Rapid Glucocorticoid Receptor Exchange at a Promoter Is Coupled to Transcription and Regulated by Chaperones and Proteasomes
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James G. McNally | J. McNally | G. Hager | Carolyn L. Smith | D. Stavreva | W. G. Müller | Gordon L. Hager | Diana A. Stavreva | Waltraud G. Müller
[1] B. O’Malley,et al. FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent , 2000, Nature Cell Biology.
[2] James G. McNally,et al. Large-scale chromatin decondensation and recondensation regulated by transcription from a natural promoter , 2001, The Journal of cell biology.
[3] T. Ho,et al. The mechanism of inhibition of Ran-dependent nuclear transport by cellular ATP depletion , 2002, The Journal of cell biology.
[4] R K Jain,et al. Quantification of transport and binding parameters using fluorescence recovery after photobleaching. Potential for in vivo applications. , 1990, Biophysical journal.
[5] N. Holbrook,et al. Glucocorticoid-receptor complexes in rat thymus cells. Rapid kinetic behavior and a cyclic model. , 1984, The Journal of biological chemistry.
[6] K. Yamamoto,et al. Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones , 2002, Science.
[7] R. Rimerman,et al. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent , 1995, Molecular and cellular biology.
[8] Tom Misteli,et al. Dynamic binding of histone H1 to chromatin in living cells , 2000, Nature.
[9] J. Cidlowski,et al. Molecular Determinants of Glucocorticoid Receptor Mobility in Living Cells: the Importance of Ligand Affinity , 2003, Molecular and Cellular Biology.
[10] M. Hendzel,et al. Rapid exchange of histone H1.1 on chromatin in living human cells , 2000, Nature.
[11] Anne E Carpenter,et al. Ligand-Mediated Assembly and Real-Time Cellular Dynamics of Estrogen Receptor α-Coactivator Complexes in Living Cells , 2001, Molecular and Cellular Biology.
[12] J. Höhfeld,et al. The Ubiquitin-related BAG-1 Provides a Link between the Molecular Chaperones Hsc70/Hsp70 and the Proteasome* , 2000, The Journal of Biological Chemistry.
[13] Z. Nawaz,et al. Specific ubiquitin-conjugating enzymes promote degradation of specific nuclear receptor coactivators. , 2003, Molecular endocrinology.
[14] B. O’Malley,et al. FRAP reveals that mobility of oestrogen receptor-alpha is ligand- and proteasome-dependent. , 2001, Nature cell biology.
[15] W. Pratt,et al. Steroid receptor interactions with heat shock protein and immunophilin chaperones. , 1997, Endocrine reviews.
[16] M. Mancini,et al. Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components , 2002, Nature Cell Biology.
[17] D. DeFranco,et al. Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. , 1999, Molecular endocrinology.
[18] Eric Verdin,et al. Reduced Mobility of the Alternate Splicing Factor (Asf) through the Nucleoplasm and Steady State Speckle Compartments , 2000, The Journal of cell biology.
[19] Myles Brown,et al. Cofactor Dynamics and Sufficiency in Estrogen Receptor–Regulated Transcription , 2000, Cell.
[20] J. McNally,et al. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. , 2000, Science.
[21] A. Goldberg,et al. Proteasome inhibitors: valuable new tools for cell biologists. , 1998, Trends in cell biology.
[22] G. Hager,et al. ATP-Dependent Mobilization of the Glucocorticoid Receptor during Chromatin Remodeling , 2002, Molecular and Cellular Biology.
[23] L. Freedman,et al. Reciprocal Recruitment of DRIP/Mediator and p160 Coactivator Complexes in Vivo by Estrogen Receptor* , 2002, The Journal of Biological Chemistry.
[24] Allan MunckS,et al. Glucocorticoid-Receptor Complexes in Rat Thymus Cells , 1984 .
[25] M. Galigniana,et al. Geldanamycin, a heat shock protein 90-binding benzoquinone ansamycin, inhibits steroid-dependent translocation of the glucocorticoid receptor from the cytoplasm to the nucleus. , 1997, Biochemistry.
[26] J. Ellenberg,et al. Cyclic, proteasome-mediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. , 2003, Molecular cell.
[27] T. Misteli,et al. High mobility of proteins in the mammalian cell nucleus , 2000, Nature.
[28] M. Gilman,et al. Proteasome‐mediated degradation of transcriptional activators correlates with activation domain potency in vivo , 1999, The EMBO journal.
[29] A. Bamberger,et al. Inhibition of mineralocorticoid and glucocorticoid receptor function by the heat shock protein 90-binding agent geldanamycin 1 Supported by the Deutsche Forschungsgemeinschaft (DFG-Grant Ka 1039/2-1). 1 , 1997, Molecular and Cellular Endocrinology.
[30] G. Hager,et al. Using inducible vectors to study intracellular trafficking of GFP-tagged steroid/nuclear receptors in living cells. , 1999, Methods.
[31] P. Kloetzel,et al. Inhibition of the ubiquitin-proteasome pathway induces differential heat-shock protein response in cardiomyocytes and renders early cardiac protection. , 2002, Biochemical and biophysical research communications.
[32] James G McNally,et al. Dynamic behavior of transcription factors on a natural promoter in living cells , 2002, EMBO reports.
[33] T. Misteli,et al. A Kinetic Framework for a Mammalian RNA Polymerase in Vivo , 2002, Science.
[34] D. DeFranco,et al. Proteasomal Inhibition Enhances Glucocorticoid Receptor Transactivation and Alters Its Subnuclear Trafficking , 2002, Molecular and Cellular Biology.
[35] L. Pearl,et al. Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin. , 1999, Journal of medicinal chemistry.
[36] T. Misteli,et al. Quantitation of GFP-fusion proteins in single living cells. , 2002, Journal of structural biology.
[37] P. Connell,et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins , 2000, Nature Cell Biology.
[38] D. Soumpasis. Theoretical analysis of fluorescence photobleaching recovery experiments. , 1983, Biophysical journal.
[39] Sreenath V. Sharma,et al. Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones. , 1999, Molecular endocrinology.
[40] Thomas Kodadek,et al. Recruitment of a 19S Proteasome Subcomplex to an Activated Promoter , 2002, Science.
[41] A. Caudy,et al. Regulation of Transcriptional Activation Domain Function by Ubiquitin , 2001, Science.
[42] D. Picard,et al. Heat-shock protein 90, a chaperone for folding and regulation , 2002, Cellular and Molecular Life Sciences CMLS.
[43] R. Sinden,et al. Transcriptional State of the Mouse Mammary Tumor Virus Promoter Can Affect Topological Domain Size in Vivo * , 1999, The Journal of Biological Chemistry.
[44] S. Gottesman,et al. Posttranslational quality control: folding, refolding, and degrading proteins. , 1999, Science.
[45] M. Muratani,et al. How the ubiquitin–proteasome system controls transcription , 2003, Nature Reviews Molecular Cell Biology.
[46] D. DeFranco. Navigating steroid hormone receptors through the nuclear compartment. , 2002, Molecular endocrinology.