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9-methyl group (38) 38
biochemistry & molecular biology (30) 30
animals (25) 25
index medicus (18) 18
rhodopsin (18) 18
rhodopsin - chemistry (13) 13
cattle (12) 12
humans (12) 12
retinaldehyde - chemistry (12) 12
bovine rhodopsin (11) 11
chromophore (11) 11
schiff-base (11) 11
retinaldehyde - metabolism (10) 10
bacteriorhodopsin (9) 9
protein conformation (9) 9
spectrophotometry, ultraviolet (9) 9
analysis (7) 7
bacteriorhodopsins - chemistry (7) 7
biophysics (7) 7
hydrogen bonding (7) 7
light (7) 7
metarhodopsin-ii (7) 7
models, molecular (7) 7
photochemistry (7) 7
research (7) 7
retinaldehyde - analogs & derivatives (7) 7
spectroscopy (7) 7
transducin activation (7) 7
mutagenesis, site-directed (6) 6
mutation (6) 6
protein-coupled receptor (6) 6
proteins (6) 6
protons (6) 6
rhodopsin - metabolism (6) 6
stereoisomerism (6) 6
activation (5) 5
bacteriorhodopsins - genetics (5) 5
chemical properties (5) 5
genetic structures (5) 5
pharmacology & pharmacy (5) 5
photocycle (5) 5
retinal pigments - metabolism (5) 5
rhodopsin - genetics (5) 5
sense organs (5) 5
spectroscopy, fourier transform infrared (5) 5
structural-changes (5) 5
transducin - metabolism (5) 5
tryptophan - chemistry (5) 5
amino acids (4) 4
binding-site (4) 4
chemistry, medicinal (4) 4
chemistry, organic (4) 4
crystal-structure (4) 4
halobacterium-halobium (4) 4
hydrogen-ion concentration (4) 4
protein structure, secondary (4) 4
proton translocation (4) 4
proton uptake (4) 4
tryptophan (4) 4
visual pigment (4) 4
visual pigments (4) 4
9-methyl-beta-carboline (3) 3
angstrom resolution (3) 3
bacteriorhodopsins - metabolism (3) 3
binding sites (3) 3
biochemistry (3) 3
carbolines - pharmacology (3) 3
cell line, tumor (3) 3
cercopithecus aethiops (3) 3
cos cells (3) 3
energy-storage (3) 3
halobacterium salinarum - chemistry (3) 3
isomerism (3) 3
l-intermediate (3) 3
ligands (3) 3
membrane proteins - chemistry (3) 3
molecular structure (3) 3
molecular-dynamics (3) 3
neurosciences (3) 3
opsin (3) 3
phenylalanine - genetics (3) 3
pigments (3) 3
quantum theory (3) 3
regeneration (3) 3
retina (3) 3
retinal chromophore (3) 3
retinal cone photoreceptor cells - metabolism (3) 3
retinaldehyde - genetics (3) 3
rhodopsin - agonists (3) 3
schiff bases (3) 3
schiff-base counterion (3) 3
side-chain conformation (3) 3
signaling states (3) 3
spectra (3) 3
spectrophotometry (3) 3
steric interaction (3) 3
structure-activity relationship (3) 3
temperature (3) 3
visual pigment analogs (3) 3
vitamin-a (3) 3
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1. Full Text Intramolecular and Intermolecular Contributions to the Barriers for Rotation of Methyl Groups in Crystalline Solids: Electronic Structure Calculations and Solid-State NMR Relaxation Measurements
by Wang, Xianlong and Beckmann, Peter A and Mallory, Clelia W and Rheingold, Arnold L and DiPasquale, Antonio G and Carroll, Patrick J and Mallory, Frank B
The Journal of Organic Chemistry, ISSN 0022-3263, 07/2011, Volume 76, Issue 13, pp. 5170 - 5176
The rotation barriers for 10 different methyl groups in five methyl-substituted phenanthrenes and three methyl-substituted naphthalenes were determined by ab... 
SPIN-LATTICE-RELAXATION | METHYLPHENANTHRENES | ENERGY | 9-METHYL | INTERNAL-ROTATION | CHEMISTRY, ORGANIC | X-RAY-DIFFRACTION | SYSTEMS | REORIENTATION | MOLECULES | Naphthalenes - chemistry | Phenanthrenes - chemistry | Quantum Theory | Magnetic Resonance Spectroscopy | Stereoisomerism | Molecular Conformation | Crystallization | Molecular Structure | Rotation | Electrons | Molecular rotation | Naphthalene | Analysis | Methyl groups | Crystals | Atomic properties | Structure
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2. Full Text Complex binding pathways determine the regeneration of mammalian green cone opsin with a locked retinal analogue
by Alexander, Nathan S and Katayama, Kota and Sun, Wenyu and Salom, David and Gulati, Sahil and Zhang, Jianye and Mogi, Muneto and Palczewski, Krzysztof and Jastrzebska, Beata
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 26, pp. 10983 - 10997
Phototransduction is initiated when the absorption of light converts the 11-cis-retinal chromophore to its all-trans configuration in both rod and cone... 
COLOR-VISION | 9-METHYL GROUP | VISUAL PIGMENTS | CRYSTAL-STRUCTURE | HUMAN RED | BIOCHEMISTRY & MOLECULAR BIOLOGY | MOUSE MODEL | RPE65 MUTATIONS | MOLECULAR-DYNAMICS SIMULATIONS | COUPLED RECEPTOR RHODOPSIN | 9-CIS-RETINYL ACETATE | Sf9 Cells | Animals | Opsins - chemistry | Opsins - genetics | Humans | Opsins - metabolism | Models, Molecular | Retinaldehyde - chemistry | Retinaldehyde - metabolism | Retinaldehyde - genetics | Spodoptera | Index Medicus | rhodopsin | G protein-coupled receptor (GPCR) | Protein Structure and Folding | membrane protein | retinoid | photoreceptor
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3. Full Text Photoactivation-induced instability of rhodopsin mutants T4K and T17M in rod outer segments underlies retinal degeneration in X. laevis transgenic models of retinitis pigmentosa
by Tam, Beatrice M and Noorwez, Syed M and Kaushal, Shalesh and Kono, Masahiro and Moritz, Orson L
Journal of Neuroscience, ISSN 0270-6474, 10/2014, Volume 34, Issue 40, pp. 13336 - 13348
Retinitis pigmentosa (RP) is an inherited neurodegenerative disease involving progressive vision loss, and is often linked to mutations in the rhodopsin gene.... 
Instability | Rhodopsin | Glycosylation | Misfolding | Cell death | Retinitis pigmentosa | cell death | CRYSTAL-STRUCTURE | glycosylation | GENE MUTATION | NEUROSCIENCES | misfolding | VITAMIN-A | rhodopsin | XENOPUS-LAEVIS | 9-METHYL GROUP | PROTEIN-COUPLED RECEPTOR | instability | MOUSE MODEL | IN-VIVO | retinitis pigmentosa | MONOCLONAL-ANTIBODIES | OPSIN MUTANT | Retinal Degeneration - diet therapy | Animals, Genetically Modified | Humans | Xenopus laevis | Cercopithecus aethiops | Retinitis Pigmentosa - genetics | Retinal Degeneration - etiology | Wheat Germ Agglutinins - metabolism | Mutation - genetics | Vitamin A - administration & dosage | Vitamin A - metabolism | Microscopy, Confocal | Animals | Rhodopsin - genetics | Transfection | Analysis of Variance | Retinitis Pigmentosa - complications | Light | Statistics, Nonparametric | Rod Cell Outer Segment - pathology | COS Cells | Retinitis Pigmentosa - pathology | Disease Models, Animal
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4. Full Text Mechanism by which Untwisting of Retinal Leads to Productive Bacteriorhodopsin Photocycle States
by Wolter, Tino and Elstner, Marcus and Fischer, Stefan and Smith, Jeremy C and Bondar, Ana-Nicoleta and Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
The Journal of Physical Chemistry B, ISSN 1520-6106, 02/2015, Volume 119, Issue 6, pp. 2229 - 2240
Relaxation of the twisted-retinal photoproduct state triggers proton-coupled reaction cycle in retinal proteins. Given the crowded protein environments in... 
MOLECULAR-DYNAMICS | PRIMARY PROTON-TRANSFER | 9-METHYL GROUP | RESOLVED FTIR SPECTROSCOPY | STRUCTURAL-CHANGES | CHEMISTRY, PHYSICAL | SCHIFF-BASE | ENERGY-STORAGE | WATER-MOLECULES | L-INTERMEDIATE | LOW-TEMPERATURE | Quantum Theory | Temperature | Movement | Stereoisomerism | Bacteriorhodopsins - metabolism | Retinaldehyde - chemistry | Protein Conformation | Retinaldehyde - metabolism | Bacteriorhodopsins - chemistry | Molecular Dynamics Simulation | Photochemical Processes | Rhodopsin | Chemical properties | Electric properties | BASIC BIOLOGICAL SCIENCES
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5. Full Text Photocycle of Sensory Rhodopsin II from Halobacterium salinarum (HsSRII): Mutation of D103 Accelerates M Decay and Changes the Decay Pathway of a 13‐cis O‐like Species
by Dai, Gang and Geng, Xiong and Chaoluomeng and Tamogami, Jun and Kikukawa, Takashi and Demura, Makoto and Kamo, Naoki and Iwasa, Tatsuo
Photochemistry and Photobiology, ISSN 0031-8655, 07/2018, Volume 94, Issue 4, pp. 705 - 714
Aspartic acid 103 (D103) of sensory rhodopsin II from Halobacterium salinarum (HsSRII, or also called phoborhodopsin) corresponds to D115 of bacteriorhodopsin... 
9-METHYL GROUP | BIOPHYSICS | PRIMARY PHOTOPRODUCT | PHOTOCHEMICAL-REACTION CYCLE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | PHOTOREACTION CYCLE | RETINAL BINDING POCKET | PROTON UPTAKE | NEGATIVE PHOTOTAXIS | PHARAONIS PHOBORHODOPSIN | LOW-TEMPERATURE SPECTROPHOTOMETRY | Cold Temperature | Spectroscopy, Fourier Transform Infrared | Halobacterium salinarum - chemistry | Sensory Rhodopsins - chemistry | Halorhodopsins - chemistry | Photochemical Processes | Hydrogen Bonding | Photolysis | Light | Aspartic Acid - chemistry | Mutation | Amino Acid Substitution | Asparagine - chemistry | Glutamic Acid - chemistry | Bacteriorhodopsin | Amino acids | Rhodopsin | Genetic aspects | Glutamate | Analysis | Glutamic acid | Rhodopsin II | Decay rate | Substitution reactions | Recovery | Acids | Decay | Asparagine | Aspartic acid | Species
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6. Full Text Efficiencies of Activation of Transducin by Cone and Rod Visual Pigments
by Imamoto, Yasushi and Seki, Ichirota and Yamashita, Takahiro and Shichida, Yoshinori
Biochemistry, ISSN 0006-2960, 04/2013, Volume 52, Issue 17, pp. 3010 - 3018
How the light-induced transducin (Gt) activation process differs biochemically between cone visual pigments and rod visual pigment (rhodopsin) has remained... 
ALPHA-SUBUNITS | FLUORESCENCE SPECTROSCOPY | CONFORMATIONAL-CHANGES | 9-METHYL GROUP | CHICKEN GREEN | BIOCHEMISTRY & MOLECULAR BIOLOGY | PHOTORECEPTOR MEMBRANES | RHODOPSIN | AMINO-ACID-RESIDUES | METARHODOPSIN-II | MOLECULAR-PROPERTIES | Hydrolysis | Retinal Pigments - metabolism | Animals | Chickens | Fluorescence | Transducin - metabolism | Retinal Rod Photoreceptor Cells - metabolism | Retinal Cone Photoreceptor Cells - metabolism | Usage | Analysis | Conformational analysis | Research | Enzyme activation | Protein binding
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7. Full Text Rod and cone visual pigments and phototransduction through pharmacological, genetic, and physiological approaches
by Kefalov, Vladimir J
Journal of Biological Chemistry, ISSN 0021-9258, 01/2012, Volume 287, Issue 3, pp. 1635 - 1641
Activation of the visual pigment by light in rod and cone photoreceptors initiates our visual perception. As a result, the signaling properties of visual... 
9-METHYL GROUP | NIGHT BLINDNESS | FRIEDENWALD-LECTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | VERTEBRATE PHOTORECEPTORS | DARK-ADAPTATION | OPSIN ACTIVATION | KNOCKOUT MICE | RETINOID-BINDING PROTEIN | ZEBRAFISH RETINA | OUTER SEGMENTS | Vision, Ocular - physiology | Animals | Humans | Retinal Cone Photoreceptor Cells - cytology | Retinal Rod Photoreceptor Cells - cytology | Retinal Rod Photoreceptor Cells - physiology | Opsins - metabolism | Retinal Cone Photoreceptor Cells - physiology | Signal Transduction - physiology | Retinaldehyde - metabolism | Visual Cycle | G Protein-coupled Receptors (GPCR) | Phototransduction | Rhodopsin | Cones | Visual Pigment | 11-cis-Retinal | Vision | Minireviews | Photoreceptors | Rods
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8. Full Text 9-Demethylrhodopsin: Theoretical Evidence for a Relaxed Batho Intermediate
by Sugihara, Minoru and Buss, Volker
Biochemistry, ISSN 0006-2960, 12/2008, Volume 47, Issue 52, pp. 13733 - 13735
The 9-methyl group of retinal is crucial for the photoreaction of rhodopsin. On the basis of the results of QM/MM simulations, we propose that the primary... 
ORIGIN | ACTIVATION | 9-METHYL GROUP | RETINAL CHROMOPHORE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHODOPSIN | BOND | Models, Chemical | Models, Biological | Retinaldehyde - chemistry | Protein Conformation | Structure-Activity Relationship | Energy Transfer | Binding Sites | Photochemistry | Rhodopsin - chemistry | Rhodopsin | Chromophores | Chemical properties | Structure | Methyl groups
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9. Full Text The Action of 11-cis-Retinol on Cone Opsins and Intact Cone Photoreceptors
by Petri Ala-Laurila and M. Carter Cornwall and Rosalie K. Crouch and Masahiro Kono
Journal of Biological Chemistry, ISSN 0021-9258, 06/2009, Volume 284, Issue 24, pp. 16492 - 16500
11- cis -Retinol has previously been shown in physiological experiments to promote dark adaptation and recovery of photoresponsiveness of bleached salamander... 
SALAMANDER | ROD PHOTORECEPTORS | ACTIVATION | 9-METHYL GROUP | REGENERATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DARK-ADAPTATION | RETINA | VISUAL-PIGMENT | PHOTOTRANSDUCTION | CYCLE | Vitamin A - pharmacology | Retinal Pigment Epithelium - metabolism | Humans | Cone Opsins - metabolism | Dark Adaptation - physiology | Retinal Rod Photoreceptor Cells - metabolism | Vitamins - pharmacology | Cone Opsins - agonists | Animals | Cell-Free System | Drug Inverse Agonism | Rod Opsins - metabolism | Ambystoma | Retinal Cone Photoreceptor Cells - drug effects | Retinal Cone Photoreceptor Cells - metabolism | Retinal Rod Photoreceptor Cells - drug effects | Dark Adaptation - drug effects | Index Medicus | Mechanisms of Signal Transduction
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10. Full Text Crystal Structure of the L Intermediate of Bacteriorhodopsin: Evidence for Vertical Translocation of a Water Molecule during the Proton Pumping Cycle
by Kouyama, Tsutomu and Nishikawa, Taichi and Tokuhisa, Takeshi and Okumura, Hideo
Journal of Molecular Biology, ISSN 0022-2836, 2004, Volume 335, Issue 2, pp. 531 - 546
For structural investigation of the L intermediate of bacteriorhodopsin, a 3D crystal belonging to the space group P622 was illuminated with green light at 160... 
X-ray crystallography | retinal | proton pump | radiation damage | reaction intermediate | Reaction intermediate | Proton pump | Retinal | Radiation damage | N-INTERMEDIATE | CHROMOPHORE | 3-DIMENSIONAL CRYSTAL | BIOCHEMISTRY & MOLECULAR BIOLOGY | MEMBRANE-PROTEIN | x-ray crystallography | ANGSTROM RESOLUTION | 9-METHYL GROUP | M-STATE | PHOTOCYCLE | SCHIFF-BASE | K-INTERMEDIATE | Protons | Models, Molecular | Retinaldehyde - chemistry | Crystallography, X-Ray | Purple Membrane - chemistry | Purple Membrane - metabolism | Halobacterium salinarum - chemistry | Leucine - chemistry | Hydrogen Bonding | Water - chemistry | Halobacterium salinarum - metabolism | Protein Conformation | Schiff Bases | Bacteriorhodopsins - chemistry | Leucine - genetics | Bacteriorhodopsins - genetics | Photochemistry
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11. Full Text Probing Human Red Cone Opsin Activity with Retinal Analogues
by Kono, Masahiro and Crouch, Rosalie K
Journal of Natural Products, ISSN 0163-3864, 03/2011, Volume 74, Issue 3, pp. 391 - 394
Retinal analogues have been used to probe the chromophore binding pocket and function of the rod visual pigment rhodopsin. Despite the high homology between... 
CHEMISTRY, MEDICINAL | CHROMOPHORE | VISUAL PIGMENT ANALOGS | SPECTRAL PROPERTIES | PLANT SCIENCES | COLOR-VISION | 9-METHYL GROUP | RHODOPSIN | AMINO-ACID-RESIDUES | BINDING-SITE | SCHIFF-BASE | GECKO CONE | PHARMACOLOGY & PHARMACY | Retinal Pigments - metabolism | Stereoisomerism | Humans | Cone Opsins - metabolism | Retinaldehyde - chemistry | Retinaldehyde - metabolism | Rhodopsin - metabolism | Retina - chemistry | Retinaldehyde - analogs & derivatives | Animals | Cattle | Transducin - metabolism | Molecular Structure | Cone Opsins - chemistry
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12. Full Text Agonists and Partial Agonists of Rhodopsin:  Retinal Polyene Methylation Affects Receptor Activation
by Vogel, Reiner and Lüdeke, Steffen and Siebert, Friedrich and Sakmar, Thomas P and Hirshfeld, Amiram and Sheves, Mordechai
Biochemistry, ISSN 0006-2960, 02/2006, Volume 45, Issue 6, pp. 1640 - 1652
Using Fourier transform infrared (FTIR) difference spectroscopy, we have studied the impact of sites and extent of methylation of the retinal polyene with... 
9-METHYL GROUP | META-II | BOVINE RHODOPSIN | PROTEIN-COUPLED RECEPTOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | SCHIFF-BASE | SIGNALING STATES | ACID SIDE-CHAINS | TRANSDUCIN ACTIVATION | VISUAL PIGMENT | METARHODOPSIN-II | Polyenes - chemistry | Protons | Rod Cell Outer Segment | Retinaldehyde - chemistry | Polyenes - metabolism | Thermodynamics | Animals | Rhodopsin - agonists | Hydrogen Bonding | Cattle | Light | Rhodopsin - antagonists & inhibitors | Spectroscopy, Fourier Transform Infrared - methods | Methylation | Hydrogen-Ion Concentration | Rhodopsin - chemistry | Rhodopsin | Research | Chemical properties | Polyenes
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13. Full Text Cyclopropyl and Isopropyl Derivatives of 11-cis and 9-cis Retinals at C-9 and C-13: Subtle Steric Differences with Major Effects on Ligand Efficacy in Rhodopsin
by deGrip, Willem J and Bovee-Geurts, Petra H. M and Wang, Yajie and Verhoeven, Michiel A and Lugtenburg, Johan
Journal of Natural Products, ISSN 0163-3864, 03/2011, Volume 74, Issue 3, pp. 383 - 390
Retinal is the natural ligand (chromophore) of the vertebrate rod visual pigment. It occurs in either the 11-cis (rhodopsin) or the 9-cis (isorhodopsin)... 
PARTIAL AGONISTS | CHEMISTRY, MEDICINAL | VISUAL PIGMENTS | SCHIFF-BASE COUNTERION | PLANT SCIENCES | 9-METHYL GROUP | BOVINE RHODOPSIN | PROTEIN-COUPLED RECEPTOR | CHROMOPHORE STRUCTURE | PRIMARY PHOTOCHEMICAL EVENTS | ENERGY-STORAGE | BINDING-SITE | PHARMACOLOGY & PHARMACY | Retinal Pigments - metabolism | Rod Cell Outer Segment - drug effects | Stereoisomerism | Molecular Conformation | Retinaldehyde - chemistry | Retinaldehyde - metabolism | Rhodopsin - metabolism | Spectroscopy, Fourier Transform Infrared | Retinaldehyde - analogs & derivatives | Cyclopropanes - chemistry | Animals | Transducin - drug effects | Cattle | Retinal Pigments - chemistry | Rhodopsin - chemistry
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14. Full Text Rhodopsin and 9-demethyl-retinal analog: Effect of a partial agonist on displacement of transmembrane helix 6 in class A G protein-coupled receptors
by Knierim, Bernhard and Hofmann, Klaus Peter and Gärtner, Wolfgang and Hubbell, Wayne L and Ernst, Oliver P
Journal of Biological Chemistry, ISSN 0021-9258, 02/2008, Volume 283, Issue 8, pp. 4967 - 4974
Rhodopsin is the visual pigment of rod cells and a prototypical G protein-coupled receptor. It is activated by cis -> trans photoisomerization of the... 
LINKING | 9-METHYL GROUP | BOVINE RHODOPSIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | DYNAMICS | STATE | TRANSDUCIN ACTIVATION | PHOTOINTERMEDIATE | PROTON UPTAKE | METARHODOPSIN-II | REGION | Protein Structure, Tertiary | Protons | Animals | Rhodopsin - agonists | Electron Spin Resonance Spectroscopy | Protein Structure, Secondary | Retinaldehyde - chemistry | Spin Labels | Schiff Bases | Spectrophotometry, Ultraviolet | Retinaldehyde - analogs & derivatives | Rhodopsin - chemistry
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15. Full Text Engineering a "steric doorstop" in rhodopsin: Converting an inverse agonist to an agonist
by McKee, Timothy D and Lewis, Margaret R and Kono, Masahiro
Biochemistry, ISSN 0006-2960, 10/2007, Volume 46, Issue 43, pp. 12248 - 12252
The crystal structures of rhodopsin depict the inactive conformation of rhodopsin in the dark. The 11-cis retinoid chromophore, the inverse agonist holding... 
TRANSDUCIN | AMINO-ACID | MUTANTS | 9-METHYL GROUP | CHROMOPHORE | CONSTITUTIVE ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | METHYL-GROUP | HYDROLYSIS | OPSIN | STATE | Rhodopsin - isolation & purification | Cercopithecus aethiops | Models, Molecular | Spectrophotometry, Ultraviolet | Animals | Rhodopsin - agonists | Rhodopsin - genetics | Cattle | Rhodopsin - antagonists & inhibitors | Protein Engineering | Mutation | COS Cells | Rhodopsin - chemistry
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16. Full Text Coupling of Protonation Switches During Rhodopsin Activation
by Vogel, Reiner and Sakmar, Thomas P and Sheves, Mordechai and Siebert, Friedrich
Photochemistry and Photobiology, ISSN 0031-8655, 03/2007, Volume 83, Issue 2, pp. 286 - 292
Recent studies of the activation mechanism of rhodopsin involving Fourier‐transform infrared spectroscopy and a combination of chromophore modifications and... 
PARTIAL AGONISTS | STATES | 9-METHYL GROUP | BIOPHYSICS | BOVINE RHODOPSIN | CHROMOPHORE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ARTIFICIAL PIGMENTS | SCHIFF-BASE | RECEPTOR ACTIVATION | METARHODOPSIN-II | VISUAL PIGMENT | Protons | Mutagenesis, Site-Directed | Allosteric Regulation | Models, Molecular | Retinaldehyde - chemistry | Binding Sites - genetics | Rhodopsin - metabolism | Rhodopsin - radiation effects | Animals | Rhodopsin - genetics | Schiff Bases - chemistry | Ligands | In Vitro Techniques | Photochemistry | Rhodopsin - chemistry | Changes | Proteins | Pigments | Retina | Entropy | Equilibrium
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17. Full Text Mechanism of Rhodopsin Activation as Examined with Ring-constrained Retinal Analogs and the Crystal Structure of the Ground State Protein
by Geeng-Fu Jang and Vladimir Kuksa and Stawomir Filipek and Franz Bartl and Eglof Ritter and Michael H. Gelb and Klaus Peter Hofmann and Krzysztof Palczewski
Journal of Biological Chemistry, ISSN 0021-9258, 07/2001, Volume 276, Issue 28, pp. 26148 - 26153
The guanine nucleotide-binding protein (G-protein)-coupled receptor superfamily (GPCR) is comprised of a large group of membrane proteins involved in a wide... 
LIGHT-STABLE RHODOPSIN | 9-METHYL GROUP | BOVINE RHODOPSIN | CHROMOPHORE | SPECTROSCOPY | FTIR | BIOCHEMISTRY & MOLECULAR BIOLOGY | BINDING-SITE | TRANSDUCIN ACTIVATION | BETA-IONONE RING | VISUAL PIGMENT | Retina - metabolism | Animals | Cattle | Protein Conformation | Structure-Activity Relationship | Rhodopsin - metabolism | Rhodopsin - chemistry
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18. Full Text Binding Specificity of Retinal Analogs to Photoactivated Visual Pigments Suggest Mechanism for Fine-Tuning GPCR-Ligand Interactions
by Srinivasan, Sundaramoorthy and Ramon, Eva and Cordomí, Arnau and Garriga, Pere
Chemistry & Biology, ISSN 1074-5521, 03/2014, Volume 21, Issue 3, pp. 369 - 378
11- -retinal acts as an inverse agonist stabilizing the inactive conformation of visual pigments, and upon photoactivation, it isomerizes to all- retinal,... 
CRYSTALLOGRAPHIC ANALYSIS | 9-METHYL GROUP | PROTEIN-COUPLED RECEPTOR | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | RHODOPSIN | COVALENT BOND | CONFORMATIONAL STABILITY | II DECAY | CONE | MOLECULAR-BASIS | Protein Structure, Tertiary | Retinal Pigments - metabolism | Receptors, G-Protein-Coupled - metabolism | Humans | Cercopithecus aethiops | Retinaldehyde - metabolism | Rhodopsin - metabolism | Isomerism | Molecular Dynamics Simulation | Retinaldehyde - analogs & derivatives | Regeneration | Animals | Rhodopsin - genetics | Cattle | Light | Protein Binding | Ligands | Transducin - metabolism | Receptors, G-Protein-Coupled - genetics | Kinetics | Binding Sites | COS Cells | Receptors, G-Protein-Coupled - chemistry | Rhodopsin - chemistry | Oligomers | Rhodopsin | Chemical properties | Analysis
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