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Volumn 43, Issue 28, 2004, Pages 8957-8964

Alanine-scanning mutagenesis reveals a cytosine deaminase mutant with altered substrate preference

Author keywords

[No Author keywords available]

Indexed keywords

DRUG PRODUCTS; ENZYMES; GENES; MUTAGENESIS; ONCOLOGY; SUBSTRATES;

EID: 3142668353     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049720z     Document Type: Article
Times cited : (44)

References (25)
  • 1
    • 0029857743 scopus 로고    scopus 로고
    • The use of cationic liposomes DC-CHOL/DOPE and DDAB/DOPE for direct transfer of Escherichia coli cytosine deaminase gene into growing melanoma tumors
    • Szala, S., Missol, E., Sochanik, A., and Strozyk, M. (1996) The use of cationic liposomes DC-CHOL/DOPE and DDAB/DOPE for direct transfer of Escherichia coli cytosine deaminase gene into growing melanoma tumors, Gene Ther. 3, 1026-1031.
    • (1996) Gene Ther. , vol.3 , pp. 1026-1031
    • Szala, S.1    Missol, E.2    Sochanik, A.3    Strozyk, M.4
  • 2
    • 0032710575 scopus 로고    scopus 로고
    • Construction and testing of gene therapy retroviral vector expressing bacterial cytosine deaminase gene
    • Hlavaty, J., Hlubinova, K., and Altaner, C. (1999) Construction and testing of gene therapy retroviral vector expressing bacterial cytosine deaminase gene, Neoplasma 46, 267-276.
    • (1999) Neoplasma , vol.46 , pp. 267-276
    • Hlavaty, J.1    Hlubinova, K.2    Altaner, C.3
  • 3
    • 0035342191 scopus 로고    scopus 로고
    • Cancer gene therapy by adenovirus-mediated gene transfer
    • Wu, Q., Moyana, T., and Xiang, J. (2001) Cancer gene therapy by adenovirus-mediated gene transfer, Curr. Gene Ther. 1, 101-122.
    • (2001) Curr. Gene Ther. , vol.1 , pp. 101-122
    • Wu, Q.1    Moyana, T.2    Xiang, J.3
  • 4
    • 0027523517 scopus 로고
    • A first step in the development of gene therapy for colorectal carcinoma: Cloning, sequencing, and expression of Escherichia coli cytosine deaminase
    • Austin, E. A., and Huber, B. E. (1992) A first step in the development of gene therapy for colorectal carcinoma: Cloning, sequencing, and expression of Escherichia coli cytosine deaminase, Mol. Pharmacol. 43, 380-387.
    • (1992) Mol. Pharmacol. , vol.43 , pp. 380-387
    • Austin, E.A.1    Huber, B.E.2
  • 5
    • 0026599586 scopus 로고
    • Transfer of the bacterial gene for cytosine deaminase to mammalian cells confers lethal sensitivity to 5-fluorocytosine: A negative selection system
    • Mullen, C. A., Kilstrup, M., and Blaese, R. M. (1992) Transfer of the bacterial gene for cytosine deaminase to mammalian cells confers lethal sensitivity to 5-fluorocytosine: A negative selection system, Proc. Natl. Acad. Sci. U.S.A. 89, 33-37.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 33-37
    • Mullen, C.A.1    Kilstrup, M.2    Blaese, R.M.3
  • 6
    • 0027496518 scopus 로고
    • In vivo antitumor activity of 5-fluorocytosine on human colorectal carcinoma cells genetically modified to express cytosine deaminase
    • Huber, B. E., Austin, E. A., Good, S. S., Knick, V. C., Tibbels, S., and Richards, C. A. (1993) In vivo antitumor activity of 5-fluorocytosine on human colorectal carcinoma cells genetically modified to express cytosine deaminase, Cancer Res. 53, 4619-4626.
    • (1993) Cancer Res. , vol.53 , pp. 4619-4626
    • Huber, B.E.1    Austin, E.A.2    Good, S.S.3    Knick, V.C.4    Tibbels, S.5    Richards, C.A.6
  • 7
    • 0028795075 scopus 로고
    • In vivo adenovirus-mediated gene transfer of the Escherichia coli cytosine deaminase gene to human colon carcinoma-derived tumors induces chemosensitivity to 5-fluorocytosine
    • Hirschowitz, E. A., Ohwada, A., Pascal, W. R., Russi, T. J., and Crystal, R. G. (1995) In vivo adenovirus-mediated gene transfer of the Escherichia coli cytosine deaminase gene to human colon carcinoma-derived tumors induces chemosensitivity to 5-fluorocytosine, Hum. Gene Ther. 6, 1055-1063.
    • (1995) Hum. Gene Ther. , vol.6 , pp. 1055-1063
    • Hirschowitz, E.A.1    Ohwada, A.2    Pascal, W.R.3    Russi, T.J.4    Crystal, R.G.5
  • 8
    • 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., and Rehemtulla, A. (1999) Superiority of yeast over bacterial cytosine deaminase for enzyme/prodrug gene therapy in colon cancer xenografts, Cancer Res. 59, 1417-1421.
    • (1999) Cancer Res. , vol.59 , 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
  • 9
    • 0022485359 scopus 로고
    • Tumor chemosensitivity conferred by inserted herpes thymidine kinase genes: Paradigm for a prospective cancer control strategy
    • Moolten, F. L. (1986) Tumor chemosensitivity conferred by inserted herpes thymidine kinase genes: Paradigm for a prospective cancer control strategy, Cancer Res. 46, 5276-5281.
    • (1986) Cancer Res. , vol.46 , pp. 5276-5281
    • Moolten, F.L.1
  • 10
    • 0027787053 scopus 로고
    • In vitro evidence that metabolic cooperation is responsible for the bystander effect observed with HSV-tk retroviral gene therapy
    • Bi, W. L., Parysek, L. M., Warnick, R., and Stambrook, P. J. (1993) In vitro evidence that metabolic cooperation is responsible for the bystander effect observed with HSV-tk retroviral gene therapy, Hum. Gene Ther. 4, 725-731.
    • (1993) Hum. Gene Ther. , vol.4 , pp. 725-731
    • Bi, W.L.1    Parysek, L.M.2    Warnick, R.3    Stambrook, P.J.4
  • 11
    • 0029996360 scopus 로고    scopus 로고
    • Bystander killing of cancer cells by herpes simplex virus thymidine kinase gene is mediated by connexins
    • Mesnil, M., Piccoli, C., Tiraby, G., Willecke, K., and Yamasaki, H. (1996) Bystander killing of cancer cells by herpes simplex virus thymidine kinase gene is mediated by connexins, Proc. Natl. Acad. Sci. U.S.A. 93, 1831-1835.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1831-1835
    • Mesnil, M.1    Piccoli, C.2    Tiraby, G.3    Willecke, K.4    Yamasaki, H.5
  • 12
    • 0031727713 scopus 로고    scopus 로고
    • Long-term connexin-mediated bystander effect in highly tumorigenic human cells in vivo in herpes simplex virus thymidine kinase/ganciclovir gene therapy
    • Duflot-Dancer, A., Piccoli, C., Rolland, A., Yamasaki, H., and Mesnil, M. (1998) Long-term connexin-mediated bystander effect in highly tumorigenic human cells in vivo in herpes simplex virus thymidine kinase/ganciclovir gene therapy, Gene Ther. 5, 1372-1378.
    • (1998) Gene Ther. , vol.5 , pp. 1372-1378
    • Duflot-Dancer, A.1    Piccoli, C.2    Rolland, A.3    Yamasaki, H.4    Mesnil, M.5
  • 13
    • 0027268254 scopus 로고
    • Transport of 5-fluorouracil and uracil into human erythrocytes
    • Domin, B. A., Mahony, W. B., and Zimmerman, T. P. (1993) Transport of 5-fluorouracil and uracil into human erythrocytes, Biochem. Pharmacol. 46, 503-510.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 503-510
    • Domin, B.A.1    Mahony, W.B.2    Zimmerman, T.P.3
  • 14
    • 0036304598 scopus 로고    scopus 로고
    • The structure of E. coli cytosine deaminase at 1.5 Å resolution
    • Ireton, G. C., McDermitt, G., Black, M. E., and Stoddard, B. L. (2002) The structure of E. coli cytosine deaminase at 1.5 Å resolution, J. Mol. Bio. 315, 687-697.
    • (2002) J. Mol. Bio. , vol.315 , pp. 687-697
    • Ireton, G.C.1    McDermitt, G.2    Black, M.E.3    Stoddard, B.L.4
  • 15
    • 0029896252 scopus 로고    scopus 로고
    • Cloning, characterization, and modeling of mouse and human guanylate kinases
    • Brady, W. A., Kokoris, M. S., Fitzgibbon, M., and Black, M. E. (1996) Cloning, characterization, and modeling of mouse and human guanylate kinases, J. Biol. Chem. 271, 16734-16749.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16734-16749
    • Brady, W.A.1    Kokoris, M.S.2    Fitzgibbon, M.3    Black, M.E.4
  • 16
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection, Proc. Natl. Acad. Sci. U.S.A. 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 17
    • 0017796138 scopus 로고
    • Cytosine and cytidine deaminase from yeast
    • Ipata, P. L., and Cercignani, G. (1978) Cytosine and cytidine deaminase from yeast, Methods Enzymol. 51, 395-400.
    • (1978) Methods Enzymol. , vol.51 , pp. 395-400
    • Ipata, P.L.1    Cercignani, G.2
  • 18
    • 0032029743 scopus 로고    scopus 로고
    • Cloning, overexpression, and purification of cytosine deaminase from Saccharomyces cerevisiae
    • Hayden, M. S., Linsley, P. S., Wallace, A. R., Marquardt, H., and Kerr, D. E. (1998) Cloning, overexpression, and purification of cytosine deaminase from Saccharomyces cerevisiae, Protein Expression Purif 12, 173-184.
    • (1998) Protein Expression Purif. , vol.12 , pp. 173-184
    • Hayden, M.S.1    Linsley, P.S.2    Wallace, A.R.3    Marquardt, H.4    Kerr, D.E.5
  • 21
    • 0028057520 scopus 로고
    • Cytidine deaminase. The 2.4-Å crystal structure of an enzyme: Transition-state analog complex
    • Betts, L., Xiang, S., Short, S. A., Wolfenden, R., and Carter, C. W., Jr. (1994) Cytidine deaminase. The 2.4-Å crystal structure of an enzyme: Transition-state analog complex, J. Mol. Biol. 235, 635-656.
    • (1994) J. Mol. Biol. , vol.235 , pp. 635-656
    • Betts, L.1    Xiang, S.2    Short, S.A.3    Wolfenden, R.4    Carter Jr., C.W.5
  • 22
    • 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
    • Ireton, G. C., Black, M. E., and Stoddard, B. L. (2003) The 1.14-Å crystal structure of yeast cytosine deaminase: Evolution of nucleotide salvage enzymes and implications for genetic chemotherapy, Structure 11, 961-972.
    • (2003) Structure , vol.11 , pp. 961-972
    • Ireton, G.C.1    Black, M.E.2    Stoddard, B.L.3
  • 23
    • 0026434561 scopus 로고
    • Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations
    • Wilson, D. K., Rudolph, F. B., and Quiocho, F. A. (1991) Atomic structure of adenosine deaminase complexed with a transition-state analog: Understanding catalysis and immunodeficiency mutations, Science 252, 1278-1284.
    • (1991) Science , vol.252 , pp. 1278-1284
    • Wilson, D.K.1    Rudolph, F.B.2    Quiocho, F.A.3
  • 24
    • 0032499630 scopus 로고    scopus 로고
    • Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH maximum activity
    • Wang, Z., and Quiocho, F. A. (1998) Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH maximum activity, Biochemistry 37, 8314-8324.
    • (1998) Biochemistry , vol.37 , pp. 8314-8324
    • Wang, Z.1    Quiocho, F.A.2
  • 25
    • 0027398949 scopus 로고
    • A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water
    • Wilson, D. K., and Quiocho, F. A. (1993) A pre-transition-state mimic of an enzyme: X-ray structure of adenosine deaminase with bound 1-deazaadenosine and zinc-activated water, Biochemistry 32, 1689-1694.
    • (1993) Biochemistry , vol.32 , pp. 1689-1694
    • Wilson, D.K.1    Quiocho, F.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.