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New naturally occurring missense mutations of the human mineralocorticoid receptor disclose important residues involved in dynamic interactions with deoxyribonucleic acid, intracellular trafficking, and ligand binding.
Sartorato P, Cluzeaud F, Fagart J, Viengchareun S, Lombès M, Zennaro MC. Sartorato P, et al. Among authors: fagart j. Mol Endocrinol. 2004 Sep;18(9):2151-65. doi: 10.1210/me.2003-0408. Epub 2004 Jun 10. Mol Endocrinol. 2004. PMID: 15192075
Antagonism in the human mineralocorticoid receptor.
Fagart J, Wurtz JM, Souque A, Hellal-Levy C, Moras D, Rafestin-Oblin ME. Fagart J, et al. EMBO J. 1998 Jun 15;17(12):3317-25. doi: 10.1093/emboj/17.12.3317. EMBO J. 1998. PMID: 9628869 Free PMC article.
Photoaffinity labelling of the human mineralocorticoid receptor with steroids having a reactive group at position 3, 18 or 21.
Fagart J, Couette B, Souque A, Davioud E, Marquet A, Rafestin-Oblin ME. Fagart J, et al. Biochim Biophys Acta. 1998 Oct 14;1388(1):35-44. doi: 10.1016/s0167-4838(98)00160-5. Biochim Biophys Acta. 1998. PMID: 9774704
As the 30 kDa fragment generated by chymotrypsin has been shown to encompass the entire ligand-binding domain of the hMR (B. Couette, J. Fagart, S. Jalaguier, M. Lombes, A. Souque, M.E. Rafestin-Oblin, Biochem. J. 315 (1996) 421-427), the present experiments …
As the 30 kDa fragment generated by chymotrypsin has been shown to encompass the entire ligand-binding domain of the hMR (B. Couette, J
53 results