Functional Characterization of the Natural Human Glucocorticoid Receptor (hGR) Mutants hGRαR477H and hGRαG679S Associated with Generalized Glucocorticoid Resistance | Zendy

Evangelia Charmandari | Zendy; Tomoshige Kino | Zendy; Takamasa Ichijo | Zendy; Keith Zachman | Zendy; Anton Alatsatianos | Zendy; George P. Chrousos | Zendy

Open Access

Functional Characterization of the Natural Human Glucocorticoid Receptor (hGR) Mutants hGRαR477H and hGRαG679S Associated with Generalized Glucocorticoid Resistance

Author(s) -

Evangelia Charmandari,

Tomoshige Kino,

Takamasa Ichijo,

Keith Zachman,

Anton Alatsatianos,

George P. Chrousos

Publication year - 2006

Publication title -

the journal of clinical endocrinology and metabolism

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.206

H-Index - 353

eISSN - 1945-7197

pISSN - 0021-972X

DOI - 10.1210/jc.2005-1893

Subject(s) - glucocorticoid receptor , glucocorticoid , wild type , mutant , microbiology and biotechnology , biology , mouse mammary tumor virus , receptor , electrophoretic mobility shift assay , gene , chemistry , gene expression , biochemistry , endocrinology

Glucocorticoid resistance is often a result of mutations in the human glucocorticoid receptor alpha (hGRalpha) gene, which impair one or more of hGRalpha's functions. We investigated the molecular mechanisms through which two previously described mutant receptors, hGRalphaR477H and hGRalphaG679S, with amino acid substitutions in the DNA- and ligand-binding domains, respectively, affect glucocorticoid signal transduction.

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