메뉴 건너뛰기




Volumn 12, Issue 5, 2005, Pages 497-508

A virus-directed enzyme prodrug therapy (VDEPT) strategy for lung cancer using a CYP2B6/NADPH-cytochrome P450 reductase fusion protein

Author keywords

Cyclophosphamide; Lung cancer; P450 based gene therapy; VDEPT

Indexed keywords

ADENOVIRUS VECTOR; CYCLOPHOSPHAMIDE; CYTOCHROME P450 2B6; HEME; HYBRID PROTEIN; MESSENGER RNA; PRODRUG; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE;

EID: 18244404281     PISSN: 09291903     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cgt.7700817     Document Type: Article
Times cited : (36)

References (48)
  • 1
    • 0034478186 scopus 로고    scopus 로고
    • Approaches to gene-directed enzyme prodrug therapy (GDEPT)
    • Springer CJ, Niculescu-Duvaz I. Approaches to gene-directed enzyme prodrug therapy (GDEPT). Adv Exp Med Biol. 2000;465:403-409.
    • (2000) Adv Exp Med Biol , vol.465 , pp. 403-409
    • Springer, C.J.1    Niculescu-Duvaz, I.2
  • 2
    • 0036909628 scopus 로고    scopus 로고
    • Cytochrome P450-based cancer gene therapy: Current status
    • Kan O, Kingsman S, Naylor S. Cytochrome P450-based cancer gene therapy: current status. Expert Opin Biol Ther. 2002;2:857-868.
    • (2002) Expert Opin Biol Ther , vol.2 , pp. 857-868
    • Kan, O.1    Kingsman, S.2    Naylor, S.3
  • 3
    • 0028936342 scopus 로고
    • Intratumoral activation and enhanced chemotherapeutic effect of oxazaphosphorines following cytochrome P-450 gene transfer: Development of a combined chemotherapy/cancer gene therapy strategy
    • Chen L, Waxman DJ. Intratumoral activation and enhanced chemotherapeutic effect of oxazaphosphorines following cytochrome P-450 gene transfer: development of a combined chemotherapy/cancer gene therapy strategy. Cancer Res. 1995;55:581-589.
    • (1995) Cancer Res , vol.55 , pp. 581-589
    • Chen, L.1    Waxman, D.J.2
  • 4
    • 0030739223 scopus 로고    scopus 로고
    • Human cytochrome P4502B6: Interindividual hepatic expression, substrate specificity, and role in procarcinogen activation
    • Code EL, Crespi CL, Penman BW, et al. Human cytochrome P4502B6: interindividual hepatic expression, substrate specificity, and role in procarcinogen activation. Drug Metab Dispos. 1997;25:985-993.
    • (1997) Drug Metab Dispos , vol.25 , pp. 985-993
    • Code, E.L.1    Crespi, C.L.2    Penman, B.W.3
  • 5
    • 0032791111 scopus 로고    scopus 로고
    • Human CYP2B6: Expression, inducibility and catalytic activities
    • Gervot L, Rochat B, Gautier JC, et al. Human CYP2B6: expression, inducibility and catalytic activities. Pharmacogenetics. 1999;9:295-306.
    • (1999) Pharmacogenetics , vol.9 , pp. 295-306
    • Gervot, L.1    Rochat, B.2    Gautier, J.C.3
  • 6
    • 0023945947 scopus 로고
    • Metabolism of oxazaphosphorines
    • Sladek NE. Metabolism of oxazaphosphorines. Pharmacol Ther. 1988;37:301-355.
    • (1988) Pharmacol Ther , vol.37 , pp. 301-355
    • Sladek, N.E.1
  • 7
    • 0030765658 scopus 로고    scopus 로고
    • An overview of cyclophosphamide and ifosfamide pharmacology
    • Fleming RA. An overview of cyclophosphamide and ifosfamide pharmacology. Pharmacotherapy. 1997;17:146S-154S.
    • (1997) Pharmacotherapy , vol.17
    • Fleming, R.A.1
  • 8
    • 0034053590 scopus 로고    scopus 로고
    • Metabolism and pharmacokinetics of oxazaphosphorines
    • Boddy AV, Yule SM. Metabolism and pharmacokinetics of oxazaphosphorines. Clin Pharmacokinet. 2000;38:291-304.
    • (2000) Clin Pharmacokinet , vol.38 , pp. 291-304
    • Boddy, A.V.1    Yule, S.M.2
  • 9
    • 0024533623 scopus 로고
    • Oxidative metabolism of cyclophosphamide: Identification of the hepatic monooxygenase catalysts of drug activation
    • Clarke L, Waxman DJ. Oxidative metabolism of cyclophosphamide: identification of the hepatic monooxygenase catalysts of drug activation. Cancer Res. 1989;49:2344-2350.
    • (1989) Cancer Res , vol.49 , pp. 2344-2350
    • Clarke, L.1    Waxman, D.J.2
  • 10
    • 0030951908 scopus 로고    scopus 로고
    • Enhanced cyclophosphamide and ifosfamide activation in primary human hepatocyte cultures: Response to cytochrome P-450 inducers and autoinduction by oxazaphosphorines
    • Chang TK, Yu L, Maurel P, et al. Enhanced cyclophosphamide and ifosfamide activation in primary human hepatocyte cultures: response to cytochrome P-450 inducers and autoinduction by oxazaphosphorines. Cancer Res. 1997;57:1946-1954.
    • (1997) Cancer Res , vol.57 , pp. 1946-1954
    • Chang, T.K.1    Yu, L.2    Maurel, P.3
  • 11
    • 0026698173 scopus 로고
    • Apoptosis induced by anticancer drugs
    • Hickman JA. Apoptosis induced by anticancer drugs. Cancer Metastasis Rev. 1992;11:121-139.
    • (1992) Cancer Metastasis Rev , vol.11 , pp. 121-139
    • Hickman, J.A.1
  • 12
    • 0035210529 scopus 로고    scopus 로고
    • Cyclophosphamide induces Caspase 9-dependent apoptosis in 9L tumor cells
    • Schwartz PS, Waxman DJ. Cyclophosphamide induces Caspase 9-dependent apoptosis in 9L tumor cells. Mol Pharmacol. 2001;60:1268-1279.
    • (2001) Mol Pharmacol , vol.60 , pp. 1268-1279
    • Schwartz, P.S.1    Waxman, D.J.2
  • 13
    • 0035116213 scopus 로고    scopus 로고
    • Intraneoplastic polymer-based delivery of cyclophosphamide for intratumoral bioconversion by a replicating oncolytic viral vector
    • Ichikawa T, Petros WP, Ludeman SM, et al. Intraneoplastic polymer-based delivery of cyclophosphamide for intratumoral bioconversion by a replicating oncolytic viral vector. Cancer Res. 2001;61:864-868.
    • (2001) Cancer Res , vol.61 , pp. 864-868
    • Ichikawa, T.1    Petros, W.P.2    Ludeman, S.M.3
  • 14
    • 0028832191 scopus 로고
    • Diffusible cytotoxic metabolites contribute to the in vitro bystander effect associated with the cyclophosphamide/cytochrome P450 2B1 cancer gene therapy paradigm
    • Wei MX, Tamiya T, Rhee RJ, et al. Diffusible cytotoxic metabolites contribute to the in vitro bystander effect associated with the cyclophosphamide/cytochrome P450 2B1 cancer gene therapy paradigm. Clin Cancer Res. 1995;1:1171-1177.
    • (1995) Clin Cancer Res , vol.1 , pp. 1171-1177
    • Wei, M.X.1    Tamiya, T.2    Rhee, R.J.3
  • 15
    • 0027483695 scopus 로고
    • The "bystander effect": Tumor regression when a fraction of the tumor mass is genetically modified
    • Freeman SM, Abboud CN, Whartenby KA, et al. The "bystander effect": tumor regression when a fraction of the tumor mass is genetically modified. Cancer Res. 1993;53:5274-5283.
    • (1993) Cancer Res , vol.53 , pp. 5274-5283
    • Freeman, S.M.1    Abboud, C.N.2    Whartenby, K.A.3
  • 16
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components
    • Lu AY, Junk KW, Coon MJ. Resolution of the cytochrome P-450-containing omega-hydroxylation system of liver microsomes into three components. J Biol Chem. 1969;244:3714-3721.
    • (1969) J Biol Chem , vol.244 , pp. 3714-3721
    • Lu, A.Y.1    Junk, K.W.2    Coon, M.J.3
  • 17
    • 0015011537 scopus 로고
    • Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control
    • Estabrook RW, Franklin MR, Cohen B, et al. Biochemical and genetic factors influencing drug metabolism. Influence of hepatic microsomal mixed function oxidation reactions on cellular metabolic control. Metabolism. 1971;20:187-199.
    • (1971) Metabolism , vol.20 , pp. 187-199
    • Estabrook, R.W.1    Franklin, M.R.2    Cohen, B.3
  • 18
    • 0021703594 scopus 로고
    • Turnover of membrane proteins: Kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydrolase
    • Shiraki H, Guengerich FP. Turnover of membrane proteins: kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPH-cytochrome P-450 reductase, and epoxide hydrolase. Arch Biochem Biophys. 1984;235:86-96.
    • (1984) Arch Biochem Biophys , vol.235 , pp. 86-96
    • Shiraki, H.1    Guengerich, F.P.2
  • 19
    • 0030810198 scopus 로고    scopus 로고
    • Potentiation of cytochrome P450/cyclophosphamide-based cancer gene therapy by coexpression of the P450 reductase gene
    • Chen L, Yu LJ, Waxman DJ. Potentiation of cytochrome P450/ cyclophosphamide-based cancer gene therapy by coexpression of the P450 reductase gene. Cancer Res. 1997;57:4830-4837.
    • (1997) Cancer Res , vol.57 , pp. 4830-4837
    • Chen, L.1    Yu, L.J.2    Waxman, D.J.3
  • 20
    • 0035111995 scopus 로고    scopus 로고
    • P450 enzyme expression patterns in the NCI human tumor cell line panel
    • Yu LJ, Matias J, Scudiero DA, et al. P450 enzyme expression patterns in the NCI human tumor cell line panel. Drug Metab Dispos. 2001;29:304-312.
    • (2001) Drug Metab Dispos , vol.29 , pp. 304-312
    • Yu, L.J.1    Matias, J.2    Scudiero, D.A.3
  • 21
    • 0027146638 scopus 로고
    • Human cytochrome P450 3A4: Enzymatic properties of a purified recombinant fusion protein containing NADPH-P450 reductase
    • Shet MS, Fisher CW, Holmans PL, et al. Human cytochrome P450 3A4: enzymatic properties of a purified recombinant fusion protein containing NADPH-P450 reductase. Proc Natl Acad Sci USA. 1993;90:11748-11752.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11748-11752
    • Shet, M.S.1    Fisher, C.W.2    Holmans, P.L.3
  • 22
    • 0023184975 scopus 로고
    • A genetically engineered P450 monooxygenase: Construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase
    • Murakami H, Yabusaki Y, Sakaki T, et al. A genetically engineered P450 monooxygenase: construction of the functional fused enzyme between rat cytochrome P450c and NADPH-cytochrome P450 reductase. DNA. 1987;6:189-197.
    • (1987) DNA , vol.6 , pp. 189-197
    • Murakami, H.1    Yabusaki, Y.2    Sakaki, T.3
  • 23
    • 0029738284 scopus 로고    scopus 로고
    • Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase
    • Fisher CW, Shet MS, Estabrook RW. Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase. Methods Enzymol. 1996;272:15-25.
    • (1996) Methods Enzymol , vol.272 , pp. 15-25
    • Fisher, C.W.1    Shet, M.S.2    Estabrook, R.W.3
  • 24
    • 0026485793 scopus 로고
    • High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes F450 and NADPH-P450 reductase flavoprotein
    • Fisher CW, Shet MS, Caudle DL, et al. High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes F450 and NADPH-P450 reductase flavoprotein. Proc Natl Acad Sci USA. 1992;89:10817-10821.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10817-10821
    • Fisher, C.W.1    Shet, M.S.2    Caudle, D.L.3
  • 25
    • 0029884802 scopus 로고    scopus 로고
    • Construction of a human cytochrome P450 1A1: Rat NADPH-cytochrome F450 reductase fusion protein cDNA and expression in Escherichia coli, purification, and catalytic properties of the enzyme in bacterial cells and after purification
    • Chun YJ, Shimada T, Guengerich FP. Construction of a human cytochrome P450 1A1: rat NADPH-cytochrome F450 reductase fusion protein cDNA and expression in Escherichia coli, purification, and catalytic properties of the enzyme in bacterial cells and after purification. Arch Biochem Biophys. 1996;330:48-58.
    • (1996) Arch Biochem Biophys , vol.330 , pp. 48-58
    • Chun, Y.J.1    Shimada, T.2    Guengerich, F.P.3
  • 26
    • 0032190113 scopus 로고    scopus 로고
    • Retroviral transfer of human cytochrome F450 genes for oxazaphosphorine-based cancer gene therapy
    • Jounaidi Y, Hecht JE, Waxman DJ. Retroviral transfer of human cytochrome F450 genes for oxazaphosphorine-based cancer gene therapy. Cancer Res. 1998;58:4391-4401.
    • (1998) Cancer Res , vol.58 , pp. 4391-4401
    • Jounaidi, Y.1    Hecht, J.E.2    Waxman, D.J.3
  • 27
    • 0031947191 scopus 로고    scopus 로고
    • An oncolytic viral mutant that delivers the CYP2B1 transgene and augments cyclophosphamide chemotherapy
    • Chase M, Chung RY, Chiocca EA. An oncolytic viral mutant that delivers the CYP2B1 transgene and augments cyclophosphamide chemotherapy. Nat Biotechnol. 1998;16:444-448.
    • (1998) Nat Biotechnol , vol.16 , pp. 444-448
    • Chase, M.1    Chung, R.Y.2    Chiocca, E.A.3
  • 28
    • 0342467852 scopus 로고    scopus 로고
    • Microencapsulated cell-mediated treatment of inoperable pancreatic carcinoma
    • Lohr M, Hoffmeyer A, Kroger J, et al. Microencapsulated cell-mediated treatment of inoperable pancreatic carcinoma. Lancet. 2001;357:1591-1592.
    • (2001) Lancet , vol.357 , pp. 1591-1592
    • Lohr, M.1    Hoffmeyer, A.2    Kroger, J.3
  • 29
    • 7344268645 scopus 로고    scopus 로고
    • Targeted chemotherapy by intratumour injection of encapsulated cells engineered to produce CYP2B1, an ifosfamide activating cytochrome P450
    • Lohr M, Muller P, Karle P, et al. Targeted chemotherapy by intratumour injection of encapsulated cells engineered to produce CYP2B1, an ifosfamide activating cytochrome P450. Gene Ther. 1998;5:1070-1078.
    • (1998) Gene Ther , vol.5 , pp. 1070-1078
    • Lohr, M.1    Muller, P.2    Karle, P.3
  • 30
    • 0019332750 scopus 로고
    • Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen
    • Knowles BB, Howe CC, Aden DP. Human hepatocellular carcinoma cell lines secrete the major plasma proteins and hepatitis B surface antigen. Science. 1980;209:497-499.
    • (1980) Science , vol.209 , pp. 497-499
    • Knowles, B.B.1    Howe, C.C.2    Aden, D.P.3
  • 31
    • 0032478271 scopus 로고    scopus 로고
    • A simplified system for generating recombinant adenoviruses
    • He TC, Zhou S, da Costa LT, et al. A simplified system for generating recombinant adenoviruses. Proc Natl Acad Sci USA. 1998;95:2509-2514.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2509-2514
    • He, T.C.1    Zhou, S.2    Da Costa, L.T.3
  • 32
    • 0029671175 scopus 로고    scopus 로고
    • Human cytochromes P450 expressed in Escherichia coli: Production of specific antibodies
    • Belloc C, Baird S, Cosme J, et al. Human cytochromes P450 expressed in Escherichia coli: production of specific antibodies. Toxicology. 1996;106:207-219.
    • (1996) Toxicology , vol.106 , pp. 207-219
    • Belloc, C.1    Baird, S.2    Cosme, J.3
  • 33
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T, Sato R. The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem. 1964;239:2370-2378.
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 34
    • 0019041323 scopus 로고
    • Comparison of the properties of detergent-solubilized NADPH-cytochrome P-450 reductases from pig liver and kidney. Immunochemical, kinetic, and reconstitutive properties
    • Yasukochi Y, Okita RT, Masters BS. Comparison of the properties of detergent-solubilized NADPH-cytochrome P-450 reductases from pig liver and kidney. Immunochemical, kinetic, and reconstitutive properties. Arch Biochem Biophys. 1980;202:491-498.
    • (1980) Arch Biochem Biophys , vol.202 , pp. 491-498
    • Yasukochi, Y.1    Okita, R.T.2    Masters, B.S.3
  • 35
    • 0016283072 scopus 로고
    • The identity of glutathione S-transferase B with ligandin, a major binding protein of liver
    • Habig WH, Pabst MJ, Fleischner G, et al. The identity of glutathione S-transferase B with ligandin, a major binding protein of liver. Proc Natl Acad Sci USA. 1974;71:3879-3882.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3879-3882
    • Habig, W.H.1    Pabst, M.J.2    Fleischner, G.3
  • 36
    • 0018077763 scopus 로고
    • Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae
    • Bostian KA, Betts GF. Kinetics and reaction mechanism of potassium-activated aldehyde dehydrogenase from Saccharomyces cerevisiae. Biochem J. 1978;173:787-798.
    • (1978) Biochem J , vol.173 , pp. 787-798
    • Bostian, K.A.1    Betts, G.F.2
  • 37
    • 0034534311 scopus 로고    scopus 로고
    • Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism
    • Vasiliou V, Pappa A, Petersen DR. Role of aldehyde dehydrogenases in endogenous and xenobiotic metabolism. Chem Biol Interactions. 2000;129:1-19.
    • (2000) Chem Biol Interactions , vol.129 , pp. 1-19
    • Vasiliou, V.1    Pappa, A.2    Petersen, D.R.3
  • 38
    • 0001045385 scopus 로고
    • A new cytochrome in liver microsomes
    • Omura T, Sato R. A new cytochrome in liver microsomes. J Biol Chem. 1962;237:1375-1376.
    • (1962) J Biol Chem , vol.237 , pp. 1375-1376
    • Omura, T.1    Sato, R.2
  • 39
    • 0026471538 scopus 로고
    • Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide
    • McMillan K, Bredt DS, Hirsch DJ, et al. Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide. Proc Natl Acad Sci USA. 1992;89:11141-11145.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11141-11145
    • McMillan, K.1    Bredt, D.S.2    Hirsch, D.J.3
  • 40
    • 0016373637 scopus 로고
    • Omega-2) hydroxylation of fatty acids by a soluble system from bacillus megaterium
    • Miura Y, Fulco AJ. Omega-2) hydroxylation of fatty acids by a soluble system from bacillus megaterium. J Biol Chem. 1974;249:1880-1888.
    • (1974) J Biol Chem , vol.249 , pp. 1880-1888
    • Miura, Y.1    Fulco, A.J.2
  • 41
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MP, Waterman MR. Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc Natl Acad Sci USA. 1991;88:5597-5601.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 42
    • 0020490599 scopus 로고
    • Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region
    • Black SD, Coon MJ. Structural features of liver microsomal NADPH-cytochrome P-450 reductase. Hydrophobic domain, hydrophilic domain, and connecting region. J Biol Chem. 1982;257:5929-5938.
    • (1982) J Biol Chem , vol.257 , pp. 5929-5938
    • Black, S.D.1    Coon, M.J.2
  • 43
    • 0025048753 scopus 로고
    • Expression of bovine cytochrome P450c21 and its fused enzymes with yeast NADPH-cytochrome P450 reductase in Saccharomyces cerevisiae
    • Sakaki T, Shibata M, Yabusaki Y, et al. Expression of bovine cytochrome P450c21 and its fused enzymes with yeast NADPH-cytochrome P450 reductase in Saccharomyces cerevisiae. DNA Cell Biol. 1990;9:603-614.
    • (1990) DNA Cell Biol , vol.9 , pp. 603-614
    • Sakaki, T.1    Shibata, M.2    Yabusaki, Y.3
  • 44
    • 0025802732 scopus 로고
    • Glutathione conjugation with phosphoramide mustard and cyclophosphamide. A mechanistic study using tandem mass spectrometry
    • Yuan ZM, Smith PB, Brundrett RB, et al. Glutathione conjugation with phosphoramide mustard and cyclophosphamide. A mechanistic study using tandem mass spectrometry. Drug Metab Dispos. 1991;19:625-629.
    • (1991) Drug Metab Dispos , vol.19 , pp. 625-629
    • Yuan, Z.M.1    Smith, P.B.2    Brundrett, R.B.3
  • 45
    • 0034257012 scopus 로고    scopus 로고
    • Inactivation of aldophosphamide by human aldehyde dehydrogenase isozyme 3
    • Giorgianni F, Bridson PK, Sorrentino BP, et al. Inactivation of aldophosphamide by human aldehyde dehydrogenase isozyme 3. Biochem Pharmacol. 2000;60:325-338.
    • (2000) Biochem Pharmacol , vol.60 , pp. 325-338
    • Giorgianni, F.1    Bridson, P.K.2    Sorrentino, B.P.3
  • 46
    • 0346310513 scopus 로고    scopus 로고
    • Use of replication-conditional adenovirus as a helper system to enhance delivery of P450 prodrug-activation genes for cancer therapy
    • Jounaidi Y, Waxman DJ. Use of replication-conditional adenovirus as a helper system to enhance delivery of P450 prodrug-activation genes for cancer therapy. Cancer Res. 2004;64:292-303.
    • (2004) Cancer Res , vol.64 , pp. 292-303
    • Jounaidi, Y.1    Waxman, D.J.2
  • 48
    • 17344365922 scopus 로고    scopus 로고
    • Adenovirus-mediated herpes simplex virus thymidine kinase/ganciclovir gene therapy in patients with localized malignancy: Results of a phase I clinical trial in malignant mesothelioma
    • Sterman DH, Treat J, Litzky LA, et al. Adenovirus-mediated herpes simplex virus thymidine kinase/ganciclovir gene therapy in patients with localized malignancy: results of a phase I clinical trial in malignant mesothelioma. Hum Gene Ther. 1998;9:1083-1092.
    • (1998) Hum Gene Ther , vol.9 , pp. 1083-1092
    • Sterman, D.H.1    Treat, J.2    Litzky, L.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.