Localization and characterization of melatonin binding sites in the brain of the rabbit (Oryctolagus cuniculus) by autoradiography and in vitro ligand-receptor binding

1991 ◽  
Vol 133 (1) ◽  
pp. 68-72 ◽  
Author(s):  
Bojidar Stankov ◽  
Bruno Cozzi ◽  
Valeria Lucini ◽  
Simona Capsoni ◽  
Jan Fauteck ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Oryctolagus Cuniculus ◽  
The Brain

Localization and characterization of endothelin receptor binding sites in the rat brain visualized by in vitro autoradiography4

Neuroscience ◽  
1991 ◽  
Vol 42 (1) ◽  
pp. 245-260 ◽  
Author(s):  
M. Kohzuki ◽  
S.Y. Chai ◽  
G. Paxinos ◽  
A. Karavas ◽  
D.J. Casley ◽  
...  
Keyword(s):  
Rat Brain ◽  
Receptor Binding ◽  
Binding Sites ◽  
Endothelin Receptor

scholarly journals Design, Synthesis and Characterization of a New Series of Fluorescent Metabotropic Glutamate Receptor Type 5 Negative Allosteric Modulators

Molecules ◽  
2020 ◽  
Vol 25 (7) ◽  
pp. 1532
Author(s):  
Víctor Fernández-Dueñas ◽  
Mingcheng Qian ◽  
Josep Argerich ◽  
Carolina Amaral ◽  
Martijn D.P. Risseeuw ◽  
...  
Keyword(s):  
Binding Sites ◽  
Metabotropic Glutamate Receptor ◽  
Allosteric Modulators ◽  
Design Synthesis ◽  
Metabotropic Glutamate ◽  
Animal Disease Models ◽  
Fluorescent Ligands ◽  
The Brain

In recent years, new drug discovery approaches based on novel pharmacological concepts have emerged. Allosteric modulators, for example, target receptors at sites other than the orthosteric binding sites and can modulate agonist-mediated activation. Interestingly, allosteric regulation may allow a fine-tuned regulation of unbalanced neurotransmitter’ systems, thus providing safe and effective treatments for a number of central nervous system diseases. The metabotropic glutamate type 5 receptor (mGlu5R) has been shown to possess a druggable allosteric binding domain. Accordingly, novel allosteric ligands are being explored in order to finely regulate glutamate neurotransmission, especially in the brain. However, before testing the activity of these new ligands in the clinic or even in animal disease models, it is common to characterize their ability to bind mGlu5Rs in vitro. Here, we have developed a new series of fluorescent ligands that, when used in a new NanoBRET-based binding assay, will facilitate screening for novel mGlu5R allosteric modulators.

A comparison of in vivo and in vitro neuroimaging of 5-HT1A receptor binding sites in the cat brain

2006 ◽  
Vol 31 (3) ◽  
pp. 226-232 ◽  
Author(s):  
Nicolas Aznavour ◽  
Latifa Rbah ◽  
Lucienne Léger ◽  
Colette Buda ◽  
Jean-Pierre Sastre ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Binding Sites ◽  
Cat Brain

scholarly journals A domain of the even-skipped protein represses transcription by preventing TFIID binding to a promoter: repression by cooperative blocking.

1995 ◽  
Vol 15 (9) ◽  
pp. 4683-4693 ◽  
Author(s):  
R J Austin ◽  
M D Biggin
Keyword(s):  
Glucocorticoid Receptor ◽  
Rna Polymerase Ii ◽  
Receptor Binding ◽  
Binding Sites ◽  
In Vitro System ◽  
Cooperative Interactions ◽  
General Transcription Factors ◽  
Promoter Dna ◽  
Template Dna

We examined the mechanism by which the C-terminal 236 amino acids of the even-skipped protein (region CD) repress transcription. A fusion protein, CDGB, was created that contains region CD fused to the glucocorticoid receptor DNA binding domain. This protein repressed transcription in an in vitro system containing purified fractions of the RNA polymerase II general transcription factors, and repression was dependent upon the presence of high-affinity glucocorticoid receptor binding sites in the promoter. Repression by CDGB was prevented when the promoter DNA was preincubated with TFIID or TBP, whereas preincubation of the template DNA with CDGB prevented TFIID binding. Together, these results strongly imply that CDGB represses transcription by inhibiting TFIID binding, and further experiments suggested a mechanism by which this may occur. Region CD can mediate cooperative interactions between repressor molecules such that molecules bound at the glucocorticoid receptor binding sites stabilize binding of additional CDGB molecules to low-affinity binding sites throughout the basal promoter. Binding to some of these low-affinity sites was shown to contribute to repression. Further experiments suggested that the full-length eve protein also represses transcription by the same mechanism. We speculate that occupancy of secondary sites within the basal promoter by CDGB or the eve protein inhibits subsequent TFIID binding to repress transcription, a mechanism we term cooperative blocking.

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