Perturbation of benzodiazepine receptor binding by pyrazolopyridines involves picrotoxinin/barbiturate receptor sites
نویسندگان
چکیده
منابع مشابه
Optimum Conditions of Radioligand Receptor Binding Assay of Ligands of Benzodiazepine Receptors
To obtain drugs which are more selective at benzodiazepine (BZD) receptors, design and synthesis of functionally selective ligands for BZD receptors is the current strategy of our pharmaceutical chemistry department. The affinity of newly synthesized ligands is assessed by radioligand receptor binding assays. Based on our previous studies, 2-phenyl-5-oxo-7-methyl-1,3,4-oxadiazolo[a,2,3]-pyrimid...
متن کاملOptimum Conditions of Radioligand Receptor Binding Assay of Ligands of Benzodiazepine Receptors
To obtain drugs which are more selective at benzodiazepine (BZD) receptors, design and synthesis of functionally selective ligands for BZD receptors is the current strategy of our pharmaceutical chemistry department. The affinity of newly synthesized ligands is assessed by radioligand receptor binding assays. Based on our previous studies, 2-phenyl-5-oxo-7-methyl-1,3,4-oxadiazolo[a,2,3]-pyrimid...
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The ability of a variety of detergents to solubilize peripheral benzodiazepine-binding sites from rat kidney was tested. Of all the detergents tested, only digitonin was found to be suitable for solubilization. This detergent solubilized 21% of the binding activity; 47% was inactivated, and 32% remained in the pellet. Specific binding of [3H]Ro 5-4884 to membranebound and solubilized peripheral...
متن کاملFunctional regulation of the cardiac ryanodine receptor by suramin and calmodulin involves multiple binding sites.
Suramin and structurally related compounds increase not only the open probability (P(o)) of ryanodine receptor (RyR) channels but also the single-channel conductance in a unique characteristic manner. In this report, we examine the mechanisms underlying the complex changes to cardiac RyR channel function caused by suramin and the evidence that these changes result from an interaction with calmo...
متن کاملMembrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
Cotranslational protein targeting in bacteria is mediated by the signal recognition particle (SRP) and FtsY, the bacterial SRP receptor (SR). FtsY is homologous to the SRalpha subunit of eukaryotes, which is tethered to the membrane via its interaction with the membrane-integral SRbeta subunit. Despite the lack of a membrane-anchoring subunit, 30% of FtsY in Escherichia coli are found stably as...
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ژورنال
عنوان ژورنال: The Journal of Neuroscience
سال: 1981
ISSN: 0270-6474,1529-2401
DOI: 10.1523/jneurosci.01-05-00471.1981