Nuclear-receptor interactions on DNA-response elements.
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[1] S. Khorasanizadeh,et al. Transcription factors: The right combination for the DNA lock , 1999, Current Biology.
[2] V. Chatterjee,et al. Functional analysis of a transactivation domain in the thyroid hormone beta receptor. , 1994, The Journal of biological chemistry.
[3] R. Shukin,et al. Determinants of DNA sequence specificity of the androgen, progesterone, and glucocorticoid receptors: evidence for differential steroid receptor response elements. , 1999, Molecular endocrinology.
[4] P. Chambon,et al. Activation function 2 (AF‐2) of retinoic acid receptor and 9‐cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF‐2 activity. , 1994, The EMBO journal.
[5] K. Umesono,et al. The nuclear receptor superfamily: The second decade , 1995, Cell.
[6] P. Sigler,et al. The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex , 1995, Nature Structural Biology.
[7] B. O’Malley,et al. Orphan receptors: in search of a unifying hypothesis for activation. , 1992, Molecular endocrinology.
[8] C. Glass,et al. Coactivator and corepressor complexes in nuclear receptor function. , 1999, Current opinion in genetics & development.
[9] H. Gronemeyer,et al. The nuclear receptor ligand-binding domain: structure and function. , 1998, Current opinion in cell biology.
[10] R J Fletterick,et al. Structure and specificity of nuclear receptor-coactivator interactions. , 1998, Genes & development.
[11] M. Cleary,et al. Structure of a HoxB1–Pbx1 Heterodimer Bound to DNA Role of the Hexapeptide and a Fourth Homeodomain Helix in Complex Formation , 1999, Cell.
[12] L. Guarente,et al. Structure of HAP1-18–DNA implicates direct allosteric effect of protein–DNA interactions on transcriptional activation , 1999, Nature Structural Biology.
[13] Song Tan,et al. Crystal structure of the yeast MATα2/MCM1/DNA ternary complex , 1998, Nature.
[14] John W. R. Schwabe,et al. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements , 1993, Cell.
[15] K. Umesono,et al. Determinants for selective RAR and TR recognition of direct repeat HREs. , 1993, Genes & development.
[16] D. Barettino,et al. Characterization of the ligand‐dependent transactivation domain of thyroid hormone receptor. , 1994, The EMBO journal.
[17] P. Sigler,et al. Structural determinants of nuclear receptor assembly on DNA direct repeats , 1995, Nature.
[18] C. Wolberger,et al. Crystal Structure of the MATa1/MATα2 Homeodomain Heterodimer Bound to DNA , 1995, Science.
[19] J. Gustafsson,et al. Structural determinants of DNA-binding specificity by steroid receptors. , 1995, Molecular endocrinology.
[20] M. Lazar,et al. Interdomain communication regulating ligand binding by PPAR-γ , 1998, Nature.
[21] M. Lazar,et al. Structural elements of an orphan nuclear receptor-DNA complex. , 1998, Molecular cell.
[22] R. Evans,et al. The RXR heterodimers and orphan receptors , 1995, Cell.
[23] S. Khorasanizadeh,et al. Structure of the RXR–RAR DNA‐binding complex on the retinoic acid response element DR1 , 2000, The EMBO journal.
[24] P. Sigler,et al. DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B , 1999, Nature Structural Biology.
[25] David A. Agard,et al. The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen , 1998, Cell.
[26] Millard H. Lambert,et al. Asymmetry in the PPARγ/RXRα Crystal Structure Reveals the Molecular Basis of Heterodimerization among Nuclear Receptors , 2000 .
[27] M. Lazar,et al. direct repeat . represses transcription as a dimer on a novel The monomer-binding orphan receptor RevErb , 1995 .
[28] K. Yamamoto,et al. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA , 2003, Nature.
[29] R. Kaptein,et al. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. , 1999, Biochemistry.
[30] P. Chambon,et al. The patterns of binding of RAR, RXR and TR homo‐ and heterodimers to direct repeats are dictated by the binding specificites of the DNA binding domains. , 1993, The EMBO journal.
[31] P. Chambon,et al. Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains. , 2000, Molecular cell.
[32] F. Rastinejad. Retinoid X receptor and its partners in the nuclear receptor family. , 2001, Current opinion in structural biology.
[33] Myles Brown,et al. Polarity-specific activities of retinoic acid receptors determined by a co-repressor , 1995, Nature.
[34] S. Safe,et al. Reciprocal Activation of Xenobiotic Response Genes by Nuclear Receptors Sxr/pxr and Car , 2000 .
[35] J. Lees,et al. Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors. , 1992, The EMBO journal.
[36] Li Zhang,et al. Structure of a HAP1–DNA complex reveals dramatically asymmetric DNA binding by a homodimeric protein , 1999, Nature Structural Biology.
[37] A. Vershon,et al. A short, disordered protein region mediates interactions between the homeodomain of the yeast α2 protein and the MCM1 protein , 1993, Cell.
[38] C. Glass,et al. Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding , 1994, Nature.
[39] L. Freedman,et al. Nuclear receptor cofactors as chromatin remodelers. , 1999, Current opinion in genetics & development.
[40] T. Shinoda,et al. Characterization and DNA-binding properties of GRF, a novel monomeric binding orphan receptor related to GCNF and betaFTZ-F1. , 1999, European journal of biochemistry.
[41] M. Sierk,et al. Structural basis of RXR-DNA interactions. , 2000, Journal of molecular biology.
[42] F. Claessens,et al. Differences in DNA Binding Characteristics of the Androgen and Glucocorticoid Receptors Can Determine Hormone-specific Responses* , 2000, The Journal of Biological Chemistry.
[43] A. Takeshita,et al. Nuclear receptor coactivators facilitate vitamin D receptor homodimer action on direct repeat hormone response elements. , 2000, Endocrinology.
[44] H. Dyson,et al. DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid X receptor. , 1998, Journal of molecular biology.
[45] S. Harrison,et al. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA , 1998, Nature.
[46] Aneel K. Aggarwal,et al. Structure of a DNA-bound Ultrabithorax–Extradenticle homeodomain complex , 1999, Nature.
[47] V. Giguère,et al. Determinants of target gene specificity for ROR alpha 1: monomeric DNA binding by an orphan nuclear receptor , 1995, Molecular and cellular biology.
[48] K. Yamamoto,et al. The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain , 1988, Nature.
[49] A. Johnson,et al. Molecular mechanisms of cell-type determination in budding yeast. , 1995, Current opinion in genetics & development.
[50] P. Chambon,et al. The dimerization interfaces formed between the DNA binding domains of RXR, RAR and TR determine the binding specificity and polarity of the full‐length receptors to direct repeats. , 1994, The EMBO journal.