The mammalian beta 2-adrenergic receptor: reconstitution of functional interactions between pure receptor and pure stimulatory nucleotide binding protein of the adenylate cyclase system.
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Summary
The established hormone responsive activity retains the beta 2-adrenergic specificity conferred by the pure receptor, and similar extents of stimulation are observed with pure receptor from frog erythrocytes, indicating a similar efficiency of coupling between receptors from different species and NS.
- Type
- article
- Published
- 1984-09-25
- Cited by
- 191
- References
- 24
- OpenAlex
- https://openalex.org/W2046753575
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24068164
Keywords
Receptor, Cyclase, Agonist, Adenylate kinase, GTPase
References
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- Constitutive activity of bitter taste receptors (T2Rs).
- Detecting constitutive activity and protean agonism at cannabinoid-2 receptor.
- Regulation of hormone receptors and adenylyl cyclases by guanine nucleotide binding N proteins.
- Constitutively active μ-opioid receptors.
- Reconstitution of calmodulin-sensitive adenylate cyclase from bovine brain with phospholipids, calmodulin, and beta-adrenergic receptors.
- The ins and outs of adrenergic signaling
- Molecular Determinants of Orexin Receptor Ligand Interaction : Studies on Ligand Selectivity and Impact of Calcium
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- Considerations in the evaluation of inverse agonism and protean agonism at G protein-coupled receptors.
- The 47-kD protein increased in neutrophil actin dysfunction with 47- and 89-kD protein abnormalities is lymphocyte-specific protein.
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