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GraphPad Software Inc prism 5.01 dose response-special-allosteric ec 50 shift
<t>Allosteric</t> EC50 shifts of endomorphin-1-stimulated β-arrestin recruitment in CHO-μ PathHunter cells in the presence of increasing concentrations of PAM: MS1 (A), MS2 (B), MS3 (C), and BMS-986121 (D). Kb = calculated binding affinity of PAM to free receptor; α = allosteric cooperativity factor.
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Allosteric EC50 shifts of endomorphin-1-stimulated β-arrestin recruitment in CHO-μ PathHunter cells in the presence of increasing concentrations of PAM: MS1 (A), MS2 (B), MS3 (C), and BMS-986121 (D). Kb = calculated binding affinity of PAM to free receptor; α = allosteric cooperativity factor.

Journal: Journal of chemical information and modeling

Article Title: Ligand-Based Discovery of a New Scaffold for Allosteric Modulation of the μ -Opioid Receptor

doi: 10.1021/acs.jcim.5b00388

Figure Lengend Snippet: Allosteric EC50 shifts of endomorphin-1-stimulated β-arrestin recruitment in CHO-μ PathHunter cells in the presence of increasing concentrations of PAM: MS1 (A), MS2 (B), MS3 (C), and BMS-986121 (D). Kb = calculated binding affinity of PAM to free receptor; α = allosteric cooperativity factor.

Article Snippet: Y = bottom + (top − bottom)/(1 + 10 ((logEC 50 − X )×Hill slope) ) (1) The β -arrestin curve shift assays in were analyzed using an allosteric ternary complex model (Graphpad Prism 5.01 Dose response-Special-Allosteric EC 50 shift), to determine log K b and the cooperativity factor ( α ) of the PAMs. fig ft0 fig mode=article f1 fig/graphic|fig/alternatives/graphic mode="anchored" m1 Open in a separate window caption a7 Allosteric EC 50 shifts of endomorphin-1-stimulated β -arrestin recruitment in CHO- μ PathHunter cells in the presence of increasing concentrations of PAM: MS1 (A), MS2 (B), MS3 (C), and BMS-986121 (D).

Techniques: Binding Assay