"Receptors, Epoprostenol" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Cell surface receptors for EPOPROSTENOL. They are coupled to HETEROTRIMERIC G-PROTEINS.
| Descriptor ID |
D044006
|
| MeSH Number(s) |
D12.776.543.750.695.200.700.299
|
| Concept/Terms |
Receptors, Epoprostenol- Receptors, Epoprostenol
- Epoprostenol Receptors
- PGI2 Receptors
- Receptors, PGI2
- Prostaglandin I2 Receptors
- Receptors, Prostaglandin I2
- Receptors, Prostacyclin
- Prostacyclin Receptors
- Receptor, Prostaglandin I2
- Prostaglandin I2 Receptor
- Prostacyclin Receptor
- Receptor, Prostacyclin
- PGI2 Receptor
- Receptor, PGI2
- Prostaglandins X Receptors
- Receptors, Prostaglandins X
|
Below are MeSH descriptors whose meaning is more general than "Receptors, Epoprostenol".
Below are MeSH descriptors whose meaning is more specific than "Receptors, Epoprostenol".
This graph shows the total number of publications written about "Receptors, Epoprostenol" by people in this website by year, and whether "Receptors, Epoprostenol" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2002 | 0 | 1 | 1 |
| 2003 | 0 | 1 | 1 |
| 2005 | 2 | 0 | 2 |
| 2006 | 1 | 2 | 3 |
| 2007 | 2 | 1 | 3 |
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Below are the most recent publications written about "Receptors, Epoprostenol" by people in Profiles.
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A profile of the residues in the second extracellular loop that are critical for ligand recognition of human prostacyclin receptor. FEBS J. 2008 Jan; 275(1):128-37.
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Prostacyclin receptor signaling and early embryo development in the mouse. Hum Reprod. 2007 Nov; 22(11):2851-6.
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The role of the prostacyclin receptor antagonist RO3244019 in treating neurogenic detrusor overactivity after spinal cord injury in rats. BJU Int. 2007 Feb; 99(2):442-6.
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Characterization of the molecular mechanisms of the coupling between intracellular loops of prostacyclin receptor with the C-terminal domain of the Galphas protein in human coronary artery smooth muscle cells. Arch Biochem Biophys. 2006 Oct 01; 454(1):80-8.
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Solution structure of the first intracellular loop of prostacyclin receptor and implication of its interaction with the C-terminal segment of G alpha s protein. Biochemistry. 2006 Feb 14; 45(6):1734-44.
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Implications of the molecular basis of prostacyclin biosynthesis and signaling in pharmaceutical designs. Curr Pharm Des. 2006; 12(8):925-41.
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A strategy using NMR peptide structures of thromboxane A2 receptor as templates to construct ligand-recognition pocket of prostacyclin receptor. BMC Biochem. 2005 Nov 04; 6:23.
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A profile of the residues in the first intracellular loop critical for Gs-mediated signaling of human prostacyclin receptor characterized by an integrative approach of NMR-experiment and mutagenesis. Biochemistry. 2005 Aug 30; 44(34):11389-401.
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Evidence of the residues involved in ligand recognition in the second extracellular loop of the prostacyclin receptor characterized by high resolution 2D NMR techniques. Arch Biochem Biophys. 2003 Oct 01; 418(1):25-33.
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Prostacyclin is an autocrine regulator in the contraction of oviductal smooth muscle. Hum Reprod. 2002 Dec; 17(12):3053-9.