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- W2079543349 abstract "The coexistence of ERα and ERβ suggests that active receptor complexes are present as homo- or heterodimers. In addition each of three forms of active receptors may trigger different cellular responses. A real-time biosensor based on surface plasmon resonance was used as instrument to determine binding kinetics of homo- and heterodimerization of estrogen receptor α and β. Partially purified full-length estrogen receptor α was expressed intracellularly as a C-terminal fusion to a hexa-histidine tag using the baculovirus-expression system. Purified estrogen receptor α and β without tags were used as partners in the dimerization process. An association rate constant of 3.6×103 to 1.5×104 M−1 s−1 for the homodimer formation of ERα and 5.7×103 to 1.5×104 M−1 s−1 for the heterodimer formation was found assuming a pseudo first-order reaction kinetic. The equilibrium dissociation constant for homodimerization of ERα was 2.2×10−8 to 5.4×10−8 and 1.8×10−8 to 2.6×10−8 M for the heterodimer formation. The homo- and heterodimer formation was characterized by a slow association kinetics and kinetic rate constants were within the same range." @default.
- W2079543349 created "2016-06-24" @default.
- W2079543349 creator A5012851765 @default.
- W2079543349 creator A5068237857 @default.
- W2079543349 date "2003-02-01" @default.
- W2079543349 modified "2023-10-17" @default.
- W2079543349 title "Kinetic analysis of estrogen receptor homo- and heterodimerization in vitro" @default.
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- W2079543349 doi "https://doi.org/10.1016/s0960-0760(03)00023-2" @default.
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