Transactivation of the human retinoid X receptor by organotins: use of site-directed mutagenesis to identify critical amino acid residues for organotin-induced transactivation
Author(s) -
Youhei Hiromori,
Akira Aoki,
Junichi Nishikawa,
Hisamitsu Nagase,
Tsuyoshi Nakanishi
Publication year - 2015
Publication title -
metallomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.012
H-Index - 75
eISSN - 1756-591X
pISSN - 1756-5901
DOI - 10.1039/c5mt00086f
Subject(s) - transactivation , retinoid x receptor , chemistry , mutant , biochemistry , retinoid x receptor alpha , peroxisome proliferator activated receptor , amino acid , receptor , nuclear receptor , retinoid , retinoic acid , gene , transcription factor
Organotins, such as tributyltin (TBT) and triphenyltin (TPT), may disrupt endocrine activity in mammals arising from their ability to act as ligands for the retinoid X receptor (RXR) and the peroxisome proliferator-activated receptor γ (PPARγ).
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