransferase deficiency and 6-mercaptopurine toxicity during treatment for acute lymphoblastic leukaemia
    • L. Lennard, B.E. Gibson, T. Nicole, and J.S. Lilleyman Congenital thiopurine methyltransferase deficiency and 6-mercaptopurine toxicity during treatment for acute lymphoblastic leukaemia Arch. Dis. Child 69 1993 577 579
    • (1993) Arch. Dis. Child , vol.69 , pp. 577-579
    • Lennard, L.1    Gibson, B.E.2    Nicole, T.3    Lilleyman, J.S.4
  • 23
    • 0035166331 scopus 로고    scopus 로고
    • Possible implication of thiopurine S-methyltransferase in the occurrence of infectious episodes during maintenance therapy of acute leukemia with mercaptopurine
    • T. Dervieux, Y. Medard, P. Verpillat, V. Guigonis, M. Duval, B. Lescoeur, S. Suciu, E Vilmer, and E Jacqz-Aigrain Possible implication of thiopurine S-methyltransferase in the occurrence of infectious episodes during maintenance therapy of acute leukemia with mercaptopurine Leukemia 15 11 2001 1706 1712
    • (2001) Leukemia , vol.15 , Issue.11 , pp. 1706-1712
    • Dervieux, T.1    Medard, Y.2    Verpillat, P.3    Guigonis, V.4    Duval, M.5    Lescoeur, B.6    Suciu, S.7    Vilmer, E.8    Jacqz-Aigrain, E.9
  • 24
    • 0038299414 scopus 로고    scopus 로고
    • Azathioprine-induced fatal myelosuppression in a renal-transplant recipient who carried heterozygous TPMT* 1/*3C
    • W. Tassaneeyakul, S. Srimarthpirom, S. Reungjui, K. Chansung, and A. Romphruk Azathioprine-induced fatal myelosuppression in a renal-transplant recipient who carried heterozygous TPMT* 1/*3C Transplantation 76 2003 265 266
    • (2003) Transplantation , vol.76 , pp. 265-266
    • Tassaneeyakul, W.1    Srimarthpirom, S.2    Reungjui, S.3    Chansung, K.4    Romphruk, A.5
  • 25
    • 0027401302 scopus 로고
    • Azathioprine-induced myelosuppression in thiopurine methyltransferase deficient heart transplant recipient
    • E. Schutz, J. Gummert, F. Mohr, and M. Oellerich Azathioprine-induced myelosuppression in thiopurine methyltransferase deficient heart transplant recipient Lancet 341 1993 436
    • (1993) Lancet , vol.341 , pp. 436
    • Schutz, E.1    Gummert, J.2    Mohr, F.3    Oellerich, M.4
  • 26
    • 1242297064 scopus 로고    scopus 로고
    • Pharmacoeconomic analysis of thiopurine methyltransferase polymorphism screening by polymerase chain reaction for treatment with azathioprine in Korea
    • K.T. Oh, A.H. Anis, and S.C. Bae Pharmacoeconomic analysis of thiopurine methyltransferase polymorphism screening by polymerase chain reaction for treatment with azathioprine in Korea Rheumatology (Oxford) 43 2004 156 163
    • (2004) Rheumatology (Oxford) , vol.43 , pp. 156-163
    • Oh, K.T.1    Anis, A.H.2    Bae, S.C.3
  • 27
    • 0036894866 scopus 로고    scopus 로고
    • Practical pharmacogenetics: The cost effectiveness of screening for thiopurine S-methyltransferase polymorphisms in patients with rheumatological conditions treated with azathioprine
    • C.A. Marra, J.M. Esdaile, and A.H. Anis Practical pharmacogenetics: the cost effectiveness of screening for thiopurine S-methyltransferase polymorphisms in patients with rheumatological conditions treated with azathioprine J. Rheumatol. 29 2002 2507 2512
    • (2002) J. Rheumatol. , vol.29 , pp. 2507-2512
    • Marra, C.A.1    Esdaile, J.M.2    Anis, A.H.3
  • 28
    • 0033135738 scopus 로고    scopus 로고
    • Prognostic importance of 6- mercaptopurine dose intensity in acute lymphoblastic leukemia
    • M.V. Relling, M.L. Hancock, J.M. Boyett, C.-H. Pui, and W.E. Evans Prognostic importance of 6- mercaptopurine dose intensity in acute lymphoblastic leukemia Blood 93 1999 2817 2823
    • (1999) Blood , vol.93 , pp. 2817-2823
    • Relling, M.V.1    Hancock, M.L.2    Boyett, J.M.3    Pui, C.-H.4    Evans, W.E.5
  • 29
    • 2342420871 scopus 로고    scopus 로고
    • Thiopurine methyltransferase activity influences clinical response to azathioprine in inflammatory bowel disease
    • C. Cuffari, T. Dassopoulos, L. Turnbough, R.E. Thompson, and T.M. Bayless Thiopurine methyltransferase activity influences clinical response to azathioprine in inflammatory bowel disease Clin. Gastroenterol. Hepatol. 2 2004 410 417
    • (2004) Clin. Gastroenterol. Hepatol. , vol.2 , pp. 410-417
    • Cuffari, C.1    Dassopoulos, T.2    Turnbough, L.3    Thompson, R.E.4    Bayless, T.M.5
  • 30
    • 1842788679 scopus 로고    scopus 로고
    • Methylated metabolites of 6-mercaptopurine are associated with hepatotoxicity
    • U. Nygaard, N. Toft, and K. Schmiegelow Methylated metabolites of 6-mercaptopurine are associated with hepatotoxicity Clin. Pharmacol. Ther. 75 2004 274 281
    • (2004) Clin. Pharmacol. Ther. , vol.75 , pp. 274-281
    • Nygaard, U.1    Toft, N.2    Schmiegelow, K.3
  • 31
    • 0036202803 scopus 로고    scopus 로고
    • 6-MP metabolite profiles provide a biochemical explanation for 6-MP resistance in patients with inflammatory bowel disease
    • M.C. Dubinsky, H. Yang, P.V. Hassard, E.G. Seidman, L.Y. Kam, and M.T. Abreu 6-MP metabolite profiles provide a biochemical explanation for 6-MP resistance in patients with inflammatory bowel disease Gastroenterology 122 2002 904 915
    • (2002) Gastroenterology , vol.122 , pp. 904-915
    • Dubinsky, M.C.1    Yang, H.2    Hassard, P.V.3    Seidman, E.G.4    Kam, L.Y.5    Abreu, M.T.6
  • 32
    • 12144285961 scopus 로고    scopus 로고
    • Adverse drug reactions to azathioprine therapy are associated with polymorphism in the gene encoding inosine triphosphate pyrophosphatase (ITPase)
    • A.M. Marinaki, A. Ansari, J.A. Duley, M. Arenas, S. Sumi, and C.M. Lewis Adverse drug reactions to azathioprine therapy are associated with polymorphism in the gene encoding inosine triphosphate pyrophosphatase (ITPase) Pharmacogenetics 14 2004 181 187
    • (2004) Pharmacogenetics , vol.14 , pp. 181-187
    • Marinaki, A.M.1    Ansari, A.2    Duley, J.A.3    Arenas, M.4    Sumi, S.5    Lewis, C.M.6
  • 33
    • 2342499810 scopus 로고    scopus 로고
    • Toward a better understanding of methotrexate
    • J.M. Kremer Toward a better understanding of methotrexate Arth. Rheum. 50 2004 1370 1382
    • (2004) Arth. Rheum. , vol.50 , pp. 1370-1382
    • Kremer, J.M.1
  • 34
    • 0014410041 scopus 로고
    • Carrier-mediated transport of the folic acid analogue, methotrexate, in the L1210 leukemia cell
    • I.D. Goldman, N.S. Lichtenstein, and V.T. Oliverio Carrier-mediated transport of the folic acid analogue, methotrexate, in the L1210 leukemia cell J. Biol. Chem. 243 1968 5007 5017
    • (1968) J. Biol. Chem. , vol.243 , pp. 5007-5017
    • Goldman, I.D.1    Lichtenstein, N.S.2    Oliverio, V.T.3
  • 35
    • 0041305877 scopus 로고
    • Membrane transport of folates
    • L.H. Matherly, and D.I. Goldman Membrane transport of folates Vit. Horm. 66 1904 403 456
    • (1904) Vit. Horm. , vol.66 , pp. 403-456
    • Matherly, L.H.1    Goldman, D.I.2
  • 38
    • 0032518281 scopus 로고    scopus 로고
    • Methotrexate and sulfasalazine promote adenosine release by a mechanism that requires ecto-5′-nucleotidase-mediated conversion of adenine nucleotides
    • L. Morabito, M.C. Montesinos, D.M. Schreibman, L. Balter, L.F. Thompson, and R. Resta Methotrexate and sulfasalazine promote adenosine release by a mechanism that requires ecto-5′-nucleotidase-mediated conversion of adenine nucleotides J. Clin. Invest. 101 1998 295 300
    • (1998) J. Clin. Invest. , vol.101 , pp. 295-300
    • Morabito, L.1    Montesinos, M.C.2    Schreibman, D.M.3    Balter, L.4    Thompson, L.F.5    Resta, R.6
  • 39
    • 0037207972 scopus 로고    scopus 로고
    • Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68
    • M.C. Montesinos, A. Desai, D. Delano, J.F. Chen, J.S. Fink, and M.A. Jacobson Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68 Arth. Rheum. 48 2003 240 247
    • (2003) Arth. Rheum. , vol.48 , pp. 240-247
    • Montesinos, M.C.1    Desai, A.2    Delano, D.3    Chen, J.F.4    Fink, J.S.5    Jacobson, M.A.6
  • 40
    • 0027139914 scopus 로고
    • The anti-inflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation
    • B.N. Cronstein, D. Naime, and E. Ostad The anti-inflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation J. Clin. Invest. 92 1993 2675 2682
    • (1993) J. Clin. Invest. , vol.92 , pp. 2675-2682
    • Cronstein, B.N.1    Naime, D.2    Ostad, E.3
  • 41
    • 0029049553 scopus 로고
    • A candidate genetic risk factor for vascular disease: A common mutation in methylenetetrahydrofolate reductase
    • P. Frosst, H.J. Blom, R. Milos, P. Goyette, C.A. Sheppard, and R.G. Matthews A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase Nat. Genet. 10 1995 111 113
    • (1995) Nat. Genet. , vol.10 , pp. 111-113
    • Frosst, P.1    Blom, H.J.2    Milos, R.3    Goyette, P.4    Sheppard, C.A.5    Matthews, R.G.6
  • 42
    • 0028487161 scopus 로고
    • Human methylenetetrahydrofolate reductase: Isolation of cDNA, mapping and mutation identification
    • P. Goyette, J.S. Sumner, R. Milos, A.M. Duncan, D.S. Rosenblatt, and R.G. Matthews Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification Nat. Genet. 7 1994 195 200
    • (1994) Nat. Genet. , vol.7 , pp. 195-200
    • Goyette, P.1    Sumner, J.S.2    Milos, R.3    Duncan, A.M.4    Rosenblatt, D.S.5    Matthews, R.G.6
  • 43
    • 0035412398 scopus 로고    scopus 로고
    • Pharmacogenetics of methotrexate: Toxicity among marrow transplantation patients varies with the methylenetetrahydrofolate reductase C677T polymorphism
    • C.M. Ulrich, Y. Yasui, R. Storb, M.M. Schubert, J.L. Wagner, and J. Bigler Pharmacogenetics of methotrexate: toxicity among marrow transplantation patients varies with the methylenetetrahydrofolate reductase C677T polymorphism Blood 98 2001 231 234
    • (2001) Blood , vol.98 , pp. 231-234
    • Ulrich, C.M.1    Yasui, Y.2    Storb, R.3    Schubert, M.M.4    Wagner, J.L.5    Bigler, J.6
  • 44
    • 0030955502 scopus 로고    scopus 로고
    • Thermolabile variant of 5, 10-methylenetetrahydrofolate reductase associated with low red-cell folates: Implications for folate intake recommendations
    • A.M. Molloy, S. Daly, J.L. Mills, P.N. Kirke, A.S. Whitehead, and D. Ramsbottom Thermolabile variant of 5, 10-methylenetetrahydrofolate reductase associated with low red-cell folates: implications for folate intake recommendations Lancet 349 1997 1591 1593
    • (1997) Lancet , vol.349 , pp. 1591-1593
    • Molloy, A.M.1    Daly, S.2    Mills, J.L.3    Kirke, P.N.4    Whitehead, A.S.5    Ramsbottom, D.6
  • 45
    • 2142820811 scopus 로고    scopus 로고
    • Predictors of oral mucositis in patients receiving hematopoietic cell transplants for chronic myelogenous leukemia
    • K. Robien, M.M. Schubert, B. Bruemmer, M.E. Lloid, J.D. Potter, and C.M. Ulrich Predictors of oral mucositis in patients receiving hematopoietic cell transplants for chronic myelogenous leukemia J. Clin. Oncol. 22 2004 1268 1275
    • (2004) J. Clin. Oncol. , vol.22 , pp. 1268-1275
    • Robien, K.1    Schubert, M.M.2    Bruemmer, B.3    Lloid, M.E.4    Potter, J.D.5    Ulrich, C.M.6
  • 46
    • 0036928840 scopus 로고    scopus 로고
    • Preponderance of methylenetetrahydrofolate reductase C677T homozygosity among leukemia patients intolerant to methotrexate
    • P. Chiusolo, G. Reddiconto, I. Casorelli, L. Laurenti, F. Sora, and L. Mele Preponderance of methylenetetrahydrofolate reductase C677T homozygosity among leukemia patients intolerant to methotrexate Ann. Oncol. 13 2002 1915 1918
    • (2002) Ann. Oncol. , vol.13 , pp. 1915-1918
    • Chiusolo, P.1    Reddiconto, G.2    Casorelli, I.3    Laurenti, L.4    Sora, F.5    Mele, L.6
  • 47
    • 0036263469 scopus 로고    scopus 로고
    • Polymorphisms in the methylenetetrahydrofolate reductase gene were associated with both the efficacy and the toxicity of methotrexate used for the treatment of rheumatoid arthritis, as evidenced by single locus and haplotype analyses
    • W. Urano, A. Taniguchi, H. Yamanaka, E. Tanaka, H. Nakajima, and Y. Matsuda Polymorphisms in the methylenetetrahydrofolate reductase gene were associated with both the efficacy and the toxicity of methotrexate used for the treatment of rheumatoid arthritis, as evidenced by single locus and haplotype analyses Pharmacogenetics 12 2002 183 190
    • (2002) Pharmacogenetics , vol.12 , pp. 183-190
    • Urano, W.1    Taniguchi, A.2    Yamanaka, H.3    Tanaka, E.4    Nakajima, H.5    Matsuda, Y.6
  • 48
    • 0035157121 scopus 로고    scopus 로고
    • The C677T mutation in the methylenetetrahydrofolate reductase gene: A genetic risk factor for methotrexate-related elevation of liver enzymes in rheumatoid arthritis patients
    • A.E. van Ede, R.F. Laan, H.J. Blom, T.W. Huizinga, C.J. Haagsma, and B.A. Giesendorf The C677T mutation in the methylenetetrahydrofolate reductase gene: a genetic risk factor for methotrexate-related elevation of liver enzymes in rheumatoid arthritis patients Arth. Rheum. 44 2001 2525 2530
    • (2001) Arth. Rheum. , vol.44 , pp. 2525-2530
    • Van Ede, A.E.1    Laan, R.F.2    Blom, H.J.3    Huizinga, T.W.4    Haagsma, C.J.5    Giesendorf, B.A.6
  • 49
    • 4444376725 scopus 로고    scopus 로고
    • Polyglutamation of methotrexate with common polymorphism in reduced folate carrier, AICAR transformylase and thymidylate synthase are associated with methotrexate effects in rheumatoid arthritis
    • T. Dervieux, D.E. Furst, D. Orentas, R. Lein, K. Capps, M. Smith, J.M. Walsh, and Kremer Polyglutamation of methotrexate with common polymorphism in reduced folate carrier, AICAR transformylase and thymidylate synthase are associated with methotrexate effects in rheumatoid arthritis Arth. Rheum. 50 9 2004 2766 2774
    • (2004) Arth. Rheum. , vol.50 , Issue.9 , pp. 2766-2774
    • Dervieux, T.1    Furst, D.E.2    Orentas, D.3    Lein, R.4    Capps, K.5    Smith Walsh, M.J.M.6    Kremer7
  • 50
    • 0034771885 scopus 로고    scopus 로고
    • A novel single-nucleotide polymorphism in the 3′-untranslated region of the human dihydrofolate reductase gene with enhanced expression
    • Y. Goto, L. Yue, A. Yokoi, R. Nishimura, T. Uehara, and S. Koizumi A novel single-nucleotide polymorphism in the 3′-untranslated region of the human dihydrofolate reductase gene with enhanced expression Clin. Cancer Res. 7 2001 1952 1956
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1952-1956
    • Goto, Y.1    Yue, L.2    Yokoi, A.3    Nishimura, R.4    Uehara, T.5    Koizumi, S.6
  • 51
    • 0036606023 scopus 로고    scopus 로고
    • Analysis of methotrexate and folate transport by multidrug resistance protein 4 (ABCC4): MRP4 is a component of the methotrexate efflux system
    • Z.S. Chen, K. Lee, S. Walther, R.B. Raftogianis, M. Kuwano, and H. Zeng Analysis of methotrexate and folate transport by multidrug resistance protein 4 (ABCC4): MRP4 is a component of the methotrexate efflux system Cancer Res. 62 2002 3144 3150
    • (2002) Cancer Res. , vol.62 , pp. 3144-3150
    • Chen, Z.S.1    Lee, K.2    Walther, S.3    Raftogianis, R.B.4    Kuwano, M.5    Zeng, H.6
  • 52
    • 0034614112 scopus 로고    scopus 로고
    • Analysis of the MRP4 drug resistance profile in transfected NIH3T3 cells
    • K. Lee, A.J. Klein-Szanto, and G.D. Kruh Analysis of the MRP4 drug resistance profile in transfected NIH3T3 cells J. Natl. Cancer Inst. 92 2000 1934 1940
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 1934-1940
    • Lee, K.1    Klein-Szanto, A.J.2    Kruh, G.D.3
  • 53
    • 0022202645 scopus 로고
    • Evidence from chemical degradation studies for a covalent bond from 5-fluoro-2′-deoxyuridylate to N-5 of tetrahydrofolate in the ternary complex of thymidylate synthetase-5-fluoro-2′-deoxyuridylate-5,10- methylenetetrahydrofolate
    • A.M. Pellino, and P.V. Danenberg Evidence from chemical degradation studies for a covalent bond from 5-fluoro-2′-deoxyuridylate to N-5 of tetrahydrofolate in the ternary complex of thymidylate synthetase-5-fluoro- 2′-deoxyuridylate-5,10-methylenetetrahydrofolate J. Biol. Chem. 260 1985 10996 11000
    • (1985) J. Biol. Chem. , vol.260 , pp. 10996-11000
    • Pellino, A.M.1    Danenberg, P.V.2
  • 54
    • 0024164649 scopus 로고
    • Fluorouracil: Biochemistry and pharmacology
    • H.M. Pinedo, and G.F. Peters Fluorouracil: biochemistry and pharmacology J. Clin. Oncol. 6 1988 1653 1664
    • (1988) J. Clin. Oncol. , vol.6 , pp. 1653-1664
    • Pinedo, H.M.1    Peters, G.F.2
  • 55
    • 0023187085 scopus 로고
    • Clinical pharmacokinetics of 5-fluorouracil and its metabolites in plasma, urine, and bile
    • G.D. Heggie, J.P. Sommadossi, D.S. Cross, W.J. Huster, and R.B. Diasio Clinical pharmacokinetics of 5-fluorouracil and its metabolites in plasma, urine, and bile Cancer Res. 47 1987 2203 2206
    • (1987) Cancer Res. , vol.47 , pp. 2203-2206
    • Heggie, G.D.1    Sommadossi, J.P.2    Cross, D.S.3    Huster, W.J.4    Diasio, R.B.5
  • 57
    • 0027426408 scopus 로고
    • Dihydropyrimidine dehydrogenase activity in human peripheral blood mononuclear cells and liver: Population characteristics, newly identified deficient patients, and clinical implication in 5-fluorouracil chemotherapy
    • Z. Lu, R. Zhang, and R.B. Diasio Dihydropyrimidine dehydrogenase activity in human peripheral blood mononuclear cells and liver: population characteristics, newly identified deficient patients, and clinical implication in 5-fluorouracil chemotherapy Cancer Res. 53 1993 5433 5438
    • (1993) Cancer Res. , vol.53 , pp. 5433-5438
    • Lu, Z.1    Zhang, R.2    Diasio, R.B.3
  • 58
    • 0032795865 scopus 로고    scopus 로고
    • Life-threatening toxicity in a dihydropyrimidine dehydrogenase-deficient patient after treatment with topical 5-fluorouracil
    • M.R. Johnson, A. Hageboutros, K. Wang, L. High, J.B. Smith, and R.B. Diasio Life-threatening toxicity in a dihydropyrimidine dehydrogenase-deficient patient after treatment with topical 5-fluorouracil Clin. Cancer Res. 5 1999 2006 2011
    • (1999) Clin. Cancer Res. , vol.5 , pp. 2006-2011
    • Johnson, M.R.1    Hageboutros, A.2    Wang, K.3    High, L.4    Smith, J.B.5    Diasio, R.B.6
  • 59
    • 0023902287 scopus 로고
    • Familial deficiency of dihydropyrimidine dehydrogenase. Biochemical basis for familial pyrimidinemia and severe 5-fluorouracil-induced toxicity
    • R.B. Diasio, T.L. Beavers, and J.T. Carpenter Familial deficiency of dihydropyrimidine dehydrogenase. Biochemical basis for familial pyrimidinemia and severe 5-fluorouracil-induced toxicity J. Clin. Invest. 81 1988 47 51
    • (1988) J. Clin. Invest. , vol.81 , pp. 47-51
    • Diasio, R.B.1    Beavers, T.L.2    Carpenter, J.T.3
  • 60
    • 0029133354 scopus 로고
    • Diagnostic analysis, clinical importance and molecular basis of dihydropyrimidine dehydrogenase deficiency
    • F.J. Gonzalez, and P. Fernandez-Salguero Diagnostic analysis, clinical importance and molecular basis of dihydropyrimidine dehydrogenase deficiency Trends Pharmacol. Sci. 16 1995 325 327
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 325-327
    • Gonzalez, F.J.1    Fernandez-Salguero, P.2
  • 61
    • 0021275335 scopus 로고
    • Dihydropyrimidine dehydrogenase deficiency leading to thymine-uraciluria. An inborn error of pyrimidine metabolism
    • R. Berger, S.A. Stoker-de Vries, S.K. Wadman, M. Duran, F.A. Beemer, and P.K. de Bree Dihydropyrimidine dehydrogenase deficiency leading to thymine-uraciluria. An inborn error of pyrimidine metabolism Clin. Chim. Acta 141 1984 227 234
    • (1984) Clin. Chim. Acta , vol.141 , pp. 227-234
    • Berger, R.1    Stoker-De Vries, S.A.2    Wadman, S.K.3    Duran, M.4    Beemer, F.A.5    De Bree, P.K.6
  • 62
    • 0029973215 scopus 로고    scopus 로고
    • Molecular basis of the human dihydropyrimidine dehydrogenase deficiency and 5-fluorouracil toxicity
    • X. Wei, H.L. McLeod, J. McMurrough, F.J. Gonzalez, and P. Fernandez-Salguero Molecular basis of the human dihydropyrimidine dehydrogenase deficiency and 5-fluorouracil toxicity J. Clin. Invest. 98 1996 610 615
    • (1996) J. Clin. Invest. , vol.98 , pp. 610-615
    • Wei, X.1    McLeod, H.L.2    McMurrough, J.3    Gonzalez, F.J.4    Fernandez-Salguero, P.5
  • 63
    • 0034901306 scopus 로고    scopus 로고
    • Lethal outcome of a patient with a complete dihydropyrimidine dehydrogenase (DPD) deficiency after administration of 5-fluorouracil: Frequency of the common IVS14 + 1G > a mutation causing DPD deficiency
    • A.B. Van Kuilenburg, E.W. Muller, J. Haasjes, R. Meinsma, L. Zoetekouw, and H.R. Waterham Lethal outcome of a patient with a complete dihydropyrimidine dehydrogenase (DPD) deficiency after administration of 5-fluorouracil: frequency of the common IVS14 + 1G > A mutation causing DPD deficiency Clin. Cancer Res. 7 2001 1149 1153
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1149-1153
    • Van Kuilenburg, A.B.1    Muller, E.W.2    Haasjes, J.3    Meinsma, R.4    Zoetekouw, L.5    Waterham, H.R.6
  • 65
    • 0025083351 scopus 로고
    • Regional assignment of the human thymidylate synthase (TS) gene to chromosome band 18p11.32 by nonisotopic in situ hybridization
    • T. Hori, E. Takahashi, D. Ayusawa, K. Takeishi, S. Kaneda, and T. Seno Regional assignment of the human thymidylate synthase (TS) gene to chromosome band 18p11.32 by nonisotopic in situ hybridization Hum. Genet. 85 1990 576 580
    • (1990) Hum. Genet. , vol.85 , pp. 576-580
    • Hori, T.1    Takahashi, E.2    Ayusawa, D.3    Takeishi, K.4    Kaneda, S.5    Seno, T.6
  • 66
    • 0035868667 scopus 로고    scopus 로고
    • Polymorphisms of the repeated sequences in the enhancer region of the thymidylate synthase gene promoter may predict downstaging after preoperative chemoradiation in rectal cancer
    • E. Villafranca, Y. Okruzhnov, M.A. Dominguez, J. Garcia-Foncillas, I. Azinovic, and E. Martinez Polymorphisms of the repeated sequences in the enhancer region of the thymidylate synthase gene promoter may predict downstaging after preoperative chemoradiation in rectal cancer J. Clin. Oncol. 19 2001 1779 1786
    • (2001) J. Clin. Oncol. , vol.19 , pp. 1779-1786
    • Villafranca, E.1    Okruzhnov, Y.2    Dominguez, M.A.3    Garcia-Foncillas, J.4    Azinovic, I.5    Martinez, E.6
  • 67
    • 0035430487 scopus 로고    scopus 로고
    • Polymorphism in the thymidylate synthase promoter enhancer region in colorectal cancer
    • S. Marsh, J.A. McKay, J. Cassidy, and H.L. McLeod Polymorphism in the thymidylate synthase promoter enhancer region in colorectal cancer Int. J. Oncol. 19 2001 383 386
    • (2001) Int. J. Oncol. , vol.19 , pp. 383-386
    • Marsh, S.1    McKay, J.A.2    Cassidy, J.3    McLeod, H.L.4
  • 68
    • 0028940399 scopus 로고
    • Thymidylate synthase gene and protein expression correlate and are associated with response to 5-fluorouracil in human colorectal and gastric tumors
    • P.G. Johnston, H.J. Lenz, C.G. Leichman, K.D. Danenberg, C.J. Allegra, and P.V. Danenberg Thymidylate synthase gene and protein expression correlate and are associated with response to 5-fluorouracil in human colorectal and gastric tumors Cancer Res. 55 1995 1407 1412
    • (1995) Cancer Res. , vol.55 , pp. 1407-1412
    • Johnston, P.G.1    Lenz, H.J.2    Leichman, C.G.3    Danenberg, K.D.4    Allegra, C.J.5    Danenberg, P.V.6
  • 69
    • 0030883708 scopus 로고    scopus 로고
    • Quantitation of intratumoral thymidylate synthase expression predicts for disseminated colorectal cancer response and resistance to protracted-infusion fluorouracil and weekly leucovorin
    • C.G. Leichman, H.J. Lenz, L. Leichman, K. Danenberg, J. Baranda, and S. Groshen Quantitation of intratumoral thymidylate synthase expression predicts for disseminated colorectal cancer response and resistance to protracted-infusion fluorouracil and weekly leucovorin J. Clin. Oncol. 15 1997 3223 3229
    • (1997) J. Clin. Oncol. , vol.15 , pp. 3223-3229
    • Leichman, C.G.1    Lenz, H.J.2    Leichman, L.3    Danenberg, K.4    Baranda, J.5    Groshen, S.6
  • 70
    • 0033427561 scopus 로고    scopus 로고
    • Polymorphic tandem repeats in the thymidylate synthase gene is associated with its protein expression in human gastrointestinal cancers
    • K. Kawakami, K. Omura, E. Kanehira, and Y. Watanabe Polymorphic tandem repeats in the thymidylate synthase gene is associated with its protein expression in human gastrointestinal cancers Anticancer Res. 19 1999 3249 3252
    • (1999) Anticancer Res. , vol.19 , pp. 3249-3252
    • Kawakami, K.1    Omura, K.2    Kanehira, E.3    Watanabe, Y.4
  • 71
    • 0029122937 scopus 로고
    • Functional analysis and DNA polymorphism of the tandemly repeated sequences in the 5′-terminal regulatory region of the human gene for thymidylate synthase
    • N. Horie, H. Aiba, K. Oguro, H. Hojo, and K. Takeishi Functional analysis and DNA polymorphism of the tandemly repeated sequences in the 5′-terminal regulatory region of the human gene for thymidylate synthase Cell Struct. Funct. 20 1995 191 197
    • (1995) Cell Struct. Funct. , vol.20 , pp. 191-197
    • Horie, N.1    Aiba, H.2    Oguro, K.3    Hojo, H.4    Takeishi, K.5
  • 72
    • 0037990003 scopus 로고    scopus 로고
    • Methylenetetrahydrofolate reductase polymorphism in advanced colorectal cancer: A novel genomic predictor of clinical response to fluoropyrimidine-based chemotherapy
    • V. Cohen, V. Panet-Raymond, N. Sabbaghian, I. Morin, G. Batist, and R. Rozen Methylenetetrahydrofolate reductase polymorphism in advanced colorectal cancer: a novel genomic predictor of clinical response to fluoropyrimidine-based chemotherapy Clin. Cancer Res. 9 2003 1611 1615
    • (2003) Clin. Cancer Res. , vol.9 , pp. 1611-1615
    • Cohen, V.1    Panet-Raymond, V.2    Sabbaghian, N.3    Morin, I.4    Batist, G.5    Rozen, R.6
  • 73
    • 0032585197 scopus 로고    scopus 로고
    • Randomised trial of irinotecan versus fluorouracil by continuous infusion after fluorouracil failure in patients with metastatic colorectal cancer
    • P. Rougier, E. Van Cutsem, E. Bajetta, N. Niederle, K. Possinger, and R. Labianca Randomised trial of irinotecan versus fluorouracil by continuous infusion after fluorouracil failure in patients with metastatic colorectal cancer Lancet 352 1998 1407 1412
    • (1998) Lancet , vol.352 , pp. 1407-1412
    • Rougier, P.1    Van Cutsem, E.2    Bajetta, E.3    Niederle, N.4    Possinger, K.5    Labianca, R.6
  • 74
    • 0025996996 scopus 로고
    • Intracellular roles of SN-38, a metabolite of the camptothecin derivative CPT-11, in the antitumor effect of CPT-11
    • Y. Kawato, M. Aonuma, Y. Hirota, H. Kuga, and K. Sato Intracellular roles of SN-38, a metabolite of the camptothecin derivative CPT-11, in the antitumor effect of CPT-11 Cancer Res. 51 1991 4187 4191
    • (1991) Cancer Res. , vol.51 , pp. 4187-4191
    • Kawato, Y.1    Aonuma, M.2    Hirota, Y.3    Kuga, H.4    Sato, K.5
  • 75
    • 0028867826 scopus 로고
    • The genetic basis of the reduced expression of bilirubin UDP-glucuronosyltransferase 1 in Gilbert's syndrome
    • P.J. Bosma, J.R. Chowdhury, C. Bakker, S. Gantla, A. De Boer, and B.A. Oostra The genetic basis of the reduced expression of bilirubin UDP-glucuronosyltransferase 1 in Gilbert's syndrome N. Engl. J. Med. 333 1995 1171 1175
    • (1995) N. Engl. J. Med. , vol.333 , pp. 1171-1175
    • Bosma, P.J.1    Chowdhury, J.R.2    Bakker, C.3    Gantla, S.4    De Boer, A.5    Oostra, B.A.6
  • 76
    • 0028022585 scopus 로고
    • Metabolic fate of irinotecan in humans: Correlation of glucuronidation with diarrhea
    • E. Gupta, T.M. Lestingi, R. Mick, J. Ramirez, E.E. Vokes, and M.J. Ratain Metabolic fate of irinotecan in humans: correlation of glucuronidation with diarrhea Cancer Res. 54 1994 3723 3725
    • (1994) Cancer Res. , vol.54 , pp. 3723-3725
    • Gupta, E.1    Lestingi, T.M.2    Mick, R.3    Ramirez, J.4    Vokes, E.E.5    Ratain, M.J.6
  • 77
    • 0034671387 scopus 로고    scopus 로고
    • Polymorphisms of UDP-glucuronosyltransferase gene and irinotecan toxicity: A pharmacogenetic analysis
    • Y. Ando, H. Saka, M. Ando, T. Sawa, K. Muro, and H. Ueoka Polymorphisms of UDP-glucuronosyltransferase gene and irinotecan toxicity: a pharmacogenetic analysis Cancer Res. 60 2000 6921 6926
    • (2000) Cancer Res. , vol.60 , pp. 6921-6926
    • Ando, Y.1    Saka, H.2    Ando, M.3    Sawa, T.4    Muro, K.5    Ueoka, H.6
  • 78
    • 0032519431 scopus 로고    scopus 로고
    • Genetic predisposition to the metabolism of irinotecan (CPT-11). Role of uridine diphosphate glucuronosyltransferase isoform 1 A1 in the glucuronidation of its active metabolite (SN- 38) in human liver microsomes
    • L. Iyer, C.D. King, P.F. Whitington, M.D. Green, S.K. Roy, and T.R. Tephly Genetic predisposition to the metabolism of irinotecan (CPT-11). Role of uridine diphosphate glucuronosyltransferase isoform 1 A1 in the glucuronidation of its active metabolite (SN- 38) in human liver microsomes J. Clin. Invest. 101 1998 847 854
    • (1998) J. Clin. Invest. , vol.101 , pp. 847-854
    • Iyer, L.1    King, C.D.2    Whitington, P.F.3    Green, M.D.4    Roy, S.K.5    Tephly, T.R.6
  • 79
    • 0032934383 scopus 로고    scopus 로고
    • Phenotype-genotype correlation of in vitro SN-38 (active metabolite of irinotecan) and bilirubin glucuronidation in human liver tissue with UGT1A1 promoter polymorphism
    • L. Iyer, D. Hall, S. Das, M.A. Mortell, J. Ramirez, and S. Kim Phenotype-genotype correlation of in vitro SN-38 (active metabolite of irinotecan) and bilirubin glucuronidation in human liver tissue with UGT1A1 promoter polymorphism Clin. Pharmacol. Therap. 65 1999 576 582
    • (1999) Clin. Pharmacol. Therap. , vol.65 , pp. 576-582
    • Iyer, L.1    Hall, D.2    Das, S.3    Mortell, M.A.4    Ramirez, J.5    Kim, S.6
  • 80
    • 0033661491 scopus 로고    scopus 로고
    • Tissue distribution and interindividual variation in human UDP-glucuronosyltransferase activity: Relationship between UGT1A1 promoter genotype and variability in a liver bank
    • M.B. Fisher, M. Vandenbranden, K. Findlay, B. Burchell, K.E. Thummel, and S.D. Hall Tissue distribution and interindividual variation in human UDP-glucuronosyltransferase activity: relationship between UGT1A1 promoter genotype and variability in a liver bank Pharmacogenetics 10 2000 727 739
    • (2000) Pharmacogenetics , vol.10 , pp. 727-739
    • Fisher, M.B.1    Vandenbranden, M.2    Findlay, K.3    Burchell, B.4    Thummel, K.E.5    Hall, S.D.6
  • 81
    • 0026764632 scopus 로고
    • Identification of a genetic alteration in the code for bilirubin UDP-glucuronosyltransferase in the UGT1 gene complex of a Crigler-Najjar type I patient
    • J.K. Ritter, M.T. Yeatman, P. Ferreira, and I.S. Owens Identification of a genetic alteration in the code for bilirubin UDP-glucuronosyltransferase in the UGT1 gene complex of a Crigler-Najjar type I patient J. Clin. Invest. 90 1992 150 155
    • (1992) J. Clin. Invest. , vol.90 , pp. 150-155
    • Ritter, J.K.1    Yeatman, M.T.2    Ferreira, P.3    Owens, I.S.4
  • 82
    • 0029972534 scopus 로고    scopus 로고
    • Crigler-Najjar syndrome type II is inherited both as a dominant and as a recessive trait
    • O. Koiwai, S. Aono, Y. Adachi, T. Kamisako, Y. Yasui, and M. Nishizawa Crigler-Najjar syndrome type II is inherited both as a dominant and as a recessive trait Hum. Mol. Genet. 5 1996 645 647
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 645-647
    • Koiwai, O.1    Aono, S.2    Adachi, Y.3    Kamisako, T.4    Yasui, Y.5    Nishizawa, M.6
  • 83
    • 2342459714 scopus 로고    scopus 로고
    • Genetic variants in the UDP-glucuronosyltransferase 1A1 gene predict the risk of severe neutropeniaofirinotecan
    • F. Innocenti, S.D. Undevia, L. Iyer, P.X. Chen, S. Das, and M. Kocherginsky Genetic variants in the UDP-glucuronosyltransferase 1A1 gene predict the risk of severe neutropeniaofirinotecan J. Clin. Oncol. 22 2004 1382 1388
    • (2004) J. Clin. Oncol. , vol.22 , pp. 1382-1388
    • Innocenti, F.1    Undevia, S.D.2    Iyer, L.3    Chen, P.X.4    Das, S.5    Kocherginsky, M.6
  • 85
    • 0034162687 scopus 로고    scopus 로고
    • Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2
    • R. Humerickhouse, K. Lohrbach, L. Li, W.F. Bosron, and M.E. Dolan Characterization of CPT-11 hydrolysis by human liver carboxylesterase isoforms hCE-1 and hCE-2 Cancer Res. 60 2000 1189 1192
    • (2000) Cancer Res. , vol.60 , pp. 1189-1192
    • Humerickhouse, R.1    Lohrbach, K.2    Li, L.3    Bosron, W.F.4    Dolan, M.E.5
  • 86
    • 0034282809 scopus 로고    scopus 로고
    • Proficient metabolism of irinotecan by a human intestinal carboxylesterase
    • R. Khanna, C.L. Morton, M.K. Danks, and P.M. Potter Proficient metabolism of irinotecan by a human intestinal carboxylesterase Cancer Res. 60 2000 4725 4728
    • (2000) Cancer Res. , vol.60 , pp. 4725-4728
    • Khanna, R.1    Morton, C.L.2    Danks, M.K.3    Potter, P.M.4
  • 88
  • 89
    • 0034872136 scopus 로고
    • Pharmacogenetics of warfarin elimination and its clinical implications
    • H. Takahashi, and H. Echizen Pharmacogenetics of warfarin elimination and its clinical implications Clin. Pharmacokinet. 40 1904 587 603
    • (1904) Clin. Pharmacokinet. , vol.40 , pp. 587-603
    • Takahashi, H.1    Echizen, H.2
  • 90
    • 0141832724 scopus 로고
    • Pharmacogenetics of CYP2C9 and interindividual variability in anticoagulant response to warfarin
    • H. Takahashi, and H. Echizen Pharmacogenetics of CYP2C9 and interindividual variability in anticoagulant response to warfarin Pharmacogenomics J. 3 1904 202 214
    • (1904) Pharmacogenomics J. , vol.3 , pp. 202-214
    • Takahashi, H.1    Echizen, H.2
  • 91
    • 0037012465 scopus 로고    scopus 로고
    • Association between CYP2C9 genetic variants and anti-coagulation-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 anti-coagulation-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
  • 93
    • 0030587544 scopus 로고    scopus 로고
    • Allelic variants of human cytochrome P450 2C9: Baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms
    • R.L. Haining, A.P. Hunter, M.E. Veronese, W.F. Trager, and A.E. Rettie Allelic variants of human cytochrome P450 2C9: baculovirus-mediated expression, purification, structural characterization, substrate stereoselectivity, and prochiral selectivity of the wild-type and I359L mutant forms Arch. Biochem. Biophys. 333 1996 447 458
    • (1996) Arch. Biochem. Biophys. , vol.333 , pp. 447-458
    • Haining, R.L.1    Hunter, A.P.2    Veronese, M.E.3    Trager, W.F.4    Rettie, A.E.5
  • 94
    • 7844247934 scopus 로고    scopus 로고
    • Comparisons between in vitro and in vivo metabolism of (S)-warfarin: Catalytic activities of cDNA-expressed CYP2C9, its Leu359 variant and their mixture versus unbound clearance in patients with the corresponding CYP2C9 genotypes
    • H. Takahashi, T. Kashima, S. Nomoto, K. Iwade, H. Tainaka, and T. Shimizu Comparisons between in vitro and in vivo metabolism of (S)-warfarin: catalytic activities of cDNA-expressed CYP2C9, its Leu359 variant and their mixture versus unbound clearance in patients with the corresponding CYP2C9 genotypes Pharmacogenetics 8 1998 365 373
    • (1998) Pharmacogenetics , vol.8 , pp. 365-373
    • Takahashi, H.1    Kashima, T.2    Nomoto, S.3    Iwade, K.4    Tainaka, H.5    Shimizu, T.6
  • 95
    • 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
  • 96
    • 0037006623 scopus 로고    scopus 로고
    • Association between presence of HLA-B*5701, HLA-DR7, and HLA-DQ3 and hypersensitivity to HIV-1 reverse-transcriptase inhibitor abacavir
    • S. Mallal, D. Nolan, C. Witt, G. Masel, A.M. Martin, and C. Moore Association between presence of HLA-B*5701, HLA-DR7, and HLA-DQ3 and hypersensitivity to HIV-1 reverse-transcriptase inhibitor abacavir Lancet 359 2002 727 732
    • (2002) Lancet , vol.359 , pp. 727-732
    • Mallal, S.1    Nolan, D.2    Witt, C.3    Masel, G.4    Martin, A.M.5    Moore, C.6
  • 98
    • 0035811174 scopus 로고    scopus 로고
    • The heartbreak of drug pricing
    • F. Davidoff The heartbreak of drug pricing Ann. Int. Med. 134 2001 1068 1071
    • (2001) Ann. Int. Med. , vol.134 , pp. 1068-1071
    • Davidoff, F.1
  • 99
    • 0033763969 scopus 로고    scopus 로고
    • The distribution of sales revenues from pharmaceutical innovation
    • H.G. Grabowski, and J. Vernon The distribution of sales revenues from pharmaceutical innovation Pharmacoeconomics 18 suppl. 1 2000 21 32
    • (2000) Pharmacoeconomics , vol.18 , Issue.1 SUPPL. , pp. 21-32
    • Grabowski, H.G.1    Vernon, J.2
  • 101
    • 17044372917 scopus 로고    scopus 로고
    • Next step: Drug pricing controls
    • J. Oberlander, J. Jaffe, Next step: drug pricing controls, Washington Post, vol. B07, 2003, pp. 12-14.
    • (2003) Washington Post , vol.B07 , pp. 12-14
    • Oberlander, J.1    Jaffe, J.2
  • 103
    • 0035818059 scopus 로고    scopus 로고
    • Race and responsiveness to drugs for heart failure
    • H.L. McLeod Race and responsiveness to drugs for heart failure N. Engl. J. Med. 345 2001 766 767
    • (2001) N. Engl. J. Med. , vol.345 , pp. 766-767
    • McLeod, H.L.1
  • 104
    • 0031769098 scopus 로고    scopus 로고
    • Pharmacoeconomics of cancer therapy
    • EDAT-2000/04/13 MHDA-2000/04/13 PST-publish
    • S.E. Beltz, G.C. Yee, Pharmacoeconomics of cancer therapy. Cancer Control EDAT-2000/04/13 MHDA-2000/04/13 PST-publish (1998) vol. 5, pp. 415-424.
    • (1998) Cancer Control , vol.5 , pp. 415-424
    • Beltz, S.E.1    Yee, G.C.2
  • 106
    • 0032887737 scopus 로고    scopus 로고
    • Cost-utility analysis of chemotherapy using paclitaxel, docetaxel, or vinorelbine for patients with anthracycline-resistant breast cancer
    • P.P. Leung, I.F. Tannock, A.M. Oza, A. Puodziunas, and G. Dranitsaris Cost-utility analysis of chemotherapy using paclitaxel, docetaxel, or vinorelbine for patients with anthracycline-resistant breast cancer J. Clin. Oncol. 17 1999 3082 3090
    • (1999) J. Clin. Oncol. , vol.17 , pp. 3082-3090
    • Leung, P.P.1    Tannock, I.F.2    Oza, A.M.3    Puodziunas, A.4    Dranitsaris, G.5
  • 107
    • 85030794011 scopus 로고    scopus 로고
    • Blue Cross Blue Shield Technology Evaluation, Center Assessment Program 17, 12.2002.
    • Chemotherapy sensitivity and resistance assays. Blue Cross Blue Shield Technology Evaluation, Center Assessment Program 17, 12.2002.
    • Chemotherapy Sensitivity and Resistance Assays
  • 109
    • 0036894866 scopus 로고    scopus 로고
    • Practical pharmacogenetics: The cost effectiveness of screening for thiopurine S-methyltransferase polymorphisms in patients with rheumatological conditions treated with azathioprine
    • C.A. Marra, J.M. Esdaile, and A.H. Anis Practical pharmacogenetics: the cost effectiveness of screening for thiopurine S-methyltransferase polymorphisms in patients with rheumatological conditions treated with azathioprine J. Rheumatol. 29 2002 2507 2512
    • (2002) J. Rheumatol. , vol.29 , pp. 2507-2512
    • Marra, C.A.1    Esdaile, J.M.2    Anis, A.H.3
  • 110
    • 3042634326 scopus 로고    scopus 로고
    • Cost-effectiveness analysis of HLA B*5701 genotyping in preventing abacavir hypersensitivity
    • D.A. Hughes, F.J. Vilar, C.C. Ward, A. Alfirevic, B.K. Park, and M. Pirmohamed Cost-effectiveness analysis of HLA B*5701 genotyping in preventing abacavir hypersensitivity Pharmacogenetics 14 2004 335 342
    • (2004) Pharmacogenetics , vol.14 , pp. 335-342
    • Hughes, D.A.1    Vilar, F.J.2    Ward, C.C.3    Alfirevic, A.4    Park, B.K.5    Pirmohamed, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.