메뉴 건너뛰기




Volumn 17, Issue 10, 2003, Pages 2013-2027

Various Phosphorylation Pathways, Depending on Agonist and Antagonist Binding to Endogenous Estrogen Receptor α (ERα), Differentially Affect ERα Extractability, Proteasome-Mediated Stability, and Transcriptional Activity in Human Breast Cancer Cells

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 11 [4 [[5 [(4,4,5,5,5 PENTAFLUOROPENTYL)SULFONYL]PENTYL]OXY]PHENYL]ESTRADIOL; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 HYDROXYTAMOXIFEN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLOHEXIMIDE; ENZYME ACTIVATOR; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; FULVESTRANT; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PROTEASOME; PROTEIN KINASE; PROTEIN KINASE C; PROTEIN P42; PROTEIN P44; SB 023580; SB 203190; SYNAPTOPHYSIN; UNCLASSIFIED DRUG;

EID: 0142056952     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2002-0269     Document Type: Article
Times cited : (129)

References (71)
  • 2
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt WB, Toft DO 1997 Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr Rev 18:306-360
    • (1997) Endocr Rev , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 3
    • 0142016045 scopus 로고    scopus 로고
    • Functional relationships between steroid receptors and immunophilins
    • Trivandrum, India: Research Trends
    • Marsaud V, Radanyi C, Renoir J-M 1998 Functional relationships between steroid receptors and immunophilins. In: Current topics in steroid research, vol 1. Trivandrum, India: Research Trends; 59-71
    • (1998) Current Topics in Steroid Research , vol.1 , pp. 59-71
    • Marsaud, V.1    Radanyi, C.2    Renoir, J.-M.3
  • 4
    • 0031611355 scopus 로고    scopus 로고
    • Transcriptional activation by oestrogen receptors
    • Parker MG 1998 Transcriptional activation by oestrogen receptors. Biochem Soc Symp 63:45-50
    • (1998) Biochem Soc Symp , vol.63 , pp. 45-50
    • Parker, M.G.1
  • 5
    • 0034454583 scopus 로고    scopus 로고
    • Nuclear hormone receptor coregulators in action: Diversity for shared tasks
    • Robyr D, Wolffe AP, Wahli W 2000 Nuclear hormone receptor coregulators in action: diversity for shared tasks. Mol Endocrinol 14:329-347
    • (2000) Mol Endocrinol , vol.14 , pp. 329-347
    • Robyr, D.1    Wolffe, A.P.2    Wahli, W.3
  • 6
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T 1999 Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 9:40-48
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 8
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau AK, Barstad D, Loria PM, Cheng L, Kushner P, Agard DA, Greene GL 1998 The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927-937
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.5    Agard, D.A.6    Greene, G.L.7
  • 11
    • 0037211754 scopus 로고    scopus 로고
    • Estrogen receptor phosphorylation
    • Lannigan DA 2003 Estrogen receptor phosphorylation. Steroids 68:1-9
    • (2003) Steroids , vol.68 , pp. 1-9
    • Lannigan, D.A.1
  • 12
    • 0021147928 scopus 로고
    • The estrogen receptor in MCF-7 cells: Evidence from dense amino acid labeling for rapid turnover and a dimeric model of activated nuclear receptor
    • Scholl S, Lippman ME 1984 The estrogen receptor in MCF-7 cells: evidence from dense amino acid labeling for rapid turnover and a dimeric model of activated nuclear receptor. Endocrinology 115:1295-1301
    • (1984) Endocrinology , vol.115 , pp. 1295-1301
    • Scholl, S.1    Lippman, M.E.2
  • 13
    • 0021327660 scopus 로고
    • Estrogen receptor synthesis and turnover in MCF-7 breast cancer cells measured by a density shift technique
    • Eckert RL, Mullick A, Rorke EA, Katzenellenbogen BS 1984 Estrogen receptor synthesis and turnover in MCF-7 breast cancer cells measured by a density shift technique. Endocrinology 114:629-637
    • (1984) Endocrinology , vol.114 , pp. 629-637
    • Eckert, R.L.1    Mullick, A.2    Rorke, E.A.3    Katzenellenbogen, B.S.4
  • 14
    • 0029100143 scopus 로고
    • Ubiquitination of the rat uterine estrogen receptor: Dependence on estradiol
    • Nirmala PB, Thampan RV 1995 Ubiquitination of the rat uterine estrogen receptor: dependence on estradiol. Biochem Biophys Res Commun 213:24-31
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 24-31
    • Nirmala, P.B.1    Thampan, R.V.2
  • 16
    • 0033304776 scopus 로고    scopus 로고
    • Proteasome-mediated proteolysis of estrogen receptor: A novel component in autologous down regulation
    • Alarid ET, Bakopoulos NS, Solodin N 1999 Proteasome-mediated proteolysis of estrogen receptor: a novel component in autologous down regulation. Mol Endocrinol 13:1522-1534
    • (1999) Mol Endocrinol , vol.13 , pp. 1522-1534
    • Alarid, E.T.1    Bakopoulos, N.S.2    Solodin, N.3
  • 17
    • 0033060824 scopus 로고    scopus 로고
    • Implication of proteasome in estrogen receptor degradation
    • El Khissiin A, Leclercq G 1999 Implication of proteasome in estrogen receptor degradation. FEBS Lett 448:160-166
    • (1999) FEBS Lett , vol.448 , pp. 160-166
    • El Khissiin, A.1    Leclercq, G.2
  • 18
    • 0033638393 scopus 로고    scopus 로고
    • The 26S proteasome is required for estrogen receptor α and coactivator turnover and for efficient ER-α transactivation
    • Lonard DM, Nawaz Z, Smith CL, O'Malley BW 2000 The 26S proteasome is required for estrogen receptor α and coactivator turnover and for efficient ER-α transactivation. Mol Cell 5:939-948
    • (2000) Mol Cell , vol.5 , pp. 939-948
    • Lonard, D.M.1    Nawaz, Z.2    Smith, C.L.3    O'Malley, B.W.4
  • 19
    • 0035929585 scopus 로고    scopus 로고
    • The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differently by agonists, antagonists and selective estrogen receptor modulators
    • Wijayaratne AL, McDonnell DP 2001 The human estrogen receptor-α is a ubiquitinated protein whose stability is affected differently by agonists, antagonists and selective estrogen receptor modulators. J Biol Chem 276:35684-35692
    • (2001) J Biol Chem , vol.276 , pp. 35684-35692
    • Wijayaratne, A.L.1    McDonnell, D.P.2
  • 21
    • 0026560435 scopus 로고
    • Antiestrogen ICI164,384 reduces cellular estrogen receptor content by increasing its turnover
    • Dauvois S, Daniellian PS, White R, Parker MG 1992 Antiestrogen ICI164, 384 reduces cellular estrogen receptor content by increasing its turnover. Proc Natl Acad Sci USA 89:4037-4041
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4037-4041
    • Dauvois, S.1    Daniellian, P.S.2    White, R.3    Parker, M.G.4
  • 24
    • 0029877913 scopus 로고    scopus 로고
    • Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation
    • Bunone G, Briand PA, Miksicek RJ, Picard D 1996 Activation of the unliganded estrogen receptor by EGF involves the MAP kinase pathway and direct phosphorylation. EMBO J 15:2174-2183
    • (1996) EMBO J , vol.15 , pp. 2174-2183
    • Bunone, G.1    Briand, P.A.2    Miksicek, R.J.3    Picard, D.4
  • 25
    • 0035971181 scopus 로고    scopus 로고
    • Phosphatidylinositol-3-kinase/AKT-mediated activation of estradiol receptor α. A new model for anti-estrogen resistance
    • Campbell RA, Bhat-Nakshatri P, Patel NM, Constantinidou D, Ali S, Nakshatri H 2001 Phosphatidylinositol-3-kinase/AKT-mediated activation of estradi receptor α. A new model for anti-estrogen resistance. J Biol Chem 276:9817-9824
    • (2001) J Biol Chem , vol.276 , pp. 9817-9824
    • Campbell, R.A.1    Bhat-Nakshatri, P.2    Patel, N.M.3    Constantinidou, D.4    Ali, S.5    Nakshatri, H.6
  • 26
    • 0026317212 scopus 로고
    • Dopaminergic and ligand-independent activation of steroid hormone receptor
    • Power RF, Mani SK, Codina J, Conneely OM, O'Malley BW 1991 Dopaminergic and ligand-independent activation of steroid hormone receptor. Science 254:1636-1639
    • (1991) Science , vol.254 , pp. 1636-1639
    • Power, R.F.1    Mani, S.K.2    Codina, J.3    Conneely, O.M.4    O'Malley, B.W.5
  • 27
    • 0027964862 scopus 로고
    • Estrogen action via the cAmp signaling pathway: Stimulation of adenylate cyclase and cAMP-regulated gene transcription
    • Aronica SM, Kraus WL, Katzenellenbogen BS 1994 Estrogen action via the cAmp signaling pathway: stimulation of adenylate cyclase and cAMP-regulated gene transcription. Proc Natl Acad Sci USA 91:8517-8521
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8517-8521
    • Aronica, S.M.1    Kraus, W.L.2    Katzenellenbogen, B.S.3
  • 30
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at serine-194 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange CA, Shen T, Horwitz KB 2000 Phosphorylation of human progesterone receptors at serine-194 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc Natl Acad Sci USA 97:1032-1037
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 32
    • 0028267222 scopus 로고
    • Anti-proliferative and anti-estrogenic effects of ICI164384 and ICI 182780 in 4-OH-tamoxifen-resistant breast cancer cells
    • Coopman P, Garcia M, Brünner N, Derocq D, Clarke R, Rochefort H 1994 Anti-proliferative and anti-estrogenic effects of ICI164384 and ICI 182780 in 4-OH-tamoxifen-resistant breast cancer cells. Int J Cancer 56:295-300
    • (1994) Int J Cancer , vol.56 , pp. 295-300
    • Coopman, P.1    Garcia, M.2    Brünner, N.3    Derocq, D.4    Clarke, R.5    Rochefort, H.6
  • 36
    • 0024549892 scopus 로고
    • Regulation of estrogen receptor messenger ribonucleic acid and protein levels in human breast cancer cell lines by sex steroid hormones, their antagonists, and growth factors
    • Read LD, Greene GL, Katzenellenbogen BS 1989 Regulation of estrogen receptor messenger ribonucleic acid and protein levels in human breast cancer cell lines by sex steroid hormones, their antagonists, and growth factors. Mol Endocrinol 3:295-304
    • (1989) Mol Endocrinol , vol.3 , pp. 295-304
    • Read, L.D.1    Greene, G.L.2    Katzenellenbogen, B.S.3
  • 37
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomycin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity
    • Meng L, Mohan R, Kwok BHB, Elofsson M, Sin N, Crews CM 1999 Epoxomycin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity. Proc Natl Acad Sci USA 96:10403-10408
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.B.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 38
    • 0025332216 scopus 로고
    • Cell-free interaction of the estrogen receptor with mouse uterine nuclear matrix; evidence of saturability, specificity, and resistance to KCl extraction
    • Metzger DA, Korach KS 1990 Cell-free interaction of the estrogen receptor with mouse uterine nuclear matrix; evidence of saturability, specificity, and resistance to KCl extraction. Endocrinology 126:2190-2195
    • (1990) Endocrinology , vol.126 , pp. 2190-2195
    • Metzger, D.A.1    Korach, K.S.2
  • 39
    • 0032919564 scopus 로고    scopus 로고
    • Direct visualisation of the human estrogen receptor α reveals a role for ligand in the nuclear distribution of the receptor
    • Htun H, Holth LT, Walker D, Davie JR, Hager GL 1999 Direct visualisation of the human estrogen receptor α reveals a role for ligand in the nuclear distribution of the receptor. Mol Biol Cell 10:471-486
    • (1999) Mol Biol Cell , vol.10 , pp. 471-486
    • Htun, H.1    Holth, L.T.2    Walker, D.3    Davie, J.R.4    Hager, G.L.5
  • 41
    • 2642680837 scopus 로고    scopus 로고
    • Partial antagonism between steroidal and nonsteroidal antiestrogens in human breast cancer cell lines
    • Müller V, Jensen EV, Knabbe C 1998 Partial antagonism between steroidal and nonsteroidal antiestrogens in human breast cancer cell lines. Cancer Res 58:263-267
    • (1998) Cancer Res , vol.58 , pp. 263-267
    • Müller, V.1    Jensen, E.V.2    Knabbe, C.3
  • 42
    • 0033824336 scopus 로고    scopus 로고
    • 2 activation is via the MKP-1 down-regulation and ERK activation
    • 2 activation is via the MKP-1 down-regulation and ERK activation. Cell Signal 12:457-461
    • (2000) Cell Signal , vol.12 , pp. 457-461
    • Lin, W.-W.1    Hsu, Y.-W.2
  • 43
    • 0034725927 scopus 로고    scopus 로고
    • Regulation of c-fos gene expression by lipopolysaccharide and cycloheximide in C6 rat glioma cells
    • Kim Y-H, Choi M-R, Song D-K, Huh S-O, Jang C-G, Suh H-W 2000 Regulation of c-fos gene expression by lipopolysaccharide and cycloheximide in C6 rat glioma cells. Brain Res 872:227-230
    • (2000) Brain Res , vol.872 , pp. 227-230
    • Kim, Y.-H.1    Choi, M.-R.2    Song, D.-K.3    Huh, S.-O.4    Jang, C.-G.5    Suh, H.-W.6
  • 45
    • 0034014355 scopus 로고    scopus 로고
    • Inhibition of mitogen-activated protein kinase and phosphatidylinositol 3-kinase activity in MCF-7 cells prevents estrogen-induced mitogenesis
    • Lobenhofer EK, Huper G, Iglehart JD, Marks JR 2000 Inhibition of mitogen-activated protein kinase and phosphatidylinositol 3-kinase activity in MCF-7 cells prevents estrogen-induced mitogenesis. Cell Growth Diff 11:99-110
    • (2000) Cell Growth Diff , vol.11 , pp. 99-110
    • Lobenhofer, E.K.1    Huper, G.2    Iglehart, J.D.3    Marks, J.R.4
  • 49
    • 0025781261 scopus 로고
    • Influence of di-and tri-phenylethylene estrogen/antiestrogen structure on the mechanisms of protein kinase C inhibition and activation as revealed by a multivariate analysis
    • Bignon E, Pons M, Dore JC, Gilbert J, Ojasoo T, Miquel JF, Raynaud JP, Crastes de Paulet A 1991 Influence of di-and tri-phenylethylene estrogen/antiestrogen structure on the mechanisms of protein kinase C inhibition and activation as revealed by a multivariate analysis. Biochem Pharmacol 42:1373-1383
    • (1991) Biochem Pharmacol , vol.42 , pp. 1373-1383
    • Bignon, E.1    Pons, M.2    Dore, J.C.3    Gilbert, J.4    Ojasoo, T.5    Miquel, J.F.6    Raynaud, J.P.7    Crastes De Paulet, A.8
  • 50
    • 0028337218 scopus 로고
    • Stimulation of calcium sequestration by mezerein, a protein kinase C activator, in saponized rabbit platelets
    • Nishio H, Ikegami Y, Segawa, T, Nakata Y 1994 Stimulation of calcium sequestration by mezerein, a protein kinase C activator, in saponized rabbit platelets. Gen Pharmacol 25:413-416
    • (1994) Gen Pharmacol , vol.25 , pp. 413-416
    • Nishio, H.1    Ikegami, Y.2    Segawa, T.3    Nakata, Y.4
  • 51
    • 0035101145 scopus 로고    scopus 로고
    • Cellular and molecular pharmacology of antiestrogen action and resistance
    • Clarke R, Leonessa F, Welch J, Skaar TD 2001 Cellular and molecular pharmacology of antiestrogen action and resistance. Pharmacol Rev 53:25-71
    • (2001) Pharmacol Rev , vol.53 , pp. 25-71
    • Clarke, R.1    Leonessa, F.2    Welch, J.3    Skaar, T.D.4
  • 52
    • 0032230245 scopus 로고    scopus 로고
    • Interaction and dissociation by ligands of estrogen receptor and Hsp90: The antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm
    • Devin-Leclerc J, Meng X, Delahaye F, Leclerc P, Baulieu EE, Catelli MG 1998 Interaction and dissociation by ligands of estrogen receptor and Hsp90: the antiestrogen RU 58668 induces a protein synthesis-dependent clustering of the receptor in the cytoplasm. Mol Endocrinol 12:842-854
    • (1998) Mol Endocrinol , vol.12 , pp. 842-854
    • Devin-Leclerc, J.1    Meng, X.2    Delahaye, F.3    Leclerc, P.4    Baulieu, E.E.5    Catelli, M.G.6
  • 53
    • 0032907106 scopus 로고    scopus 로고
    • The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily
    • Nawaz Z, Lonard D, Smith CL, Lev-Lheman E, Tsai SY, Tsai M-J, O'Malley BW 1999 The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily. Mol Cell Biol 19:1182-1189
    • (1999) Mol Cell Biol , vol.19 , pp. 1182-1189
    • Nawaz, Z.1    Lonard, D.2    Smith, C.L.3    Lev-Lheman, E.4    Tsai, S.Y.5    Tsai, M.-J.6    O'Malley, B.W.7
  • 54
    • 0028890361 scopus 로고
    • Interaction of thyroid hormone receptor with a conserved transcriptional mediator
    • Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD 1995 Interaction of thyroid hormone receptor with a conserved transcriptional mediator. Nature 374:91-94
    • (1995) Nature , vol.374 , pp. 91-94
    • Lee, J.W.1    Ryan, F.2    Swaffield, J.C.3    Johnston, S.A.4    Moore, D.D.5
  • 58
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitinates unfolded protein
    • Murata S, Minami Y, Minami M, Chiba T, Tanaka K 2001 CHIP is a chaperone-dependent E3 ligase that ubiquitinates unfolded protein. EMBO Rep 21:1-6
    • (2001) EMBO Rep , vol.21 , pp. 1-6
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 59
    • 0029918905 scopus 로고    scopus 로고
    • Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA
    • Renz A, Fackelmayer FO 1996 Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA. Nucleic Acids Res 24:843-849
    • (1996) Nucleic Acids Res , vol.24 , pp. 843-849
    • Renz, A.1    Fackelmayer, F.O.2
  • 60
    • 0034463079 scopus 로고    scopus 로고
    • Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation
    • Oesterreich S, Zhang Q, Hopp T, Fuqua SAW, Michaelis M, Zhao HH, Davie J, Osborne CK, Lee AV 2000 Tamoxifen-bound estrogen receptor (ER) strongly interacts with the nuclear matrix protein HET/SAF-B, a novel inhibitor of ER-mediated transactivation. Mol Endocrinol 14: 369-381
    • (2000) Mol Endocrinol , vol.14 , pp. 369-381
    • Oesterreich, S.1    Zhang, Q.2    Hopp, T.3    Fuqua, S.A.W.4    Michaelis, M.5    Zhao, H.H.6    Davie, J.7    Osborne, C.K.8    Lee, A.V.9
  • 63
    • 0037339988 scopus 로고    scopus 로고
    • The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-α and essential for the anti-proliferative activity of ICI 182,780 in ERα-positive breast cancer cells
    • Fan M, Bigsby R, Nephew K P 2003 The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-α and essential for the anti-proliferative activity of ICI 182,780 in ERα-positive breast cancer cells. Mol Endocrinol 17:356-365
    • (2003) Mol Endocrinol , vol.17 , pp. 356-365
    • Fan, M.1    Bigsby, R.2    Nephew, K.P.3
  • 64
    • 0037064199 scopus 로고    scopus 로고
    • Two antiestrogens affect differently chromatin remodeling of trefoil factor 1 (pS2) gene and the fate of estrogen receptor in MCF-7
    • Giamarchi C, Chailleux C, Calligé M, Rochaix P, Trouche D, Richard-Foy H 2002 Two antiestrogens affect differently chromatin remodeling of trefoil factor 1 (pS2) gene and the fate of estrogen receptor in MCF-7. Biochem Biophys Acta 1578:12-20
    • (2002) Biochem Biophys Acta , vol.1578 , pp. 12-20
    • Giamarchi, C.1    Chailleux, C.2    Calligé, M.3    Rochaix, P.4    Trouche, D.5    Richard-Foy, H.6
  • 65
    • 0027996763 scopus 로고
    • Signalling from TPA to MAP kinase requires protein kinase C, raf and MEK: Reconstitution of the signaling pathway in vitro
    • Marquardt B, Fritz D, Stabel S 1994 Signalling from TPA to MAP kinase requires protein kinase C, raf and MEK: reconstitution of the signaling pathway in vitro. Oncogene 9:3213-3218
    • (1994) Oncogene , vol.9 , pp. 3213-3218
    • Marquardt, B.1    Fritz, D.2    Stabel, S.3
  • 67
    • 0034458854 scopus 로고    scopus 로고
    • Regulation of the functional interaction between cyclin D1 and the estrogen receptor
    • Lamb J, Ladha MH, McMahon C, Sutherland RL, Ewen ME 2000 Regulation of the functional interaction between cyclin D1 and the estrogen receptor. Mol Cell Biol 20:8667-8675
    • (2000) Mol Cell Biol , vol.20 , pp. 8667-8675
    • Lamb, J.1    Ladha, M.H.2    McMahon, C.3    Sutherland, R.L.4    Ewen, M.E.5
  • 68
    • 0037036452 scopus 로고    scopus 로고
    • Proteasome inhibitors reduce luciferase and β galactosidase activity in tissue culture cells
    • Deroo BJ, Archer TK 2002 Proteasome inhibitors reduce luciferase and β galactosidase activity in tissue culture cells. J Biol Chem 227:20120-20123
    • (2002) J Biol Chem , vol.227 , pp. 20120-20123
    • Deroo, B.J.1    Archer, T.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.