Agonist-receptor efficacy II: agonist trafficking of receptor signals
Public Deposited- Creator
-
Kenakin, Terry
- Other Affiliation: Department of Cellular Biochemistry, Glaxo Research Institute, Five Moore Drive, PO Box 13358, Research Triangle Park, NC 27709, USA
- Abstract
- There is evidence to suggest that receptors with seven transmembrane domains can exist in G protein-activating conformations. It is not known how many activated receptor forms exist for each receptor. Furthermore, if there are multiple forms, does the chemical structure of the agonist determine which form dominates, and therefore, which response pathway is activated? This latter scheme is referred to as agonist-receptor trafficking, and is discussed in this, the second of two articles by Terry Kenakin. One way to approach these questions is to study receptors that couple to more than one G protein and, in essence, to try to allow the G protein to indicate the receptor state.
- Date of publication
- 1995
- Keyword
- [4 [(3 chlorophenyl)carbamoyloxy] 2 butynyl]trimethylammonium
- guanine nucleotide binding protein
- short survey
- preclamol
- Cell Surface
- agonist
- acetylcholine
- Receptors
- nonhuman
- priority journal
- protein conformation
- oxymetazoline
- pilocarpine
- substance p
- GTP-Binding Proteins
- carbachol
- theory Animal
- signal transduction
- quinpirole
- conformational transition
- protein domain
- receptor occupancy
- 7 diphenylperhydroisoindol 4 one
- Signal Transduction
- adrenalin
- 2 [1 imino 2 (2 methoxyphenyl)ethyl] 7
- drug potency
- drug receptor binding
- concentration response
- septide
- DOI
- Identifier
- https://doi.org/10.1016/S0165-6147(00)89032-X
- 2-s2.0-0029054965
- Related resource URL
- Resource type
- Article
- Rights statement
- In Copyright
- Journal title
- Trends in Pharmacological Sciences
- Journal volume
- 16
- Journal issue
- 7
- Page start
- 232
- Page end
- 238
- Language
- English
- Version
- Postprint
- ISSN
- 0165-6147
Relations
- Parents:
This work has no parents.
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