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Science, ISSN 0036-8075, 2/2012, Volume 335, Issue 6070, pp. 851 - 855
Journal Article
FEBS Letters, ISSN 0014-5793, 10/2015, Volume 589, Issue 20, pp. 3119 - 3125
Mutations in rhodopsin can cause misfolding and aggregation of the receptor, which leads to retinitis pigmentosa, a progressive retinal degenerative disease.... 
G protein-coupled receptor | Retinal degeneration | Membrane protein | Protein aggregation | Protein misfolding | Secondary structure | Förster resonance energy transfer | cyan fluorescent protein | circular dichroism | mTq | CFP | WT-KKYL | mTurquoise | FTIR | yellow fluorescent protein | FRET | wild-type with an ER retention sequence | wheat germ agglutinin | Fourier transform infrared | polymerase chain reaction | YFP | metarhodopsin II | MII | n-dodecyl-β-d-maltoside | WGA | retinitis pigmentosa | GPCR | wild-type | murine rhodopsin | endoplasmic reticulum | mRho | PCR | UBIQUITIN-PROTEASOME SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | SEGMENT DISC MEMBRANES | PROTEIN-COUPLED RECEPTORS | RHODOPSIN MUTATIONS | DOMINANT RETINITIS-PIGMENTOSA | CELL BIOLOGY | ORGANIZATION | XENOPUS-LAEVIS | BIOPHYSICS | THIOFLAVINE-T | DEGRADATION | AGGREGATION | Opsins - genetics | Protein Structure, Secondary | Humans | Endoplasmic Reticulum - metabolism | Retinitis Pigmentosa - genetics | Rhodopsin - metabolism | Spectroscopy, Fourier Transform Infrared | Protein Folding | Microscopy, Confocal | Animals | Opsins - chemistry | Rhodopsin - genetics | HEK293 Cells | Opsins - metabolism | Fluorescence Resonance Energy Transfer | Luminescent Proteins - genetics | Mice | Mutation | Spectrophotometry | Luminescent Proteins - metabolism | Index Medicus | BASIC BIOLOGICAL SCIENCES | secondary structure | membrane protein | retinal degeneration | protein aggregation | protein misfolding
Journal Article
Nature, ISSN 0028-0836, 12/2016, Volume 540, Issue 7634, pp. 602 - 606
The human cannabinoid G-protein-coupled receptors (GPCRs) CB1 and CB2 mediate the functional responses to the endocannabinoids anandamide and 2-arachidonyl... 
ACTIVATION | INVERSE AGONISM | PROTEIN-COUPLED RECEPTOR | AFFINITY | LIGAND COMPLEXES | MEMBRANE | DOCKING | ENDOCANNABINOIDS | MULTIDISCIPLINARY SCIENCES | BINDING | INSIGHTS | Physiological aspects | Cannabinoids | Structure | Observations | Crystals | Lipids | Nervous system | Ligands | Chemical compounds | Binding sites | Crystal structure | crystal structure | GPCR | taranabant | cannabinoid | THC
Journal Article
Pharmacology and Therapeutics, ISSN 0163-7258, 06/2015, Volume 150, pp. 129 - 142
Journal Article