Distinct Glucocorticoid Receptor Transcriptional Regulatory Surfaces Mediate the Cytotoxic and Cytostatic Effects of Glucocorticoids

REFERENCES

• Adams, J. M., and J. Cory 1998. The Bcl-2 protein family: arbiters of cell survival. Science 281:1322–1326.
   PubMed Web of Science ®Google Scholar
• Alam, J., and J. Cook 1990. Reporter genes: application to the study of mammalian gene transcription. Anal. Biochem. 188:245–254.
   PubMed Web of Science ®Google Scholar
• Alessandrini, A., D. S. Chiaur, and J. Pagano 1997. Regulation of the cyclin-dependent kinase inhibitor p27 by degradation and phosphorylation. Leukemia 11:342–345.
   PubMedGoogle Scholar
• Almlof, T., J. A. Gustafsson, and J. Wright 1997. Role of hydrophobic amino acid clusters in the transactivation activity of the human glucocorticoid receptor. Mol. Cell. Biol. 17:934–945.
   PubMed Web of Science ®Google Scholar
• Alnemri, E. S., T. F. Fernandes, S. Haldar, C. M. Croce, and J. Litwack 1992. Involvement of Bcl-2 in glucocorticoid-induced apoptosis of human pre-B-leukemias. Cancer Res. 52:491–495.
   PubMed Web of Science ®Google Scholar
• Barde, Y. A. 1989. Trophic factors and neuronal survival. Neuron 2:1525–1534.
   PubMed Web of Science ®Google Scholar
• Blanco, J. C., S. Minucci, J. Lu, X. J. Yang, K. K. Walker, H. Chen, R. M. Evans, Y. Nakatani, and J. Ozato 1998. The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev. 12:1638–1651.
   PubMed Web of Science ®Google Scholar
• Brehm, A., E. A. Miska, D. J. McCance, J. L. Reid, A. J. Bannister, and J. Kouzarides 1998. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391:597–601.
   PubMed Web of Science ®Google Scholar
• Brinkmann, U., E. Brinkmann, M. Gallo, and J. Pastan 1995. Cloning and characterization of a cellular apoptosis susceptibility gene, the human homologue to the yeast chromosome segregation gene CSE1. Proc. Natl. Acad. Sci. USA 92:10427–10431.
   PubMed Web of Science ®Google Scholar
• Brinkmann, U., M. Gallo, M. H. Polymeropoulos, and J. Pastan 1996. The human CAS (cellular apoptosis susceptibility) gene mapping on chromosome 20q13 is amplified in BT474 breast cancer cells and part of aberrant chromosomes in breast and colon cancer cell lines. Genome Res. 6:187–194.
   PubMedGoogle Scholar
• Brostjan, C., J. Anrather, V. Csizmadia, D. Stroka, M. Soares, F. H. Bach, and J. Winkler 1996. Glucocorticoid-mediated repression of NFκB activity in endothelial cells does not involve induction of IκBα synthesis. J. Biol. Chem. 271:19612–19616.
   PubMed Web of Science ®Google Scholar
• Burnstein, K. L., C. M. Jewell, M. Sar, and J. Cidlowski 1994. Intragenic sequences of the human glucocorticoid receptor complementary DNA mediate hormone-inducible receptor messenger RNA down-regulation through multiple mechanisms. Mol. Endocrinol. 8:1764–1773.
   PubMedGoogle Scholar
• Cha, H. H., E. J. Cram, E. C. Wang, A. J. Huang, H. G. Kasler, and J. Firestone 1998. Glucocorticoids stimulate p21 gene expression by targeting multiple transcriptional elements within a steroid responsive region of the p21waf1/cip1 promoter in rat hepatoma cells. J. Biol. Chem. 273:1998–2007.
   PubMedGoogle Scholar
• Chandler, V. L., B. A. Maler, and J. Yamamoto 1983. DNA sequences bound specifically by glucocorticoid receptor in vitro render a heterologous promoter hormone responsive in vivo. Cell 33:489–499.
   PubMed Web of Science ®Google Scholar
• Chandra, J., J. Gilbreath, E. J. Freireich, K. O. Kliche, M. Andreeff, M. Keating, and J. McConkey 1997. Protease activation is required for glucocorticoid-induced apoptosis in chronic lymphocytic leukemic lymphocytes. Blood 90:3673–3681.
   PubMed Web of Science ®Google Scholar
• Chapman, M. S., D. J. Askew, U. Kuscuoglu, and J. Miesfeld 1996. Transcriptional control of steroid-regulated apoptosis in murine thymoma cells. Mol. Endocrinol. 10:967–978.
   PubMed Web of Science ®Google Scholar
• Chen, H., R. J. Lin, R. L. Schiltz, D. Chakravarti, A. Nash, L. Nagy, M. L. Privalsky, Y. Nakatani, and J. Evans 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569–580.
   PubMed Web of Science ®Google Scholar
• Cidlowski, J. A., K. L. King, R. B. Evans-Storms, J. W. Montague, C. D. Bortner, F. M. Hughes Jr.. 1996. The biochemistry and molecular biology of glucocorticoid-induced apoptosis in the immune system. Recent Prog. Horm. Res. 51:457–490.
   PubMedGoogle Scholar
• Cohen, G. M. 1997. Caspases: the executioners of apoptosis. Biochem. J. 326:1–16.
   PubMed Web of Science ®Google Scholar
• Coleman, R. E. 1992. Glucocorticoids in cancer therapy. Biotherapy 4:37–44.
   PubMedGoogle Scholar
• Coleman, T. R., and J. Dunphy 1994. Cdc2 regulatory factors. Curr. Opin. Cell Biol. 6:877–882.
   PubMed Web of Science ®Google Scholar
• Cram, E. J., R. A. Ramos, E. C. Wang, H. H. Cha, Y. Nishio, and J. Firestone 1998. Role of the CCAAT/enhancer binding protein-transcription factor in the glucocorticoid stimulation of p21waf1/cip1 gene promoter activity in growth-arrested rat hepatoma cells. J. Biol. Chem. 273:2008–2014.
   PubMed Web of Science ®Google Scholar
• De Bosscher, K., M. L. Schmitz, W. Vanden Berghe, S. Plaisance, W. Fiers, and J. Haegeman 1997. Glucocorticoid-mediated repression of nuclear factor-κB-dependent transcription involves direct interference with transactivation. Proc. Natl. Acad. Sci. USA 94:13504–13509.
   PubMed Web of Science ®Google Scholar
• Dempster, D. W., B. S. Moonga, L. S. Stein, W. R. Horbert, and J. Antakly 1997. Glucocorticoids inhibit bone resorption by isolated rat osteoclasts by enhancing apoptosis. J. Endocrinol. 154:397–406.
   PubMed Web of Science ®Google Scholar
• Diamond, M. I., J. N. Miner, S. K. Yoshinaga, and J. Yamamoto 1990. Transcription factor interactions: selectors of positive or negative regulation from a single DNA element. Science 249:1266–1272.
   PubMed Web of Science ®Google Scholar
• Ewen, M. E., H. K. Sluss, C. J. Sherr, H. Matsushime, J. Kato, and J. Livingston 1993. Functional interactions of the retinoblastoma protein with mammalian D-type cyclins. Cell 73:487–497.
   PubMed Web of Science ®Google Scholar
• Farrow, S. N., and J. Brown 1996. New members of the Bcl-2 family and their protein partners. Curr. Opin. Genet. Dev. 6:45–49.
   PubMed Web of Science ®Google Scholar
• Frasch, S. C., J. A. Nick, V. A. Fadok, D. L. Bratton, G. S. Worthen, and J. Henson 1998. p38 mitogen-activated protein kinase-dependent and -independent intracellular signal transduction pathways leading to apoptosis in human neutrophils. J. Biol. Chem. 273:8389–8397.
   PubMedGoogle Scholar
• Gametchu, B., and J. Harrison 1984. Characterization of a monoclonal antibody to the rat liver glucocorticoid receptor. Endocrinology 114:274–279.
   PubMedGoogle Scholar
• Gaynon, P. S., and J. Lustig 1995. The use of glucocorticoids in acute lymphoblastic leukemia of childhood. Molecular, cellular, and clinical considerations. J. Pediatr. Hematol. Oncol. 17:1–12.
   PubMed Web of Science ®Google Scholar
• Godowski, P. J., D. D. Sakai, and J. Yamamoto 1989. Signal transduction and transcriptional regulation by the glucocorticoid receptor. UCLA Symp. Mol. Cell. Biol. 95:197–210.
   Google Scholar
• Hakem, R., A. Hakem, G. S. Duncan, J. T. Henderson, M. Woo, M. S. Soengas, A. Elia, J. L. de la Pompa, D. Kagi, W. Khoo, J. Potter, R. Yoshida, S. A. Kaufman, S. W. Lowe, J. M. Penninger, and J. Mak 1998. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 94:339–352.
   PubMed Web of Science ®Google Scholar
• Harper, J. W., and J. Elledge 1996. Cdk inhibitors in development and cancer. Curr. Opin. Genet. Dev. 6:56–64.
   PubMed Web of Science ®Google Scholar
• Harvey, K. J., J. F. Blomquist, and J. Ucker 1998. Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2 caspase and cyclin-dependent kinase activities. Mol. Cell. Biol. 18:2912–22.
   PubMed Web of Science ®Google Scholar
• Heck, S., K. Bender, M. Kullmann, M. Gottlicher, P. Herrlich, and J. Cato 1997. IκBα-independent downregulation of NF-κB activity by glucocorticoid receptor. EMBO J. 16:4698–4707.
   PubMed Web of Science ®Google Scholar
• Heck, S., M. Kullmann, A. Gast, H. Ponta, H. J. Rahmsdorf, P. Herrlich, and J. Cato 1994. A distinct modulating domain in glucocorticoid receptor monomers in the repression of activity of the transcription factor AP-1. EMBO J. 13:4087–4095.
   PubMed Web of Science ®Google Scholar
• Helmberg, A., N. Auphan, C. Caelles, and J. Karin 1995. Glucocorticoid-induced apoptosis of human leukemic cells is caused by the repressive function of the glucocorticoid receptor. EMBO J. 14:452–460.
   PubMed Web of Science ®Google Scholar
• Herrlich, P., M. Gottlicher 1998. Transcriptional cross-talk by steroid hormone receptors, p. 191–207. In L. P. Freedman (ed.), The molecular biology of steroid and nuclear hormone receptors. Birkhauser, Boston, Mass.
   Google Scholar
• Hinds, P. W., S. Mittnacht, V. Dulic, A. Arnold, S. I. Reed, and J. Weinberg 1992. Regulation of retinoblastoma protein functions by ectopic expression of human cyclins. Cell 70:993–1006.
   PubMed Web of Science ®Google Scholar
• Hong, H., K. Kohli, M. J. Garabedian, and J. Stallcup 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735–2744.
   PubMed Web of Science ®Google Scholar
• Hong, H., K. Kohli, A. Trivedi, D. L. Johnson, and J. Stallcup 1996. GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors. Proc. Natl. Acad. Sci. USA 93:4948–4952.
   PubMedGoogle Scholar
• Hughes, F. M. Jr., and J. Cidlowski 1998. Glucocorticoid-induced thymocyte apoptosis: protease-dependent activation of cell shrinkage and DNA degradation. J. Steroid Biochem. Mol. Biol. 65:207–217.
   PubMedGoogle Scholar
• Iniguez-Lluhi, J. A., D. Y. Lou, and J. Yamamoto 1997. Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus. J. Biol. Chem. 272:4149–4156.
   PubMed Web of Science ®Google Scholar
• Jacobson, M. D., M. Weil, and J. Raff 1997. Programmed cell death in animal development. Cell 88:347–354.
   PubMed Web of Science ®Google Scholar
• Karin, M. 1998. New twists in gene regulation by glucocorticoid receptor: is DNA binding dispensable? Cell 93:487–490.
   PubMed Web of Science ®Google Scholar
• Karin, M., A. Haslinger, H. Holtgreve, R. I. Richards, P. Krauter, H. M. Westphal, and J. Beato 1984. Characterization of DNA sequences through which cadmium and glucocorticoid hormones induce human metallothionein-IIA gene. Nature 308:513–519.
   PubMed Web of Science ®Google Scholar
• Kawakami, A., Q. Tian, X. Duan, M. Streuli, S. F. Schlossman, and J. Anderson 1992. Identification and functional characterization of a TIA-1-related nucleolysin. Proc. Natl. Acad. Sci. USA 89:8681–8685.
   PubMed Web of Science ®Google Scholar
• Kraus, W. L., E. M. McInerney, and J. Katzenellenbogen 1995. Ligand-dependent, transcriptionally productive association of the amino- and carboxyl-terminal regions of a steroid hormone nuclear receptor. Proc. Natl. Acad. Sci. USA 92:12314–12318.
   PubMed Web of Science ®Google Scholar
• Krstic, M. D., I. Rogatsky, K. R. Yamamoto, and J. Garabedian 1997. Mitogen-activated and cyclin-dependent protein kinases selectively and differentially modulate transcriptional enhancement by the glucocorticoid receptor. Mol. Cell. Biol. 17:3947–3954.
   PubMed Web of Science ®Google Scholar
• Kuida, K., T. F. Haydar, C. Y. Kuan, Y. Gu, C. Taya, H. Karasuyama, M. S. Su, P. Rakic, and J. Flavell 1998. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94:325–337.
   PubMed Web of Science ®Google Scholar
• Kuida, K., T. S. Zheng, S. Na, C. Kuan, D. Yang, H. Karasuyama, P. Rakic, and J. Flavell 1996. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384:368–372.
   PubMed Web of Science ®Google Scholar
• Lefstin, J. A., J. R. Thomas, and J. Yamamoto 1994. Influence of a steroid receptor DNA-binding domain on transcriptional regulatory functions. Genes Dev. 8:2842–2856.
   PubMed Web of Science ®Google Scholar
• Liden, J., F. Delaunay, I. Rafter, J. Gustafsson, and J. Okret 1997. A new function for the C-terminal zinc finger of the glucocorticoid receptor. Repression of RelA transactivation. J. Biol. Chem. 272:21467–21472.
   PubMedGoogle Scholar
• Linette, G. P., and J. Korsmeyer 1994. Differentiation and cell death: lessons from the immune system. Curr. Opin. Cell Biol. 6:809–815.
   PubMedGoogle Scholar
• Liu, W., A. G. Hillmann, and J. Harmon 1995. Hormone-independent repression of AP-1-inducible collagenase promoter activity by glucocorticoid receptors. Mol. Cell. Biol. 15:1005–1013.
   PubMedGoogle Scholar
• Liu, W., J. Wang, N. K. Sauter, and J. Pearce 1995. Steroid receptor heterodimerization demonstrated in vitro and in vivo. Proc. Natl. Acad. Sci. USA 92:12480–12484.
   PubMed Web of Science ®Google Scholar
• Liu, W., J. Wang, G. Yu, and J. Pearce 1996. Steroid receptor transcriptional synergy is potentiated by disruption of the DNA-binding domain dimer interface. Mol. Endocrinol. 10:1399–1406.
   PubMedGoogle Scholar
• Luisi, B. F., W. X. Xu, Z. Otwinowski, L. P. Freedman, K. R. Yamamoto, and J. Sigler 1991. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352:497–505.
   PubMed Web of Science ®Google Scholar
• Magnaghi-Jaulin, L., R. Groisman, I. Naguibneva, P. Robin, S. Lorain, J. P. Le Villain, F. Troalen, D. Trouche, and J. Harel-Bellan 1998. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. Nature 391:601–605.
   PubMed Web of Science ®Google Scholar
• Martin-Castellanos, C., and J. Moreno 1997. Recent advances on cyclins, CDKs and CDK inhibitors. Trends Cell Biol. 7:95–98.
   PubMedGoogle Scholar
• McInerney, E. M., M. J. Tsai, B. W. O’Malley, and J. Katzenellenbogen 1996. Analysis of estrogen receptor transcriptional enhancement by a nuclear hormone receptor coactivator. Proc. Natl. Acad. Sci. USA 93:10069–10073.
   PubMed Web of Science ®Google Scholar
• Meagher, L. C., J. M. Cousin, J. R. Seckl, and J. Haslett 1996. Opposing effects of glucocorticoids on the rate of apoptosis in neutrophilic and eosinophilic granulocytes. J. Immunol. 156:4422–4428.
   PubMed Web of Science ®Google Scholar
• Miner, J. N., M. I. Diamond, and J. Yamamoto 1991. Joints in the regulatory lattice: composite regulation by steroid receptor-AP1 complexes. Cell Growth Differ. 2:525–530.
   PubMedGoogle Scholar
• Miyoshi, H., M. Ohki, T. Nakagawa, and J. Honma 1997. Glucocorticoids induce apoptosis in acute myeloid leukemia cell lines with A t(8;21) chromosome translocation. Leuk Res. 21:45–50.
   PubMed Web of Science ®Google Scholar
• Muller, R. 1995. Transcriptional regulation during the mammalian cell cycle. Trends Genet. 11:173–178.
   PubMedGoogle Scholar
• Oakley, R. H., and J. Cidlowski 1993. Homologous down regulation of the glucocorticoid receptor: the molecular machinery. Crit. Rev. Eukaryot. Gene Expr. 3:63–88.
   PubMedGoogle Scholar
• Onate, S. A., V. Boonyaratanakornkit, T. E. Spencer, S. Y. Tsai, M. J. Tsai, D. P. Edwards, and J. O’Malley 1998. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors. J. Biol. Chem. 273:12101–12108.
   PubMed Web of Science ®Google Scholar
• Onate, S. A., S. Y. Tsai, M. J. Tsai, and J. O’Malley 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354–1357.
   PubMed Web of Science ®Google Scholar
• Pagano, M., S. W. Tam, A. M. Theodoras, P. Beer-Romero, G. Del Sal, V. Chau, P. R. Yew, G. F. Draetta, and J. Rolfe 1995. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 269:682–685.
   PubMed Web of Science ®Google Scholar
• Perlman, H., M. Sata, A. Le Roux, T. W. Sedlak, D. Branellec, and J. Walsh 1998. Bax-mediated cell death by the Gax homeoprotein requires mitogen activation but is independent of cell cycle activity. EMBO J. 17:3576–3586.
   PubMedGoogle Scholar
• Pirotte, B., M. Levivier, S. Goldman, J. M. Brucher, J. Brotchi, and J. Hildebrand 1997. Glucocorticoid-induced long-term remission in primary cerebral lymphoma: case report and review of the literature. J. Neurooncol. 32:63–69.
   PubMedGoogle Scholar
• Ramalingam, A., A. Hirai, and J. Thompson 1997. Glucocorticoid inhibition of fibroblast proliferation and regulation of the cyclin kinase inhibitor p21Cip1. Mol. Endocrinol. 11:577–586.
   PubMedGoogle Scholar
• Ramos, R. A., Y. Nishio, A. C. Maiyar, K. E. Simon, C. C. Ridder, Y. Ge, and J. Firestone 1996. Glucocorticoid-stimulated CCAAT/enhancer-binding protein α expression is required for steroid-induced G1 cell cycle arrest of minimal-deviation rat hepatoma cells. Mol. Cell. Biol. 16:5288–5301.
   PubMedGoogle Scholar
• Reichardt, H. M., K. H. Kaestner, J. Tuckermann, O. Kretz, O. Wessely, R. Bock, P. Gass, W. Schmid, P. Herrlich, P. Angel, and J. Schutz 1998. DNA binding of the glucocorticoid receptor is not essential for survival. Cell 93:531–541.
   PubMed Web of Science ®Google Scholar
• Rhee, K., W. Bresnahan, A. Hirai, M. Hirai, and J. Thompson 1995. C-Myc and cyclin D3 (CcnD3) genes are independent targets for glucocorticoid inhibition of lymphoid cell proliferation. Cancer Res. 55:4188–4195.
   PubMed Web of Science ®Google Scholar
• Rogatsky, I., S. K. Logan, and J. Garabedian 1998. Antagonism of glucocorticoid receptor transcriptional activation by the cJun N-terminal kinase. Proc. Natl. Acad. Sci. USA 95:2050–2055.
   PubMed Web of Science ®Google Scholar
• Rogatsky, I., J. M. Trowbridge, and J. Garabedian 1997. Glucocorticoid receptor-mediated cell cycle arrest is achieved through distinct cell-specific transcriptional regulatory mechanisms. Mol. Cell. Biol. 17:3181–3193.
   PubMed Web of Science ®Google Scholar
• Rogatsky, I., C. M. Waase, and J. Garabedian 1998. Phosphorylation and inhibition of the rat glucocorticoid receptor transcriptional activity by glycogen synthase kinase-3. J. Biol. Chem. 273:15315–15321.
   Google Scholar
• Sambrook, J., E. F. Fritsch, T. Maniatis 1989. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Schule, R., P. Rangarajan, S. Kliewer, L. J. Ransone, J. Bolado, N. Yang, I. M. Verma, and J. Evans 1990. Functional antagonism between oncoprotein c-Jun and the glucocorticoid receptor. Cell 62:1217–1226.
   PubMed Web of Science ®Google Scholar
• Sentman, C. L., J. R. Shutter, D. Hockenbery, O. Kanagawa, and J. Korsmeyer 1991. bcl-2 inhibits multiple forms of apoptosis but not negative selection in thymocytes. Cell 67:879–888.
   PubMed Web of Science ®Google Scholar
• Smith, C. L., S. A. Onate, M. J. Tsai, and J. O’Malley 1996. CREB binding protein acts synergistically with steroid receptor coactivator-1 to enhance steroid receptor-dependent transcription. Proc. Natl. Acad. Sci. USA 93:8884–8888.
   PubMed Web of Science ®Google Scholar
• Stallcup, M. Personal communication.
   Google Scholar
• Steffen, M., U. Scherdin, C. Duvigneau, and J. Holzel 1988. Glucocorticoid-induced alterations of morphology and growth of fibrosarcoma cells derived from 7,12-dimethylbenz(a)anthracene rat mammary tumor. Cancer Res. 48:7212–7218.
   PubMedGoogle Scholar
• Stoecklin, E., M. Wissler, F. Gouilleux, and J. Groner 1996. Functional interactions between Stat5 and the glucocorticoid receptor. Nature 383:726–728.
   PubMedGoogle Scholar
• Stoecklin, E., M. Wissler, R. Moriggl, and J. Groner 1997. Specific DNA binding of Stat5, but not of glucocorticoid receptor, is required for their functional cooperation in the regulation of gene transcription. Mol. Cell. Biol. 17:6708–6716.
   PubMedGoogle Scholar
• Taya, Y. 1997. RB kinases and RB-binding proteins: new points of view. Trends Biochem. Sci. 22:14–17.
   PubMedGoogle Scholar
• Tchekneva, E., and J. Serafin 1994. Kirsten sarcoma virus-immortalized mast cell lines. Reversible inhibition of growth by dexamethasone and evidence for the presence of an autocrine growth factor. J. Immunol. 152:5912–5921.
   PubMedGoogle Scholar
• Templeton, D. J., S. H. Park, L. Lanier, and J. Weinberg 1991. Nonfunctional mutants of the retinoblastoma protein are characterized by defects in phosphorylation, viral oncoprotein association, and nuclear tethering. Proc. Natl. Acad. Sci. USA 88:3033–3037.
   PubMed Web of Science ®Google Scholar
• Thornberry, N. A., and J. Lazebnik 1998. Caspases: enemies within. Science 281:1312–1316.
   PubMed Web of Science ®Google Scholar
• Tiemann, F., and J. Hinds 1998. Induction of DNA synthesis and apoptosis by regulated inactivation of a temperature-sensitive retinoblastoma protein. EMBO J. 17:1040–1052.
   PubMedGoogle Scholar
• Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and J. Rosenfeld 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677–684.
   PubMed Web of Science ®Google Scholar
• Wang, J., K. Guo, K. N. Wills, and J. Walsh 1997. Rb functions to inhibit apoptosis during myocyte differentiation. Cancer Res 57:351–354.
   PubMed Web of Science ®Google Scholar
• Wang, J., and J. Walsh 1996. Resistance to apoptosis conferred by Cdk inhibitors during myocyte differentiation. Science 273:359–361.
   PubMedGoogle Scholar
• Wang, L., M. Miura, L. Bergeron, H. Zhu, and J. Yuan 1994. Ich-1, an Ice/ced-3-related gene, encodes both positive and negative regulators of programmed cell death. Cell 78:739–750.
   PubMed Web of Science ®Google Scholar
• Webb, P., P. Nguyen, J. Shinsako, C. Anderson, W. Feng, M. P. Nguyen, D. Chen, S. M. Huang, S. Subramanian, E. McKinerney, B. S. Katzenellenbogen, M. R. Stallcup, and J. Kushner 1998. Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol. Endocrinol. 12:1605–1618.
   PubMed Web of Science ®Google Scholar
• Weinberg, R. A. 1995. The retinoblastoma protein and cell cycle control. Cell 81:323–330.
   PubMed Web of Science ®Google Scholar
• Wellmann, A., L. Krenacs, T. Fest, U. Scherf, I. Pastan, M. Raffeld, and J. Brinkmann 1997. Localization of the cell proliferation and apoptosis-associated CAS protein in lymphoid neoplasms. Am. J. Pathol. 150:25–30.
   PubMedGoogle Scholar
• Williams, S. P., and J. Sigler 1998. Atomic structure of progesterone complexed with its receptor. Nature 393:392–396.
   PubMed Web of Science ®Google Scholar
• Wissink, S., E. C. van Heerde, M. L. Schmitz, E. Kalkhoven, B. van der Burg, P. A. Baeuerle, and J. van der Saag 1997. Distinct domains of the RelA NF-κB subunit are required for negative cross-talk and direct interaction with the glucocorticoid receptor. J. Biol. Chem. 272:22278–22284.
   PubMedGoogle Scholar
• Woo, M., R. Hakem, M. S. Soengas, G. S. Duncan, A. Shahinian, D. Kagi, A. Hakem, M. McCurrach, W. Khoo, S. A. Kaufman, G. Senaldi, T. Howard, S. W. Lowe, and J. Mak 1998. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 12:806–819.
   PubMed Web of Science ®Google Scholar
• Yamamoto, K. R., D. Pearce, J. Thomas, and J. Miner 1992. Combinatorial regulation at mammalian composite response elements Transcriptional regulation In S. L. McKnight, K. R. Yamamoto (ed.), 2:1169–92 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Yang, E., and J. Korsmeyer 1996. Molecular thanatopsis: a discourse on the BCL2 family and cell death. Blood 88:386–401.
   PubMed Web of Science ®Google Scholar
• Yang-Yen, H.-F., J.-C. Chambard, Y.-L. Sun, T. Smeal, T. J. Schmidt, J. Drouin, and J. Karin 1990. Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction. Cell 62:1205–1215.
   PubMed Web of Science ®Google Scholar