| receptors, dopamine | Cell-surface proteins that bind dopamine with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
|---|---|
| receptors, dopamine d1 | A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, by their mode of action. (12 Dec 1998) |
| receptors, dopamine d2 | A class of dopamine receptors identified by their binding profiles for synthetic ligands, their molecular biology, and, perhaps, their mode of action. (12 Dec 1998) |
| receptors, drug | Proteins that bind specific drugs with high affinity and trigger intracellular changes influencing the behaviour of cells. Drug receptors are generally thought to be receptors for some endogenous substance not otherwise specified. (12 Dec 1998) |
| receptors, eicosanoid | Cell surface proteins that bind eicosanoids with high affinity and trigger intracellular changes influencing the behaviour of cells. Among the eicosanoid receptors are receptors for the prostaglandins, thromboxanes, and leukotrienes. (12 Dec 1998) |
| receptors, endothelin | Cell surface proteins that bind endothelin with high affinity and trigger intracellular changes which influence the behaviour of cells. (12 Dec 1998) |
| receptors, epidermal growth factor-urogastrone | Glycoproteins of about 170 kD that have protein kinase activity and span the plasma membranes of growing cells, including tumours. They are activated by the binding of epidermal growth factor-urogastrone which then initiates DNA and protein synthesis. They are not found on mitotically quiescent cells except in the stomach where they control the synthesis and release of digestive enzymes and gastric acid. Transforming growth factor alpha also binds to and activates these receptors. (12 Dec 1998) |
| receptors, erythropoietin | Cell surface proteins that bind erythropoietin with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, estradiol | Cytoplasmic proteins that bind estradiol, migrate to the nucleus, and regulate DNA transcription. (12 Dec 1998) |
| receptors, fc | Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognise and combine with the fc (crystallizable) portion of immunoglobulin molecules. (12 Dec 1998) |
| receptors, fibroblast growth factor | Specific molecular sites or structures on cell membranes that react with fibroblast growth factors (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity. (12 Dec 1998) |
| receptors, fibronectin | Specific sites or molecular structures on or in cells with which fibronectins react or to which they bind. Studies have shown that these receptors function in certain types of adhesive contact as well as playing a major role in matrix assembly. These are the traditional fibronectin receptors, also called vla-5 receptors or alpha 5 beta 1 integrins. There are also other integrins that bind fibronectin, including alpha v beta 1. (12 Dec 1998) |
| receptors, fsh | Cell surface proteins that bind follicle-stimulating hormone (follitropin, fsh) with high affinity and trigger intracellular changes influencing the behaviour of cells. (12 Dec 1998) |
| receptors, gaba | Cell-surface proteins that bind gaba with high affinity and trigger changes that influence the behaviour of cells. Gaba-a receptors control chloride channels formed by the receptor complex itself. They are blocked by bicuculline and usually have modulatory sites sensitive to benzodiazepines and barbiturates. Gaba-b receptors act through g-proteins on several effector systems, are insensitive to bicuculline, and have a high affinity for l-baclofen. (12 Dec 1998) |
| receptors, gaba-a | Cell surface proteins which bind gaba and control an integral membrane chloride channel. Gaba-a receptors are the most prevalent inhibitory neurotransmitter receptors in the brain. Several isoforms have been cloned, and they belong to a superfamily which includes nicotinic receptors, glycine receptors, and 5ht-3 receptors. Most gaba-a receptors have separate modulatory sites sensitive to benzodiazepines and to barbiturates. (12 Dec 1998) |