PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19521113-2 2009 The successful adaptation to stress involves negative feedback at the level of the hypothalamic-pituitary-adrenal (HPA) axis provided by the glucocorticoid receptor (GR), which is a steroid-dependent transcription factor found in a heterocomplex with heat shock proteins Hsp90 and Hsp70. Steroids 182-189 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 141-164 22465009-9 2012 Thus, although steroids that bind GR with high affinity can induce GR and p300 occupancy of target promoters, they may not induce a conformation of GR capable of activating transcription. Steroids 15-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 34-36 22465009-9 2012 Thus, although steroids that bind GR with high affinity can induce GR and p300 occupancy of target promoters, they may not induce a conformation of GR capable of activating transcription. Steroids 15-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 67-69 22465009-9 2012 Thus, although steroids that bind GR with high affinity can induce GR and p300 occupancy of target promoters, they may not induce a conformation of GR capable of activating transcription. Steroids 15-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 67-69 22457708-1 2012 GLUCOCORTICOIDS are steroid hormones that strongly influence intermediary carbohydrate metabolism by increasing the transcription rate of glucose-6-phosphatase (G6Pase), a key enzyme of gluconeogenesis, and suppress the immune system through the glucocorticoid receptor (GR). Steroids 20-27 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 246-269 22457708-1 2012 GLUCOCORTICOIDS are steroid hormones that strongly influence intermediary carbohydrate metabolism by increasing the transcription rate of glucose-6-phosphatase (G6Pase), a key enzyme of gluconeogenesis, and suppress the immune system through the glucocorticoid receptor (GR). Steroids 20-27 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 271-273 21764896-7 2011 We also illustrate the basic aspects of the expression, localization, function, and regulation of the GR by steroid hormones (androgens and glucocorticoids) within the epididymis. Steroids 110-126 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 103-105 20637751-18 2010 All of the above results suggested that the GR-mediated reduction of Na(+), K(+)-ATPase may contribute to the formation of steroid-induced cataract. Steroids 123-130 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 44-46 20392829-9 2010 However, GR alone appears involved in the sensitization of the cells to the chronotropic regulation through the cAMP pathway and in the hypertrophic response to steroids. Steroids 161-169 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 9-11 20573576-0 2010 Glucocorticoid receptor in the rat epididymis: expression, cellular distribution and regulation by steroid hormones. Steroids 99-115 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 0-23 19521113-2 2009 The successful adaptation to stress involves negative feedback at the level of the hypothalamic-pituitary-adrenal (HPA) axis provided by the glucocorticoid receptor (GR), which is a steroid-dependent transcription factor found in a heterocomplex with heat shock proteins Hsp90 and Hsp70. Steroids 182-189 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 166-168 17258455-0 2007 Discovery of novel phosphorus-containing steroids as selective glucocorticoid receptor antagonist. Steroids 41-49 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 63-86 9645683-4 1998 We have examined adrenal steroid regulation of the neurotrophins brain-derived neurotrophic factor, neurotrophin-3, and basic fibroblast growth factor, as well as the growth associated protein GAP-43, through activation of GR or mineralocorticoid receptor with selective agonists. Steroids 25-32 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 223-225 11361002-5 2001 The presence of glucocorticoid receptor in brain mitochondria supports the concept of a direct action of glucocorticoids on mitochondrial gene transcription, parallel to the established primary actions of the hormones on nuclear gene transcription, as a mechanism of coordinate regulation of respiratory enzyme biosynthesis by steroid hormones. Steroids 327-343 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 16-39 10588816-5 1999 Using Northern analysis we investigated the uterine expression of 11betaHSD1, 11betaHSD2 and GR mRNA in relation to serum levels of sex steroid hormones and uterine progesterone receptor mRNA expression in an animal model. Steroids 136-152 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 93-95 12767484-1 2003 Focusing on the hippocampal CA1 region, effects of peripheral gonadal and adrenal steroids on the glucocorticoid receptor (GR) were immunohistochemically evaluated in male and female adult rat brains after adrenalectomy (ADX), gonadectomy (GDX), and administration of estradiol (E2) and/or corticosterone (CS). Steroids 82-90 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 98-121 12767484-1 2003 Focusing on the hippocampal CA1 region, effects of peripheral gonadal and adrenal steroids on the glucocorticoid receptor (GR) were immunohistochemically evaluated in male and female adult rat brains after adrenalectomy (ADX), gonadectomy (GDX), and administration of estradiol (E2) and/or corticosterone (CS). Steroids 82-90 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 123-125 11154266-4 2001 In this report, we describe the steroid-induced homomeric interaction of the rat glucocorticoid receptor (GR) in solution in vivo. Steroids 32-39 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 81-104 11154266-4 2001 In this report, we describe the steroid-induced homomeric interaction of the rat glucocorticoid receptor (GR) in solution in vivo. Steroids 32-39 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 106-108 10630412-1 1999 Trypsin digestion of steroid-free, but not steroid-bound, rat glucocorticoid receptor (GR) has recently been reported to occur at arginine-651 (R651). Steroids 21-28 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 87-89 10630412-3 1999 This hypothesis is supported by the current model of the GR ligand binding domain (LBD), which is based on the X-ray structures of several related receptor LBDs and places R651 in the middle of the putative alpha-helix 6 (649-EQRMS-653 of rat GR), close to the bound steroid. Steroids 267-274 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 57-59 10580842-0 1999 Steroid-induced conformational changes of rat glucocorticoid receptor cause altered trypsin cleavage of the putative helix 6 in the ligand binding domain. Steroids 0-7 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 46-69 10580842-7 1999 This was supported by the observation that trypsin digestion of the steroid-free R651A mutant GR gave rise to the 30-kDa meroreceptor (amino acids 518-795), which displayed wild type affinity. Steroids 68-75 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 94-96 10580842-8 1999 This 30-kDa species is thus the smallest non-associated fragment of GR possessing wild type steroid binding affinity. Steroids 92-99 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 68-70 10580842-11 1999 However, unlike the estrogen receptor or the more closely related progesterone receptor, the precise proteolytic cleavage points of both the steroid-free and -bound GR fall within regions that are predicted, on the basis of X-ray crystal structures of related receptors, to be alpha-helical and resistant to proteolysis. Steroids 141-148 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 165-167 9645683-2 1998 Adrenal steroids act through two receptor subtypes, the glucocorticoid receptor (GR) and the mineralocorticoid receptor, and activation of each receptor subtype has distinct biochemical and physiological consequences. Steroids 8-16 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 56-79 9645683-2 1998 Adrenal steroids act through two receptor subtypes, the glucocorticoid receptor (GR) and the mineralocorticoid receptor, and activation of each receptor subtype has distinct biochemical and physiological consequences. Steroids 8-16 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 81-83 9501302-0 1998 Polymorphisms of the glucocorticoid receptor gene in laboratory and wild rats: steroid binding properties of trinucleotide CAG repeat length variants. Steroids 79-86 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 21-44 9528966-2 1998 In the rat hippocampus, the actions of adrenal steroids are mediated by two receptor types, the glucocorticoid receptor (GR) and the mineralocorticoid receptor (MR). Steroids 47-55 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 96-119 9528966-2 1998 In the rat hippocampus, the actions of adrenal steroids are mediated by two receptor types, the glucocorticoid receptor (GR) and the mineralocorticoid receptor (MR). Steroids 47-55 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 121-123 9593740-1 1998 The glucocorticoid receptor (GR) HBD must be bound to the protein chaperone hsp90 in order to acquire the high affinity steroid binding conformation. Steroids 120-127 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 4-27 9593740-1 1998 The glucocorticoid receptor (GR) HBD must be bound to the protein chaperone hsp90 in order to acquire the high affinity steroid binding conformation. Steroids 120-127 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 29-31 9593740-10 1998 Thus, a region of GR that has not been thought to be relevant for hsp90 binding is now seen to be of critical importance, and these data argue strongly against the commonly accepted model of receptor-hsp90 heterocomplex assembly in which the chaperone initially interacts nonspecifically with hydrophobic regions of the partially denatured HBD and subsequently assists its folding to the steroid binding confirmation. Steroids 388-395 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 18-20 9483579-3 1997 The GR is associated with heat-shock proteins (HSPs) as a functional complex with a high affinity for steroid binding. Steroids 102-109 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 4-6 9442037-9 1998 Our results have established a functional link between the glucocorticoid receptor signaling pathway that mediates a G1 cell cycle arrest of rat hepatoma cells and the transcriptional control of p21 by a cascade that requires the steroid induction of C/EBP alpha gene expression. Steroids 230-237 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 59-82 9261164-8 1997 In addition, we found that the steroid analog ZK98299 known to induce GR transrepression of AP-1 had no inhibitory effect on RelA activity. Steroids 31-38 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 70-72 9295350-0 1997 Steroid-induced conformational changes at ends of the hormone-binding domain in the rat glucocorticoid receptor are independent of agonist versus antagonist activity. Steroids 0-7 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 88-111 9295350-4 1997 Steroid binding did cause a conformational change in the GR that was detected by partial trypsin digestion, as described previously (Simons, S. S., Jr., Sistare, F. D., and Chakraborti, P. K. (1989) J. Biol. Steroids 0-7 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 57-59 7980630-3 1994 Pre-treatment of rats with the glucocorticoid receptor antagonist RU38486 (20 mg/kg) prevented the steroid induction of extracellular LC1 at both the 3 and 6 hr time-points. Steroids 99-106 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 31-54 8969928-11 1996 These studies suggest that altered MR- and GR-mediated mechanisms may contribute to the resistance of the W/Fu rat strain to steroid-induced hypertension. Steroids 125-132 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 43-45 8938989-2 1996 In glucocorticoid-deprived animals, stress-induced decrease in the cytoplasmic steroid binding was followed by parallel increases in its nuclear binding and TAT activity, suggesting a stimulation of TAT gene transcription by the GR in the absence of the ligand. Steroids 79-86 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 229-231 7580937-0 1995 Synthetic peptides derived from the steroid binding domain block modulator and molybdate action toward the rat glucocorticoid receptor. Steroids 36-43 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 111-134 7956914-1 1994 Adrenal steroids exert their effects through two distinct adrenal steroid receptor subtypes; the high affinity type I, or mineralocorticoid, receptor and the lower affinity type II, or glucocorticoid, receptor. Steroids 8-16 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 111-209 8975639-1 1996 The effects of cadmium (Cd) administration to intact rats on hepatic glucocorticoid receptor (GR) steroid binding capacity and DNA-binding ability were examined and correlated with the influence of the metal on rat liver tyrosine aminotransferase (TAT) activity and its induction by dexamethasone. Steroids 98-105 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 94-96 8975639-3 1996 administration of Cd doses ranging from 0.5 to 4 mg/kg, the GR steroid- and DNA-binding activities were significantly reduced in a dose-dependent manner. Steroids 63-70 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 60-62 7577705-1 1995 Autoregulation of glucocorticoid receptor (GR) concentration in vivo may be an important determinant of steroid sensitivity. Steroids 104-111 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 18-41 7577705-1 1995 Autoregulation of glucocorticoid receptor (GR) concentration in vivo may be an important determinant of steroid sensitivity. Steroids 104-111 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 43-45 7854350-8 1994 These results indicate that at least part of glucocorticoid regulation of WAP gene expression is mediated through the direct interaction of GR with glucocorticoid response elements in the distal promoter region resulting in steroid hormone-dependent alterations in chromatin structure. Steroids 224-239 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 140-142 8255389-2 1993 Presently, we found that bromocriptine (BROM) treatment increased the levels of GCR in DES-T, demonstrated by steroid binding assays and immunocytochemistry using a monoclonal antibody against the type II GCR. Steroids 110-117 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 80-83 7969784-2 1994 The endogenous steroid hormone CT has tenfold higher affinity for the MR than the GR. Steroids 15-30 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 82-84 8180104-2 1994 We previously reported that activated glucocorticoid receptor-steroid complexes from rat HTC cell cytosol exist as at least two sub-populations, one of which requires a low molecular weight (700-3000 Da) factor(s) for binding to DNA. Steroids 62-69 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 38-61 8166236-0 1994 Mineralocorticoid and glucocorticoid receptor steroid binding and localization in colonic cells. Steroids 46-53 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 22-45 19912962-3 1993 Previous studies have indicated that in the hippocampus adrenal steroids negatively regulate the expression of the mRNAs encoding the glucocorticoid receptor (GR), the mineralocorticoid receptor (MR), and the growth-associated protein GAP-43, while the preproenkephalin (ppENK) mRNA is positively regulated by glucocorticoids. Steroids 64-72 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 134-157 19912962-3 1993 Previous studies have indicated that in the hippocampus adrenal steroids negatively regulate the expression of the mRNAs encoding the glucocorticoid receptor (GR), the mineralocorticoid receptor (MR), and the growth-associated protein GAP-43, while the preproenkephalin (ppENK) mRNA is positively regulated by glucocorticoids. Steroids 64-72 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 159-161 8255389-8 1993 In this respect, inefficient steroid negative feedback on PRL synthesis due to down-regulation of GCR may contribute to hyperprolactinemia. Steroids 29-36 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 98-101 8510182-5 1993 Samples taken 20-40 min after the steroid treatment demonstrated pyramidal cells expressing GR IR in both the cytoplasmic and nuclear pools. Steroids 34-41 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 92-94 8461255-7 1993 These data strongly suggest that compounds bearing bulky substituents on the steroid A and/or C rings, like deacylcortivazol and RU486, are positioned differently from canonical glucocorticoids in the steroid binding groove of the GR. Steroids 77-84 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 231-233 19912921-14 1993 These results indicate that GR and MR mRNAs exhibit hippocampus-specific diurnal rhythms in expression which are controlled to a greater (MR) or lesser (GR) extent by circulating steroids. Steroids 179-187 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 28-30 19912921-14 1993 These results indicate that GR and MR mRNAs exhibit hippocampus-specific diurnal rhythms in expression which are controlled to a greater (MR) or lesser (GR) extent by circulating steroids. Steroids 179-187 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 153-155 8382211-2 1993 It was found that GST gene expression was induced in steroid-sensitive cells within 4 hr of dexamethasone treatment, required functional glucocorticoid receptor, and was dose-dependent with regard to hormone. Steroids 53-60 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 137-160 8461255-7 1993 These data strongly suggest that compounds bearing bulky substituents on the steroid A and/or C rings, like deacylcortivazol and RU486, are positioned differently from canonical glucocorticoids in the steroid binding groove of the GR. Steroids 201-208 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 231-233 1597467-1 1992 The involvement of a vicinally spaced dithiol group in steroid binding to the glucocorticoid receptor has been deduced from experiments with the thiol-specific reagent methyl methanethiolsulfonate and the vicinal dithiol-specific reagent sodium arsenite. Steroids 55-62 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 78-101 1511313-0 1992 Regulation of glucocorticoid receptor immunoreactivity in the rat hippocampus by androgenic-anabolic steroids. Steroids 101-109 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 14-37 19912844-9 1992 The relatively high percentage of pyknotic cells that were GR-immunoreactive suggests that adrenal steroids influence cell survival directly through GRs. Steroids 99-107 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 59-61 1572314-1 1992 Monoclonal antibodies directed against four different polypeptide epitopes on the Mr approximately 94,000 steroid-binding subunit of the rat liver cytosolic glucocorticoid receptor (GcR) were used to probe Western blots of epididymal spermatozoa from rats and mice. Steroids 106-113 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 157-180 1572314-1 1992 Monoclonal antibodies directed against four different polypeptide epitopes on the Mr approximately 94,000 steroid-binding subunit of the rat liver cytosolic glucocorticoid receptor (GcR) were used to probe Western blots of epididymal spermatozoa from rats and mice. Steroids 106-113 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 182-185 1310618-1 1992 Modulators are proposed to be novel ether aminophosphoglycerides that stabilize unoccupied and occupied glucocorticoid receptor steroid binding and inhibit glucocorticoid receptor complex activation. Steroids 128-135 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 104-127 1310618-1 1992 Modulators are proposed to be novel ether aminophosphoglycerides that stabilize unoccupied and occupied glucocorticoid receptor steroid binding and inhibit glucocorticoid receptor complex activation. Steroids 128-135 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 156-179 2039516-1 1991 We have recently described a 16 kDa steroid binding core (Thr537-Arg673) of the rat glucocorticoid receptor [Simons et al. Steroids 36-43 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 84-107 1299410-3 1992 Using a structural approach to identify domains of the glucocorticoid receptor responsible for interactions with affiliated transacting factors and DNA, we have identified a putative helix-turn-zipper motif that is conserved in all steroid, thyroid hormone, retinoic acid, and vitamin-D3 receptors. Steroids 232-239 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 55-78 1996987-0 1991 Hepatic glucocorticoid receptor behaves differently when its hormone binding site is occupied by agonist (triamcinolone acetonide) or antagonist (RU486) steroid ligands. Steroids 153-160 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 8-31 1996987-7 1991 These results indicate that either a) the interaction of GR with the agonist or antagonist steroid ligands causes differential structural alterations, which are more readily detectable in the presence of SH-modifying agents or b) the agonist and the antagonist interact with distinct steroid binding sites. Steroids 91-98 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 57-59 1996987-7 1991 These results indicate that either a) the interaction of GR with the agonist or antagonist steroid ligands causes differential structural alterations, which are more readily detectable in the presence of SH-modifying agents or b) the agonist and the antagonist interact with distinct steroid binding sites. Steroids 284-291 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 57-59 2278831-0 1990 The steroid-binding properties of recombinant glucocorticoid receptor: a putative role for heat shock protein hsp90. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 46-69 1985950-3 1991 Experimental evidence indicates that the purified nonactivated glucocorticoid receptor contains a single steroid-binding protein and two approximately 90-kDa nonsteroid-binding subunits identified as heat shock protein (hsp) 90. Steroids 105-112 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 63-86 1985950-5 1991 The cell-free synthesized glucocorticoid receptor is able to bind steroid and can be activated further to the DNA-binding form. Steroids 66-73 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 26-49 1985950-6 1991 To test the hypothesis of an active role played by hsp90 in the stabilization of a competent steroid-binding conformation of the glucocorticoid receptor, we have synthesized the receptor in a reticulocyte lysate that has been depleted of hsp90 by immunoadsorption with AC88 anti-hsp90. Steroids 93-100 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 129-152 2278831-2 1990 The recombinant proteins were found to bind steroids with the normal specificity for a glucocorticoid receptor but with reduced affinity (Kd for triamcinolone acetonide approximately 70 nM). Steroids 44-52 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 87-110 2770702-3 1989 Western blot analysis revealed that TCDD treatment did not cause a comparable decrease in the levels of immunodetectable receptor protein, which suggests that the steroid-binding properties of the hepatic GRc are altered, rather than the absolute concentration of receptor protein. Steroids 163-170 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 205-208 2226278-3 1990 Both the natural and synthetic steroid caused a rapid decrease of receptor binding in the cytosol but the time course of glucocorticoid receptor depletion was different. Steroids 31-38 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 121-144 2226332-0 1990 Localization of the vicinal dithiols involved in steroid binding to the rat glucocorticoid receptor. Steroids 49-56 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 76-99 2387249-10 1990 These results show that glucocorticoid hormone interacts with the nuclear envelope via binding to the transformed glucocorticoid receptor, lending support to the two-step model of steroid hormone action. Steroids 180-195 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 114-137 2811360-3 1989 The ability to preserve the steroid-binding capacity of the glucocorticoid receptor is not a universal property of all sulfhydryl compounds since many of the compounds tested were inactive. Steroids 28-35 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 60-83 2811360-4 1989 The steroid-binding capacity of the glucocorticoid receptor of the 100,000 g supernatant of rat liver homogenate is preserved/restored by sulfhydryl compounds containing a mercaptoethylamine or mercaptopropylamine subunit. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 36-59 2503518-1 1989 The steroid binding domain of the rat glucocorticoid receptor is considered as extending from amino acids 550 to 795. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 38-61 2503518-7 1989 These results show that glucocorticoid receptor fragments smaller than 34 kDa do bind steroids and that the amino acids Thr537-Arg673 constitute a core sequence for ligand binding within the larger steroid binding domain. Steroids 86-94 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 24-47 2503518-7 1989 These results show that glucocorticoid receptor fragments smaller than 34 kDa do bind steroids and that the amino acids Thr537-Arg673 constitute a core sequence for ligand binding within the larger steroid binding domain. Steroids 86-93 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 24-47 2649238-2 1989 In its nonactivated state, stabilized by sodium molybdate, the glucocorticoid receptor exists as a 9S heteromeric complex containing a single Mr approximately 94,000 steroid-binding unit and a dimer of hsp90. Steroids 166-173 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 63-86 2930536-1 1989 The untransformed rat glucocorticoid receptor is assumed to be a hetero-oligomeric complex, containing a non-steroid binding component, the 90K heat-shock protein (HSP 90). Steroids 109-116 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 22-45 2724956-4 1989 There was no measurable binding at time 0; the values of Bmax for the glucocorticoid receptor with decreased at 12, 24 and 48 h after the steroid withdrawal. Steroids 138-145 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 70-93 2724956-9 1989 We conclude that both steroids cause down regulation of the glucocorticoid receptor in rat liver cytosol, with both the extent and the duration of depletion being dependent on the biopotency of the glucocorticoid. Steroids 22-30 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 60-83 3192546-0 1988 Interaction of the Mr = 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor. Steroids 59-66 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 89-112 3248623-0 1988 [The studies on the loss and recovery of the steroid binding ability of rat liver glucocorticoid receptor]. Steroids 45-52 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 82-105 3248623-1 1988 We examined the mechanism of loss and recovery of steroid binding activity (inactivation and reactivation) of the rat liver glucocorticoid receptor (GR) in the cell free condition. Steroids 50-57 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 124-147 3248623-1 1988 We examined the mechanism of loss and recovery of steroid binding activity (inactivation and reactivation) of the rat liver glucocorticoid receptor (GR) in the cell free condition. Steroids 50-57 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 149-151 3192546-8 1988 Furthermore, the Mr approximately 27,000 steroid-binding fragment generated in the presence of molybdate could be immunoprecipitated by antibodies specific for the glucocorticoid receptor-associated Mr approximately 90,000 heat shock protein. Steroids 41-48 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 164-187 3192546-9 1988 These results provide direct evidence for an interaction of the Mr approximately 90,000 heat shock protein with the steroid-binding domain of the glucocorticoid receptor, known to correspond to the C-terminal third of the receptor protein. Steroids 116-123 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 146-169 2851057-8 1988 Moreover, the microanatomy of MR and GR expression provides insight into molecular mechanisms underlying the characteristic action of various steroids on behaviors involved in stress and circadian regulation. Steroids 142-150 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 37-39 3342067-0 1988 RU 486 stabilizes a high molecular weight form of the glucocorticoid receptor containing the 90K non-steroid binding protein in intact thymus cells. Steroids 101-108 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 54-77 2897467-1 1988 The relative binding affinities of over 30 steroids have been measured for the cytosol glucocorticoid receptor (GR) of thymus, liver, and hepatoma tissue culture cells and for progestin, androgen, and mineralocorticoid receptors. Steroids 43-51 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 87-110 2897467-1 1988 The relative binding affinities of over 30 steroids have been measured for the cytosol glucocorticoid receptor (GR) of thymus, liver, and hepatoma tissue culture cells and for progestin, androgen, and mineralocorticoid receptors. Steroids 43-51 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 112-114 3360809-0 1988 Identification of hormone-interacting amino acid residues within the steroid-binding domain of the glucocorticoid receptor in relation to other steroid hormone receptors. Steroids 69-76 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 99-122 3343254-7 1988 The purified modulator inhibits heat activation of the rat liver glucocorticoid-receptor complex and stabilizes the steroid binding ability of the unoccupied rat liver glucocorticoid receptor in a dose-dependent manner. Steroids 116-123 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 168-191 3348810-3 1988 This interaction of "activated" glucocorticoid-receptor complexes of rat liver with histone-agarose suggests a role of histones in the mechanism of action of steroid hormone. Steroids 158-173 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 32-55 3422744-2 1988 Purified modulator inhibits glucocorticoid-receptor complex activation and stabilizes the steroid-binding ability of the unoccupied glucocorticoid receptor. Steroids 90-97 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 132-155 3342067-5 1988 Western blot analysis of the fractions obtained after HPSEC separation was performed using a monoclonal antibody able to recognize the 90K non steroid binding protein associated with the molybdate stabilized glucocorticoid receptor complexes. Steroids 143-150 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 208-231 3609019-1 1987 The molybdate-stabilized rat liver glucocorticoid receptor complex was purified 9000-fold with a 46% yield by steroid-affinity chromatography and DEAE-Sephacel ion-exchange chromatography. Steroids 110-117 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 35-58 3347046-3 1988 Ligand-free GR interacted with both resins and was eluted without loss of its steroid binding ability. Steroids 78-85 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 12-14 3609019-7 1987 Highly purified glucocorticoid receptor could be covalently modified with biotin to retain its steroid-binding activity but with a 50% decrease in nuclear binding capacity. Steroids 95-102 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 16-39 3386251-0 1988 Relationship between glucocorticoid receptor steroid-binding capacity and association of the Mr 90,000 heat shock protein with the unliganded receptor. Steroids 45-52 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 21-44 3386251-1 1988 Treatment of rat liver cytosol with hydrogen peroxide (H2O2) or sodium molybdate (MoO4(2-)) inhibits thermal inactivation of glucocorticoid receptor steroid-binding capacity at 25 degrees C. Dithiothreitol (DTT) prevents the stabilization of receptors by H2O2. Steroids 149-156 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 125-148 3386251-2 1988 Heating (25 degrees C) of immune pellets formed by immunoadsorption of L-cell murine glucocorticoid receptor complexes to protein-A-Sepharose with an anti-receptor monoclonal antibody (BuGR2) results in dissociation of the M 90,000 heat shock protein (hsp90) from the steroid binding protein. Steroids 268-275 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 85-108 3386251-5 1988 These data suggest a role for hsp90 in maintaining an active steroid-binding conformation of the glucocorticoid receptor. Steroids 61-68 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 97-120 3319051-10 1987 The steroid-induced changes in cell nuclear immunoreactive GR staining intensity suggest possible cytoplasmic-cell nuclear translocation of GR and/or exposure of immunogenic GR domains. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 59-61 3319051-10 1987 The steroid-induced changes in cell nuclear immunoreactive GR staining intensity suggest possible cytoplasmic-cell nuclear translocation of GR and/or exposure of immunogenic GR domains. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 140-142 2441143-8 1987 5-20 mM sodium molybdate also shifted approximately 7 S to approximately 5 S. These results indicate that the approximately 7 S transformed form of the glucocorticoid receptor observed in low salt conditions might be an oligomer, probably including both approximately 5 S steroid-binding component and RNA/ribonucleoprotein, and that molybdate dissociates these interactions in a specific manner. Steroids 272-279 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 152-175 3558388-2 1987 A 1-h incubation of hepatic cytosol with 1-3 M urea at 0 or at 23 degrees C caused a progressive decrease in the steroid binding efficiency of GR. Steroids 113-120 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 143-145 3558388-8 1987 These results suggest that urea is a potent in vitro modulator of the physicochemical behavior of GR, influencing both the steroid binding and the process of receptor transformation. Steroids 123-130 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 98-100 3016408-5 1986 All three putative domains of the GCR molecule: the steroid binding, immunoreactive, and DNA binding have been conserved between two divergent species. Steroids 52-59 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 34-37 4046600-0 1985 Formation of a fluorescent glucocorticoid receptor-steroid complex in HTC cell cytosol. Steroids 51-58 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 27-50 3707584-0 1986 Evidence for differences in the steroid binding domains of the glucocorticoid receptor versus the idiotype antibody. Steroids 32-39 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 63-86 4084295-1 1985 The kinetics of steroid binding to rat liver glucocorticoid receptor (GR) and receptor denaturation were dependent upon the nature of the molecule occupying GR. Steroids 16-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 45-68 4084295-1 1985 The kinetics of steroid binding to rat liver glucocorticoid receptor (GR) and receptor denaturation were dependent upon the nature of the molecule occupying GR. Steroids 16-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 70-72 4084295-1 1985 The kinetics of steroid binding to rat liver glucocorticoid receptor (GR) and receptor denaturation were dependent upon the nature of the molecule occupying GR. Steroids 16-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 157-159 3486322-6 1986 Four steroids had an affinity for the glucocorticoid receptor higher than for the androgen receptor. Steroids 5-13 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 38-61 3486322-7 1986 The assumption is made that the steroids tested also behave as antagonists when binding to the glucocorticoid receptor in muscle and behave as agonists when binding to the androgen receptor. Steroids 32-40 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 95-118 3486322-9 1986 These indices might be of predictive value to determine whether these steroids exert their anabolic action in muscle through the glucocorticoid receptor or through the androgen receptor. Steroids 70-78 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 129-152 3543532-2 1986 In studies combining physicochemical separation methods with antibody methodology, we established that the molybdate-stabilised GR contains one steroid-binding monomer. Steroids 144-151 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 128-130 4063391-3 1985 The new glucocorticoid-binding protein, Peak C, was characterized by Scatchard analysis and competition with other steroids as a glucocorticoid receptor. Steroids 115-123 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 129-152 4046600-5 1985 This appears to be the first report of a fluorescent glucocorticoid receptor-steroid complex. Steroids 77-84 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 53-76 4020434-3 1985 Cultured chromaffin cells were found to have a cytosolic, high affinity, saturable glucocorticoid-binding protein with the steroid specificity of a classical glucocorticoid receptor and a Kd of approximately 1 nM. Steroids 123-130 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 158-181 3972844-11 1985 Our results indicate that rat liver glucocorticoid receptor is a phosphoprotein and that both the phosphorylated peptides 90K and 45K also contain the steroid and the DNA binding regions of the glucocorticoid receptor. Steroids 151-158 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 36-59 3858857-1 1985 The Mr 94,000 steroid binding component of rat hepatic glucocorticoid receptor purified 5000-fold under-goes calcium-stimulated phosphorylation in vitro by [gamma-32P]ATP. Steroids 14-21 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 55-78 3858857-7 1985 Phosphorylation of the glucocorticoid receptor is steroid dependent. Steroids 50-57 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 23-46 3972844-11 1985 Our results indicate that rat liver glucocorticoid receptor is a phosphoprotein and that both the phosphorylated peptides 90K and 45K also contain the steroid and the DNA binding regions of the glucocorticoid receptor. Steroids 151-158 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 194-217 6747497-0 1984 Effect of adrenalectomy and steroid treatment on rat skin cytosol glucocorticoid receptor. Steroids 28-35 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 66-89 3965467-5 1985 In this paper we show that NADPH-dependent conversion of the rat liver glucocorticoid receptor from a nonbinding to a steroid-binding form is blocked in an immune-specific manner by antisera raised against purified rat liver thioredoxin reductase or thioredoxin. Steroids 118-125 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 71-94 6529586-0 1984 Comparison of DNA binding properties of activated, covalent and noncovalent glucocorticoid receptor-steroid complexes from HTC cells. Steroids 100-107 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 76-99 6529586-1 1984 Several differences in the interaction with DNA of noncovalent vs. covalent glucocorticoid receptor-steroid complexes are described. Steroids 100-107 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 76-99 6503050-6 1984 These results suggest that the number of nuclear binding sites of the glucocorticoid-receptor complex depends on the ligand steroid which is bound to the receptor of the cytoplasmic fraction and may be involved in physiological and pharmacological potencies of the glucocorticoid in addition to the affinity of the glucocorticoid to the receptor. Steroids 124-131 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 70-93 6747497-1 1984 Using an exchange assay to measure occupied and unoccupied binding sites, the glucocorticoid receptor in rat skin cytosol has been measured after adrenalectomy and parenteral steroid administration. Steroids 175-182 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 78-101 6307658-2 1983 One of the ways to study Type I receptors isolated from Type II receptors is to block the latter with a steroid which shows high affinity for the glucocorticoid receptor and low affinity for the mineralocorticoid receptor. Steroids 104-111 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 146-169 6626981-7 1983 The effect of the steroid seemed related to the extent of occupation of the pool of glucocorticoid receptor sites in cytosol of rat hippocampus. Steroids 18-25 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 84-107 6726343-9 1984 Taken together, our findings indicate that the glucocorticoid receptor deficit in the Brattleboro rat probably represents a vasopressin-influenced defect in the synthesis or degradation of the receptor, whereas in the aged rat the deficit originates from loss of both receptor per neuron and the steroid-concentrating neurons themselves, and thus is most likely a permanent and pharmacologically insensitive deficit. Steroids 296-303 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 47-70 7075758-0 1982 [Effect of transformed steroid compounds on mRNA synthesis and glucocorticoid-receptor interaction in thymocytes of adrenalectomized rats]. Steroids 23-30 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 63-86 7096539-4 1982 The free glucocorticoid receptor-binding activity was determined by the extent to which steroids present in the sample inhibit binding of the 3H-labeled steroids. Steroids 88-96 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 9-32 7096539-4 1982 The free glucocorticoid receptor-binding activity was determined by the extent to which steroids present in the sample inhibit binding of the 3H-labeled steroids. Steroids 153-161 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 9-32 6181503-0 1982 Immunochemical analysis of the glucocorticoid receptor: identification of a third domain separate from the steroid-binding and DNA-binding domains. Steroids 107-114 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 31-54 6181503-9 1982 The immunoactive domain could be separated from the half of the glucocorticoid receptor containing the steroid-binding and the DNA-binding domains (Stokes radius, 3.3 nm), by limited proteolysis of the receptor by alpha-chymotrypsin followed by gel filtration or chromatography on DNA-cellulose. Steroids 103-110 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 64-87 6308415-5 1983 Since there is some evidence that ATP may bind to glucocorticoid receptor, our findings indicate that an ATP-receptor complex may be essential for steroid binding. Steroids 147-154 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 50-73 7173118-0 1982 Effect of transformed steroid compounds on mRNA synthesis and glucocorticoid-receptor interaction in the thymocytes of adrenalectomized rats. Steroids 22-29 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 62-85 7245288-3 1981 The former in low concentration dissociates the steroid from the glucocorticoid receptor complex in relatively short time. Steroids 48-55 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 65-88 6974862-4 1981 Almost all the steroids inhibiting 3H-uridine incorporation into RNA, competed actively with triamcinolone acetonide, concerning thymocyte cytosol binding with glucocorticoid receptor. Steroids 15-23 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 160-183 6113950-3 1981 We conclude that the steroidal inhibition of amino acid transport, at steroid concentrations of 10(-5) M or less is mediated by the same glucocorticoid receptor mechanisms as the induction of tyrosine aminotransferase. Steroids 21-28 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 137-160 173716-0 1976 Interaction of glucocorticoid receptor-steroid complexes with acceptor sites. Steroids 39-46 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 15-38 7288743-6 1981 The uterine glucocorticoid receptor exhibited the appropriate steroid specificity. Steroids 62-69 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 12-35 474286-5 1979 In the present study, the smallest fragment of the glucocorticoid receptor containing the steroid-binding site, the mero-receptor, was characterized with respect to the Stokes radius (RS = 23 +/- 3 A) and the isoelectric point (pI = 5.9 at 4 degrees). Steroids 90-97 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 51-74 189839-3 1977 Additional results suggest the existence of two forms of the activated glucocorticoid receptor-steroid complex in about equal amounts: one form binds only to nuclei and the other binds to DNA and nuclei. Steroids 95-102 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 71-94 189840-0 1977 Glucocorticoid receptor-steroid complex binding to DNA. Steroids 24-31 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 0-23 189840-2 1977 The binding of the glucocorticoid receptor-steroid complex from a line of rat hepatoma tissue culture (HTC) cells to DNA has been examined. Steroids 43-50 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 19-42 7470080-6 1980 The steroid-binding properties of glucocorticoid receptor remained intact under the above conditions. Steroids 4-11 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 34-57 168296-0 1975 Proceedings: The role of SH-groups in the interaction of steroids with the cytoplasmic glucocorticoid receptor from rat thymus. Steroids 57-65 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 87-110 173192-0 1975 Interaction of anabolic steroids with glucocorticoid receptor sites in rat muscle cytosol. Steroids 24-32 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 38-61 170996-0 1975 The involvement of receptro sulphydryl groups in the binding of steroids to the cytoplasmic glucocorticoid receptor from rat thymus. Steroids 64-72 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 92-115 170996-1 1975 The glucocorticoid receptor protein present in the high-speed supernant fraction of rat thymus tissue is extremely unstable, having a half-life of about 2 h at 4 degrees C. It was found that the decline in steroid-binding capacity could be slowed, though not arrested completely, by the addition of sulphydryl-protecting agents such as 2-mercaptoethanol or dithiothreitol, and by EDTA. Steroids 206-213 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 4-27 33007359-2 2020 The MR is a steroid receptor in the same family as the glucocorticoid receptor, with which it shares the ligand corticosterone in addition to the MR selective ligand aldosterone. Steroids 12-19 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 55-78 31263381-0 2019 Computational and Biological Comparisons of Plant Steroids as Modulators of Inflammation through Interacting with Glucocorticoid Receptor. Steroids 50-58 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 114-137 31990732-2 2020 Clinically used steroids target the glucocorticoid receptor (GR) for its anti-inflammatory effects. Steroids 16-24 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 36-59 31990732-2 2020 Clinically used steroids target the glucocorticoid receptor (GR) for its anti-inflammatory effects. Steroids 16-24 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 61-63 31990732-15 2020 The observed downregulation of the GR in sensory neurons may have a significant impact on the use of steroids as treatment in these conditions and on the regulatory effects of endogenous glucocorticoids. Steroids 101-109 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 35-37 30524245-1 2018 Low back pain, a leading cause of disability, is commonly treated by epidural steroid injections that target the anti-inflammatory glucocorticoid receptor (GR). Steroids 78-85 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 131-154 30524245-1 2018 Low back pain, a leading cause of disability, is commonly treated by epidural steroid injections that target the anti-inflammatory glucocorticoid receptor (GR). Steroids 78-85 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 156-158 30524245-12 2018 The results suggest that EPL may enhance the effectiveness of clinically used epidural steroid injections, in part by enhancing the availability of the GR. Steroids 87-94 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 152-154 30524245-13 2018 Thus, the glucocorticoid-mineralocorticoid interactions may limit the effectiveness of epidural steroids through the regulation of the GR in the DRG. Steroids 96-104 nuclear receptor subfamily 3, group C, member 1 Rattus norvegicus 135-137