메뉴 건너뛰기




Volumn 6, Issue 3, 2009, Pages 801-812

Antitumor therapy mediated by 5-fluorocytosine and a recombinant fusion protein containing TSG-6 hyaluronan binding domain and yeast cytosine deaminase

Author keywords

Cancer; Drug delivery; Enzyme prodrug therapy; Protein engineering; Tumor matrix

Indexed keywords

CYTOSINE DEAMINASE; DRINKING WATER; FLUCYTOSINE; FLUOROURACIL; HYALURONIC ACID; HYBRID PROTEIN; LINK CYTOSINE DEAMINASE; UNCLASSIFIED DRUG;

EID: 67249100785     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp800013c     Document Type: Article
Times cited : (19)

References (57)
  • 1
    • 0035980983 scopus 로고    scopus 로고
    • Selective activation of anticancer prodrugs by monoclonal antibody-enzyme conjugates
    • Senter, P. D.; Springer, C. J. Selective activation of anticancer prodrugs by monoclonal antibody-enzyme conjugates. Adv. Drug Delivery Rev. 2001, 53, 247-264.
    • (2001) Adv. Drug Delivery Rev. , vol.53 , pp. 247-264
    • Senter, P.D.1    Springer, C.J.2
  • 2
    • 0021169796 scopus 로고
    • Accessibility of circulating immunoglobulin G to the extravascular compartment of solid rat tumors
    • O'Connor, S. W.; Bale, W. F. Accessibility of circulating immunoglobulin G to the extravascular compartment of solid rat tumors. Cancer Res. 1984, 44, 3719-3723. (Pubitemid 14041580)
    • (1984) Cancer Research , vol.44 , Issue.9 , pp. 3719-3723
    • O'Connor, S.W.1    Bale, W.F.2
  • 3
    • 0023619243 scopus 로고
    • Antibody directed enzymes revive anti-cancer prodrugs concept
    • Bagshawe, K. D. Antibody directed enzymes revive anti-cancer prodrugs concept. Br. J. Cancer 1987, 56, 531-532. (Pubitemid 17165643)
    • (1987) British Journal of Cancer , vol.56 , Issue.5 , pp. 531-532
    • Bagshawe, K.D.1
  • 5
    • 0028335819 scopus 로고
    • Intratumoral generation of 5-fluorouracil mediated by an antibody-cytosine deaminase conjugate in combination with 5-fluorocytosine
    • Wallace, P. M.; MacMaster, J. F.; Smith, V. F.; Kerr, D. E.; Senter, P. D.; Cosand, W. L. Intratumoral generation of 5-fluorouracil mediated by an antibody-cytosine deaminase conjugate in combination with 5-fluorocytosine. Cancer Res. 1994, 54, 2719-2723. (Pubitemid 24173764)
    • (1994) Cancer Research , vol.54 , Issue.10 , pp. 2719-2723
    • Wallace, P.M.1    MacMaster, J.F.2    Smith, V.F.3    Kerr, D.E.4    Senter, P.D.5    Cosand, W.L.6
  • 6
    • 0033119291 scopus 로고    scopus 로고
    • Superiority of yeast over bacterial cytosine deaminase for enzyme/prodrug gene therapy in colon cancer xenografts
    • Kievit, E.; Bershad, E.; Ng, E.; Sethna, P.; Dev, I.; Lawrence, T. S.; Rehemtulla, A. Superiority of yeast over bacterial cytosine deaminase for enzyme/prodrug gene therapy in colon cancer xenografts. Cancer Res. 1999, 59, 1417-1421. (Pubitemid 29160102)
    • (1999) Cancer Research , vol.59 , Issue.7 , pp. 1417-1421
    • Kievit, E.1    Bershad, E.2    Ng, E.3    Sethna, P.4    Dev, I.5    Lawrence, T.S.6    Rehemtulla, A.7
  • 7
    • 0036468901 scopus 로고    scopus 로고
    • Intratumoral 5-fluorouracil produced by cytosine deaminase/5- fluorocytosine gene therapy is effective for experimental human glioblastomas
    • Miller, C. R.; Williams, C. R.; Buchsbaum, D. J.; Gillespie, G. Y. Intratumoral 5-fluorouracil produced by cytosine deaminase/5- fluorocytosine gene therapy is effective for experimental human glioblastomas. Cancer Res. 2002, 62, 773-780. (Pubitemid 34126953)
    • (2002) Cancer Research , vol.62 , Issue.3 , pp. 773-780
    • Miller, C.R.1    Williams, C.R.2    Buchsbaum, D.J.3    Gillespie, G.Y.4
  • 8
    • 0036789520 scopus 로고    scopus 로고
    • Combined radiation and gene therapy for brain tumors with adenovirus-mediated transfer of cytosine deaminase and uracil phosphoribosyltransferase genes
    • Kambara, H.; Tamiya, T.; Ono, Y.; Ohtsuka, S.; Terada, K.; Adachi, Y.; Ichikawa, T.; Hamada, H.; Ohmoto, T. Combined radiation and gene therapy for brain tumors with adenovirus-mediated transfer of cytosine deaminase and uracil phosphoribosyltransferase genes. Cancer Gene Ther. 2002, 9, 840-845.
    • (2002) Cancer Gene Ther. , vol.9 , pp. 840-845
    • Kambara, H.1    Tamiya, T.2    Ono, Y.3    Ohtsuka, S.4    Terada, K.5    Adachi, Y.6    Ichikawa, T.7    Hamada, H.8    Ohmoto, T.9
  • 9
    • 0242584508 scopus 로고    scopus 로고
    • A33scFV-cytosine deaminase: A recombinant protein construct for antibody-directed enzyme-prodrug therapy
    • DOI 10.1038/sj.bjc.6600751
    • Deckert, P. M.; Renner, C.; Cohen, L. S.; Jungbluth, A.; Ritter, G.; Bertino, J. R.; Old, L. J.; Welt, S. A33scFv-cytosine deaminase: a recombinant protein construct for antibody-directed enzyme-prodrug therapy. Br. J. Cancer 2003, 88, 937-939. (Pubitemid 36520883)
    • (2003) British Journal of Cancer , vol.88 , Issue.6 , pp. 937-939
    • Deckert, P.M.1    Renner, C.2    Cohen, L.S.3    Jungbluth, A.4    Ritter, G.5    Bertino, J.R.6    Old, L.J.7    Welt, S.8
  • 10
    • 27744448427 scopus 로고    scopus 로고
    • Single-shot, multicycle suicide gene therapy by replication-competent retrovirus vectors achieves long-term survival benefit in experimental glioma
    • Tai, C. K.; Wang, W. J.; Chen, T. C.; Kasahara, N. Single-shot, multicycle suicide gene therapy by replication-competent retrovirus vectors achieves long-term survival benefit in experimental glioma. Mol. Ther. 2005, 12, 842-851.
    • (2005) Mol. Ther. , vol.12 , pp. 842-851
    • Tai, C.K.1    Wang, W.J.2    Chen, T.C.3    Kasahara, N.4
  • 13
    • 0035123128 scopus 로고    scopus 로고
    • Gene directed enzyme/prodrug therapy of cancer: Historical appraisal and future prospectives
    • Greco, O.; Dachs, G. U. Gene directed enzyme/prodrug therapy of cancer: historical appraisal and future prospectives. J. Cell. Physiol. 2001, 187, 22-36.
    • (2001) J. Cell. Physiol. , vol.187 , pp. 22-36
    • Greco, O.1    Dachs, G.U.2
  • 14
    • 51049098968 scopus 로고    scopus 로고
    • Anticancer therapeutics: Targeting molecules and nanocarriers to hyaluronan or CD44, a hyaluronan receptor
    • Platt, V. M.; Szoka, F. C., Jr. Anticancer therapeutics: targeting molecules and nanocarriers to hyaluronan or CD44, a hyaluronan receptor. Mol. Pharmaceutics 2008, 5, 474-486.
    • (2008) Mol. Pharmaceutics , vol.5 , pp. 474-486
    • Platt, V.M.1    Szoka Jr., F.C.2
  • 15
    • 0030820092 scopus 로고    scopus 로고
    • Hyaluronan: Its nature, distribution, functions and turnover
    • Fraser, J. R.; Laurent, T. C.; Laurent, U. B. Hyaluronan: its nature, distribution, functions and turnover. J. Intern. Med. 1997, 242, 27-33.
    • (1997) J. Intern. Med. , vol.242 , pp. 27-33
    • Fraser, J.R.1    Laurent, T.C.2    Laurent, U.B.3
  • 16
    • 0033562998 scopus 로고    scopus 로고
    • Relationship between hyaluronan production and metastatic potential of mouse mammary carcinoma cells
    • Itano, N.; Sawai, T.; Miyaishi, O.; Kimata, K. Relationship between hyaluronan production and metastatic potential of mouse mammary carcinoma cells. Cancer Res. 1999, 59, 2499-2504. (Pubitemid 29242303)
    • (1999) Cancer Research , vol.59 , Issue.10 , pp. 2499-2504
    • Itano, N.1    Sawai, T.2    Miyaishi, O.3    Kimata, K.4
  • 17
    • 0033106004 scopus 로고    scopus 로고
    • Overproduction of hyaluronan by expression of the hyaluronan synthase Has2 enhances anchorage-independent growth and tumorigenicity
    • Kosaki, R.; Watanabe, K.; Yamaguchi, Y. Overproduction of hyaluronan by expression of the hyaluronan synthase Has2 enhances anchorage-independent growth and tumorigenicity. Cancer Res. 1999, 59, 1141-1145. (Pubitemid 29135978)
    • (1999) Cancer Research , vol.59 , Issue.5 , pp. 1141-1145
    • Kosaki, R.1    Watanabe, K.2    Yamaguchi, Y.3
  • 18
    • 3042697038 scopus 로고    scopus 로고
    • Hyaluronan: From extracellular glue to pericellular cue
    • Toole, B. P. Hyaluronan: from extracellular glue to pericellular cue. Nat. Rev. Cancer 2004, 4, 528-539.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 528-539
    • Toole, B.P.1
  • 19
    • 0033970911 scopus 로고    scopus 로고
    • High levels of stromal hyaluronan predict poor disease outcome in epithelial ovarian cancer
    • Anttila, M. A.; Tammi, R. H.; Tammi, M. I.; Syrjanen, K. J.; Saarikoski, S. V.; Kosma, V. M. High levels of stromal hyaluronan predict poor disease outcome in epithelial ovarian cancer. Cancer Res. 2000, 60, 150-155. (Pubitemid 30058745)
    • (2000) Cancer Research , vol.60 , Issue.1 , pp. 150-155
    • Anttila, M.A.1    Tammi, R.H.2    Tammi, M.I.3    Syrjanen, K.J.4    Saarikoski, S.V.5    Kosma, V.-M.6
  • 21
    • 0033215242 scopus 로고    scopus 로고
    • Carcinoma-associated fibroblasts direct tumor progression of initiated human prostatic epithelium
    • Olumi, A. F.; Grossfeld, G. D.; Hayward, S. W.; Carroll, P. R.; Tlsty, T. D.; Cunha, G. R. Carcinoma-associated fibroblasts direct tumor progression of initiated human prostatic epithelium. Cancer Res. 1999, 59, 5002-5011. (Pubitemid 29472907)
    • (1999) Cancer Research , vol.59 , Issue.19 , pp. 5002-5011
    • Olumi, A.F.1    Grossfeld, G.D.2    Hayward, S.W.3    Carroll, P.R.4    Tlsty, T.D.5    Cunha, G.R.6
  • 22
    • 0035821780 scopus 로고    scopus 로고
    • Soluble CD44 inhibits melanoma tumor growth by blocking cell surface CD44 binding to hyaluronic acid
    • DOI 10.1038/sj.onc.1204435
    • Ahrens, T.; Sleeman, J. P.; Schempp, C. M.; Howells, N.; Hofmann, M.; Ponta, H.; Herrlich, P.; Simon, J. C. Soluble CD44 inhibits melanoma tumor growth by blocking cell surface CD44 binding to hyaluronic acid. Oncogene 2001, 20, 3399-3408. (Pubitemid 32588988)
    • (2001) Oncogene , vol.20 , Issue.26 , pp. 3399-3408
    • Ahrens, T.1    Sleeman, J.P.2    Schempp, C.M.3    Howells, N.4    Hofmann, M.5    Ponta, H.6    Herrlich, P.7    Simon, J.C.8
  • 23
    • 0033895822 scopus 로고    scopus 로고
    • Perturbation of hyaluronan interactions by soluble CD44 inhibits growth of murine mammary carcinoma cells in ascites
    • Peterson, R. M.; Yu, Q.; Stamenkovic, I.; Toole, B. P. Perturbation of hyaluronan interactions by soluble CD44 inhibits growth of murine mammary carcinoma cells in ascites. Am. J. Pathol. 2000, 156, 2159-2167.
    • (2000) Am. J. Pathol. , vol.156 , pp. 2159-2167
    • Peterson, R.M.1    Yu, Q.2    Stamenkovic, I.3    Toole, B.P.4
  • 24
    • 0642333840 scopus 로고    scopus 로고
    • Functional roles of hyaluronan in B16-F10 melanoma growth and experimental metastasis in mice
    • Mummert, M. E.; Mummert, D. I.; Ellinger, L.; Takashima, A. Functional roles of hyaluronan in B16-F10 melanoma growth and experimental metastasis in mice. Mol. Cancer. Ther. 2003, 2, 295-300.
    • (2003) Mol. Cancer. Ther. , vol.2 , pp. 295-300
    • Mummert, M.E.1    Mummert, D.I.2    Ellinger, L.3    Takashima, A.4
  • 25
    • 0141483365 scopus 로고    scopus 로고
    • A peptide with three hyaluronan binding motifs inhibits tumor growth and induces apoptosis
    • Xu, X. M.; Chen, Y.; Chen, J.; Yang, S.; Gao, F.; Underhill, C. B.; Creswell, K.; Zhang, L. A peptide with three hyaluronan binding motifs inhibits tumor growth and induces apoptosis. Cancer Res. 2003, 63, 5685-5690. (Pubitemid 37203377)
    • (2003) Cancer Research , vol.63 , Issue.18 , pp. 5685-5690
    • Xu, X.-M.1    Chen, Y.2    Chen, J.3    Yang, S.4    Gao, F.5    Underhill, C.B.6    Creswell, K.7    Zhang, L.8
  • 26
    • 0037085372 scopus 로고    scopus 로고
    • Hyaluronan-binding proteins: Tying up the giant
    • Day, A. J.; Prestwich, G. D. Hyaluronan-binding proteins: tying up the giant. J. Biol. Chem. 2002, 277, 4585-4588.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4585-4588
    • Day, A.J.1    Prestwich, G.D.2
  • 27
    • 22844432511 scopus 로고    scopus 로고
    • Towards a structure for a TSG-6 hyaluronan complex by modeling and NMR spectroscopy: Insights into other members of the link module superfamily
    • Blundell, C. D.; Almond, A.; Mahoney, D. J.; DeAngelis, P. L.; Campbell, I. D.; Day, A. J. Towards a structure for a TSG-6 hyaluronan complex by modeling and NMR spectroscopy: insights into other members of the link module superfamily. J. Biol. Chem. 2005, 280, 18189-18201.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18189-18201
    • Blundell, C.D.1    Almond, A.2    Mahoney, D.J.3    Deangelis, P.L.4    Campbell, I.D.5    Day, A.J.6
  • 29
    • 0037135550 scopus 로고    scopus 로고
    • Hyaluronan binding properties of a CD44 chimera containing the link module of TSG-6
    • Lesley, J.; English, N. M.; Gal, I.; Mikecz, K.; Day, A. J.; Hyman, R. Hyaluronan binding properties of a CD44 chimera containing the link module of TSG-6. J. Biol. Chem. 2002, 277, 26600-26608.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26600-26608
    • Lesley, J.1    English, N.M.2    Gal, I.3    Mikecz, K.4    Day, A.J.5    Hyman, R.6
  • 30
    • 0017859809 scopus 로고
    • Flucytosine kinetics in subjects with normal and impaired renal function
    • Cutler, R. E.; Blair, A. D.; Kelly, M. R. Flucytosine kinetics in subjects with normal and impaired renal function. Clin. Pharmacol. Ther. 1978, 24, 333-342.
    • (1978) Clin. Pharmacol. Ther. , vol.24 , pp. 333-342
    • Cutler, R.E.1    Blair, A.D.2    Kelly, M.R.3
  • 32
    • 33749005129 scopus 로고    scopus 로고
    • Efficient synthesis of an aldehyde functionalized hyaluronic acid and its application in the preparation of hyaluronan-lipid conjugates
    • Ruhela, D.; Riviere, K.; Szoka, F. C., Jr. Efficient synthesis of an aldehyde functionalized hyaluronic acid and its application in the preparation of hyaluronan-lipid conjugates. Bioconjugate Chem. 2006, 17, 1360-1363.
    • (2006) Bioconjugate Chem. , vol.17 , pp. 1360-1363
    • Ruhela, D.1    Riviere, K.2    Szoka Jr., F.C.3
  • 33
    • 14644429125 scopus 로고    scopus 로고
    • A human biotin acceptor domain allows site-specific conjugation of an enzyme to an antibody-avidin fusion protein for targeted drug delivery
    • Asai, T.; Trinh, R.; Ng, P. P.; Penichet, M. L.; Wims, L. A.; Morrison, S. L. A human biotin acceptor domain allows site-specific conjugation of an enzyme to an antibody-avidin fusion protein for targeted drug delivery. Biomol. Eng. 2005, 21, 145-155.
    • (2005) Biomol. Eng. , vol.21 , pp. 145-155
    • Asai, T.1    Trinh, R.2    Ng, P.P.3    Penichet, M.L.4    Wims, L.A.5    Morrison, S.L.6
  • 34
    • 0043133654 scopus 로고    scopus 로고
    • The 1.14 Å crystal structure of yeast cytosine deaminase: Evolution of nucleotide salvage enzymes and implications for genetic chemotherapy
    • DOI 10.1016/S0969-2126(03)00153-9
    • Ireton, G. C.; Black, M. E.; Stoddard, B. L. The 1.14 A crystal structure of yeast cytosine deaminase: evolution of nucleotide salvage enzymes and implications for genetic chemotherapy. Structure 2003, 11, 961-972. (Pubitemid 36966785)
    • (2003) Structure , vol.11 , Issue.8 , pp. 961-972
    • Ireton, G.C.1    Black, M.E.2    Stoddard, B.L.3
  • 35
    • 0038482076 scopus 로고    scopus 로고
    • Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution
    • Ko, T. P.; Lin, J. J.; Hu, C. Y.; Hsu, Y. H.; Wang, A. H.; Liaw, S. H. Crystal structure of yeast cytosine deaminase. Insights into enzyme mechanism and evolution. J. Biol. Chem. 2003, 278, 19111-19117.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19111-19117
    • Ko, T.P.1    Lin, J.J.2    Hu, C.Y.3    Hsu, Y.H.4    Wang, A.H.5    Liaw, S.H.6
  • 36
    • 21344468592 scopus 로고    scopus 로고
    • PEGylation of yeast cytosine deaminase for pretargeting
    • Xiong, M. P.; Kwon, G. S. PEGylation of yeast cytosine deaminase for pretargeting. J. Pharm. Sci. 2005, 94, 1249-1258.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1249-1258
    • Xiong, M.P.1    Kwon, G.S.2
  • 37
    • 18244373419 scopus 로고    scopus 로고
    • Computational thermostabilization of an enzyme
    • DOI 10.1126/science.1107387
    • Korkegian, A.; Black, M. E.; Baker, D.; Stoddard, B. L. Computational thermostabilization of an enzyme. Science 2005, 308, 857-860. (Pubitemid 40629266)
    • (2005) Science , vol.308 , Issue.5723 , pp. 857-860
    • Korkegian, A.1    Black, M.E.2    Baker, D.3    Stoddard, B.L.4
  • 38
    • 0034662177 scopus 로고    scopus 로고
    • Localization and characterization of the hyaluronan-binding site on the Link module from human TSG-6
    • DOI 10.1016/S0969-2126(00)00163-5
    • Kahmann, J. D.; O'Brien, R.; Werner, J. M.; Heinegard, D.; Ladbury, J. E.; Campbell, I. D.; Day, A. J. Localization and characterization of the hyaluronan-binding site on the link module from human TSG-6. Structure 2000, 8, 763-774. (Pubitemid 30469994)
    • (2000) Structure , vol.8 , Issue.7 , pp. 763-774
    • Kahmann, J.D.1    O'Brien, R.2    Werner, J.M.3    Heinegard, D.4    Ladbury, J.E.5    Campbell, I.D.6    Day, A.J.7
  • 39
    • 0031927798 scopus 로고    scopus 로고
    • Tumor pH: Implications for treatment and novel drug design
    • Gerweck, L. E. Tumor pH: implications for treatment and novel drug design. Semin. Radiat. Oncol. 1998, 8, 176-182.
    • (1998) Semin. Radiat. Oncol. , vol.8 , pp. 176-182
    • Gerweck, L.E.1
  • 40
    • 33845222070 scopus 로고    scopus 로고
    • Facile synthesis of multivalent nitrilotriacetic acid (NTA) and NTA conjugates for analytical and drug delivery applications
    • Huang, Z.; Park, J. I.; Watson, D. S.; Hwang, P.; Szoka, F. C., Jr. Facile synthesis of multivalent nitrilotriacetic acid (NTA) and NTA conjugates for analytical and drug delivery applications. Bioconjugate Chem. 2006, 17, 1592-1600.
    • (2006) Bioconjugate Chem. , vol.17 , pp. 1592-1600
    • Huang, Z.1    Park, J.I.2    Watson, D.S.3    Hwang, P.4    Szoka Jr., F.C.5
  • 41
    • 0030221293 scopus 로고    scopus 로고
    • Overexpression, purification, and refolding of link module from human TSG-6 in Escherichia coli: Effect of temperature, media, and mutagenesis on lysine misincorporation at arginine AGA codons
    • DOI 10.1006/prep.1996.0068
    • Day, A. J.; Aplin, R. T.; Willis, A. C. Overexpression, purification, and refolding of link module from human TSG-6 in Escherichia coli: effect of temperature, media, and mutagenesis on lysine misincorporation at arginine AGA codons. Protein Expression Purif. 1996, 8, 1-16. (Pubitemid 26326208)
    • (1996) Protein Expression and Purification , vol.8 , Issue.1 , pp. 1-16
    • Day, A.J.1    Aplin, R.T.2    Willis, A.C.3
  • 42
    • 0031127761 scopus 로고    scopus 로고
    • Method for quantitative refolding of the link module from human TSG-6
    • DOI 10.1006/prep.1996.0694
    • Kahmann, J. D.; Koruth, R.; Day, A. J. Method for quantitative refolding of the link module from human TSG-6. Protein Expression Purif. 1997, 9, 315-318. (Pubitemid 27210699)
    • (1997) Protein Expression and Purification , vol.9 , Issue.3 , pp. 315-318
    • Kahmann, J.D.1    Koruth, R.2    Day, A.J.3
  • 43
    • 0032420055 scopus 로고    scopus 로고
    • Characterization of a functional hyaluronan-binding domain from the human CD44 molecule expressed in Escherichia coil
    • DOI 10.1006/prep.1998.0971
    • Banerji, S.; Day, A. J.; Kahmann, J. D.; Jackson, D. G. Characterization of a functional hyaluronan-binding domain from the human CD44 molecule expressed in Escherichia coli. Protein Expression Purif. 1998, 14, 371-381. (Pubitemid 29020371)
    • (1998) Protein Expression and Purification , vol.14 , Issue.3 , pp. 371-381
    • Banerji, S.1    Day, A.J.2    Kahmann, J.D.3    Jackson, D.G.4
  • 44
    • 0041360024 scopus 로고    scopus 로고
    • Fusion protein of the hyaluronan binding domain from human TSG-6 with luciferase for assay of hyaluronan
    • Chang, T. S.; Wan, H. M.; Chen, C. C.; Giridhar, R.; Wu, W. T. Fusion protein of the hyaluronan binding domain from human TSG-6 with luciferase for assay of hyaluronan. Biotechnol. Lett. 2003, 25, 1037-1040.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1037-1040
    • Chang, T.S.1    Wan, H.M.2    Chen, C.C.3    Giridhar, R.4    Wu, W.T.5
  • 45
    • 0035933770 scopus 로고    scopus 로고
    • Mapping the hyaluronan-binding site on the Link module from human tumor necrosis factor-stimulated gene-6 by site-directed mutagenesis
    • Mahoney, D. J.; Blundell, C. D.; Day, A. J. Mapping the hyaluronan-binding site on the Link module from human tumor necrosis factor-stimulated gene-6 by site-directed mutagenesis. J. Biol. Chem. 2001, 276, 22764-22771.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22764-22771
    • Mahoney, D.J.1    Blundell, C.D.2    Day, A.J.3
  • 46
    • 0344267645 scopus 로고    scopus 로고
    • Enhancement of 5-fluorouracil cytotoxicity by human thymidine- Phosphorylase expression in cancer cells: In vitro and in vivo study
    • DOI 10.1002/(SICI)1097-0215(19990129)80:3<465::AID-IJC21>3.0.CO;2-6
    • Evrard, A.; Cuq, P.; Robert, B.; Vian, L.; Pelegrin, A.; Cano, J. P. Enhancement of 5-fluorouracil cytotoxicity by human thymidine-phosphorylase expression in cancer cells: in vitro and in vivo study. Int. J. Cancer 1999, 80, 465-470. (Pubitemid 29019637)
    • (1999) International Journal of Cancer , vol.80 , Issue.3 , pp. 465-470
    • Evrard, A.1    Pierre, C.2    Robert, B.3    Vian, L.4    Pelegrin, A.5    Cano, J.-P.6
  • 47
    • 33646351049 scopus 로고    scopus 로고
    • Immunotherapy with dendritic cells and CpG oligonucleotides can be combined with chemotherapy without loss of efficacy in a mouse model of colon cancer
    • DOI 10.1002/ijc.21681
    • Bourquin, C.; Schreiber, S.; Beck, S.; Hartmann, G.; Endres, S. Immunotherapy with dendritic cells and CpG oligonucleotides can be combined with chemotherapy without loss of efficacy in a mouse model of colon cancer. Int. J. Cancer 2006, 118, 2790-2795. (Pubitemid 43673358)
    • (2006) International Journal of Cancer , vol.118 , Issue.11 , pp. 2790-2795
    • Bourquin, C.1    Schreiber, S.2    Beck, S.3    Hartmann, G.4    Endres, S.5
  • 48
    • 16644368560 scopus 로고    scopus 로고
    • Per os administration of 5-fluorocytosine is effective in the regression of CD-expressing liver metastases in rats
    • Gavelli, A.; Baque, P.; Brossettej, N.; Bourgeon, A.; Staccini, P.; Rossi, B.; Pierrefite-Carle, V. Per os administration of 5-fluorocytosine is effective in the regression of CD-expressing liver metastases in rats. Int. J. Mol. Med. 2004, 14, 323-325.
    • (2004) Int. J. Mol. Med. , vol.14 , pp. 323-325
    • Gavelli, A.1    Baque, P.2    Brossettej, N.3    Bourgeon, A.4    Staccini, P.5    Rossi, B.6    Pierrefite-Carle, V.7
  • 51
    • 0027656118 scopus 로고
    • Application of monoclonal antibodies against cytosine deaminase for the in vivo clearance of a cytosine deaminase immunoconjugate
    • Kerr, D. E.; Garrigues, U. S.; Wallace, P. M.; Hellstrom, K. E.; Hellstrom, I.; Senter, P. D. Application of monoclonal antibodies against cytosine deaminase for the in vivo clearance of a cytosine deaminase immunoconjugate. Bioconjugate Chem. 1993, 4, 353-357.
    • (1993) Bioconjugate Chem. , vol.4 , pp. 353-357
    • Kerr, D.E.1    Garrigues, U.S.2    Wallace, P.M.3    Hellstrom, K.E.4    Hellstrom, I.5    Senter, P.D.6
  • 52
    • 35848952531 scopus 로고    scopus 로고
    • Design, construction, and in vitro analysis of A33scFv::CDy, a recombinant fusion protein for antibody-directed enzyme prodrug therapy in colon cancer
    • Coelho, V.; Dernedde, J.; Petrausch, U.; Panjideh, H.; Fuchs, H.; Menzel, C.; Dubel, S.; Keilholz, U.; Thiel, E.; Deckert, P. M. Design, construction, and in vitro analysis of A33scFv::CDy, a recombinant fusion protein for antibody-directed enzyme prodrug therapy in colon cancer. Int. J. Oncol. 2007, 31, 951-957.
    • (2007) Int. J. Oncol. , vol.31 , pp. 951-957
    • Coelho, V.1    Dernedde, J.2    Petrausch, U.3    Panjideh, H.4    Fuchs, H.5    Menzel, C.6    Dubel, S.7    Keilholz, U.8    Thiel, E.9    Deckert, P.M.10
  • 55
    • 0036211035 scopus 로고    scopus 로고
    • Clinical protocol. Liposomal gene therapy with the herpes simplex thymidine kinase gene/ganciclovir system for the treatment of glioblastoma multiforme
    • Voges, J.; Weber, F.; Reszka, R.; Sturm, V.; Jacobs, A.; Heiss, W. D.; Wiestler, O.; Kapp, J. F. Clinical protocol. Liposomal gene therapy with the herpes simplex thymidine kinase gene/ganciclovir system for the treatment of glioblastoma multiforme. Hum. Gene Ther. 2002, 13, 675-685.
    • (2002) Hum. Gene Ther. , vol.13 , pp. 675-685
    • Voges, J.1    Weber, F.2    Reszka, R.3    Sturm, V.4    Jacobs, A.5    Heiss, W.D.6    Wiestler, O.7    Kapp, J.F.8
  • 56
    • 13844262865 scopus 로고    scopus 로고
    • Distribution in brain of liposomes after convection enhanced delivery; modulation by particle charge, particle diameter, and presence of steric coating
    • MacKay, J. A.; Deen, D. F.; Szoka, F. C., Jr. Brain Res. 2005, 1035, 139-153, Distribution in brain of liposomes after convection enhanced delivery; modulation by particle charge, particle diameter, and presence of steric coating.
    • (2005) Brain Res. , vol.1035 , pp. 139-153
    • MacKay, J.A.1    Deen, D.F.2    Szoka Jr., F.C.3
  • 57
    • 18844370132 scopus 로고    scopus 로고
    • Biological evaluation of polyester dendrimer: Poly(ethylene oxide) "bow-tie" hybrids with tunable molecular weight and architecture
    • Gillies, E. R.; Dy, E.; Frechet, J. M.; Szoka, F. C. Biological evaluation of polyester dendrimer: poly(ethylene oxide) "bow-tie" hybrids with tunable molecular weight and architecture. Mol. Pharmaceutics 2005, 2, 129-138.
    • (2005) Mol. Pharmaceutics , vol.2 , pp. 129-138
    • Gillies, E.R.1    Dy, E.2    Frechet, J.M.3    Szoka, F.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.