Matches in Nanopublications for { ?s ?p "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." ?g. }
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- _6 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.
- _4 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.
- _4 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.
- _6 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.
- _6 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.
- _6 value "Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57]." provenance.