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Articles related to 18827003 [Unique ID], provided by the PubMed system
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Charmandari E, Ichijo T, Jubiz W, et al. 
A Novel Point Mutation in the Amino Terminal Domain of the Human Glucocorticoid Receptor (hGR) Gene Enhancing hGR-mediated Gene Expression. [JOURNAL ARTICLE]
J Clin Endocrinol Metab 2008 Sep 30.
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Charmandari E, Raji A, Kino T, et al. 
A novel point mutation in the ligand-binding domain (LBD) of the human glucocorticoid receptor (hGR) causing generalized glucocorticoid resistance: the importance of the C terminus of hGR LBD in conferring transactivational activity. [Case Reports, Journal Article]
J Clin Endocrinol Metab 2005 Jun; 90(6):3696-705.
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Charmandari E, Kino T, Ichijo T, et al. 
A Novel Point Mutation in Helix 11 of the Ligand-binding Domain of the Human Glucocorticoid Receptor Gene Causing Generalized Glucocorticoid Resistance. [JOURNAL ARTICLE]
J Clin Endocrinol Metab 2007 Jul 17.
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Charmandari E, Kino T, Ichijo T, et al. 
Functional characterization of the natural human glucocorticoid receptor (hGR) mutants hGRalphaR477H and hGRalphaG679S associated with generalized glucocorticoid resistance. [Journal Article]
J Clin Endocrinol Metab 2006 Apr; 91(4):1535-43.
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Vottero A, Kino T, Combe H, et al. 
A novel, C-terminal dominant negative mutation of the GR causes familial glucocorticoid resistance through abnormal interactions with p160 steroid receptor coactivators. [Case Reports, Journal Article]
J Clin Endocrinol Metab 2002 Jun; 87(6):2658-67.
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Jewell CM, Webster JC, Burnstein KL, et al. 
Immunocytochemical analysis of hormone mediated nuclear translocation of wild type and mutant glucocorticoid receptors. [Journal Article]
J Steroid Biochem Mol Biol 1995 Nov; 55(2):135-46.
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Kino T, Stauber RH, Resau JH, et al. 
Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking. [Journal Article]
J Clin Endocrinol Metab 2001 Nov; 86(11):5600-8.
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Charmandari E, Chrousos GP, Ichijo T, et al. 
The human glucocorticoid receptor (hGR) beta isoform suppresses the transcriptional activity of hGRalpha by interfering with formation of active coactivator complexes. [Journal Article]
Mol Endocrinol 2005 Jan; 19(1):52-64.
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Yu C, Warriar N, Govindan MV 
Cysteines 638 and 665 in the hormone binding domain of human glucocorticoid receptor define the specificity to glucocorticoids. [Journal Article]
Biochemistry 1995 Oct 31; 34(43):14163-73.
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