Molecular chaperones function as steroid receptor nuclear mobility factors.
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Cem Elbi | G. Hager | D. DeFranco | C. Elbi | D. Toft | D. Walker | Dawn A Walker | Guillermo Romero | William P Sullivan | David O Toft | Gordon L Hager | Donald B DeFranco | W. Sullivan | G. Romero
[1] K. Yamamoto,et al. Isolation of Hsp90 mutants by screening for decreased steroid receptor function. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[2] N. McKenna,et al. Minireview: Nuclear Receptor Coactivators-An Update. , 2002, Endocrinology.
[3] James G McNally,et al. Dynamic behavior of transcription factors on a natural promoter in living cells , 2002, EMBO reports.
[4] Á. Pascual,et al. Nuclear hormone receptors and gene expression. , 2001, Physiological reviews.
[5] G. Hager,et al. Dynamic Shuttling and Intranuclear Mobility of Nuclear Hormone Receptors* , 2003, The Journal of Biological Chemistry.
[6] J. McNally,et al. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. , 2000, Science.
[7] L. Pearl,et al. Identification and Structural Characterization of the ATP/ADP-Binding Site in the Hsp90 Molecular Chaperone , 1997, Cell.
[8] C. Allis,et al. Steroid receptor coactivator-1 is a histone acetyltransferase , 1997, Nature.
[9] W. Pratt,et al. Steroid receptor interactions with heat shock protein and immunophilin chaperones. , 1997, Endocrine reviews.
[10] D. DeFranco,et al. Subnuclear Trafficking of Glucocorticoid Receptors In Vitro: Chromatin Recycling and Nuclear Export , 1997, The Journal of cell biology.
[11] T. Misteli,et al. Quantitation of GFP-fusion proteins in single living cells. , 2002, Journal of structural biology.
[12] F. Hartl,et al. In Vivo Function of Hsp90 Is Dependent on ATP Binding and ATP Hydrolysis , 1998, The Journal of cell biology.
[13] J. Clardy,et al. Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a component of steroid receptor complexes , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[14] G. Hager,et al. Using inducible vectors to study intracellular trafficking of GFP-tagged steroid/nuclear receptors in living cells. , 1999, Methods.
[15] C. Glass,et al. The coregulator exchange in transcriptional functions of nuclear receptors. , 2000, Genes & development.
[16] S. Lindquist,et al. Reduced levels of hsp90 compromise steroid receptor action in vivo , 1990, Nature.
[17] R. Tsien,et al. green fluorescent protein , 2020, Catalysis from A to Z.
[18] K. Yamamoto,et al. Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones , 2002, Science.
[19] P. Connell,et al. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins , 2000, Nature Cell Biology.
[20] R. Rimerman,et al. Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent , 1995, Molecular and cellular biology.
[21] Tom Misteli,et al. Applications of the green fluorescent protein in cell biology and biotechnology , 1997, Nature Biotechnology.
[22] 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.
[23] R. Evans,et al. Regulation of Hormone-Induced Histone Hyperacetylation and Gene Activation via Acetylation of an Acetylase , 1999, Cell.
[24] S. Adam,et al. Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors , 1990, The Journal of cell biology.
[25] G. Hager,et al. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[26] Tom Misteli,et al. Kinetic modelling approaches to in vivo imaging , 2001, Nature Reviews Molecular Cell Biology.
[27] D. Toft,et al. Steroid receptors and their associated proteins. , 1993, Molecular endocrinology.
[28] W. Pratt,et al. Folding of the Glucocorticoid Receptor by the Reconstituted hsp90-based Chaperone Machinery , 1997, The Journal of Biological Chemistry.
[29] J. Cidlowski,et al. Importance of Ligand Affinity Receptor Mobility in Living Cells : the Molecular Determinants of Glucocorticoid , 2003 .
[30] B. O’Malley,et al. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. , 1994, Annual review of biochemistry.
[31] Neal Rosen,et al. Crystal Structure of an Hsp90–Geldanamycin Complex: Targeting of a Protein Chaperone by an Antitumor Agent , 1997, Cell.
[32] D. F. Smith,et al. Molecular chaperone interactions with steroid receptors: an update. , 2000, Molecular endocrinology.
[33] M. Kann,et al. In vitro model for the nuclear transport of the hepadnavirus genome , 1997, Journal of virology.
[34] Michael Chinkers,et al. Identification of potential physiological activators of protein phosphatase 5. , 2002, Biochemistry.
[35] B. Howard,et al. The Transcriptional Coactivators p300 and CBP Are Histone Acetyltransferases , 1996, Cell.
[36] D. Toft,et al. The Assembly of Progesterone Receptor-hsp90 Complexes Using Purified Proteins* , 1998, The Journal of Biological Chemistry.
[37] L. Whitesell,et al. Stable and specific binding of heat shock protein 90 by geldanamycin disrupts glucocorticoid receptor function in intact cells. , 1996, Molecular endocrinology.
[38] D. DeFranco,et al. Chromatin recycling of glucocorticoid receptors: implications for multiple roles of heat shock protein 90. , 1999, Molecular endocrinology.
[39] T. Misteli,et al. High mobility of proteins in the mammalian cell nucleus , 2000, Nature.
[40] Carolyn L. Smith,et al. Subnuclear Trafficking of Estrogen Receptor-α and Steroid Receptor Coactivator-1 , 2000 .
[41] R. Rimerman,et al. Molecular cloning of human FKBP51 and comparisons of immunophilin interactions with Hsp90 and progesterone receptor , 1997, Molecular and cellular biology.
[42] B. O’Malley,et al. FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent , 2000, Nature Cell Biology.