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The ability of calmodulin (CaM) to modify the conformation of the hormone binding domain (HBD) rat uterine estrogen receptor (ER) was investigated. Dissociation constant of estradiol (E2) binding to HBD increased almost 2-3-fold when CaM bound to ER; two other Ca(++)-binding proteins failed to show this property, demonstrating the specificity of the(More)
Binding of (3H)-estradiol labeled estrogen receptor from uterine cytosol to calmodulin was demonstrated by both affinity chromatography and sucrose gradient sedimentation. Triphenylethylene antiestrogens (tamoxifen family) with strong antagonistic activity against the calmodulin-dependent c-AMP phosphodiesterase largely reduced the binding of the receptor.(More)
Vehicular Ad-hoc Networks (VANET) are considered as a promising approach for building a variety of applications for Intelligent Transportation Systems (ITS). They are a kind of mobile networks that enables moving vehicles to exchange information about the driving environment. Although the amount of information disseminated through a VANET provides a great(More)
We previously demonstrated the ability of calmodulin (CaM) to decrease the binding affinity of estradiol (E2) to the rat uterine estrogen receptor (ER). We show now that CaM induces a loss of E2 binding capacity especially when ER molecules exhibit a lower binding affinity for the hormone. By Western blotting and [125I]tamoxifen aziridine covalent labeling(More)
Driver behavior has long been considered as particularly relevant for the development of automotive applications, especially that recently these applications are increasingly trying to adapt to the driver. However, drivers behave differently in the different traffic situations, hence the need of techniques to enable cars to learn from their drivers and(More)
Estrogen receptor (ER), antiestrogen binding sites (AEBS) and calmodulin (CaM) are potential targets of antiestrogen (AE) action. To analyse further which of these targets are primarily involved in the antiproliferative activity of these drugs against human breast cancers, two cell clones, namely the RTx6 and LY-2 variants, selected from MCF-7 cells for(More)
Previously, two antiestrogens estradiol derivatives (3 and 4) bearing the basic side chain of tamoxifen were shown to impede the binding of the estrogen receptor (ER) to calmodulin (CaM)-Sepharose. In this study, the interaction of these and related compounds with calmodulin was examined using the cyclic AMP phosphodiesterase (cAMP-PDE) assay. Neither of(More)
Calmodulin (CaM) is known to associate with the estrogen receptor (ER). The antiestrogen tamoxifen impedes this association suggesting that the latter would play an important role in CaM-dependent enzymatic catalyses. The ethoxyaminoalkyl side-chain of tamoxifen which confers antiestrogenicity appears to be involved in this antagonism. Antiestrogenic(More)
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