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1.
Figure 1

Figure 1. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

Stereotactic conformation of the agonist form of the LBD of hGRα. The yellow arrow indicates the 9-amino acid sequence, 663YLCMKTLL670, which is located on helix 8. H: Helix

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
2.
Figure 4

Figure 4. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

Co-localization of hGRα and caveolin-1 in COS-7 cells expressing (4A) the wild-type hGRα (hGRαWT) or (4B) its mutant receptors or the hGRαWT in the presence of 2-Br. (4C) Addition of dexamethasone resulted in nuclear translocation of both the hGRαWT and the mutant receptors.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
3.
Figure 3

Figure 3. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

Cytoplasmic, membrane and nuclear localization of the hGRα in the COS-7 cells expressing the wild-type hGRα (hGRαWT) or the mutant receptors. Amounts of hGRα-related proteins were examined in subcellular fractionated samples with Western blotting.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
4.
Figure 6

Figure 6. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

(A) Time-course effect of dexamethasone on the AKT activity in COS-7 cells expressing the wild-type hGRα (hGRαWT) or its mutant receptors. (B) The effect of 2-Br on the AKT activity in COS-7 cells expressing the wild-type hGRα (hGRαWT) or its mutant receptors. Expression levels of the total AKT and p-Akt were examined with Western blotting.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
5.
Figure 7

Figure 7. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

Palmitoylation of wild-type hGRα and caveolin-1. Caveolin-1 incorporated 9,10-3H(N) palmitic acid, whereas the wild-type hGRα (hGRαWT) did not incorporate the tritiated substrate. Bars represent mean ± SEM of at least three independent experiments. **: P<0.01, n.s.: not significant, compared to control.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
6.
Figure 2

Figure 2. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

(A–D) Localization of the wild-type hGRα (hGRαWT) or its mutant receptors expressed in COS-7 cells in the absence or presence of dexamethasone. (E) Localization of hGRαWT in the presence of the palmitoylation inhibitor. The localization of hGRα-related proteins was examined with immunofluorescent staining. The yellow arrows point to membrane localization of hGRα. Dex: dexamethasone; i: palmitoylation inhibitor 2-Br.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.
7.
Figure 5

Figure 5. From: The Role of S-Palmitoylation of the Human Glucocorticoid Receptor (hGR) in Mediating the Nongenomic Glucocorticoid Actions.

(A) Time-course effects of dexamethasone on the MAPK activity in COS-7 cells expressing the wild-type hGRα (hGRαWT) or its mutant receptors. (B) The effect of 2-Br on the MAPK activity in COS7 cells expressing the wild-type hGRα (hGRαWT) or its mutant receptors. Expression levels of total ERK and p-ERK were examined by Western blotting.

Nicolas C. Nicolaides, et al. J Mol Biochem. ;6(1):3-12.

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