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Volumn 12, Issue 5, 2005, Pages 452-460

Erratum: Inhibiting estrogen responses in breast cancer cells using a fusion protein encoding estrogen receptor-α and the transcriptional repressor PLZF (Gene Therapy) (2005) vol. 12 (452-460) 10.1038/sj.gt.3302421);Inhibiting estrogen responses in breast cancer cells using a fusion protein encoding estrogen receptor-α and the transcriptional repressor PLZF

Author keywords

Breast cancer; Estrogen receptor; Gene expression; PLZF

Indexed keywords

CATHEPSIN D; ESTROGEN; ESTROGEN RECEPTOR ALPHA; HYBRID PROTEIN; PROGESTERONE RECEPTOR; PROMYELOCYTIC LEUKEMIA ZINC FINGER PROTEIN; PROTEIN PS2; REPRESSOR PROTEIN; TETRACYCLINE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 20144364363     PISSN: 09697128     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gt.3302529     Document Type: Erratum
Times cited : (15)

References (42)
  • 1
  • 2
    • 0036488531 scopus 로고    scopus 로고
    • Endocrine-responsive breast cancer and strategies for combating resistance
    • Ali S, Coombes RC. Endocrine-responsive breast cancer and strategies for combating resistance. Nat Rev Cancer 2002; 2: 101-112.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 101-112
    • Ali, S.1    Coombes, R.C.2
  • 3
    • 0034802910 scopus 로고    scopus 로고
    • Advances in aromatase inhibition: Clinical efficacy and tolerability in the treatment of breast cancer
    • Buzdar A, Howell A. Advances in aromatase inhibition: clinical efficacy and tolerability in the treatment of breast cancer. Clin Cancer Res 2001; 7: 2620-2635.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2620-2635
    • Buzdar, A.1    Howell, A.2
  • 4
    • 0035976638 scopus 로고    scopus 로고
    • Nuclear receptors and lipid physiology: Opening the X-files
    • Chawla A, Repa JJ, Evans RM, Mangelsdorf DJ. Nuclear receptors and lipid physiology: opening the X-files. Science 2001; 294: 1866-1870.
    • (2001) Science , vol.294 , pp. 1866-1870
    • Chawla, A.1    Repa, J.J.2    Evans, R.M.3    Mangelsdorf, D.J.4
  • 5
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai Mi, O'Malley BW. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu Rev Biochem 1994; 63: 451-486.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 6
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K et al. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997; 389: 251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1
  • 7
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P, Allis CD, Sassone-Corsi P. Signaling to chromatin through histone modifications. Cell 2000; 103: 263-271.
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 8
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. Translating the histone code. Science 2001; 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 9
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein M. Histone acetylation in chromatin structure and transcription. Nature 1997; 389: 349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 10
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman JL, Kingston RE. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu Rev Biochem 1998; 67: 545-579.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 11
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • Glass CK, Rosenfeld MG. The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 2000; 14: 121-141.
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 12
    • 0037154974 scopus 로고    scopus 로고
    • Combinatorial control of gene expression by nuclear receptors and coregulators
    • McKenna NJ, O'Malley BW. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 2002; 108 465-474.
    • (2002) Cell , vol.108 , pp. 465-474
    • McKenna, N.J.1    O'Malley, B.W.2
  • 13
    • 0033520325 scopus 로고    scopus 로고
    • Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase
    • Chen H et al. Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. Cell 1999; 98: 675-686.
    • (1999) Cell , vol.98 , pp. 675-686
    • Chen, H.1
  • 14
    • 0032899038 scopus 로고    scopus 로고
    • Retinoblastoma protein meets chromatin
    • Brehm A, Kouzarides T. Retinoblastoma protein meets chromatin. Trends Biochem Sci 1999; 24: 142-145.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 142-145
    • Brehm, A.1    Kouzarides, T.2
  • 15
    • 0033119780 scopus 로고    scopus 로고
    • DNA methylation and chromatin modification
    • Ng HH, Bird A. DNA methylation and chromatin modification. Curr Opin Genet Dev 1999; 9: 158-163.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 158-163
    • Ng, H.H.1    Bird, A.2
  • 16
    • 0033601073 scopus 로고    scopus 로고
    • Methylation-induced repression - Belts, braces, and chromatin
    • Bird AP, Wolffe AP. Methylation-induced repression - belts, braces, and chromatin. Cell 1999; 99: 451-454.
    • (1999) Cell , vol.99 , pp. 451-454
    • Bird, A.P.1    Wolffe, A.P.2
  • 17
    • 0033577693 scopus 로고    scopus 로고
    • A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivation
    • O'Neill LP et al. A developmental switch in H4 acetylation upstream of Xist plays a role in X chromosome inactivation. EMBO J 1999; 18: 2897-2907.
    • (1999) EMBO J. , vol.18 , pp. 2897-2907
    • O'Neill, L.P.1
  • 18
    • 0033988813 scopus 로고    scopus 로고
    • DNA methyltransferase Dnmt1 associates with histone deacetylase activity
    • Fuks F et al. DNA methyltransferase Dnmt1 associates with histone deacetylase activity. Nat Genet 2000; 24: 88-91.
    • (2000) Nat. Genet. , vol.24 , pp. 88-91
    • Fuks, F.1
  • 19
    • 0035873225 scopus 로고    scopus 로고
    • Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription
    • Fuks F et al. Dnmt3a binds deacetylases and is recruited by a sequence-specific repressor to silence transcription. EMBO J 2001; 20: 2536-2544.
    • (2001) EMBO J. , vol.20 , pp. 2536-2544
    • Fuks, F.1
  • 20
    • 0035962631 scopus 로고    scopus 로고
    • DNA methylation, methyltransferases, and cancer
    • Robertson KD. DNA methylation, methyltransferases, and cancer. Oncogene 2001; 20: 3139-3155.
    • (2001) Oncogene , vol.20 , pp. 3139-3155
    • Robertson, K.D.1
  • 21
    • 0033919595 scopus 로고    scopus 로고
    • DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters
    • Robertson KD et al. DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. Nat Genet 2000; 25: 338-342.
    • (2000) Nat. Genet. , vol.25 , pp. 338-342
    • Robertson, K.D.1
  • 22
    • 9544220768 scopus 로고    scopus 로고
    • The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein
    • Borrow J et al. The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. Nat Genet 1996; 14: 33-41.
    • (1996) Nat. Genet. , vol.14 , pp. 33-41
    • Borrow, J.1
  • 23
    • 0032080173 scopus 로고    scopus 로고
    • A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia
    • Carapeti M, Aguiar RC, Goldman JM, Cross NC. A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia. Blood 1998; 91: 3127-3133.
    • (1998) Blood , vol.91 , pp. 3127-3133
    • Carapeti, M.1    Aguiar, R.C.2    Goldman, J.M.3    Cross, N.C.4
  • 24
    • 0027411688 scopus 로고
    • Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia
    • Chen Z et al. Fusion between a novel Kruppel-like zinc finger gene and the retinoic acid receptor-alpha locus due to a variant t(11;17) translocation associated with acute promyelocytic leukaemia. EMBO J 1993; 12: 1161-1167.
    • (1993) EMBO J. , vol.12 , pp. 1161-1167
    • Chen, Z.1
  • 25
    • 0031941912 scopus 로고    scopus 로고
    • Distinct interactions of PML-RARalpha and PLZF-RARalpha with co-repressors determine differential responses to RA in APL
    • He LZ et al. Distinct interactions of PML-RARalpha and PLZF-RARalpha with co-repressors determine differential responses to RA in APL. Nat Genet 1998; 18: 126-135.
    • (1998) Nat. Genet. , vol.18 , pp. 126-135
    • He, L.Z.1
  • 26
    • 0032546017 scopus 로고    scopus 로고
    • Role of the histone deacetylase complex in acute promyelocytic leukaemia
    • Lin RJ et al. Role of the histone deacetylase complex in acute promyelocytic leukaemia. Nature 1998; 391: 811-814.
    • (1998) Nature , vol.391 , pp. 811-814
    • Lin, R.J.1
  • 27
    • 17144458786 scopus 로고    scopus 로고
    • Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia
    • Grignani F et al. Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature 1998; 391: 815-818.
    • (1998) Nature , vol.391 , pp. 815-818
    • Grignani, F.1
  • 28
    • 0032522962 scopus 로고    scopus 로고
    • Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia
    • Guidez F et al. Reduced retinoic acid-sensitivities of nuclear receptor corepressor binding to PML- and PLZF-RARalpha underlie molecular pathogenesis and treatment of acute promyelocytic leukemia. Blood 1998; 91: 2634-2642.
    • (1998) Blood , vol.91 , pp. 2634-2642
    • Guidez, F.1
  • 29
    • 0032516221 scopus 로고    scopus 로고
    • Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein
    • David G et al. Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein. Oncogene 1998; 16: 2549-2556.
    • (1998) Oncogene , vol.16 , pp. 2549-2556
    • David, G.1
  • 30
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green S, Issemann I, Sheer E. A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res 1988; 16: 369.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 369
    • Green, S.1    Issemann, I.2    Sheer, E.3
  • 31
    • 0024317270 scopus 로고
    • The human estrogen receptor has two independent nonacidic transcriptional activation functions
    • Tora L et al. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 1989; 59: 477-487.
    • (1989) Cell , vol.59 , pp. 477-487
    • Tora, L.1
  • 32
    • 0032906876 scopus 로고    scopus 로고
    • Phosphorylation of human estrogen receptor alpha by protein kinase A regulates dimerization
    • Chen D, Pace PE, Coombes RC, Ali S. Phosphorylation of human estrogen receptor alpha by protein kinase A regulates dimerization. Mol Cell Biol 1999; 19: 1002-1015.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1002-1015
    • Chen, D.1    Pace, P.E.2    Coombes, R.C.3    Ali, S.4
  • 33
    • 0027894195 scopus 로고
    • Production and characterization of monoclonal antibodies recognising defined regions of the human oestrogen receptor
    • Ali S et al. Production and characterization of monoclonal antibodies recognising defined regions of the human oestrogen receptor. Hybridoma 1993; 12: 391-405.
    • (1993) Hybridoma , vol.12 , pp. 391-405
    • Ali, S.1
  • 34
    • 0028818983 scopus 로고
    • Leukemia translocation gene, PLZF, is expressed with a speckled nuclear pattern in early hematopoietic progenitors
    • Reid A et al. Leukemia translocation gene, PLZF, is expressed with a speckled nuclear pattern in early hematopoietic progenitors. Blood 1995; 86: 4544-4552.
    • (1995) Blood , vol.86 , pp. 4544-4552
    • Reid, A.1
  • 35
    • 2542464918 scopus 로고
    • Phenol red in tissue culture media is a weak estrogen: Implications concerning the study of estrogen-responsive cells in culture
    • Berthois Y, Katzenellenbogen JA, Katzenellenbogen BS. Phenol red in tissue culture media is a weak estrogen: implications concerning the study of estrogen-responsive cells in culture. Proc Natl Acad Sci USA 1986; 83: 2496-2500.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 2496-2500
    • Berthois, Y.1    Katzenellenbogen, J.A.2    Katzenellenbogen, B.S.3
  • 36
    • 0018254898 scopus 로고
    • Nuclear mechanisms of estrogen action. Effects of estradiol and anti-estrogens on estrogen receptors and nuclear receptor processing
    • Horwitz KB, McGuire WL. Nuclear mechanisms of estrogen action. Effects of estradiol and anti-estrogens on estrogen receptors and nuclear receptor processing. J Biol Chem 1978; 253: 8185-8191.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8185-8191
    • Horwitz, K.B.1    McGuire, W.L.2
  • 37
    • 0025239785 scopus 로고
    • Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B
    • Kastner P et al. Two distinct estrogen-regulated promoters generate transcripts encoding the two functionally different human progesterone receptor forms A and B. EMBO J 1990; 9: 1603-1614.
    • (1990) EMBO J. , vol.9 , pp. 1603-1614
    • Kastner, P.1
  • 38
    • 0040390304 scopus 로고
    • Activation of pS2 gene transcription is a primary response to estrogen in the human breast cancer cell line MCF-7
    • Brown AM, Jeltsch JM, Roberts M, Chambon P. Activation of pS2 gene transcription is a primary response to estrogen in the human breast cancer cell line MCF-7. Proc Natl Acad Sci USA 1984; 81: 6344-6348.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6344-6348
    • Brown, A.M.1    Jeltsch, J.M.2    Roberts, M.3    Chambon, P.4
  • 39
    • 0022547236 scopus 로고
    • The 52-kDa estrogen-induced protein secreted by MCF7 cells is a lysosomal acidic protease
    • Morisset M, Capony F, Rochefort H. The 52-kDa estrogen-induced protein secreted by MCF7 cells is a lysosomal acidic protease. Biochem Biophys Res Commun 1986; 138: 102-109.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 102-109
    • Morisset, M.1    Capony, F.2    Rochefort, H.3
  • 40
    • 0035878743 scopus 로고    scopus 로고
    • Estrogen receptor interaction with estrogen response elements
    • Klinge CM. Estrogen receptor interaction with estrogen response elements. Nucleic Acids Res 2001; 29: 2905-2919.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2905-2919
    • Klinge, C.M.1
  • 41
    • 0033637703 scopus 로고    scopus 로고
    • Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription
    • Shang Y et al. Cofactor dynamics and sufficiency in estrogen receptor-regulated transcription. Cell 2000; 103: 843-852.
    • (2000) Cell , vol.103 , pp. 843-852
    • Shang, Y.1
  • 42
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R et al. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003; 115: 751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1


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