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Distant metastasis, which results in >90% of cancer-related deaths, is enabled by hematogenous dissemination of tumor cells via the circulation. This requires the completion of a sequence of complex steps including transit, initial arrest, extravasation, survival and proliferation. Increased understanding of the cellular and molecular players enabling each(More)
To understand the function of cysteines, we have substituted cysteines 638, 643, and 665 by serine in the hormone-binding domain (HBD) of the human glucocorticoid receptor (hGR). In hormone-binding assays using [3H]dexamethasone, hGR C643S and hGR C665S exhibited wild type receptor Kd of 2.5 nM and hGR C665SM666L displayed a Kd of 3.7 nM, while hGR C638S(More)
To determine the importance of specific amino acids in the hormone-binding domain of the human glucocorticoid receptor (hGR), we have generated mutants M565R, G567A, and A573Q. In hormone binding assays using [3H]cortisol, half-maximal saturation of dexamethasone competition was achieved at 10 pM with hGR M565R and hGRA573Q compared to 10 nM with wild type(More)
Scanning of the mRNA transcript by the preinitiation complex (PIC) requires a panel of eukaryotic initiation factors, which includes eIF1 and eIF1A, the main transducers of stringent AUG selection. eIF1A plays an important role in start codon recognition; however, its molecular contacts with eIF5 are unknown. Using nuclear magnetic resonance, we unveil(More)
We have established and characterized four human androgen receptor (AR) mutants, AR C560F, C560W, C560Y, C560S). To assess the functional significance of these substitutions, we compared the transcriptional activation, hormone binding affinity, receptor-DNA interaction, and the subcellular distribution of the hormone-receptor complexes. Binding studies(More)
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