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Titlebook: G Protein-Coupled Receptors in Drug Discovery; Methods and Protocol Marta Filizola Book 2015Latest edition Springer Science+Business Media

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楼主: Aggrief
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https://doi.org/10.1007/978-981-16-9061-7or. Fluorescence indicators of different sizes and chemical characteristics can provide insights into the nature of the binding environment, the surrounding structures, and even into conformational changes associated with receptor activation. Methods for determining fluorescence spectral analysis, f
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Ning Jiang,Wenbin Li,Weihang Li,Dou Hong intracellular signaling that cannot be attained using traditional methods. Here, we describe a detailed protocol for the use of high content imaging in combination with FRET biosensors to assess second messenger production and intracellular signaling in a time-effective manner. We use four differen
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https://doi.org/10.1007/978-981-97-0206-0 biased profiles. Biased ligands have different pharmacological properties on a molecular level (stabilization of different receptor active states) and thus can have different pharmacological profiles therapeutically. The calculation of transduction ratios (ΔΔlog(./..)) values (where . is efficacy a
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https://doi.org/10.1007/978-3-658-08454-7signer .rugs) have emerged as powerful new tools for the study of GPCR physiology. In this chapter, we present protocols employing adeno-associated viruses (AAVs) to express a G.-coupled DREADD (Dq) in two metabolically important cell types, AgRP neurons of the hypothalamus and hepatocytes of the li
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21. Deutscher Soziologentag 1982u, delta, and kappa. Highly selective radioligands are available for all three classes of traditional receptors. Of the three, the mu receptor undergoes extensive alternative splicing, generating a number of traditional mu receptor subtypes as well as a nontraditional, truncated set of variants asso
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https://doi.org/10.1007/978-3-642-76764-7 this pharmaceutically important target class. The quality of GPCR structures available for SBDD projects fall on a spectrum ranging from high resolution crystal structures (<2 Å), where all water molecules in the binding pocket are resolved, to lower resolution (>3 Å) where some protein residues ar
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