메뉴 건너뛰기




Volumn 11, Issue 1, 2006, Pages 109-131

Degradation and beyond: Control of androgen receptor activity by the proteasome system

Author keywords

AR; Degradation; Prostate cancer; Proteasome; Transcription; Ubiquitin

Indexed keywords

ANDROGEN RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; GLUCOCORTICOID; GLYCOGEN SYNTHASE KINASE 3BETA; HEAT SHOCK PROTEIN 70; HISTONE DEACETYLASE 1; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; SMALL NUCLEAR RNA; TATA BINDING PROTEIN; UBIQUITIN;

EID: 33749410233     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-006-0011-9     Document Type: Review
Times cited : (38)

References (106)
  • 1
    • 0019855782 scopus 로고
    • The hormonal control of sexual development
    • Wilson, J.D., George, F.W. and Griffin, J.E. The hormonal control of sexual development. Science 211 (1981) 1278-1284.
    • (1981) Science , vol.211 , pp. 1278-1284
    • Wilson, J.D.1    George, F.W.2    Griffin, J.E.3
  • 3
    • 0035930133 scopus 로고    scopus 로고
    • Androgen receptor signaling in androgen-refractory prostate cancer
    • Grossmann, M.E., Huang, H. and Tindall, D.J. Androgen receptor signaling in androgen-refractory prostate cancer. J. Natl. Cancer Inst. 93 (2001) 1687-1697.
    • (2001) J. Natl. Cancer Inst. , vol.93 , pp. 1687-1697
    • Grossmann, M.E.1    Huang, H.2    Tindall, D.J.3
  • 5
    • 85010224879 scopus 로고    scopus 로고
    • www.nursa.org
  • 8
    • 0036208492 scopus 로고    scopus 로고
    • Formation of androgen receptor transcription complex
    • Shang, Y., Myers, M. and Brown, M. Formation of androgen receptor transcription complex. Mol. Cell 9 (2002) 601-610.
    • (2002) Mol. Cell , vol.9 , pp. 601-610
    • Shang, Y.1    Myers, M.2    Brown, M.3
  • 9
    • 29344441929 scopus 로고    scopus 로고
    • Androgens regulate the immune/inflammatory response and cell survival pathways in rat ventral prostate epithelial cells
    • Asirvatham, A.J., Schmidt, M., Gao, B. and Chaudhary, J. Androgens regulate the immune/inflammatory response and cell survival pathways in rat ventral prostate epithelial cells. Endocrinology 147 (2006) 257-271.
    • (2006) Endocrinology , vol.147 , pp. 257-271
    • Asirvatham, A.J.1    Schmidt, M.2    Gao, B.3    Chaudhary, J.4
  • 10
    • 24744471465 scopus 로고    scopus 로고
    • Regulation of androgen receptor levels: Implications for prostate cancer progression and therapy
    • Burnstein, K.L. Regulation of androgen receptor levels: Implications for prostate cancer progression and therapy. J. Cell. Biochem. 95 (2005) 657-669.
    • (2005) J. Cell. Biochem. , vol.95 , pp. 657-669
    • Burnstein, K.L.1
  • 12
    • 0036219918 scopus 로고    scopus 로고
    • Androgen receptor (AR) coregulators: An overview
    • Heinlein, C.A. and Chang, C. Androgen receptor (AR) coregulators: an overview. Endocr. Rev. 23 (2002) 175-200.
    • (2002) Endocr. Rev. , vol.23 , pp. 175-200
    • Heinlein, C.A.1    Chang, C.2
  • 13
    • 1442351143 scopus 로고    scopus 로고
    • Coregulator function: A key to understanding tissue specificity of selective receptor modulators
    • Smith, C.L. and O'Malley, B.W. Coregulator function: a key to understanding tissue specificity of selective receptor modulators. Endocr. Rev. 25 (2004) 45-71.
    • (2004) Endocr. Rev. , vol.25 , pp. 45-71
    • Smith, C.L.1    O'Malley, B.W.2
  • 14
    • 0034675275 scopus 로고    scopus 로고
    • Inhibiting proteasomes in human HepG2 and LNCaP cells increases endogenous androgen receptor levels
    • Sheflin, L., Keegan, B., Zhang, W. and Spaulding, S.W. Inhibiting proteasomes in human HepG2 and LNCaP cells increases endogenous androgen receptor levels. Biochem. Biophys. Res. Commun. 276 (2000) 144-150.
    • (2000) Biochem. Biophys. Res. Commun. , vol.276 , pp. 144-150
    • Sheflin, L.1    Keegan, B.2    Zhang, W.3    Spaulding, S.W.4
  • 15
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart, C.M. Mechanisms underlying ubiquitination. Annu. Rev. Biochem. 70 (2001) 503-533.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 16
  • 17
    • 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.M., Smith, C.L., Lev-Lehman, E., Tsai, S.Y., Tsai, M.J. and O'Malley B.W. The Angelman syndrome-associated protein, E6-AP, is a coactivator for the nuclear hormone receptor superfamily. Mol. Cell. Biol. 19 (1999) 1182-1189.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1182-1189
    • Nawaz, Z.1    Lonard, D.M.2    Smith, C.L.3    Lev-Lehman, E.4    Tsai, S.Y.5    Tsai, M.J.6    O'Malley, B.W.7
  • 18
    • 0036135671 scopus 로고    scopus 로고
    • Genetic ablation of the steroid receptor coactivator-ubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction
    • Smith, C.L., DeVera, D.G., Lamb, D.J., Nawaz, Z., Jiang, Y.H., Beaudet, A.L. and O'Malley, B.W. Genetic ablation of the steroid receptor coactivator-ubiquitin ligase, E6-AP, results in tissue-selective steroid hormone resistance and defects in reproduction. Mol. Cell. Biol. 22 (2002) 525-535.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 525-535
    • Smith, C.L.1    DeVera, D.G.2    Lamb, D.J.3    Nawaz, Z.4    Jiang, Y.H.5    Beaudet, A.L.6    O'Malley, B.W.7
  • 19
    • 4544294361 scopus 로고    scopus 로고
    • The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors
    • Verma, S., Ismail, A., Gao, X., Fu, G., Li, X., O'Malley, B.W. and Nawaz, Z. The ubiquitin-conjugating enzyme UBCH7 acts as a coactivator for steroid hormone receptors. Mol. Cell. Biol. 24 (2004) 8716-8726.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8716-8726
    • Verma, S.1    Ismail, A.2    Gao, X.3    Fu, G.4    Li, X.5    O'Malley, B.W.6    Nawaz, Z.7
  • 21
    • 0033605597 scopus 로고    scopus 로고
    • Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor
    • Kang, H.Y., Yeh, S., Fujimoto, N. and Chang, C. Cloning and characterization of human prostate coactivator ARA54, a novel protein that associates with the androgen receptor. J. Biol. Chem. 274 (1999) 8570-8576.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8570-8576
    • Kang, H.Y.1    Yeh, S.2    Fujimoto, N.3    Chang, C.4
  • 22
    • 0034850268 scopus 로고    scopus 로고
    • N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8
    • Ito, K., Adachi, S., Iwakami, R., Yasuda, H., Muto, Y., Seki, N. and Okano, Y. N-Terminally extended human ubiquitin-conjugating enzymes (E2s) mediate the ubiquitination of RING-finger proteins, ARA54 and RNF8. Eur. J. Biochem. 268 (2001) 2725-2732.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2725-2732
    • Ito, K.1    Adachi, S.2    Iwakami, R.3    Yasuda, H.4    Muto, Y.5    Seki, N.6    Okano, Y.7
  • 23
    • 0036683093 scopus 로고    scopus 로고
    • Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase
    • Lin, H.K., Wang, L., Hu, Y.C., Altuwaijri, S. and Chang, C. Phosphorylation-dependent ubiquitylation and degradation of androgen receptor by Akt require Mdm2 E3 ligase. EMBO J. 21 (2002) 4037-4048.
    • (2002) EMBO J. , vol.21 , pp. 4037-4048
    • Lin, H.K.1    Wang, L.2    Hu, Y.C.3    Altuwaijri, S.4    Chang, C.5
  • 24
    • 0033525191 scopus 로고    scopus 로고
    • A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins
    • Moilanen, A.M., Karvonen, U., Poukka, H., Yan, W., Toppari, J., Jänne, O.A. and Palvimo, J.J. A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins. J. Biol. Chem. 274 (1999) 3700-3704.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3700-3704
    • Moilanen, A.M.1    Karvonen, U.2    Poukka, H.3    Yan, W.4    Toppari, J.5    Jänne, O.A.6    Palvimo, J.J.7
  • 25
    • 0033516662 scopus 로고    scopus 로고
    • Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription
    • Poukka, H., Aarnisalo, P., Karvonen, U., Palvimo, J.J. and Jänne, O.A. Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. J. Biol. Chem. 274 (1999) 19441-19446.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19441-19446
    • Poukka, H.1    Aarnisalo, P.2    Karvonen, U.3    Palvimo, J.J.4    Jänne, O.A.5
  • 26
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • Poukka, H., Karvonen, U., Jänne, O.A. and Palvimo, J.J. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. USA 97 (2000) 14145-14150.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Jänne, O.A.3    Palvimo, J.J.4
  • 27
    • 0036826887 scopus 로고    scopus 로고
    • PIAS1 and PIASxa function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription
    • Nishida, T. and Yasuda, H. PIAS1 and PIASxa function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. J. Biol. Chem. 277 (2002) 41311-41317.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41311-41317
    • Nishida, T.1    Yasuda, H.2
  • 28
    • 0031812159 scopus 로고    scopus 로고
    • Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription
    • Moilanen, A.M., Poukka, H., Karvonen, U., Häkli, M., Jänne, O.A. and Palvimo, J.J. Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol. Cell. Biol. 18 (1998) 5128-3519.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5128-13519
    • Moilanen, A.M.1    Poukka, H.2    Karvonen, U.3    Häkli, M.4    Jänne, O.A.5    Palvimo, J.J.6
  • 29
    • 0033829607 scopus 로고    scopus 로고
    • The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor
    • Poukka, H., Karvonen, U., Yoshikawa, N., Tanaka, H., Palvimo, J.J. and Jänne, O.A. The RING finger protein SNURF modulates nuclear trafficking of the androgen receptor. J. Cell. Sci. 113 (2000) 2991-3001.
    • (2000) J. Cell. Sci. , vol.113 , pp. 2991-3001
    • Poukka, H.1    Karvonen, U.2    Yoshikawa, N.3    Tanaka, H.4    Palvimo, J.J.5    Jänne, O.A.6
  • 30
    • 1342265499 scopus 로고    scopus 로고
    • Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity
    • Häkli, M., Lorick, K.L., Weissman, A.M., Jänne, O.A. and Palvimo, J.J. Transcriptional coregulator SNURF (RNF4) possesses ubiquitin E3 ligase activity. FEBS Letters 560 (2004) 56-62.
    • (2004) FEBS Letters , vol.560 , pp. 56-62
    • Häkli, M.1    Lorick, K.L.2    Weissman, A.M.3    Jänne, O.A.4    Palvimo, J.J.5
  • 31
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • Murata, S., Minami, Y., Minami, M., Chiba, T. and Tanaka, K. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein. EMBO Rep. 2 (2001) 1133-1138.
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 33
    • 3142672066 scopus 로고    scopus 로고
    • An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP)
    • He, B., Bai, S., Hnat, A.T., Kalman, R.I., Minges, J.T., Patterson, C. and Wilson, E.M. An androgen receptor NH2-terminal conserved motif interacts with the COOH terminus of the Hsp70-interacting protein (CHIP). J. Biol. Chem. 279 (2004) 30643-30653.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30643-30653
    • He, B.1    Bai, S.2    Hnat, A.T.3    Kalman, R.I.4    Minges, J.T.5    Patterson, C.6    Wilson, E.M.7
  • 34
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers, S.W. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21 (1996) 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 35
    • 9644300915 scopus 로고    scopus 로고
    • The proteasome: A proteolytic nanomachine of cell regulation and waste disposal
    • Wolf, D.H. and Hilt, W. The proteasome: a proteolytic nanomachine of cell regulation and waste disposal. Biochim. Biophys. Acta 1695 (2004) 19-31.
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 19-31
    • Wolf, D.H.1    Hilt, W.2
  • 36
    • 5044229903 scopus 로고    scopus 로고
    • Regulation of androgen receptor signaling by PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor through distinct mechanisms in prostate cancer cells
    • Lin, H.K., Hu, Y.C., Lee, D.K. and Chang, C. Regulation of androgen receptor signaling by PTEN (phosphatase and tensin homolog deleted on chromosome 10) tumor suppressor through distinct mechanisms in prostate cancer cells. Mol. Endocrinol. 18 (2004) 2409-2423.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2409-2423
    • Lin, H.K.1    Hu, Y.C.2    Lee, D.K.3    Chang, C.4
  • 37
    • 0037564511 scopus 로고    scopus 로고
    • Interleukin-6 differentially regulates androgen receptor transactivation via PI3K-Akt, STAT3, and MAPK, three distinct signal pathways in prostate cancer cells
    • Yang, L., Wang, L., Lin, H.K., Kan, P.Y., Xie, S., Tsai, M.Y., Wang, P.H., Chen, Y.T. and Chang, C. Interleukin-6 differentially regulates androgen receptor transactivation via PI3K-Akt, STAT3, and MAPK, three distinct signal pathways in prostate cancer cells. Biochem. Biophys. Res. Commun. 305 (2003) 462-469.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 462-469
    • Yang, L.1    Wang, L.2    Lin, H.K.3    Kan, P.Y.4    Xie, S.5    Tsai, M.Y.6    Wang, P.H.7    Chen, Y.T.8    Chang, C.9
  • 38
  • 39
    • 0035912833 scopus 로고    scopus 로고
    • Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor
    • Lin, H.K., Yeh, S., Kang, H.Y. and Chang, C. Akt suppresses androgen-induced apoptosis by phosphorylating and inhibiting androgen receptor. Proc. Natl. Acad. Sci. USA 98 (2001) 7200-7205.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7200-7205
    • Lin, H.K.1    Yeh, S.2    Kang, H.Y.3    Chang, C.4
  • 41
    • 0347696003 scopus 로고    scopus 로고
    • Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers
    • Lin, H.K., Hu, Y.C., Yang, L., Altuwaijri, S., Chen, Y.T., Kang, H.Y. and Chang, C. Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers. J. Biol. Chem. 278 (2003) 50902-50907.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50902-50907
    • Lin, H.K.1    Hu, Y.C.2    Yang, L.3    Altuwaijri, S.4    Chen, Y.T.5    Kang, H.Y.6    Chang, C.7
  • 42
    • 0034671668 scopus 로고    scopus 로고
    • HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway
    • Wen, Y., Hu, M.C., Makino, K., Spohn, B., Bartholomeusz, G., Yan, D.H. and Hung, M.C. HER-2/neu promotes androgen-independent survival and growth of prostate cancer cells through the Akt pathway. Cancer Res. 60 (2000) 6841-6845.
    • (2000) Cancer Res. , vol.60 , pp. 6841-6845
    • Wen, Y.1    Hu, M.C.2    Makino, K.3    Spohn, B.4    Bartholomeusz, G.5    Yan, D.H.6    Hung, M.C.7
  • 44
    • 2542472390 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta activity is required for androgen-stimulated gene expression in prostate cancer
    • Liao, X., Thrasher, J.B., Holzbeierlein, J., Stanley, S. and Li, B. Glycogen synthase kinase-3beta activity is required for androgen-stimulated gene expression in prostate cancer. Endocrinology 145 (2004) 2941-2949.
    • (2004) Endocrinology , vol.145 , pp. 2941-2949
    • Liao, X.1    Thrasher, J.B.2    Holzbeierlein, J.3    Stanley, S.4    Li, B.5
  • 46
    • 4143114765 scopus 로고    scopus 로고
    • Acetylation of nuclear receptors in cellular growth and apoptosis
    • Fu, M., Wang, C., Zhang, X. and Pestell, R.G. Acetylation of nuclear receptors in cellular growth and apoptosis. Biochem. Pharmacol. 68 (2004) 1199-1208.
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1199-1208
    • Fu, M.1    Wang, C.2    Zhang, X.3    Pestell, R.G.4
  • 48
    • 0019816203 scopus 로고
    • Regulation of glucocorticoid receptors by glucocorticoids in cultured HeLa S3 cells
    • Cidlowski, J.A. and Cidlowski, N.B. Regulation of glucocorticoid receptors by glucocorticoids in cultured HeLa S3 cells. Endocrinology 109 (1981) 1975-1982.
    • (1981) Endocrinology , vol.109 , pp. 1975-1982
    • Cidlowski, J.A.1    Cidlowski, N.B.2
  • 50
    • 0033592948 scopus 로고    scopus 로고
    • Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins
    • Zhu, J., Gianni, M., Kopf, E., Honore, N., Chelbi-Alix, M., Koken, M., Quignon, F., Rochette-Egly, C. and de The, H. Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins. Proc. Natl. Acad. Sci. USA 96 (1999) 14807-14812.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14807-14812
    • Zhu, J.1    Gianni, M.2    Kopf, E.3    Honore, N.4    Chelbi-Alix, M.5    Koken, M.6    Quignon, F.7    Rochette-Egly, C.8    De The, H.9
  • 51
    • 0033967491 scopus 로고    scopus 로고
    • Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome
    • Lange, C.A., Shen, T. and Horwitz, K.B. Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26S proteasome. Proc. Natl. Acad. Sci. USA 97 (2000) 1032-1037.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1032-1037
    • Lange, C.A.1    Shen, T.2    Horwitz, K.B.3
  • 53
    • 13744257306 scopus 로고    scopus 로고
    • Regulation of androgen receptor and histone deacatylase 1 by Mdm2-mediated ubiquitylation
    • Gaughan, L., Logan, I.R., Neal, D.E. and Robson, C.N. Regulation of androgen receptor and histone deacatylase 1 by Mdm2-mediated ubiquitylation. Nucleic Acids Res. 33 (2005) 13-26.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 13-26
    • Gaughan, L.1    Logan, I.R.2    Neal, D.E.3    Robson, C.N.4
  • 54
    • 0034465595 scopus 로고    scopus 로고
    • Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells
    • Tyagi, R.K., Lavrovsky, Y., Ahn, S.C., Song, C.S., Chatterjee, B. and Roy, A.K. Dynamics of intracellular movement and nucleocytoplasmic recycling of the ligand-activated androgen receptor in living cells. Mol. Endocrinol. 14 (2000) 1162-1174.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 1162-1174
    • Tyagi, R.K.1    Lavrovsky, Y.2    Ahn, S.C.3    Song, C.S.4    Chatterjee, B.5    Roy, A.K.6
  • 55
    • 0001548433 scopus 로고    scopus 로고
    • Two androgen response elements in the androgen receptor coding region are required for cell-specific up-regulation of receptor messenger RNA
    • Dai, J.L. and Burnstein, K.L. Two androgen response elements in the androgen receptor coding region are required for cell-specific up-regulation of receptor messenger RNA. Mol. Endocrinol. 10 (1996) 1582-1594.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1582-1594
    • Dai, J.L.1    Burnstein, K.L.2
  • 56
    • 1842531004 scopus 로고    scopus 로고
    • Transient, ligand-dependent arrest of the androgen receptor in subnuclear foci alters phosphorylation and coactivator interactions
    • Black, B.E., Vitto, M.J., Gioeli, D., Spencer, A., Afshar, N., Conaway, M.R., Weber, M.J. and Paschal, B.M. Transient, ligand-dependent arrest of the androgen receptor in subnuclear foci alters phosphorylation and coactivator interactions. Mol. Endocrinol. 18 (2004) 834-850.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 834-850
    • Black, B.E.1    Vitto, M.J.2    Gioeli, D.3    Spencer, A.4    Afshar, N.5    Conaway, M.R.6    Weber, M.J.7    Paschal, B.M.8
  • 57
    • 17844365062 scopus 로고    scopus 로고
    • Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors
    • Kinyamu, H.K., Chen, J. and Archer, T.K. Linking the ubiquitin-proteasome pathway to chromatin remodeling/modification by nuclear receptors. J. Mol. Endocrinol. 34 (2005) 281-297.
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 281-297
    • Kinyamu, H.K.1    Chen, J.2    Archer, T.K.3
  • 58
    • 8344272750 scopus 로고    scopus 로고
    • Coregulator recruitment and histone modifications in transcriptional regulation by the androgen receptor
    • Kang, Z., Jänne, O.A. and Palvimo, J.J. Coregulator recruitment and histone modifications in transcriptional regulation by the androgen receptor. Mol. Endocrinol. 18 (2004) 2633-2648.
    • (2004) Mol. Endocrinol. , vol.18 , pp. 2633-2648
    • Kang, Z.1    Jänne, O.A.2    Palvimo, J.J.3
  • 59
    • 0034617058 scopus 로고    scopus 로고
    • p300 and p300/cAMP response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation
    • Fu, M., Wang, C., Reutens, A.T., Wang, J., Angeletti, R.H., Siconolfi-Baez, L., Ogryzko, V., Avantaggiati, M.L. and Pestell, R.G. p300 and p300/cAMP response element-binding protein-associated factor acetylate the androgen receptor at sites governing hormone-dependent transactivation. J. Biol. Chem. 275 (2000) 20853-20860.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20853-20860
    • Fu, M.1    Wang, C.2    Reutens, A.T.3    Wang, J.4    Angeletti, R.H.5    Siconolfi-Baez, L.6    Ogryzko, V.7    Avantaggiati, M.L.8    Pestell, R.G.9
  • 60
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat, S., Bauer, U.M., Shah, V., Turner, B., Berger, S. and Kouzarides, T. Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr. Biol. 12 (2002) 2090-2097.
    • (2002) Curr. Biol. , vol.12 , pp. 2090-2097
    • Daujat, S.1    Bauer, U.M.2    Shah, V.3    Turner, B.4    Berger, S.5    Kouzarides, T.6
  • 61
    • 0041902737 scopus 로고    scopus 로고
    • Differential requirement of SWI/SNF for androgen receptor activity
    • Marshall, T.W., Link, K.A., Petre-Draviam, C.E. and Knudsen, K.E. Differential requirement of SWI/SNF for androgen receptor activity. J. Biol. Chem. 278 (2003) 30605-30613.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30605-30613
    • Marshall, T.W.1    Link, K.A.2    Petre-Draviam, C.E.3    Knudsen, K.E.4
  • 62
    • 0037044767 scopus 로고    scopus 로고
    • A coregulatory role for the TRAP-Mediator complex in androgen receptor-mediated gene expression
    • Wang, Q., Sharma, D., Ren, Y. and Fondell, J.D. A coregulatory role for the TRAP-Mediator complex in androgen receptor-mediated gene expression. J. Biol. Chem. 277 (2002) 42852-42858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42852-42858
    • Wang, Q.1    Sharma, D.2    Ren, Y.3    Fondell, J.D.4
  • 63
    • 0038558164 scopus 로고    scopus 로고
    • A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription
    • Huang, Z.Q., Li, J., Sachs, L.M., Cole, P.A. and Wong, J. A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription. EMBO J. 22 (2003) 2146-2155.
    • (2003) EMBO J. , vol.22 , pp. 2146-2155
    • Huang, Z.Q.1    Li, J.2    Sachs, L.M.3    Cole, P.A.4    Wong, J.5
  • 64
    • 0037229956 scopus 로고    scopus 로고
    • Molecular communication between androgen receptor and general transcription machinery
    • Lee, D.K. and Chang, C. Molecular communication between androgen receptor and general transcription machinery. J. Steroid Biochem. Mol. Biol. 84 (2003) 41-49.
    • (2003) J. Steroid Biochem. Mol. Biol. , vol.84 , pp. 41-49
    • Lee, D.K.1    Chang, C.2
  • 65
    • 1542328272 scopus 로고    scopus 로고
    • The RNA polymerase II transcription cycle: Cycling through chromatin
    • Svejstrup, J.Q. The RNA polymerase II transcription cycle: cycling through chromatin. Biochim. Biophys. Acta 1677 (2004) 64-73.
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 64-73
    • Svejstrup, J.Q.1
  • 66
    • 0037073728 scopus 로고    scopus 로고
    • Involvement of proteasome in the dynamic assembley of the androgen receptor transcription complex
    • Kang, Z., Pirskanen, A., Jänne, O.A. and Palvimo, J.J. Involvement of proteasome in the dynamic assembley of the androgen receptor transcription complex. J. Biol. Chem. 277 (2002) 48366-48371.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48366-48371
    • Kang, Z.1    Pirskanen, A.2    Jänne, O.A.3    Palvimo, J.J.4
  • 68
    • 18044366572 scopus 로고    scopus 로고
    • Rush hour at the promoter: How the ubiquitin-proteasome pathway polices the traffic flow of nuclear receptor-dependent transcription
    • Dennis, A.P. and O'Malley, B.W. Rush hour at the promoter: how the ubiquitin-proteasome pathway polices the traffic flow of nuclear receptor-dependent transcription. J. Steroid Biochem. Mol. Biol. 93 (2005) 139-151.
    • (2005) J. Steroid Biochem. Mol. Biol. , vol.93 , pp. 139-151
    • Dennis, A.P.1    O'Malley, B.W.2
  • 69
    • 0037184121 scopus 로고    scopus 로고
    • Proteasome activity is required for androgen receptor transcriptional activity via regulation of androgen receptor nuclear translocation and interaction with coregulators in prostate cancer cells
    • Lin, H.K., Altuwaijri, S., Lin, W.J., Kan, P.Y., Collins, L.L. and Chang, C. Proteasome activity is required for androgen receptor transcriptional activity via regulation of androgen receptor nuclear translocation and interaction with coregulators in prostate cancer cells. J. Biol. Chem. 277 (2002) 36570-36576.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36570-36576
    • Lin, H.K.1    Altuwaijri, S.2    Lin, W.J.3    Kan, P.Y.4    Collins, L.L.5    Chang, C.6
  • 70
    • 0032711876 scopus 로고    scopus 로고
    • Multiple mammalian proteasomal ATPases, but not proteasome itself, are associated with TATA-binding protein and a novel transcriptional activator, TIP120
    • Makino, Y., Yoshida, T., Yogosawa, S., Tanaka, K., Muramatsu, M. and Tamura, T. Multiple mammalian proteasomal ATPases, but not proteasome itself, are associated with TATA-binding protein and a novel transcriptional activator, TIP120. Genes Cells 4 (1999) 529-539.
    • (1999) Genes Cells , vol.4 , pp. 529-539
    • Makino, Y.1    Yoshida, T.2    Yogosawa, S.3    Tanaka, K.4    Muramatsu, M.5    Tamura, T.6
  • 71
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez, F., Delahodde, A., Kodadek, T. and Johnston, S.A. Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296 (2002) 548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 72
    • 0037159223 scopus 로고    scopus 로고
    • A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II
    • Ferdous, A., Kodadek, T. and Johnston, S.A. A nonproteolytic function of the 19S regulatory subunit of the 26S proteasome is required for efficient activated transcription by human RNA polymerase II. Biochemistry 41 (2002) 12798-12805.
    • (2002) Biochemistry , vol.41 , pp. 12798-12805
    • Ferdous, A.1    Kodadek, T.2    Johnston, S.A.3
  • 73
    • 0012316186 scopus 로고    scopus 로고
    • Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1
    • vom Baur, E., Zechel, C., Heery, D., Heine, M.J., Garnier, J.M., Vivat, V., Le Douarin, B., Gronemeyer, H., Chambon, P. and Losson, R. Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. EMBO J. 15 (1996) 110-124.
    • (1996) EMBO J. , vol.15 , pp. 110-124
    • Vom Baur, E.1    Zechel, C.2    Heery, D.3    Heine, M.J.4    Garnier, J.M.5    Vivat, V.6    Le Douarin, B.7    Gronemeyer, H.8    Chambon, P.9    Losson, R.10
  • 74
    • 1842866995 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 down-regulates prostate-specific antigen (PSA) and induces growth arrest and apoptosis of androgen-dependent human prostate cancer LNCaP cells
    • Ikezoe, T., Yang, Y., Saito, T., Koeffler, H.P. and Taguchi, H. Proteasome inhibitor PS-341 down-regulates prostate-specific antigen (PSA) and induces growth arrest and apoptosis of androgen-dependent human prostate cancer LNCaP cells. Cancer Sci. 95 (2004) 271-275.
    • (2004) Cancer Sci. , vol.95 , pp. 271-275
    • Ikezoe, T.1    Yang, Y.2    Saito, T.3    Koeffler, H.P.4    Taguchi, H.5
  • 75
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • Sun, L. and Chen, Z.J. The novel functions of ubiquitination in signaling. Curr. Opin. Cell Biol. 16 (2004) 119-126.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chen, Z.J.2
  • 76
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • Salghetti, S.E., Caudy, A.A., Chenoweth, J.G. and Tansey, W.P. Regulation of transcriptional activation domain function by ubiquitin. Science 293 (2001) 1651-1653.
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 77
    • 2342432455 scopus 로고    scopus 로고
    • TSG101 interacts with apoptosis-antagonizing transcription factor and enhances androgen receptor-mediated transcription by promoting its monoubiquitination
    • Burgdorf, S., Leister, P. and Scheidtmann, K.H. TSG101 interacts with apoptosis-antagonizing transcription factor and enhances androgen receptor-mediated transcription by promoting its monoubiquitination. J. Biol. Chem. 279 (2004) 17524-17534
    • (2004) J. Biol. Chem. , vol.279 , pp. 17524-17534
    • Burgdorf, S.1    Leister, P.2    Scheidtmann, K.H.3
  • 78
    • 0037123605 scopus 로고    scopus 로고
    • Emerging roles of ubiquitin in transcriptional regulation
    • Conaway, R.C., Brower, C.S. and Conaway, J.W. Emerging roles of ubiquitin in transcriptional regulation. Science 296 (2002) 1254-1258.
    • (2002) Science , vol.296 , pp. 1254-1258
    • Conaway, R.C.1    Brower, C.S.2    Conaway, J.W.3
  • 79
    • 0034730745 scopus 로고    scopus 로고
    • II250, a mediator of activation of gene expression in Drosophila
    • II250, a mediator of activation of gene expression in Drosophila. Science 289 (2000) 2357-2360.
    • (2000) Science , vol.289 , pp. 2357-2360
    • Pham, A.D.1    Sauer, F.2
  • 81
    • 15744388262 scopus 로고    scopus 로고
    • Stabilisation of the unliganded glucocorticoid receptor by TSG101
    • Ismaili, N., Blind, R. and Garabedian, M.J. Stabilisation of the unliganded glucocorticoid receptor by TSG101. J. Biol. Chem. 280 (2005) 11120-11126.
    • (2005) J. Biol. Chem. , vol.280 , pp. 11120-11126
    • Ismaili, N.1    Blind, R.2    Garabedian, M.J.3
  • 82
    • 15044349502 scopus 로고    scopus 로고
    • The hinge region of the androgen receptor plays a role in proteasome-mediated transcriptional activation
    • Tanner, T., Claessens, F. and Haelens, A. The hinge region of the androgen receptor plays a role in proteasome-mediated transcriptional activation. Ann. NY Acad. Sci. 1030 (2004) 587-592.
    • (2004) Ann. NY Acad. Sci. , vol.1030 , pp. 587-592
    • Tanner, T.1    Claessens, F.2    Haelens, A.3
  • 83
    • 1542319221 scopus 로고    scopus 로고
    • Androgen receptor acetylation site mutations cause trafficking defects, misfolding and aggregation similar to expanded glutamine tracts
    • Thomas, M., Dadgar, N., Aphale, A., Harrell, J.M., Kunkel, R., Pratt, W.B. and Lieberman, A.P. Androgen receptor acetylation site mutations cause trafficking defects, misfolding and aggregation similar to expanded glutamine tracts. J. Biol. Chem. 279 (2004) 8389-8395.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8389-8395
    • Thomas, M.1    Dadgar, N.2    Aphale, A.3    Harrell, J.M.4    Kunkel, R.5    Pratt, W.B.6    Lieberman, A.P.7
  • 84
    • 0029041681 scopus 로고
    • Identification of three proline-directed phosphorylation sites in the human androgen receptor
    • Zhou, Z.X., Kemppainen, J.A. and Wilson, E.M. Identification of three proline-directed phosphorylation sites in the human androgen receptor. Mol. Endocrinol. 9 (1995) 605-615.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 605-615
    • Zhou, Z.X.1    Kemppainen, J.A.2    Wilson, E.M.3
  • 87
    • 1342264315 scopus 로고    scopus 로고
    • A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors
    • Perissi, V., Aggarwal, A., Glass, C.K., Rose, D.W. and Rosenfeld, M.G. A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell 116 (2004) 511-526.
    • (2004) Cell , vol.116 , pp. 511-526
    • Perissi, V.1    Aggarwal, A.2    Glass, C.K.3    Rose, D.W.4    Rosenfeld, M.G.5
  • 88
    • 0032526024 scopus 로고    scopus 로고
    • Proteasomal regulation of nuclear receptor corepressor-mediated repression
    • Zhang, J., Guenther, M.G., Carthew, R.W. and Lazar, M.A. Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev. 12 (1998) 1775-1780.
    • (1998) Genes Dev. , vol.12 , pp. 1775-1780
    • Zhang, J.1    Guenther, M.G.2    Carthew, R.W.3    Lazar, M.A.4
  • 89
    • 15444368956 scopus 로고    scopus 로고
    • Decreased expression of E6-associated protein in breast and prostate carcinomas
    • Gao, X., Mohsin, S.K., Gatalica, Z., Fu, G., Sharma, P. and Nawaz, Z. Decreased expression of E6-associated protein in breast and prostate carcinomas. Endocrinology 146 (2005) 1707-1712.
    • (2005) Endocrinology , vol.146 , pp. 1707-1712
    • Gao, X.1    Mohsin, S.K.2    Gatalica, Z.3    Fu, G.4    Sharma, P.5    Nawaz, Z.6
  • 91
    • 0032945938 scopus 로고    scopus 로고
    • Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone
    • Stenoien, D.L., Cummings, C.J., Adams, H.P., Mancini, M.G., Patel, K., DeMartino, G.N., Marcelli, M., Weigel, N.L. and Mancini, M.A. Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperone. Hum. Mol. Genet. 8 (1999) 731-741.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 731-741
    • Stenoien, D.L.1    Cummings, C.J.2    Adams, H.P.3    Mancini, M.G.4    Patel, K.5    DeMartino, G.N.6    Marcelli, M.7    Weigel, N.L.8    Mancini, M.A.9
  • 92
    • 0037339988 scopus 로고    scopus 로고
    • The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-alpha and essential for the antiproliferative activity of ICI 182,780 in ERalpha-positive breast cancer cells
    • Fan, M., Bigsby, R.M. and Nephew, K.P. The NEDD8 pathway is required for proteasome-mediated degradation of human estrogen receptor (ER)-alpha and essential for the antiproliferative activity of ICI 182,780 in ERalpha-positive breast cancer cells. Mol. Endocrinol. 17 (2003) 356-365.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 356-365
    • Fan, M.1    Bigsby, R.M.2    Nephew, K.P.3
  • 93
    • 0032999345 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase kinase 1 activates androgen receptor-dependent transcription and apoptosis in prostate cancer
    • Abreu-Martin, M.T., Chari, A., Palladino, A.A., Craft, N.A. and Sawyers, C.L. Mitogen-activated protein kinase kinase kinase 1 activates androgen receptor-dependent transcription and apoptosis in prostate cancer. Mol. Cell. Biol. 19 (1999) 5143-5154.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5143-5154
    • Abreu-Martin, M.T.1    Chari, A.2    Palladino, A.A.3    Craft, N.A.4    Sawyers, C.L.5
  • 94
    • 0033545848 scopus 로고    scopus 로고
    • From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells
    • Yeh, S., Lin, H.K., Kang, H.Y., Thin, T.H., Lin, M.F. and Chang, C. From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc. Natl. Acad. Sci. USA 96 (1999) 5458-5463.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5458-5463
    • Yeh, S.1    Lin, H.K.2    Kang, H.Y.3    Thin, T.H.4    Lin, M.F.5    Chang, C.6
  • 95
    • 0032530494 scopus 로고    scopus 로고
    • Phorbol ester causes ligand-independent activation of the androgen receptor
    • Darne, C., Veyssiere, G. and Jean, C. Phorbol ester causes ligand-independent activation of the androgen receptor. Eur. J. Biochem. 256 (1998) 541-549.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 541-549
    • Darne, C.1    Veyssiere, G.2    Jean, C.3
  • 96
    • 0029814415 scopus 로고    scopus 로고
    • Activation of the human androgen receptor through a protein kinase a signaling pathway
    • Nazareth, L.V. and Weigel, N.L. Activation of the human androgen receptor through a protein kinase A signaling pathway. J. Biol. Chem. 271 (1996) 19900-19907.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19900-19907
    • Nazareth, L.V.1    Weigel, N.L.2
  • 98
    • 0030333504 scopus 로고    scopus 로고
    • Androgen receptor gene amplification: A novel molecular mechanism for endocrine therapy resistance in human prostate cancer
    • Koivisto, P., Visakorpi, T. and Kallioniemi, O.P. Androgen receptor gene amplification: a novel molecular mechanism for endocrine therapy resistance in human prostate cancer. Scand. J. Clin. Lab. Invest. Suppl. 226 (1996) 57-63.
    • (1996) Scand. J. Clin. Lab. Invest. Suppl. , vol.226 , pp. 57-63
    • Koivisto, P.1    Visakorpi, T.2    Kallioniemi, O.P.3
  • 100
    • 0025347279 scopus 로고
    • Unusual specificity of the androgen receptor in the human prostate tumor cell line LNCaP: High affinity for progestagenic and estrogenic steroids
    • Veldscholte, J., Voorhorst-Ogink, M.M., Bolt-de Vries, J., van Rooij, H.C., Trapman, J. and Mulder, E. Unusual specificity of the androgen receptor in the human prostate tumor cell line LNCaP: high affinity for progestagenic and estrogenic steroids. Biochim. Biophys. Acta 1052 (1990) 187-194.
    • (1990) Biochim. Biophys. Acta , vol.1052 , pp. 187-194
    • Veldscholte, J.1    Voorhorst-Ogink, M.M.2    Bolt-de Vries, J.3    Van Rooij, H.C.4    Trapman, J.5    Mulder, E.6
  • 101
    • 16844386205 scopus 로고    scopus 로고
    • Emodin down-regulates androgen receptor and inhibits prostate cancer cell growth
    • Cha, T.L., Qiu, L., Chen, C.T., Wen, Y. and Hung, M.C. Emodin down-regulates androgen receptor and inhibits prostate cancer cell growth. Cancer Res. 65 (2005) 2287-2295.
    • (2005) Cancer Res. , vol.65 , pp. 2287-2295
    • Cha, T.L.1    Qiu, L.2    Chen, C.T.3    Wen, Y.4    Hung, M.C.5
  • 102
    • 19644388720 scopus 로고    scopus 로고
    • Hyperthermia-induced proteasome inhibition and loss of androgen receptor expression in human prostate cancer cells
    • Pajonk, F., van Ophoven, A. and McBride, W.H. Hyperthermia-induced proteasome inhibition and loss of androgen receptor expression in human prostate cancer cells. Cancer Res. 65 (2005) 4836-4843.
    • (2005) Cancer Res. , vol.65 , pp. 4836-4843
    • Pajonk, F.1    Van Ophoven, A.2    McBride, W.H.3
  • 104
    • 28844481089 scopus 로고    scopus 로고
    • Molecular chaperones throughout the life cycle of androgen receptor
    • Prescott, J. and Coetzee, G.A. Molecular chaperones throughout the life cycle of androgen receptor. Cancer Lett. 231 (2006) 12-19.
    • (2006) Cancer Lett. , vol.231 , pp. 12-19
    • Prescott, J.1    Coetzee, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.