메뉴 건너뛰기




Volumn 12, Issue 11, 1999, Pages 1098-1109

Regulation of expression of N-methylpurine DNA glycosylase in human mammary epithelial cells: Role of transcription factor AP-2

Author keywords

[No Author keywords available]

Indexed keywords

DNA GLYCOSYLTRANSFERASE; MESSENGER RNA; N METHYLPURINE DNA GLYCOSYLASE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR AP 2; UNCLASSIFIED DRUG;

EID: 0344286102     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx9901027     Document Type: Article
Times cited : (8)

References (55)
  • 2
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • Lindahl, T., Sedwick, B., Sekiguchi, M., and Nakabeppu, Y. (1988) Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57, 133-157.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 133-157
    • Lindahl, T.1    Sedwick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 3
    • 0029892791 scopus 로고    scopus 로고
    • DNA repair in eukaryotes
    • Wood, R. D. (1996) DNA repair in eukaryotes. Annu. Rev. Biochem. 65, 135-167.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 135-167
    • Wood, R.D.1
  • 5
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev, M., and Laval, J. (1994) Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. U.S.A. 91, 5873-5877.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 7
    • 0028174274 scopus 로고
    • 6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human n-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase)
    • 6-Ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase). Biochemistry 33, 1624-1628.
    • (1994) Biochemistry , vol.33 , pp. 1624-1628
    • Dosanjh, M.1    Roy, R.2    Mitra, S.3    Singer, B.4
  • 8
    • 0028087282 scopus 로고
    • All four known cyclic adducts formed in DNA by the vinyl chloride metabolite chloroacetaldehyde are released by a human DNA glycosylase
    • Dosanjh, M., Chenna, A., Kim, E., Fraenkel-Conrat, H., Samson, L., and Singer, B. (1994) All four known cyclic adducts formed in DNA by the vinyl chloride metabolite chloroacetaldehyde are released by a human DNA glycosylase. Proc. Natl. Acad. Sci. U.S.A. 91, 1024-1028.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1024-1028
    • Dosanjh, M.1    Chenna, A.2    Kim, E.3    Fraenkel-Conrat, H.4    Samson, L.5    Singer, B.6
  • 9
    • 0021528507 scopus 로고
    • 3-methyladenine residues in DNA induce the SOS function sfiA in Eschericia coli
    • Boiteux, S., Huisman, O., and Laval, J. (1984) 3-Methyladenine residues in DNA induce the SOS function sfiA in Eschericia coli. EMBO J. 3, 2569-2573.
    • (1984) EMBO J. , vol.3 , pp. 2569-2573
    • Boiteux, S.1    Huisman, O.2    Laval, J.3
  • 10
    • 0022363977 scopus 로고
    • Methylation-induced blocks to in vitro DNA replication
    • Larson, K., Sahm, J., Shenkar, R., and Strauss, B. (1985) Methylation-induced blocks to in vitro DNA replication. Mutat. Res. 150, 77-84.
    • (1985) Mutat. Res. , vol.150 , pp. 77-84
    • Larson, K.1    Sahm, J.2    Shenkar, R.3    Strauss, B.4
  • 11
    • 0032570769 scopus 로고    scopus 로고
    • A chemical and genetic approach together define the biological consequences of 3-methyladenine lesions in the mammalian genome
    • Engelward, B. P., Allan, J. M., Dreslin, A. J., Kelly, J. D., Wu, M. M., Gold, B., and Samson, L. (1998) A chemical and genetic approach together define the biological consequences of 3-methyladenine lesions in the mammalian genome. J. Biol. Chem. 273, 5412-5418.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5412-5418
    • Engelward, B.P.1    Allan, J.M.2    Dreslin, A.J.3    Kelly, J.D.4    Wu, M.M.5    Gold, B.6    Samson, L.7
  • 12
    • 0000628634 scopus 로고
    • 7-methylguanine adducts in DNA are normally present at high levels and increase on aging: Analysis by HPLC with electrochemical detection
    • Park, J. W., and Ames, B. N. (1988) 7-Methylguanine adducts in DNA are normally present at high levels and increase on aging: analysis by HPLC with electrochemical detection. Proc. Natl. Acad. Sci. U.S.A. 85, 7467-7470.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 7467-7470
    • Park, J.W.1    Ames, B.N.2
  • 13
    • 0030982861 scopus 로고    scopus 로고
    • Introduction, distribution, and removal of 7-methylguanine in different liver chromatin fractions of young and old mice
    • Gaubatz, J. W., and Tan, B. H. (1997) Introduction, distribution, and removal of 7-methylguanine in different liver chromatin fractions of young and old mice. Mutat. Res. 375, 25-35.
    • (1997) Mutat. Res. , vol.375 , pp. 25-35
    • Gaubatz, J.W.1    Tan, B.H.2
  • 14
    • 0027759522 scopus 로고
    • Purification and characterization of human 3-methyl-adenine-DNA glycosylase
    • O'Connor, T. R. (1993) Purification and characterization of human 3-methyl-adenine-DNA glycosylase. Nucleic Acids Res. 21, 5561-5569.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5561-5569
    • O'Connor, T.R.1
  • 15
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti, D., Ibeanu, G. C., Tano, K., and Mitra, S. (1991) Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J. Biol. Chem. 266, 15710-15715.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 16
    • 0025990209 scopus 로고
    • Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps chromosome 16
    • Samson, L., Derfler, B., Boosalis, M., and Call, K. (1991) Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps chromosome 16. Proc. Natl. Acad. Sci. U.S.A. 88, 9127-9131.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 9127-9131
    • Samson, L.1    Derfler, B.2    Boosalis, M.3    Call, K.4
  • 17
    • 0027538469 scopus 로고
    • Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere
    • Vickers, M. A., Vyas, P., Harris, P. C., Simmons, D. L., and Higgs, D. R. (1993) Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere. Proc. Natl. Acad. Sci. U.S.A. 90, 3437-3441.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3437-3441
    • Vickers, M.A.1    Vyas, P.2    Harris, P.C.3    Simmons, D.L.4    Higgs, D.R.5
  • 18
    • 0029132769 scopus 로고
    • Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates
    • Sun, B., Latham, K. A., Dodson, M. L., and Lloyd, R. S. (1995) Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates. J. Biol. Chem. 270, 19501-19508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19501-19508
    • Sun, B.1    Latham, K.A.2    Dodson, M.L.3    Lloyd, R.S.4
  • 19
    • 0029819596 scopus 로고    scopus 로고
    • The domains of mammalian base excision repair enzyme N-methylpurine-DNA glycosylase. Interaction, conformational change, and role in DNA binding and damage recognition
    • Roy, R., Kumar, A., Lee, J. C., and Mitra, S. (1996) The domains of mammalian base excision repair enzyme N-methylpurine-DNA glycosylase. Interaction, conformational change, and role in DNA binding and damage recognition. J. Biol. Chem. 271, 23690-23697.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23690-23697
    • Roy, R.1    Kumar, A.2    Lee, J.C.3    Mitra, S.4
  • 20
    • 0029829188 scopus 로고    scopus 로고
    • Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases
    • Roy, R., Kennel, S. J., and Mitra, S. (1996) Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases. Carcinogenesis 17, 2177-2182.
    • (1996) Carcinogenesis , vol.17 , pp. 2177-2182
    • Roy, R.1    Kennel, S.J.2    Mitra, S.3
  • 21
    • 0027351670 scopus 로고
    • Regulation of repair of alkylation damage in mammalian genomes
    • Mitra, S., and Kaina, B. (1993) Regulation of repair of alkylation damage in mammalian genomes. Prog. Nucleic Acid Res. Mol. Biol. 44, 109-142.
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 109-142
    • Mitra, S.1    Kaina, B.2
  • 22
    • 0028859644 scopus 로고
    • 6-methylguanine-DNA methyltransferase and N-methylpurine-DNA glycosylase in rat liver cells exhibiting different status of differentiation
    • 6-methylguanine-DNA methyltransferase and N-methylpurine-DNA glycosylase in rat liver cells exhibiting different status of differentiation. Biochim. Biophys. Acta 127, 63-72.
    • (1995) Biochim. Biophys. Acta , vol.127 , pp. 63-72
    • Grombacher, T.1    Kaina, B.2
  • 23
    • 0031106613 scopus 로고    scopus 로고
    • Quantitative reverse transcriptase polymerase chain reaction for measuring the N-methylpurine-DNA glycosylase mRNA level in rodent cells
    • Roy, G., Roy, R., and Mitra, S. (1997) Quantitative reverse transcriptase polymerase chain reaction for measuring the N-methylpurine-DNA glycosylase mRNA level in rodent cells. Anal. Biochem. 246, 45-51.
    • (1997) Anal. Biochem. , vol.246 , pp. 45-51
    • Roy, G.1    Roy, R.2    Mitra, S.3
  • 24
    • 0025923443 scopus 로고
    • 3-methyladenine glycosylase RNA transcripts in rat hepatoma cells treated with DNA-damaging agents
    • 3-methyladenine glycosylase RNA transcripts in rat hepatoma cells treated with DNA-damaging agents. Biochem. Biophys. Res. Commun. 176, 1086-1092.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1086-1092
    • Laval, F.1
  • 25
    • 0027340166 scopus 로고
    • 3-methyladenine-DNA-glycosylase in human cells exposed to DNA-damaging agents
    • 3-methyladenine-DNA-glycosylase in human cells exposed to DNA-damaging agents. DNA Cell Biol. 12, 233-241.
    • (1993) DNA Cell Biol. , vol.12 , pp. 233-241
    • Lefebvre, P.1    Zak, P.2    Laval, F.3
  • 26
    • 0029841771 scopus 로고    scopus 로고
    • Isolation and analysis of inducibility of the rat N-methylpurine-DNA glycosylase promoter
    • Grombacher, T., and Kaina, B. (1996) Isolation and analysis of inducibility of the rat N-methylpurine-DNA glycosylase promoter. DNA Cell Biol. 15, 581-588.
    • (1996) DNA Cell Biol. , vol.15 , pp. 581-588
    • Grombacher, T.1    Kaina, B.2
  • 27
    • 0026465075 scopus 로고
    • Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alkylating agents in Chinese hamster ovary cells
    • Ibeanu, G., Hartenstein, B., Dunn, W. C., Chang, L.-Y., Hofman, E., Coquerelle, T., Mitra, S., and Kaina, B. (1992) Overexpression of human DNA repair protein N-methylpurine-DNA glycosylase results in the increased removal of N-methylpurines in DNA without a concomitant increase in resistance to alkylating agents in Chinese hamster ovary cells. Carcinogenesis 13, 1989-1995.
    • (1992) Carcinogenesis , vol.13 , pp. 1989-1995
    • Ibeanu, G.1    Hartenstein, B.2    Dunn, W.C.3    Chang, L.-Y.4    Hofman, E.5    Coquerelle, T.6    Mitra, S.7    Kaina, B.8
  • 28
    • 0027340278 scopus 로고
    • 6-alkylguanine and N-alkylpurines to the formation of sister chromatid exchanges, chromosomal aberrations, and gene mutations
    • 6-alkylguanine and N-alkylpurines to the formation of sister chromatid exchanges, chromosomal aberrations, and gene mutations. Environ. Mol. Mutagen. 22, 283-292.
    • (1993) Environ. Mol. Mutagen. , vol.22 , pp. 283-292
    • Kaina, B.1    Fritz, G.2    Coquerelle, T.3
  • 29
    • 0028861087 scopus 로고
    • Enhanced host cell reactivation capacity and expression of DNA repair genes in human breast cancer cells resistant to bifunctional alkylating agents
    • Yen, L., Woo, A., Christopoulopoulos, G., Batist, G., Panasci, L., Roy, R., Mitra, S., and Alaoui-Jamali, M. A. (1995) Enhanced host cell reactivation capacity and expression of DNA repair genes in human breast cancer cells resistant to bifunctional alkylating agents. Mutat. Res. 337, 179-189.
    • (1995) Mutat. Res. , vol.337 , pp. 179-189
    • Yen, L.1    Woo, A.2    Christopoulopoulos, G.3    Batist, G.4    Panasci, L.5    Roy, R.6    Mitra, S.7    Alaoui-Jamali, M.A.8
  • 30
    • 0029670361 scopus 로고    scopus 로고
    • 6-alkyl guanine-DNA-alkyltransferase activities and sensitivity to alkylating agents in human cancer cell lines
    • 6-alkyl guanine-DNA-alkyltransferase activities and sensitivity to alkylating agents in human cancer cell lines. Br. J. Cancer 73, 861-865.
    • (1996) Br. J. Cancer , vol.73 , pp. 861-865
    • Damia, G.1    Imperatori, L.2    Citti, L.3    Mariani, L.4    D'Incalci, M.5
  • 31
    • 0031128016 scopus 로고    scopus 로고
    • Expression of genes of potential importance in the response to chemotherapy and DNA repair in patients with ovarian cancer
    • Codegoni, A. M., Broggini, M., Pitelli, M. R., Pantarotto, M., Torri, V., Mangioni, C., and D'Incalci, M. (1997) Expression of genes of potential importance in the response to chemotherapy and DNA repair in patients with ovarian cancer. Gynecol. Oncol. 65, 130-137.
    • (1997) Gynecol. Oncol. , vol.65 , pp. 130-137
    • Codegoni, A.M.1    Broggini, M.2    Pitelli, M.R.3    Pantarotto, M.4    Torri, V.5    Mangioni, C.6    D'Incalci, M.7
  • 32
    • 0028801762 scopus 로고
    • Overexpression of N-methylpurine-DNA glycosylase in chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents: A case of unbalanced DNA repair
    • Coquerelle, T., Dosch, J., and Kaina, B. (1995) Overexpression of N-methylpurine-DNA glycosylase in Chinese hamster ovary cells renders them more sensitive to the production of chromosomal aberrations by methylating agents: a case of unbalanced DNA repair. Mutat. Res. 336, 9-17.
    • (1995) Mutat. Res. , vol.336 , pp. 9-17
    • Coquerelle, T.1    Dosch, J.2    Kaina, B.3
  • 33
    • 0030041960 scopus 로고    scopus 로고
    • Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing
    • Engelward, B. P., Dreslin, A., Christensen, J., Huszar, D., Kurahara, C., and Samson, L. (1996) Repair-deficient 3-methyladenine DNA glycosylase homozygous mutant mouse cells have increased sensitivity to alkylation-induced chromosome damage and cell killing. EMBO J. 15, 945-952.
    • (1996) EMBO J. , vol.15 , pp. 945-952
    • Engelward, B.P.1    Dreslin, A.2    Christensen, J.3    Huszar, D.4    Kurahara, C.5    Samson, L.6
  • 35
    • 0031000977 scopus 로고    scopus 로고
    • Influence of oxygen radical injury on DNA methylation
    • Cerda, S., and Weitzman, S. A. (1997) Influence of oxygen radical injury on DNA methylation. Mutat. Res. 386, 141-152.
    • (1997) Mutat. Res. , vol.386 , pp. 141-152
    • Cerda, S.1    Weitzman, S.A.2
  • 36
    • 0032504048 scopus 로고    scopus 로고
    • Altered expression of the DNA repair protein, N-methylpurine-DNA glycosylase (MPG) in breast cancer
    • Cerda, S. R., Turk, P. W., Thor, A. D., and Weitzman, S. A. (1998) Altered expression of the DNA repair protein, N-methylpurine-DNA glycosylase (MPG) in breast cancer. FEES Lett. 431, 12-18.
    • (1998) FEES Lett. , vol.431 , pp. 12-18
    • Cerda, S.R.1    Turk, P.W.2    Thor, A.D.3    Weitzman, S.A.4
  • 37
    • 0023651331 scopus 로고
    • Positive and negative regulation of transcription in vitro: Enhancer-binding protein AP-2 is inhibited by SV40 T antigen
    • Mitchell, P. J., Wang, C., and Tjian, R. (1987) Positive and negative regulation of transcription in vitro: enhancer-binding protein AP-2 is inhibited by SV40 T antigen. Cell 50, 847-861.
    • (1987) Cell , vol.50 , pp. 847-861
    • Mitchell, P.J.1    Wang, C.2    Tjian, R.3
  • 38
    • 0028352111 scopus 로고
    • N-ras oncogene causes AP-2 transcriptional self-interference, which leads to transformation
    • Kannan, P., Buettner, R., Chiao, P. J., Yim, S. O., Sarkiss, M., and Tainsky, M. A. (1994) N-ras oncogene causes AP-2 transcriptional self-interference, which leads to transformation. Genes Dev. 8, 1258-1269.
    • (1994) Genes Dev. , vol.8 , pp. 1258-1269
    • Kannan, P.1    Buettner, R.2    Chiao, P.J.3    Yim, S.O.4    Sarkiss, M.5    Tainsky, M.A.6
  • 39
    • 0027174303 scopus 로고
    • An alternatively spliced mRNA from the AP-2 gene encodes a negative regulator of transcriptional activation by AP-2
    • Buettner, R., Kannan, P., Imhof, A., Bauer, R., Yim, S. O., Glockshuber, R., Van Dyke, M. W., and Tainsky, M. A. (1993) An alternatively spliced mRNA from the AP-2 gene encodes a negative regulator of transcriptional activation by AP-2. Mol. Cell. Biol. 13, 4174-4185.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4174-4185
    • Buettner, R.1    Kannan, P.2    Imhof, A.3    Bauer, R.4    Yim, S.O.5    Glockshuber, R.6    Van Dyke, M.W.7    Tainsky, M.A.8
  • 40
    • 0028851894 scopus 로고
    • Transcription factor AP-2 regulates human insulin-like growth factor binding protein-5 gene expression
    • Duan, C., and Clemmons, D. R. (1995) Transcription factor AP-2 regulates human insulin-like growth factor binding protein-5 gene expression. J. Biol. Chem. 270, 24844-24851.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24844-24851
    • Duan, C.1    Clemmons, D.R.2
  • 41
    • 0027240998 scopus 로고
    • Culture of normal and malignant primary human mammary epithelial cells in a physiological manner simulates in vivo growth patterns and allows discrimination of cell type
    • Bergstraesser, L. M., and Weitzman, S. A. (1993) Culture of normal and malignant primary human mammary epithelial cells in a physiological manner simulates in vivo growth patterns and allows discrimination of cell type. Cancer Res. 53, 2644-2654.
    • (1993) Cancer Res. , vol.53 , pp. 2644-2654
    • Bergstraesser, L.M.1    Weitzman, S.A.2
  • 42
    • 0023647951 scopus 로고
    • Recombination at the human α-globin gene cluster: Sequence features and topological constraints
    • Nicholls, R. D., Fischel-Ghodsian, N., and Higgs, D. R. (1987) Recombination at the human α-globin gene cluster: sequence features and topological constraints. Cell 49, 369-378.
    • (1987) Cell , vol.49 , pp. 369-378
    • Nicholls, R.D.1    Fischel-Ghodsian, N.2    Higgs, D.R.3
  • 44
    • 0028566660 scopus 로고
    • Genomic cloning and sequence analyses of the bovine α-, βA- and βB-inhibin/activin genes. Identification of transcription factor AP-2 binding sites in the 5′-flanking regions by DNase I footprinting
    • Thompson, D. A., Cronini, C. N., and Martin, F. (1994) Genomic cloning and sequence analyses of the bovine α-, βA- and βB-inhibin/activin genes. Identification of transcription factor AP-2 binding sites in the 5′-flanking regions by DNase I footprinting. Eur. J. Biochem. 226, 751-764.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 751-764
    • Thompson, D.A.1    Cronini, C.N.2    Martin, F.3
  • 45
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J., Lebovitz, R. M., and Roeder, R. G. (1983) Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11, 1475-1489.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475-1489
    • Dignam, J.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 46
    • 0028939981 scopus 로고
    • Transcriptional regulation of the elastin gene by insulin-like growth factor-i involves disruption of Sp1 binding. Evidence for the role of Rb in mediating Sp1 binding in aortic smooth muscle cells
    • Jensen, D. E., Rich, C. B., Terpstra, A. J., Farmer, S. R., and Foster, J. A. (1995) Transcriptional regulation of the elastin gene by insulin-like growth factor-I involves disruption of Sp1 binding. Evidence for the role of Rb in mediating Sp1 binding in aortic smooth muscle cells. J. Biol. Chem. 270, 6555-6563.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6555-6563
    • Jensen, D.E.1    Rich, C.B.2    Terpstra, A.J.3    Farmer, S.R.4    Foster, J.A.5
  • 48
    • 0031427477 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the promoter of the human N-methylpurine-DNA glycosylase (MPG) gene
    • Izume, T., Tatsuka, M., Tano, K., Asano, M., and Mitra, S. (1997) Molecular cloning and characterization of the promoter of the human N-methylpurine-DNA glycosylase (MPG) gene. Carcinogenesis 18, 1837-1839.
    • (1997) Carcinogenesis , vol.18 , pp. 1837-1839
    • Izume, T.1    Tatsuka, M.2    Tano, K.3    Asano, M.4    Mitra, S.5
  • 51
    • 0022540321 scopus 로고
    • CpG-rich islands and the function of DNA methylation
    • Bird, A. P. (1986) CpG-rich islands and the function of DNA methylation. Nature 321, 209-213.
    • (1986) Nature , vol.321 , pp. 209-213
    • Bird, A.P.1
  • 52
    • 0028872554 scopus 로고
    • The developmentally regulated transcription factor AP-2 is involved in c-erbB-2 overexpression in human mammary carcinoma
    • Bosher, J. M., Williams, T., and Hurst, H. C. (1995) The developmentally regulated transcription factor AP-2 is involved in c-erbB-2 overexpression in human mammary carcinoma. Proc. Natl. Acad. Sci. U.S.A. 92, 744-747.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 744-747
    • Bosher, J.M.1    Williams, T.2    Hurst, H.C.3
  • 53
    • 0023663116 scopus 로고
    • Transcription factor AP-2 mediates induction by two different signal-transduction pathways: Protein kinase C and cAMP
    • Imagawa, M., Chiu, R., and Karin, M. (1987) Transcription factor AP-2 mediates induction by two different signal-transduction pathways: protein kinase C and cAMP. Cell 51, 251-260.
    • (1987) Cell , vol.51 , pp. 251-260
    • Imagawa, M.1    Chiu, R.2    Karin, M.3
  • 54
    • 0024199329 scopus 로고
    • Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements
    • Williams, T., Admon, A., Luscher, B., and Tijian, R. (1988) Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements. Genes Dev. 2, 1557-1569.
    • (1988) Genes Dev. , vol.2 , pp. 1557-1569
    • Williams, T.1    Admon, A.2    Luscher, B.3    Tijian, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.