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High-affinity tamoxifen analogues retain extensive positional disorder when bound to calmodulin
Using a combination of NMR and fluorescence measurements, we have investigated the structure and dynamics of the complexes formed between calcium-loaded calmodulin (CaM) and the potent breast cancer inhibitor idoxifene, a derivative of tamoxifen. High-affinity binding ( [Formula: see text] nM) satu...
Autores principales: | Milanesi, Lilia, Trevitt, Clare R., Whitehead, Brian, Hounslow, Andrea M., Tomas, Salvador, Hosszu, Laszlo L. P., Hunter, Christopher A., Waltho, Jonathan P. |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Copernicus GmbH
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10539762/ https://www.ncbi.nlm.nih.gov/pubmed/37905217 http://dx.doi.org/10.5194/mr-2-629-2021 |
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