PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2604728-0	1989	Schiff-base deprotonation is mandatory for light-dependent rhodopsin phosphorylation.	Schiff Bases	0-11	rhodopsin	Homo sapiens	59-68
2604728-1	1989	The absorption of light by rhodopsin leads to the formation of an activated intermediate (R*) capable of catalysing the exchange of GTP for GDP in a retinal guanine-nucleotide-binding regulatory protein (transducin).	Guanosine Triphosphate	132-135	rhodopsin	Homo sapiens	27-36
2604728-1	1989	The absorption of light by rhodopsin leads to the formation of an activated intermediate (R*) capable of catalysing the exchange of GTP for GDP in a retinal guanine-nucleotide-binding regulatory protein (transducin).	Guanosine Diphosphate	140-143	rhodopsin	Homo sapiens	27-36
2604728-3	1989	The 10 nonactive-site lysine residues of rhodopsin can be reductively dimethylated to form permethylated rhodopsin (PMRh).	Lysine	22-28	rhodopsin	Homo sapiens	41-50
2604728-3	1989	The 10 nonactive-site lysine residues of rhodopsin can be reductively dimethylated to form permethylated rhodopsin (PMRh).	Lysine	22-28	rhodopsin	Homo sapiens	105-114
2604728-5	1989	The monomethylation of the active-site lysine residue of PMRh yields active-site-methylated rhodopsin (AMRh).	Lysine	39-45	rhodopsin	Homo sapiens	92-101
2604728-11	1989	Here it is demonstrated that active-site Schiff-base deprotonation is also mandatory in the formation of the form of photolyzed rhodopsin that is susceptible to phosphorylation by rhodopsin kinase.	Schiff Bases	41-52	rhodopsin	Homo sapiens	128-137
2604728-11	1989	Here it is demonstrated that active-site Schiff-base deprotonation is also mandatory in the formation of the form of photolyzed rhodopsin that is susceptible to phosphorylation by rhodopsin kinase.	Schiff Bases	41-52	rhodopsin	Homo sapiens	180-189
2560768-1	1989	The experimental data on the cGMP decrease under continuous illumination of rod outer segment have been theoretically analysed to study the bleaching and hence the cGMP dependence of the rhodopsin phosphorylation.	Cyclic GMP	29-33	rhodopsin	Homo sapiens	187-196
2553493-0	1989	Cyclic nucleotides and GTP analogues stimulate light-induced phosphorylation of octopus rhodopsin.	Nucleotides, Cyclic	0-18	rhodopsin	Homo sapiens	88-97
2553493-0	1989	Cyclic nucleotides and GTP analogues stimulate light-induced phosphorylation of octopus rhodopsin.	Guanosine Triphosphate	23-26	rhodopsin	Homo sapiens	88-97
2553493-1	1989	Light-induced phosphorylation of octopus rhodopsin in microvillar membrane was shown to be stimulated by cyclic nucleotides in contrast to vertebrate rhodopsin kinase.	Nucleotides, Cyclic	105-123	rhodopsin	Homo sapiens	41-50
2553493-2	1989	Non-hydrolyzable GTP analogues, GTP lambda S and GppNHp, greatly enhanced the light-induced phosphorylation of octopus rhodopsin, but the non-hydrolyzable GDP analogue, GDP beta S, was not effective.	Guanosine Triphosphate	17-20	rhodopsin	Homo sapiens	119-128
2553493-2	1989	Non-hydrolyzable GTP analogues, GTP lambda S and GppNHp, greatly enhanced the light-induced phosphorylation of octopus rhodopsin, but the non-hydrolyzable GDP analogue, GDP beta S, was not effective.	Guanosine Triphosphate	32-35	rhodopsin	Homo sapiens	119-128
2509200-2	1989	In the first step of the visual transduction cascade a photoexcited rhodopsin molecule, R*ret, binds to a GDP-carrying transducin molecule, TGDP.	Guanosine Diphosphate	106-109	rhodopsin	Homo sapiens	68-77
2509200-9	1989	Upon treatment of the R*ret-Te complex by a high concentration of hydroxylamine, the retinal can be removed from the rhodopsin.	Hydroxylamine	66-79	rhodopsin	Homo sapiens	117-126
2560768-1	1989	The experimental data on the cGMP decrease under continuous illumination of rod outer segment have been theoretically analysed to study the bleaching and hence the cGMP dependence of the rhodopsin phosphorylation.	Cyclic GMP	164-168	rhodopsin	Homo sapiens	187-196
2560768-4	1989	The results of the theoretical treatment predict that (i) the presence of cGMP in rod outer segment inhibits the rhodopsin phosphorylation and (ii) rhodopsin phosphorylation process is much faster than what has been reported in the literature.	Cyclic GMP	74-78	rhodopsin	Homo sapiens	113-122
2560768-4	1989	The results of the theoretical treatment predict that (i) the presence of cGMP in rod outer segment inhibits the rhodopsin phosphorylation and (ii) rhodopsin phosphorylation process is much faster than what has been reported in the literature.	Cyclic GMP	74-78	rhodopsin	Homo sapiens	148-157
2551678-4	1989	Phorbol 12-myristate 13-acetate (PMA) enhances this phenomenon independently of rhodopsin phosphorylation.	Tetradecanoylphorbol Acetate	33-36	rhodopsin	Homo sapiens	80-89
2666414-9	1989	IP3 response is light-dependent, saturating when 0.5% of the rhodopsin is photoactivated.	Inositol 1,4,5-Trisphosphate	0-3	rhodopsin	Homo sapiens	61-70
2780545-4	1989	These are (i) the second cytoplasmic loop, which connects rhodopsin helices III and IV, (ii) the third cytoplasmic loop, which connects rhodopsin helices V and VI, and (iii) a putative fourth cytoplasmic loop formed by amino acids 310-321, as the carboxyl-terminal sequence emerges from helix VII and anchors to the lipid bilayer via palmitoylcysteines 322 and 323.	Lipid Bilayers	316-329	rhodopsin	Homo sapiens	136-145
2780545-5	1989	Evidence for these regions of interaction of rhodopsin and Gt comes from the ability of synthetic peptides comprising these regions to compete with metarhodopsin II for binding to Gt.	Peptides	98-106	rhodopsin	Homo sapiens	45-54
2529919-0	1989	[Study of thermo-stabilizing effect of tocopherol on rhodopsin in the presence of fatty acids using the method of differential scanning calorimetry].	Tocopherols	39-49	rhodopsin	Homo sapiens	53-62
2529919-0	1989	[Study of thermo-stabilizing effect of tocopherol on rhodopsin in the presence of fatty acids using the method of differential scanning calorimetry].	Fatty Acids	82-93	rhodopsin	Homo sapiens	53-62
2529919-1	1989	By the method of differential scanning calorimetry it was shown that the addition of arachidonic acid to photoreceptor membranes is accompanied by concentration-dependent shift of thermograms curve of rhodopsin value.	Arachidonic Acid	85-101	rhodopsin	Homo sapiens	201-210
2529919-2	1989	Addition of tocopherol to photoreceptor membranes prevents the turbulent effect of the fatty acid on opsin and rhodopsin.	Tocopherols	12-22	rhodopsin	Homo sapiens	111-120
2529919-2	1989	Addition of tocopherol to photoreceptor membranes prevents the turbulent effect of the fatty acid on opsin and rhodopsin.	Fatty Acids	87-97	rhodopsin	Homo sapiens	111-120
2727688-1	1989	The eye needs to biosynthesize 11-cis-retinoids because the chromophore of rhodopsin is 11-cis-retinal.	11-cis-retinoids	31-47	rhodopsin	Homo sapiens	75-84
2494995-4	1989	The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol.	Disulfides	24-33	rhodopsin	Homo sapiens	102-111
2494995-4	1989	The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol.	Disulfides	146-156	rhodopsin	Homo sapiens	102-111
2494995-4	1989	The alpha-alpha subunit disulfide bonds result in the inhibition of transducin activation by bleached rhodopsin which is restored by reducing the disulfides with dithiothreitol.	Dithiothreitol	162-176	rhodopsin	Homo sapiens	102-111
2535840-5	1989	Binding of the GTP analog 5"-guanylyl imidodiphosphate can be reduced by as much as 90% by aluminum ion following subsaturating rhodopsin stimulation.	Guanosine Triphosphate	15-18	rhodopsin	Homo sapiens	128-137
2497769-6	1989	Recombination of purified fluorescent derivatives of G-protein with purified rhodopsin reconstituted in lipid vesicles restored the light-activated Gpp(NH)p binding to a level comparable to that measured with unlabeled G-protein.	Guanylyl Imidodiphosphate	148-156	rhodopsin	Homo sapiens	77-86
2706205-9	1989	This may indicate that cellular immunity has an important role in the pathogenesis of rhodopsin-induced EAU.	Water	104-107	rhodopsin	Homo sapiens	86-95
2540811-9	1989	These data indicate that (1), in the transition from rhodopsin to metarhodopsin II, major protein conformational changes are occurring near the lysine-retinal linkage whereas the ring portion of the chromophore remains deeply buried within the protein and (2) pigment absorptions characteristic of the metarhodopsin I and II states may be due to specific protein-chromophore interactions near the region of the chromophore ring.	Lysine	144-150	rhodopsin	Homo sapiens	53-62
2535840-5	1989	Binding of the GTP analog 5"-guanylyl imidodiphosphate can be reduced by as much as 90% by aluminum ion following subsaturating rhodopsin stimulation.	Guanylyl Imidodiphosphate	26-54	rhodopsin	Homo sapiens	128-137
2535840-5	1989	Binding of the GTP analog 5"-guanylyl imidodiphosphate can be reduced by as much as 90% by aluminum ion following subsaturating rhodopsin stimulation.	Aluminum	91-99	rhodopsin	Homo sapiens	128-137
2535840-6	1989	Aluminum ion can produce either competitive or mixed noncompetitive inhibition of rhodopsin-catalyzed Gv activation and GTPase activity, as a function of whether Gv undergoes single (competitive), or multiple (mixed noncompetitive) nucleotide exchanges.	Aluminum	0-8	rhodopsin	Homo sapiens	82-91
2914607-0	1989	Calcium regulates the rate of rhodopsin disactivation and the primary amplification step in visual transduction.	Calcium	0-7	rhodopsin	Homo sapiens	30-39
2914607-4	1989	Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase.	Calcium	93-100	rhodopsin	Homo sapiens	111-120
2914607-3	1989	As a consequence of the accelerated recovery in low calcium, the time to the peak of the transducin activation process is shortened and the gain of the primary amplification step, i.e. the number of transducin molecules activated per bleached rhodopsin, is reduced.	Calcium	52-59	rhodopsin	Homo sapiens	243-252
2535840-6	1989	Aluminum ion can produce either competitive or mixed noncompetitive inhibition of rhodopsin-catalyzed Gv activation and GTPase activity, as a function of whether Gv undergoes single (competitive), or multiple (mixed noncompetitive) nucleotide exchanges.	glycylvaline	102-104	rhodopsin	Homo sapiens	82-91
2914607-4	1989	Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase.	Hydroxylamine	18-31	rhodopsin	Homo sapiens	61-70
2914607-4	1989	Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase.	Hydroxylamine	18-31	rhodopsin	Homo sapiens	111-120
2914607-5	1989	This would indicate that calcium may control visual adaptation not only by regulating guanine cyclase activity, but also by affecting the primary step in the transduction cascade, the rhodopsin-transducin coupling.	Calcium	25-32	rhodopsin	Homo sapiens	184-193
2846571-4	1988	Effects of vanadate on the function of a guanine nucleotide-binding protein were investigated in a reconstituted model system consisting of purified transducin subunits (T alpha, T beta gamma) and rhodopsin in phosphatidylcholine vesicles.	Phosphatidylcholines	210-229	rhodopsin	Homo sapiens	197-206
2631391-9	1989	These findings support the hypothesis that when rhodopsin is bleached IRBP transports all-trans retinol from the retina to the pigment epithelium and that it delivers 11-cis retinal to the rod outer segments for rhodopsin regeneration.	Vitamin A	96-103	rhodopsin	Homo sapiens	48-57
3149997-0	1988	The photoreaction of vacuum-dried rhodopsin at low temperature: evidence for charge stabilization by water.	Water	101-106	rhodopsin	Homo sapiens	34-43
3149997-2	1988	The results indicate that in dry rhodopsin, isorhodopsin and lumirhodopsin a protonation equilibrium exists between the protonated and the non-protonated Schiff base.	Schiff Bases	154-165	rhodopsin	Homo sapiens	33-42
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Water	26-31	rhodopsin	Homo sapiens	94-103
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Water	26-31	rhodopsin	Homo sapiens	109-118
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Water	170-173	rhodopsin	Homo sapiens	94-103
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Water	170-173	rhodopsin	Homo sapiens	109-118
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Hydrogen	170-172	rhodopsin	Homo sapiens	94-103
3149997-5	1988	The direct involvement of water in the retinal binding site was demonstrated by measuring the rhodopsin-bathorhodopsin FTIR difference spectra of rhodopsin hydrated with H2O and H2(18)O.	Hydrogen	170-172	rhodopsin	Homo sapiens	109-118
2914607-4	1989	Experiments using hydroxylamine as an artificial quencher of rhodopsin activity suggest that calcium acts upon rhodopsin kinase and not upon the rate of the GTPase.	Calcium	93-100	rhodopsin	Homo sapiens	61-70
3192520-13	1988	Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin.	Cysteine	37-40	rhodopsin	Homo sapiens	79-88
3192520-13	1988	Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin.	Cysteine	48-51	rhodopsin	Homo sapiens	79-88
3192520-13	1988	Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin.	Guanosine 5'-O-(3-Thiotriphosphate)	99-134	rhodopsin	Homo sapiens	79-88
3192520-13	1988	Derivatization of Gt alpha at either Cys-210 or Cys-347 by 125I-ACTP inhibited rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate binding to Gt, mimicking the effect of ADP-ribosylation of Cys-347 by pertussis toxin.	Cysteine	48-51	rhodopsin	Homo sapiens	79-88
2846571-7	1988	Binding of T alpha to rhodopsin and the ADP-ribosylation of T alpha by pertussis toxin, both of which are enhanced in the presence of T beta gamma, were inhibited by vanadate.	Vanadates	166-174	rhodopsin	Homo sapiens	22-31
3138543-1	1988	The recent cloning of the complementary DNAs and/or genes for several receptors linked to guanine nucleotide regulatory proteins including the adrenergic receptors (alpha 1, alpha 2A, alpha 2B, beta 1, beta 2), several subtypes of the muscarinic cholinergic receptors, and the visual "receptor" rhodopsin has revealed considerable similarity in the primary structure of these proteins.	Guanine Nucleotides	90-108	rhodopsin	Homo sapiens	295-304
3049609-3	1988	When the pure alpha T.GDP complex is added to lipid vesicles containing rhodopsin and the beta gamma T complex, a light- and guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S)-dependent enhancement of the fluorescence emission of alpha T is observed.	Guanosine 5'-O-(3-Thiotriphosphate)	125-160	rhodopsin	Homo sapiens	72-81
33607865-1	1988	The mechanism of the photophosphorylation of rhodopsin was studied using several synthetic peptides corresponding to the sequence of the phosphorylation domain.	Peptides	91-99	rhodopsin	Homo sapiens	45-54
2844605-5	1988	In the presence of ATP arrestin cross-linked to both PDE and rhodopsin during the quench phenomenon.	Adenosine Triphosphate	19-22	rhodopsin	Homo sapiens	61-70
2844605-6	1988	Removal of ATP from the reaction mixture essentially abolished the cross-link with PDE, just as ATP omission abolishes quench, but significantly increased the cross-link to rhodopsin.	Adenosine Triphosphate	11-14	rhodopsin	Homo sapiens	173-182
2844605-8	1988	The data are consistent with a model of quench in which photolyzed rhodopsin (R*) catalyzes the formation of an activated form of arrestin, which dissociates from R* in the presence of ATP, and binds to PDEs, thereby deactivating them.	Adenosine Triphosphate	185-188	rhodopsin	Homo sapiens	67-76
3139484-3	1988	Receptors such as those for beta- and alpha-adrenergic catecholamines, muscarinic agonists, and the retinal photoreceptor rhodopsin, catalyze the exchange of GDP for GTP binding to the alpha subunit of a specific G protein.	Catecholamines	55-69	rhodopsin	Homo sapiens	122-131
3139484-3	1988	Receptors such as those for beta- and alpha-adrenergic catecholamines, muscarinic agonists, and the retinal photoreceptor rhodopsin, catalyze the exchange of GDP for GTP binding to the alpha subunit of a specific G protein.	Guanosine Diphosphate	158-161	rhodopsin	Homo sapiens	122-131
3139484-3	1988	Receptors such as those for beta- and alpha-adrenergic catecholamines, muscarinic agonists, and the retinal photoreceptor rhodopsin, catalyze the exchange of GDP for GTP binding to the alpha subunit of a specific G protein.	Guanosine Triphosphate	166-169	rhodopsin	Homo sapiens	122-131
15977337-1	1988	The photoreceptor sensory rhodopsin was isolated from halobacterial cell membranes solubilized in laurylmaltoside.	dodecyl maltoside	98-113	rhodopsin	Homo sapiens	26-35
2837485-3	1988	The peptide-specific antibody is a potent inhibitor of the rhodopsin-stimulated GTPase activity in phospholipid vesicle systems containing pure rhodopsin and pure holo-transducin, or rhodopsin and the purified alpha T and beta/gamma (beta gamma T) subunit components, with the highest levels of inhibition (80-95%) occurring under conditions where the molar ratio of holo-transducin (or alpha T) to AS/7 approximately equal to 1.	Phospholipids	99-111	rhodopsin	Homo sapiens	59-68
2456151-2	1988	The light is absorbed by rhodopsin that activates an intermediate GTP-binding protein; this species then activates the PDE.	Guanosine Triphosphate	66-69	rhodopsin	Homo sapiens	25-34
2456151-3	1988	Photo-excited rhodopsin passes through a series of transient states, and the purpose of this study is to identify the earliest state that interacts with the GTP-binding protein and thus activate the PDE.	Guanosine Triphosphate	157-160	rhodopsin	Homo sapiens	14-23
3219348-4	1988	Rhodopsin photochemical activity is enhanced by phosphatidylethanolamine head groups and docosahexaenoyl (22:6 omega 3) acyl chains.	phosphatidylethanolamine	48-72	rhodopsin	Homo sapiens	0-9
3136547-0	1988	Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit.	Peptides	61-69	rhodopsin	Homo sapiens	29-38
3136547-5	1988	Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.	acetyl-glu311	38-51	rhodopsin	Homo sapiens	93-102
3136547-5	1988	Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.	acetyl-glu311	38-51	rhodopsin	Homo sapiens	197-206
3136547-5	1988	Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.	Amides	59-64	rhodopsin	Homo sapiens	93-102
3136547-5	1988	Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.	Amides	59-64	rhodopsin	Homo sapiens	197-206
2837485-3	1988	The peptide-specific antibody is a potent inhibitor of the rhodopsin-stimulated GTPase activity in phospholipid vesicle systems containing pure rhodopsin and pure holo-transducin, or rhodopsin and the purified alpha T and beta/gamma (beta gamma T) subunit components, with the highest levels of inhibition (80-95%) occurring under conditions where the molar ratio of holo-transducin (or alpha T) to AS/7 approximately equal to 1.	Phospholipids	99-111	rhodopsin	Homo sapiens	144-153
2837485-3	1988	The peptide-specific antibody is a potent inhibitor of the rhodopsin-stimulated GTPase activity in phospholipid vesicle systems containing pure rhodopsin and pure holo-transducin, or rhodopsin and the purified alpha T and beta/gamma (beta gamma T) subunit components, with the highest levels of inhibition (80-95%) occurring under conditions where the molar ratio of holo-transducin (or alpha T) to AS/7 approximately equal to 1.	Phospholipids	99-111	rhodopsin	Homo sapiens	144-153
3262376-0	1988	[Rhodopsin photo-oxidation: oxygen consumption and spectrum of activity].	Oxygen	28-34	rhodopsin	Homo sapiens	1-10
2844243-7	1988	Purified G-protein alone also did not turn over GTP, apparently because bleached rhodopsin is required for it to bind GTP.	Guanosine Triphosphate	118-121	rhodopsin	Homo sapiens	81-90
3283122-2	1988	Antibodies against synthetic peptides corresponding to loop 3-4, loop 5-6, and the serine/threonine-rich region of the COOH terminus recognize rhodopsin by immunoblot analysis and also recognize the native protein within the membrane, allowing these probes to be used for functional studies.	Serine	83-89	rhodopsin	Homo sapiens	143-152
3283122-2	1988	Antibodies against synthetic peptides corresponding to loop 3-4, loop 5-6, and the serine/threonine-rich region of the COOH terminus recognize rhodopsin by immunoblot analysis and also recognize the native protein within the membrane, allowing these probes to be used for functional studies.	Threonine	90-99	rhodopsin	Homo sapiens	143-152
3283122-3	1988	Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin.	Phospholipids	29-41	rhodopsin	Homo sapiens	0-9
3283122-3	1988	Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin.	Phospholipids	29-41	rhodopsin	Homo sapiens	198-207
3283122-3	1988	Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin.	Carbonic Acid	181-185	rhodopsin	Homo sapiens	0-9
3283122-3	1988	Rhodopsin reconstituted into phospholipid vesicles binds transducin in the light which significantly reduces the binding of antipeptide antibodies corresponding to loop 3-4 and the COOH terminus of rhodopsin.	Carbonic Acid	181-185	rhodopsin	Homo sapiens	198-207
3262376-4	1988	Oxygen consumption in photooxidation of rhodopsin SH-groups and lipids are determined.	Oxygen	0-6	rhodopsin	Homo sapiens	40-49
2832012-2	1988	Electron-electron double resonance (ELDOR) has been applied to the study of specific interactions of 15N-spin-labeled stearic acid with the retinal chromophore of a rhodopsin analogue containing a 14N spin-labeled retinal.	15n	101-104	rhodopsin	Homo sapiens	165-174
2966778-8	1988	In the immunoblot analyses, the lipofuscin granule fraction from a sucrose density gradient of human RPE homogenates was positive for rhodopsin only in those specimens that were found, upon ultrastructural examination, to contain recognizable phagosomes.	Lipofuscin	32-42	rhodopsin	Homo sapiens	134-143
2966778-8	1988	In the immunoblot analyses, the lipofuscin granule fraction from a sucrose density gradient of human RPE homogenates was positive for rhodopsin only in those specimens that were found, upon ultrastructural examination, to contain recognizable phagosomes.	Sucrose	67-74	rhodopsin	Homo sapiens	134-143
2966778-12	1988	Thus, these antibodies are of limited value in revealing the ultimate fate of the whole rhodopsin molecule, eg, the hydrophobic sequences that are the most likely residues in lipofuscin granules.	Lipofuscin	175-185	rhodopsin	Homo sapiens	88-97
3365420-1	1988	The inactivation of excited rhodopsin in the presence of ATP, rhodopsin kinase, and/or arrestin has been studied from its effect on the two subsequent steps in the light-induced enzymatic cascade: metarhodopsin II catalyzed activation of G-protein and G-protein-dependent activation of cGMP phosphodiesterase.	Adenosine Triphosphate	57-60	rhodopsin	Homo sapiens	28-37
3365420-4	1988	Measurements of rhodopsin phosphorylation under identical conditions show that in the presence of arrestin total metarhodopsin II inactivation is achieved when only 0.5-1.4 phosphates are bound per bleached rhodopsin, whereas in the absence of arrestin it requires binding of 12-16 phosphates per bleached rhodopsin.	Phosphates	173-183	rhodopsin	Homo sapiens	117-126
3365420-4	1988	Measurements of rhodopsin phosphorylation under identical conditions show that in the presence of arrestin total metarhodopsin II inactivation is achieved when only 0.5-1.4 phosphates are bound per bleached rhodopsin, whereas in the absence of arrestin it requires binding of 12-16 phosphates per bleached rhodopsin.	Phosphates	173-183	rhodopsin	Homo sapiens	117-126
3365420-4	1988	Measurements of rhodopsin phosphorylation under identical conditions show that in the presence of arrestin total metarhodopsin II inactivation is achieved when only 0.5-1.4 phosphates are bound per bleached rhodopsin, whereas in the absence of arrestin it requires binding of 12-16 phosphates per bleached rhodopsin.	Phosphates	282-292	rhodopsin	Homo sapiens	117-126
3365420-4	1988	Measurements of rhodopsin phosphorylation under identical conditions show that in the presence of arrestin total metarhodopsin II inactivation is achieved when only 0.5-1.4 phosphates are bound per bleached rhodopsin, whereas in the absence of arrestin it requires binding of 12-16 phosphates per bleached rhodopsin.	Phosphates	282-292	rhodopsin	Homo sapiens	117-126
2964878-1	1988	The nature of the primary photochemical events in rhodopsin and isorhodopsin is studied by using low temperature actinometry, low temperature absorption spectroscopy, and intermediate neglect of differential overlap including partial single and double configuration interaction (INDO-PSDCI) molecular orbital theory.	indo-psdci	279-289	rhodopsin	Homo sapiens	50-59
2832012-2	1988	Electron-electron double resonance (ELDOR) has been applied to the study of specific interactions of 15N-spin-labeled stearic acid with the retinal chromophore of a rhodopsin analogue containing a 14N spin-labeled retinal.	stearic acid	118-130	rhodopsin	Homo sapiens	165-174
2832012-2	1988	Electron-electron double resonance (ELDOR) has been applied to the study of specific interactions of 15N-spin-labeled stearic acid with the retinal chromophore of a rhodopsin analogue containing a 14N spin-labeled retinal.	4-(4-methylpiperazin-1-yl)benzoic acid	197-200	rhodopsin	Homo sapiens	165-174
3038611-2	1987	Transducin is a GTP-binding protein which mediates the light activation signal from photolyzed rhodopsin to cGMP phosphodiesterase and is pivotal in the visual excitation process.	Guanosine Triphosphate	16-19	rhodopsin	Homo sapiens	95-104
3422479-7	1988	The spectroscopic difference between rod rhodopsin and the red/green iodopsins is due to the influence of Glu-102 in the latter.	Glutamic Acid	106-109	rhodopsin	Homo sapiens	41-50
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	Lysine	282-285	rhodopsin	Homo sapiens	26-35
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	Lysine	282-285	rhodopsin	Homo sapiens	173-182
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	Arginine	293-296	rhodopsin	Homo sapiens	26-35
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	Arginine	293-296	rhodopsin	Homo sapiens	173-182
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	carboxylate	309-320	rhodopsin	Homo sapiens	26-35
3422479-10	1988	The geometric change (the rhodopsin "photoswitch") resulting from cis-trans isomerization in the first excited electronic state (S1), ultimately leads to RX (photoactivated rhodopsin, metarhodopsin II) and changes the activity of exobilayer groups, possibly causing dissociation of Lys-83 and Arg-85 from the carboxylate groups at positions 263 and 265.	carboxylate	309-320	rhodopsin	Homo sapiens	173-182
3118983-4	1987	Photoactivating rhodopsin triggers in rods a cascade of GTP-dependent and transducin-mediated reactions controlling cyclic-GMP hydrolysis.	Guanosine Triphosphate	56-59	rhodopsin	Homo sapiens	16-25
2826436-3	1988	This activity is the biochemical counterpart of observations on intact retina showing that a rhodopsin-activated GTP-binding protein is involved in visual transduction in invertebrates, and that InsP3 release is correlated with visual excitation and adaptation.	Guanosine Triphosphate	113-116	rhodopsin	Homo sapiens	93-102
2826436-8	1988	Invertebrate rhodopsin is homologous in sequence and function to vertebrate visual pigment, which modulates the concentration of cyclic GMP through the mediation of the GTP-binding protein transducin.	Guanosine Triphosphate	169-172	rhodopsin	Homo sapiens	13-22
19431715-8	1988	The formation of hypsorhodopsin was also found in the early stages of the irradiation of octopus rhodopsin with weak continuous light at 10 K. However bathorhodopsin is formed three times more efficiently than hypsorhodopsin at 10 K.At physiological temperatures the formation of hypsorhodopsin in D(2)O takes place more slowly than in H(2)O.	Deuterium Oxide	298-303	rhodopsin	Homo sapiens	22-31
3118983-4	1987	Photoactivating rhodopsin triggers in rods a cascade of GTP-dependent and transducin-mediated reactions controlling cyclic-GMP hydrolysis.	Cyclic GMP	116-126	rhodopsin	Homo sapiens	16-25
3118983-14	1987	Without GTP, they are linear with the amount of photoexcited rhodopsin, saturate at 10% photolysis, and thus correlate well with the light-scattering "binding signal."	Guanosine Triphosphate	8-11	rhodopsin	Homo sapiens	61-70
3118983-14	1987	Without GTP, they are linear with the amount of photoexcited rhodopsin, saturate at 10% photolysis, and thus correlate well with the light-scattering "binding signal."	saturate	72-80	rhodopsin	Homo sapiens	61-70
2826123-5	1987	Activation requires that GDP or a suitable analogue be bound to T alpha: T alpha-GDP and T alpha-GDP alpha S are activable by fluorides, but not T alpha-GDP beta S, nor T alpha that has released its nucleotide upon binding to photoexcited rhodopsin.	Guanosine Diphosphate	25-28	rhodopsin	Homo sapiens	239-248
2826123-5	1987	Activation requires that GDP or a suitable analogue be bound to T alpha: T alpha-GDP and T alpha-GDP alpha S are activable by fluorides, but not T alpha-GDP beta S, nor T alpha that has released its nucleotide upon binding to photoexcited rhodopsin.	Fluorides	126-135	rhodopsin	Homo sapiens	239-248
3102494-2	1987	Photolyzed rhodopsin acts in a catalytic manner to mediate the exchange of GTP for GDP bound to transducin.	Guanosine Triphosphate	75-78	rhodopsin	Homo sapiens	11-20
3036840-11	1987	The Km value of the enzyme for ATP is approximately 35 microM using either beta-AR or rhodopsin as substrate.	Adenosine Triphosphate	31-34	rhodopsin	Homo sapiens	86-95
3038180-1	1987	The photoreceptor protein rhodopsin has been reconstituted with a single phospholipid species, dimyristoylphosphatidylcholine, at a range of different lipid/protein ratios, and the exchange rate at the lipid-protein interface has been determined from the electron spin resonance spectra of spin-labeled phosphatidylcholine.	Dimyristoylphosphatidylcholine	95-125	rhodopsin	Homo sapiens	26-35
3607032-1	1987	13C- and 2H-labeled retinal derivatives have been used to assign normal modes in the 1100-1300-cm-1 fingerprint region of the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin.	13c	0-3	rhodopsin	Homo sapiens	153-162
3607032-1	1987	13C- and 2H-labeled retinal derivatives have been used to assign normal modes in the 1100-1300-cm-1 fingerprint region of the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin.	Deuterium	9-11	rhodopsin	Homo sapiens	153-162
3607032-2	1987	On the basis of the 13C shifts, C8-C9 stretching character is assigned at 1217 cm-1 in rhodopsin, at 1206 cm-1 in isorhodopsin, and at 1214 cm-1 in bathorhodopsin.	13c	20-23	rhodopsin	Homo sapiens	87-96
3558391-1	1987	Bovine retinal rod outer segments (ROS) support the incorporation of [3H]palmitate into rhodopsin.	[3h]palmitate	69-82	rhodopsin	Homo sapiens	88-97
3494246-1	1987	The key biochemical process of the vertebrate visual cycle required for rhodopsin regeneration, 11-cis-retinoid production from all-trans-retinoids, is shown to occur in vitro.	11-cis-retinoid	96-111	rhodopsin	Homo sapiens	72-81
3494246-1	1987	The key biochemical process of the vertebrate visual cycle required for rhodopsin regeneration, 11-cis-retinoid production from all-trans-retinoids, is shown to occur in vitro.	Retinoids	138-147	rhodopsin	Homo sapiens	72-81
3102494-2	1987	Photolyzed rhodopsin acts in a catalytic manner to mediate the exchange of GTP for GDP bound to transducin.	Guanosine Diphosphate	83-86	rhodopsin	Homo sapiens	11-20
3102494-3	1987	We have analyzed the steady-state kinetics of this activation process in order to determine the molecular mechanism of interactions between rhodopsin, transducin, and guanine nucleotides.	Guanine Nucleotides	167-186	rhodopsin	Homo sapiens	140-149
3102494-4	1987	Initial velocities (Vo) of the exchange reaction catalyzed by rhodopsin were measured for various transducin concentrations at several fixed levels of the GTP analog, [35S]guanosine 5"-(3-O-thio)triphosphate (GTP gamma S).	Guanosine Triphosphate	209-212	rhodopsin	Homo sapiens	62-71
3102494-9	1987	Furthermore, the allosteric behavior observed in the activation of transducin is also witnessed in the rhodopsin-catalyzed guanine nucleotide exchange of the G protein"s purified alpha subunit in the absence of the beta X gamma subunit complex.	Guanine Nucleotides	123-141	rhodopsin	Homo sapiens	103-112
3026986-5	1987	Photoisomerization of rhodopsin or cone pigment produces the rapid amplified activation of phosphodiesterase, which lowers the concentration of cGMP, thereby lowering the conductance of the surface membrane.	Cyclic GMP	144-148	rhodopsin	Homo sapiens	22-31
2435842-3	1987	Measurement of Ca++ content using arsenazo III spectroscopy demonstrates that incubation of OS-IS in 10 nM Ca++-Ringer"s solution containing the Ca++ ionophore A23187 reduces their Ca++ content by 93%, from 1.3 to 0.1 mol Ca++/mol rhodopsin.	Osmium	92-94	rhodopsin	Homo sapiens	231-240
2435842-3	1987	Measurement of Ca++ content using arsenazo III spectroscopy demonstrates that incubation of OS-IS in 10 nM Ca++-Ringer"s solution containing the Ca++ ionophore A23187 reduces their Ca++ content by 93%, from 1.3 to 0.1 mol Ca++/mol rhodopsin.	Calcimycin	160-166	rhodopsin	Homo sapiens	231-240
2878683-3	1986	With a flash of light bleaching 7 X 10(-2) percent of rhodopsin, cyclase activity increased by a factor of 30 when Ca2+ levels dropped from 10(-5) to 10(-8) M. In view of recent observations that shortly after a flash of light the calcium activity inside the photoreceptor cell decreases, it seems likely that Ca2+ plays a regulatory role on cGMP metabolism in visual excitation.	Calcium	231-238	rhodopsin	Homo sapiens	54-63
3040978-1	1987	Photoactivated rhodopsin (R) catalyses, by repetitively interacting with many copies of a guanosine nucleotide binding protein (transducin), the amplified binding of GTP to transducin molecules which then activate cyclic GMP phosphodiesterase.	Guanosine Triphosphate	166-169	rhodopsin	Homo sapiens	15-24
2878683-3	1986	With a flash of light bleaching 7 X 10(-2) percent of rhodopsin, cyclase activity increased by a factor of 30 when Ca2+ levels dropped from 10(-5) to 10(-8) M. In view of recent observations that shortly after a flash of light the calcium activity inside the photoreceptor cell decreases, it seems likely that Ca2+ plays a regulatory role on cGMP metabolism in visual excitation.	Cyclic GMP	342-346	rhodopsin	Homo sapiens	54-63
3020017-4	1986	At light intensities bleaching from 160 to 5.6 X 10(6) rhodopsin molecules/rod/s, decreases in the response latency for the cGMP kinetics parallel decreases in the latent period of the electrical response.	Cyclic GMP	124-128	rhodopsin	Homo sapiens	55-64
3021528-1	1986	Photolyzed rhodopsin (R) catalyzes GTP-binding to alpha-transducins (T alpha); T alpha X GTPs then activate cGMP phosphodiesterase (PDE).	Guanosine Triphosphate	35-38	rhodopsin	Homo sapiens	11-20
3021528-1	1986	Photolyzed rhodopsin (R) catalyzes GTP-binding to alpha-transducins (T alpha); T alpha X GTPs then activate cGMP phosphodiesterase (PDE).	Guanosine Triphosphate	89-93	rhodopsin	Homo sapiens	11-20
3020017-6	1986	Up to 10(5) cGMP molecules are hydrolyzed per photolyzed rhodopsin, consistent with in vitro studies showing that each bleached rhodopsin can activate over 100 phosphodiesterase molecules.	Cyclic GMP	12-16	rhodopsin	Homo sapiens	57-66
3020017-6	1986	Up to 10(5) cGMP molecules are hydrolyzed per photolyzed rhodopsin, consistent with in vitro studies showing that each bleached rhodopsin can activate over 100 phosphodiesterase molecules.	Cyclic GMP	12-16	rhodopsin	Homo sapiens	128-137
3020017-8	1986	These results are consistent with cGMP being the intracellular messenger that links rhodopsin isomerization with changes in membrane permeability upon illumination.	Cyclic GMP	34-38	rhodopsin	Homo sapiens	84-93
3756156-3	1986	Only the longest chain sucrose esters give purified rhodopsin with maximum absorbance comparable to that of the native pigment.	sucrose esters	23-37	rhodopsin	Homo sapiens	52-61
3466646-4	1986	Competition binding experiments were carried out by adding an analogue, [alpha-32P]GTP, and a catalytic amount of photoexcited rhodopsin (R) to transducin and measuring the amount of bound [gamma-32P]GTP.	gamma-32p	190-199	rhodopsin	Homo sapiens	127-136
3756156-5	1986	Sucrose esters thus prove to be mild enough to maintain rhodopsin functionality with respect to these two properties and could probably be used successfully to maintain other membrane proteins" integrity.	sucrose esters	0-14	rhodopsin	Homo sapiens	56-65
3021208-4	1986	The ATP-dependent quenching mechanism apparently requires the phosphorylation of photoactivated rhodopsin (Rho*); however, a 48-kilodalton protein (48K protein) has also been proposed to participate in the inactivation process.	Adenosine Triphosphate	4-7	rhodopsin	Homo sapiens	96-105
3021208-5	1986	Purified species of phosphorylated rhodopsin containing 0, 2, or greater than or equal to 4 (high) phosphates per rhodopsin (PO4/Rho) were reconstituted into phosphatidylcholine (PC) vesicles and reassociated with a hypotonic extract from isotonically washed disk membranes that were depleted of 48K protein; PDE activation, in response to bleaching from 0.01% to 15% of the rhodopsin present, was measured.	Phosphates	99-109	rhodopsin	Homo sapiens	35-44
3087387-0	1986	Light-induced interaction between rhodopsin and GTP-binding protein leads to the hydrolysis of GTP in the rod outer segment.	Guanosine Triphosphate	48-51	rhodopsin	Homo sapiens	34-43
3012559-0	1986	Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein.	Schiff Bases	21-32	rhodopsin	Homo sapiens	36-45
3012559-4	1986	The question of whether the deprotonation of the protonated Schiff base is obligate in the formation of activated rhodopsin was addressed by monomethylating the active-site lysine of permethylated rhodopsin and determining whether this pigment can activate the G protein upon photolysis.	Schiff Bases	60-71	rhodopsin	Homo sapiens	114-123
3012559-4	1986	The question of whether the deprotonation of the protonated Schiff base is obligate in the formation of activated rhodopsin was addressed by monomethylating the active-site lysine of permethylated rhodopsin and determining whether this pigment can activate the G protein upon photolysis.	Schiff Bases	60-71	rhodopsin	Homo sapiens	197-206
3012559-4	1986	The question of whether the deprotonation of the protonated Schiff base is obligate in the formation of activated rhodopsin was addressed by monomethylating the active-site lysine of permethylated rhodopsin and determining whether this pigment can activate the G protein upon photolysis.	Lysine	173-179	rhodopsin	Homo sapiens	114-123
3012559-4	1986	The question of whether the deprotonation of the protonated Schiff base is obligate in the formation of activated rhodopsin was addressed by monomethylating the active-site lysine of permethylated rhodopsin and determining whether this pigment can activate the G protein upon photolysis.	Lysine	173-179	rhodopsin	Homo sapiens	197-206
3012559-9	1986	It is concluded that proton transfer from the protonated Schiff base of rhodopsin is obligate for the initiation of visual transduction.	Schiff Bases	57-68	rhodopsin	Homo sapiens	72-81
3485445-1	1986	Measurements were made on the conductivity of digitonin extracts of frog rhodopsin with and without previous light exposure.	Digitonin	46-55	rhodopsin	Homo sapiens	73-82
2875689-1	1986	Rhodopsin in rod outer segment disk membranes was enzymatically modified by erythrocyte transglutaminase, which linked small primary amines to glutamine residues.	Amines	133-139	rhodopsin	Homo sapiens	0-9
2875689-1	1986	Rhodopsin in rod outer segment disk membranes was enzymatically modified by erythrocyte transglutaminase, which linked small primary amines to glutamine residues.	Glutamine	143-152	rhodopsin	Homo sapiens	0-9
2875689-2	1986	In order to avoid formation of protein crosslinks, rhodopsin was first reductively methylated to modify its lysines.	Lysine	108-115	rhodopsin	Homo sapiens	51-60
2875689-3	1986	From 1.9 to 2.5 mol of putrescine, ethanolamine, or dinitrophenylcadaverine were incorporated into rhodopsin by transglutaminase during 16 h reaction time.	Putrescine	23-33	rhodopsin	Homo sapiens	99-108
2875689-3	1986	From 1.9 to 2.5 mol of putrescine, ethanolamine, or dinitrophenylcadaverine were incorporated into rhodopsin by transglutaminase during 16 h reaction time.	Ethanolamine	35-47	rhodopsin	Homo sapiens	99-108
2875689-3	1986	From 1.9 to 2.5 mol of putrescine, ethanolamine, or dinitrophenylcadaverine were incorporated into rhodopsin by transglutaminase during 16 h reaction time.	dinitrophenylcadaverine	52-75	rhodopsin	Homo sapiens	99-108
2875689-4	1986	A maximum of 3.5 mol of [14C]putrescine was incorporated per mole of rhodopsin during 48 h. Essentially all of the rhodopsin sequence containing the putrescine could be removed by limited proteolysis of the membranes by thermolysin.	[14c]putrescine	24-39	rhodopsin	Homo sapiens	69-78
2875689-4	1986	A maximum of 3.5 mol of [14C]putrescine was incorporated per mole of rhodopsin during 48 h. Essentially all of the rhodopsin sequence containing the putrescine could be removed by limited proteolysis of the membranes by thermolysin.	[14c]putrescine	24-39	rhodopsin	Homo sapiens	115-124
2875689-4	1986	A maximum of 3.5 mol of [14C]putrescine was incorporated per mole of rhodopsin during 48 h. Essentially all of the rhodopsin sequence containing the putrescine could be removed by limited proteolysis of the membranes by thermolysin.	Putrescine	29-39	rhodopsin	Homo sapiens	69-78
2875689-4	1986	A maximum of 3.5 mol of [14C]putrescine was incorporated per mole of rhodopsin during 48 h. Essentially all of the rhodopsin sequence containing the putrescine could be removed by limited proteolysis of the membranes by thermolysin.	Putrescine	29-39	rhodopsin	Homo sapiens	115-124
2875689-5	1986	Glutamine residues in positions 236, 237, 238, and 344 were modified to approximately equal extents, as determined by isolation of the cyanogen bromide peptides of modified rhodopsin followed by further subdigestion of the peptides.	Cyanogen Bromide	135-151	rhodopsin	Homo sapiens	173-182
2875689-6	1986	The modified glutamine residues are located in the helix V-VI (or F1-F2) connecting loop and in the carboxyl-terminal region of rhodopsin.	Glutamine	13-22	rhodopsin	Homo sapiens	128-137
3094838-1	1986	Effects of the intraocular injection of three inhibitors of glycosylation (tunicamycin, castanospermine, and swainsonine) on the rhodopsin content and the integrity of disc membranes in frog retina were studied.	Tunicamycin	75-86	rhodopsin	Homo sapiens	129-138
3094838-1	1986	Effects of the intraocular injection of three inhibitors of glycosylation (tunicamycin, castanospermine, and swainsonine) on the rhodopsin content and the integrity of disc membranes in frog retina were studied.	castanospermine	88-103	rhodopsin	Homo sapiens	129-138
3094838-1	1986	Effects of the intraocular injection of three inhibitors of glycosylation (tunicamycin, castanospermine, and swainsonine) on the rhodopsin content and the integrity of disc membranes in frog retina were studied.	Swainsonine	109-120	rhodopsin	Homo sapiens	129-138
3094838-2	1986	The administration of 10 or 100 micrograms of tunicamycin resulted in a 78% loss of rhodopsin in the frog retina which also exhibited a significant reduction in the length of photoreceptor outer segments (as examined under light microscope).	Tunicamycin	46-57	rhodopsin	Homo sapiens	84-93
3094838-3	1986	This suggests that the synthesis and/or insertion of rhodopsin into the disc membrane is inhibited by tunicamycin.	Tunicamycin	102-113	rhodopsin	Homo sapiens	53-62
3094838-4	1986	In contrast, injections of up to 250 micrograms of castanospermine and swainsonine resulted in neither a decrease in rhodopsin content nor a change in the length of photoreceptor outer segments.	castanospermine	51-66	rhodopsin	Homo sapiens	117-126
3094838-4	1986	In contrast, injections of up to 250 micrograms of castanospermine and swainsonine resulted in neither a decrease in rhodopsin content nor a change in the length of photoreceptor outer segments.	Swainsonine	71-82	rhodopsin	Homo sapiens	117-126
17007793-3	1986	It was also revealed that the regeneration of rhodopsin was perturbed by the formation of retinylidene Schiff base with phosphatidylethanolamine in rod outer segment membranes, which decreased with increasing temperature.	retinylidene schiff base	90-114	rhodopsin	Homo sapiens	46-55
17007793-3	1986	It was also revealed that the regeneration of rhodopsin was perturbed by the formation of retinylidene Schiff base with phosphatidylethanolamine in rod outer segment membranes, which decreased with increasing temperature.	phosphatidylethanolamine	120-144	rhodopsin	Homo sapiens	46-55
17007793-4	1986	The activation energy of rhodopsin regeneration in rod outer segment membranes was 18.7 kcal/mol, being smaller than the value of 22 kcal/mol in 1% digitonin solution.	Digitonin	148-157	rhodopsin	Homo sapiens	25-34
3008596-2	1986	The light-induced proton uptake by rhodopsin in the rod outer segment disk membrane was enhanced at lower pH (4) but depressed at higher pHs (6 to 8) by the tertiary amine local anesthetics lidocaine, bupivacaine, tetracaine, and dibucaine.	Amines	166-171	rhodopsin	Homo sapiens	35-44
3008596-2	1986	The light-induced proton uptake by rhodopsin in the rod outer segment disk membrane was enhanced at lower pH (4) but depressed at higher pHs (6 to 8) by the tertiary amine local anesthetics lidocaine, bupivacaine, tetracaine, and dibucaine.	Lidocaine	190-199	rhodopsin	Homo sapiens	35-44
3008596-2	1986	The light-induced proton uptake by rhodopsin in the rod outer segment disk membrane was enhanced at lower pH (4) but depressed at higher pHs (6 to 8) by the tertiary amine local anesthetics lidocaine, bupivacaine, tetracaine, and dibucaine.	Bupivacaine	201-212	rhodopsin	Homo sapiens	35-44
3008596-2	1986	The light-induced proton uptake by rhodopsin in the rod outer segment disk membrane was enhanced at lower pH (4) but depressed at higher pHs (6 to 8) by the tertiary amine local anesthetics lidocaine, bupivacaine, tetracaine, and dibucaine.	Tetracaine	214-224	rhodopsin	Homo sapiens	35-44
3008596-2	1986	The light-induced proton uptake by rhodopsin in the rod outer segment disk membrane was enhanced at lower pH (4) but depressed at higher pHs (6 to 8) by the tertiary amine local anesthetics lidocaine, bupivacaine, tetracaine, and dibucaine.	Dibucaine	230-239	rhodopsin	Homo sapiens	35-44
3006038-1	1986	Each photoexcited rhodopsin (R*) molecule catalyzes binding of GTP to many copies of the guanine nucleotide-binding protein transducin, which, in its GTP-binding form, then activates cGMP phosphodiesterase (PDEase).	Guanosine Triphosphate	63-66	rhodopsin	Homo sapiens	18-27
3005307-6	1986	The maximum turnover number for the alpha 2AR-mediated epinephrine-stimulated GTPase activity in Ni is similar to the maximal turnover numbers obtained for the beta-adrenergic receptor-mediated isoproterenol-stimulated GTPase activity in Ns and the rhodopsin-mediated light-stimulated GTPase activity in transducin (0.5-1.5 mol of Pi released per min per mol of nucleotide regulatory protein).	Epinephrine	55-66	rhodopsin	Homo sapiens	249-258
3006038-1	1986	Each photoexcited rhodopsin (R*) molecule catalyzes binding of GTP to many copies of the guanine nucleotide-binding protein transducin, which, in its GTP-binding form, then activates cGMP phosphodiesterase (PDEase).	Guanosine Triphosphate	150-153	rhodopsin	Homo sapiens	18-27
3006038-7	1986	To analyze the mechanism by which ATP and 48-kDa protein deactivate PDEase, we used an ATP-free system consisting of thoroughly washed disk membranes, whose rhodopsin had been previously phosphorylated and chromophore-regenerated, and to which purified PDEase and transducin were reassociated.	Adenosine Triphosphate	34-37	rhodopsin	Homo sapiens	157-166
3863817-11	1985	When photolyzed rhodopsin and T beta gamma were present, Gpp(NH)p and GTP gamma S decreased [32P]ADP-ribosylation by pertussis toxin.	Guanylyl Imidodiphosphate	57-65	rhodopsin	Homo sapiens	16-25
3001052-2	1986	Photo-excited rhodopsin activates a guanine nucleotide-binding protein (G-protein) by catalyzing the exchange of bound GDP for GTP.	Guanosine Diphosphate	119-122	rhodopsin	Homo sapiens	14-23
3001052-2	1986	Photo-excited rhodopsin activates a guanine nucleotide-binding protein (G-protein) by catalyzing the exchange of bound GDP for GTP.	Guanosine Triphosphate	127-130	rhodopsin	Homo sapiens	14-23
2423011-4	1986	Photoexcited rhodopsin triggers transducin by catalyzing the exchange of GTP for bound GDP.	Guanosine Triphosphate	73-76	rhodopsin	Homo sapiens	13-22
2423011-4	1986	Photoexcited rhodopsin triggers transducin by catalyzing the exchange of GTP for bound GDP.	Guanosine Diphosphate	87-90	rhodopsin	Homo sapiens	13-22
3933561-0	1985	Effect of GTP on the rhodopsin-G-protein complex by transient formation of extra metarhodopsin II.	Guanosine Triphosphate	10-13	rhodopsin	Homo sapiens	21-30
3933561-1	1985	The light-induced transient interaction between rhodopsin and G-protein in the presence of GTP has been measured by the formation of extra metarhodopsin II.	Guanosine Triphosphate	91-94	rhodopsin	Homo sapiens	48-57
3933561-3	1985	Without GTP, a flash induces stable rhodopsin-G-protein complexes which dissociate upon addition of GTP.	Guanosine Triphosphate	100-103	rhodopsin	Homo sapiens	36-45
3933561-4	1985	In low GTP (less than 10 microM) transient rhodopsin X G-protein interaction is observed.	Guanosine Triphosphate	7-10	rhodopsin	Homo sapiens	43-52
3933561-5	1985	Rhodopsin X G-protein dissociates the faster, the more GTP is present (rate of dissociation, 0.3/s at 5 microM GTP; T = 3.5 degrees C).	Guanosine Triphosphate	55-58	rhodopsin	Homo sapiens	0-9
3933561-5	1985	Rhodopsin X G-protein dissociates the faster, the more GTP is present (rate of dissociation, 0.3/s at 5 microM GTP; T = 3.5 degrees C).	Guanosine Triphosphate	111-114	rhodopsin	Homo sapiens	0-9
3933561-6	1985	The results corroborate that the uptake of GTP terminates the rhodopsin-G-protein complex and allow an estimation of the rhodopsin X G-protein lifetime.	Guanosine Triphosphate	43-46	rhodopsin	Homo sapiens	62-71
3933561-6	1985	The results corroborate that the uptake of GTP terminates the rhodopsin-G-protein complex and allow an estimation of the rhodopsin X G-protein lifetime.	Guanosine Triphosphate	43-46	rhodopsin	Homo sapiens	121-130
3942531-2	1986	Rhodopsin was identified in formaldehyde-fixed, paraffin-embedded human fetal retina, and in five retinoblastomas using monoclonal antibody (MAb) MAb-E.	Formaldehyde	28-40	rhodopsin	Homo sapiens	0-9
3942531-2	1986	Rhodopsin was identified in formaldehyde-fixed, paraffin-embedded human fetal retina, and in five retinoblastomas using monoclonal antibody (MAb) MAb-E.	Paraffin	48-56	rhodopsin	Homo sapiens	0-9
3863817-11	1985	When photolyzed rhodopsin and T beta gamma were present, Gpp(NH)p and GTP gamma S decreased [32P]ADP-ribosylation by pertussis toxin.	Guanosine Triphosphate	70-73	rhodopsin	Homo sapiens	16-25
3863817-11	1985	When photolyzed rhodopsin and T beta gamma were present, Gpp(NH)p and GTP gamma S decreased [32P]ADP-ribosylation by pertussis toxin.	Phosphorus-32	93-96	rhodopsin	Homo sapiens	16-25
4084854-0	1985	Effect of phospholipids and detergents on transitions and equilibrium between the bleaching intermediates of rhodopsin.	Phospholipids	10-23	rhodopsin	Homo sapiens	109-118
3863817-11	1985	When photolyzed rhodopsin and T beta gamma were present, Gpp(NH)p and GTP gamma S decreased [32P]ADP-ribosylation by pertussis toxin.	Adenosine Diphosphate	97-100	rhodopsin	Homo sapiens	16-25
4084854-2	1985	The results are compared with rhodopsin contained in its natural phospholipid environment.	Phospholipids	65-77	rhodopsin	Homo sapiens	30-39
3863817-12	1985	Thus, pertussis toxin-catalyzed [32P]ADP-ribosylation of T alpha was affected by nucleotides, rhodopsin and light in addition to T beta gamma.	Phosphorus-32	33-36	rhodopsin	Homo sapiens	94-103
3863817-12	1985	Thus, pertussis toxin-catalyzed [32P]ADP-ribosylation of T alpha was affected by nucleotides, rhodopsin and light in addition to T beta gamma.	Adenosine Diphosphate	37-40	rhodopsin	Homo sapiens	94-103
3000435-2	1985	Reconstitution experiments show that this signal requires bleached rhodopsin, G protein (three polypeptide subunits of Mr 39 000, 37 000, and 6000 which comprise the GTPase), phosphodiesterase, cGMP, and GTP.	Guanosine Triphosphate	166-169	rhodopsin	Homo sapiens	67-76
4084506-5	1985	The positions of the C = N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis-15-deuterioretinal or 11-cis-retinal containing 13C at carbon 15 are indicative that the Schiff-base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin.	Carbon	21-22	rhodopsin	Homo sapiens	239-248
4084506-5	1985	The positions of the C = N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis-15-deuterioretinal or 11-cis-retinal containing 13C at carbon 15 are indicative that the Schiff-base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin.	Nitrogen	25-26	rhodopsin	Homo sapiens	239-248
4084506-5	1985	The positions of the C = N stretch in the deuterated pigment and the deuterated pigments regenerated with 11-cis-15-deuterioretinal or 11-cis-retinal containing 13C at carbon 15 are indicative that the Schiff-base linkage is protonated in rhodopsin, bathorhodopsin, and isorhodopsin.	Schiff Bases	202-213	rhodopsin	Homo sapiens	239-248
2995338-9	1985	The ADP-ribosylation of T alpha by pertussis toxin and binding of T alpha to rhodopsin, both of which are enhanced in the presence of T beta gamma, were inhibited by NaF and AlCl3.	Aluminum Chloride	174-179	rhodopsin	Homo sapiens	77-86
2992584-6	1985	On this basis, we conclude that the major changes in this region are due to rhodopsin carboxyls which undergo either a change in local environment or a protonation/deprotonation reaction.	carboxyls	86-95	rhodopsin	Homo sapiens	76-85
2994645-3	1985	Fluoride was also found to profoundly inhibit the ability of G-protein to bind a GTP analogue, GTP gamma S, both in the presence and absence of rhodopsin.	Fluorides	0-8	rhodopsin	Homo sapiens	144-153
3929835-2	1985	Characterization of this labeling indicated that rhodopsin was phosphorylated with [gamma-32P]-8-azido-GTP as a phosphate donor.	[gamma-32p]-8-azido-gtp	83-106	rhodopsin	Homo sapiens	49-58
3924910-3	1985	It is found that substitution of one SH hydrogen at the G alpha-subunit by N-ethylmaleimide or thionitrobenzoate still allows dark binding of the G-unit to the membrane but blocks its light binding to rhodopsin.	Hydrogen	40-48	rhodopsin	Homo sapiens	201-210
3929835-2	1985	Characterization of this labeling indicated that rhodopsin was phosphorylated with [gamma-32P]-8-azido-GTP as a phosphate donor.	Phosphates	112-121	rhodopsin	Homo sapiens	49-58
3924910-3	1985	It is found that substitution of one SH hydrogen at the G alpha-subunit by N-ethylmaleimide or thionitrobenzoate still allows dark binding of the G-unit to the membrane but blocks its light binding to rhodopsin.	Ethylmaleimide	75-91	rhodopsin	Homo sapiens	201-210
2412755-0	1985	Rhodopsin phosphorylation inhibited by adenosine in frog rods: lack of effects on excitation.	Adenosine	39-48	rhodopsin	Homo sapiens	0-9
3924910-3	1985	It is found that substitution of one SH hydrogen at the G alpha-subunit by N-ethylmaleimide or thionitrobenzoate still allows dark binding of the G-unit to the membrane but blocks its light binding to rhodopsin.	thionitrobenzoic acid	95-112	rhodopsin	Homo sapiens	201-210
3924910-6	1985	The rhodopsin-G interaction is reduced in proportion to bound N-ethylmaleimide, and the interaction kinetics remain constant over the measurable range.	Ethylmaleimide	62-78	rhodopsin	Homo sapiens	4-13
3924910-7	1985	GTP/GDP exchange at the G-protein after interaction with rhodopsin does not reduce the accessibility of the relevant SH group.	Guanosine Triphosphate	0-3	rhodopsin	Homo sapiens	57-66
3924910-7	1985	GTP/GDP exchange at the G-protein after interaction with rhodopsin does not reduce the accessibility of the relevant SH group.	Guanosine Diphosphate	4-7	rhodopsin	Homo sapiens	57-66
2987964-0	1985	Two-photon spectroscopy of locked-11-cis-rhodopsin: evidence for a protonated Schiff base in a neutral protein binding site.	Schiff Bases	78-89	rhodopsin	Homo sapiens	41-50
4027218-3	1985	When rhodopsin is incorporated into the saturated short-chain phospholipid dimyristoylphosphatidylcholine, photolysis of the protein results in an abnormal sequence of spectral transitions, and the dominant product of metarhodopsin I decay is free retinal plus opsin [Baldwin, P. A., & Hubbell, W. L. (1985) Biochemistry (preceding paper in this issue)].	Phospholipids	62-74	rhodopsin	Homo sapiens	5-14
4027218-3	1985	When rhodopsin is incorporated into the saturated short-chain phospholipid dimyristoylphosphatidylcholine, photolysis of the protein results in an abnormal sequence of spectral transitions, and the dominant product of metarhodopsin I decay is free retinal plus opsin [Baldwin, P. A., & Hubbell, W. L. (1985) Biochemistry (preceding paper in this issue)].	Dimyristoylphosphatidylcholine	75-105	rhodopsin	Homo sapiens	5-14
4027218-4	1985	By incorporation of rhodopsin into a series of phosphatidylcholines of defined composition, we have determined the properties of the lipid environment that are responsible for the altered spectral behavior.	Phosphatidylcholines	47-67	rhodopsin	Homo sapiens	20-29
3927920-0	1985	Investigation of rhodopsin catalyzed G-protein GTP-binding using [35S] GTP gamma S--effects of regeneration and hydroxylamine.	Guanosine Triphosphate	47-50	rhodopsin	Homo sapiens	17-26
3927920-0	1985	Investigation of rhodopsin catalyzed G-protein GTP-binding using [35S] GTP gamma S--effects of regeneration and hydroxylamine.	Sulfur-35	66-69	rhodopsin	Homo sapiens	17-26
3927920-0	1985	Investigation of rhodopsin catalyzed G-protein GTP-binding using [35S] GTP gamma S--effects of regeneration and hydroxylamine.	Guanosine Triphosphate	71-74	rhodopsin	Homo sapiens	17-26
3927920-0	1985	Investigation of rhodopsin catalyzed G-protein GTP-binding using [35S] GTP gamma S--effects of regeneration and hydroxylamine.	Hydroxylamine	112-125	rhodopsin	Homo sapiens	17-26
3927920-1	1985	A simple reconstitution system for studying rhodopsin-catalyzed G-protein GTP-binding is described.	Guanosine Triphosphate	74-77	rhodopsin	Homo sapiens	44-53
3927920-2	1985	Purified rhodopsin is recombined with a G-protein containing extract in the presence of [35S]GTP gamma S and after incubation the reaction is stopped by rapid cooling and filtration.	Sulfur-35	89-92	rhodopsin	Homo sapiens	9-18
3927920-2	1985	Purified rhodopsin is recombined with a G-protein containing extract in the presence of [35S]GTP gamma S and after incubation the reaction is stopped by rapid cooling and filtration.	Guanosine Triphosphate	93-96	rhodopsin	Homo sapiens	9-18
3919779-9	1985	Moreover, a comparison of rates showed that aldolase cross-linking with glutaraldehyde is significantly faster than cross-linking of membrane-bound rhodopsin.	Glutaral	72-86	rhodopsin	Homo sapiens	148-157
2982652-0	1985	Light-induced conformational change in rhodopsin detected by modification of G-protein binding, GTP gamma S binding and cGMP phosphodiesterase activation.	Guanosine 5'-O-(3-Thiotriphosphate)	96-107	rhodopsin	Homo sapiens	39-48
2412755-1	1985	The rod photocurrent was studied by recording the transretinal voltage from the aspartate-treated isolated frog retina before and after perfusion with 2 mM adenosine, which inhibited 60-80% of the light-induced rhodopsin phosphorylation.	Aspartic Acid	80-89	rhodopsin	Homo sapiens	211-220
3938969-10	1985	In the presence of G beta gamma and photolyzed rhodopsin, GDP and GDP beta S, but not Gpp(NH)p and GTP gamma S, increased the ADP-ribosylation of Gi alpha.	Guanosine Diphosphate	58-61	rhodopsin	Homo sapiens	47-56
2579769-3	1985	It is presumed now that at least two of these molecules, Ca and cGMP, may function as chemical linkers between the absorption of light by rhodopsin and the ionic channels of the plasma membrane of the rod outer segment that close when the rod is illuminated.	Cyclic GMP	64-68	rhodopsin	Homo sapiens	138-147
2412755-1	1985	The rod photocurrent was studied by recording the transretinal voltage from the aspartate-treated isolated frog retina before and after perfusion with 2 mM adenosine, which inhibited 60-80% of the light-induced rhodopsin phosphorylation.	Adenosine	156-165	rhodopsin	Homo sapiens	211-220
3938969-10	1985	In the presence of G beta gamma and photolyzed rhodopsin, GDP and GDP beta S, but not Gpp(NH)p and GTP gamma S, increased the ADP-ribosylation of Gi alpha.	guanosine 5'-O-(2-thiodiphosphate)	66-76	rhodopsin	Homo sapiens	47-56
3938969-10	1985	In the presence of G beta gamma and photolyzed rhodopsin, GDP and GDP beta S, but not Gpp(NH)p and GTP gamma S, increased the ADP-ribosylation of Gi alpha.	Adenosine Diphosphate	126-129	rhodopsin	Homo sapiens	47-56
3968531-7	1985	(c) At levels of illumination bleaching greater than 0.003% of the rhodopsin, a decrease in ATP levels becomes detectable.	Adenosine Triphosphate	92-95	rhodopsin	Homo sapiens	67-76
6439719-0	1984	Effects of guanyl nucleotides and rhodopsin on ADP-ribosylation of the inhibitory GTP-binding component of adenylate cyclase by pertussis toxin.	Adenosine Diphosphate	47-50	rhodopsin	Homo sapiens	34-43
3871471-6	1985	32Pi is incorporated into endogenous ATP and GTP pools twice as efficiently as in isolated OS, and is used in the phosphorylation of rhodopsin.	32pi	0-4	rhodopsin	Homo sapiens	133-142
6439719-0	1984	Effects of guanyl nucleotides and rhodopsin on ADP-ribosylation of the inhibitory GTP-binding component of adenylate cyclase by pertussis toxin.	Guanosine Triphosphate	82-85	rhodopsin	Homo sapiens	34-43
6439719-6	1984	259, 7378-7381) had demonstrated that rhodopsin, the retinal photon receptor protein, can replace inhibitory hormone receptors, and stimulate the hydrolysis of GTP by Gi alpha in the presence of G beta gamma.	Guanosine Triphosphate	160-163	rhodopsin	Homo sapiens	38-47
6439719-7	1984	Photolyzed rhodopsin, but not the inactive, dark protein, inhibited ADP-ribosylation of Gi alpha in the presence of G beta gamma.	Adenosine Diphosphate	68-71	rhodopsin	Homo sapiens	11-20
6439719-8	1984	ADP-ribosylation of Gi alpha, in the presence of G beta gamma and photolyzed (but not dark) rhodopsin was increased by guanosine 5"-O-(2-thiodiphosphate) or GDP, but not by (beta, gamma-methylene)guanosine triphosphate or guanosine 5"-O-(3-thiotriphosphate).	guanosine 5'-O-(2-thiodiphosphate)	119-152	rhodopsin	Homo sapiens	92-101
6093698-0	1984	Selectivity in rhodopsin-phospholipid interactions.	Phospholipids	25-37	rhodopsin	Homo sapiens	15-24
3875178-0	1985	The specific inhibition of 11-cis-retinyl palmitate formation in the frog eye by diaminophenoxypentane, an inhibitor of rhodopsin regeneration.	11-cis-Retinyl palmitate	27-51	rhodopsin	Homo sapiens	120-129
3875178-0	1985	The specific inhibition of 11-cis-retinyl palmitate formation in the frog eye by diaminophenoxypentane, an inhibitor of rhodopsin regeneration.	diaminophenoxypentane	81-102	rhodopsin	Homo sapiens	120-129
3875178-1	1985	The antischistosomal drug 1,5-di-(p-aminophenoxy) pentane (DAPP), an inhibitor of rhodopsin regeneration in the vertebrate retina, is shown to completely block the production of 11-cis-retinyl palmitate in the frog eye.	1,5-bis(p-aminophenoxy)pentane	26-57	rhodopsin	Homo sapiens	82-91
3875178-1	1985	The antischistosomal drug 1,5-di-(p-aminophenoxy) pentane (DAPP), an inhibitor of rhodopsin regeneration in the vertebrate retina, is shown to completely block the production of 11-cis-retinyl palmitate in the frog eye.	1,5-bis(p-aminophenoxy)pentane	59-63	rhodopsin	Homo sapiens	82-91
3875178-1	1985	The antischistosomal drug 1,5-di-(p-aminophenoxy) pentane (DAPP), an inhibitor of rhodopsin regeneration in the vertebrate retina, is shown to completely block the production of 11-cis-retinyl palmitate in the frog eye.	11-cis-Retinyl palmitate	178-202	rhodopsin	Homo sapiens	82-91
6093698-1	1984	This series of experiments systematically evaluated the effect of phospholipid headgroup structure on the interaction between rhodopsin and phospholipids.	Phospholipids	66-78	rhodopsin	Homo sapiens	126-135
6093698-1	1984	This series of experiments systematically evaluated the effect of phospholipid headgroup structure on the interaction between rhodopsin and phospholipids.	Phospholipids	140-153	rhodopsin	Homo sapiens	126-135
6093698-3	1984	First, ESR experiments involving spin-labeled phosphatidylserine, phosphatidic acid, and phosphatidylcholine demonstrated that, in the fluid-isotropic phase of dimyristoylphosphatidylcholine (DMPC)-rhodopsin membranes, the relative order of rhodopsin-induced immobilization was phosphatidic acid greater than phosphatidylcholine greater than phosphatidylserine.	Dimyristoylphosphatidylcholine	160-190	rhodopsin	Homo sapiens	198-207
6093698-3	1984	First, ESR experiments involving spin-labeled phosphatidylserine, phosphatidic acid, and phosphatidylcholine demonstrated that, in the fluid-isotropic phase of dimyristoylphosphatidylcholine (DMPC)-rhodopsin membranes, the relative order of rhodopsin-induced immobilization was phosphatidic acid greater than phosphatidylcholine greater than phosphatidylserine.	Dimyristoylphosphatidylcholine	160-190	rhodopsin	Homo sapiens	241-250
6093698-4	1984	Second, the effect of rhodopsin incorporation on the dimyristoylphosphatidylserine (DMPS) gel to liquid-crystalline phase transition was analyzed with ESR techniques.	dimyristoylphosphatidylserine	53-82	rhodopsin	Homo sapiens	22-31
6093698-4	1984	Second, the effect of rhodopsin incorporation on the dimyristoylphosphatidylserine (DMPS) gel to liquid-crystalline phase transition was analyzed with ESR techniques.	dimyristoylphosphatidylserine	84-88	rhodopsin	Homo sapiens	22-31
6093698-6	1984	A main result of this analysis was the finding that rhodopsin broadens and reduces the amplitude of the DMPS phase transition to a much smaller extent than it does the DMPC phase transition.	dimyristoylphosphatidylserine	104-108	rhodopsin	Homo sapiens	52-61
6093698-6	1984	A main result of this analysis was the finding that rhodopsin broadens and reduces the amplitude of the DMPS phase transition to a much smaller extent than it does the DMPC phase transition.	Dimyristoylphosphatidylcholine	168-172	rhodopsin	Homo sapiens	52-61
6093698-7	1984	When interpreted in terms of theoretical treatments of integral protein-lipid interactions, this indicates that rhodopsin has a lower affinity for DMPS than DMPC.	dimyristoylphosphatidylserine	147-151	rhodopsin	Homo sapiens	112-121
6436059-1	1984	The 48-kDa protein, a major protein of rod photoreceptor cells, is soluble in the dark but associates with the disk membranes when some (5-10%) of their rhodopsin has absorbed light and if this rhodopsin is additionally phosphorylated by ATP and rhodopsin kinase.	Adenosine Triphosphate	238-241	rhodopsin	Homo sapiens	194-203
6436059-2	1984	If rhodopsin has been phosphorylated and regenerated prior to the protein binding experiment, the binding of 48-kDa protein depends on light but no longer on the presence of ATP.	Adenosine Triphosphate	174-177	rhodopsin	Homo sapiens	3-12
6436059-3	1984	Another photoreceptor protein, GTP-binding protein, associates with both phosphorylated and unphosphorylated rhodopsin upon illumination.	Guanosine Triphosphate	31-34	rhodopsin	Homo sapiens	109-118
6436059-4	1984	Excess GTP-binding protein thereby displaces 48-kDa protein from phosphorylated disks; this indicates competition between these two proteins for binding sites on illuminated phosphorylated rhodopsin molecules.	Guanosine Triphosphate	7-10	rhodopsin	Homo sapiens	189-198
6705917-1	1984	The effect of sulfhydryl modification on the light-induced interaction between rhodopsin and the peripheral GTP-binding protein of the photoreceptor membrane (G-protein) has been investigated by time-resolved near-infrared light-scattering and polyacrylamide gel electrophoresis.	Guanosine Triphosphate	108-111	rhodopsin	Homo sapiens	79-88
6332991-3	1984	Rhodopsin, the visual pigment of retinal rod photoreceptor cells, is a membrane glycoprotein which consists of a single polypeptide chain (opsin) to which a chromophoric prosthetic group (II-cis-retinaldehyde) and two asparagine-linked oligosaccharide chains are covalently attached.	ii-cis-retinaldehyde	188-208	rhodopsin	Homo sapiens	0-9
6332991-3	1984	Rhodopsin, the visual pigment of retinal rod photoreceptor cells, is a membrane glycoprotein which consists of a single polypeptide chain (opsin) to which a chromophoric prosthetic group (II-cis-retinaldehyde) and two asparagine-linked oligosaccharide chains are covalently attached.	asparagine-linked oligosaccharide	218-251	rhodopsin	Homo sapiens	0-9
6091733-3	1984	In isotonic media, the PDE strongly associates with phospholipid membranes as well as with ROS and rhodopsin-phospholipid membranes.	Phospholipids	109-121	rhodopsin	Homo sapiens	99-108
6091733-5	1984	At a constant G-protein concentration, the PDE activity observed at saturation is 4 times greater for unilamellar rhodopsin-phospholipid vesicles with a lipid to rhodopsin ratio of 460 than for those with a ratio of 120.	Phospholipids	124-136	rhodopsin	Homo sapiens	114-123
6091733-5	1984	At a constant G-protein concentration, the PDE activity observed at saturation is 4 times greater for unilamellar rhodopsin-phospholipid vesicles with a lipid to rhodopsin ratio of 460 than for those with a ratio of 120.	Phospholipids	124-136	rhodopsin	Homo sapiens	162-171
6091733-9	1984	Rhodopsin-phospholipid vesicles devoid of enzyme activity were exposed to a light flash and then mixed in the dark in isotonic media with unilluminated ROS membranes which contained PDE and G protein.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
6092516-2	1984	The antibody (4A) inhibits guanine nucleotide binding to G-protein, the intermediate that links rhodopsin excitation to cGMP phosphodiesterase (PDE), inhibiting light-induced PDE activity as a consequence.	Guanine Nucleotides	27-45	rhodopsin	Homo sapiens	96-105
6429273-5	1984	A microspectrophotometer is used to examine the properties of rhodopsin in the two ends of the toad ROS.	ros	100-103	rhodopsin	Homo sapiens	62-71
6722121-7	1984	The chromatofocusing profile suggests that there may be multiple forms of rhodopsin with the same number of phosphates among some of the other phosphorylated forms of rhodopsin.	Phosphates	108-118	rhodopsin	Homo sapiens	74-83
6327365-3	1984	Adding GTP in the dark stimulates the production of 0.0003-0.001 mol cyclic GMP/mol rhodopsin per min.	Guanosine Triphosphate	7-10	rhodopsin	Homo sapiens	84-93
6090950-2	1984	Photoexcited rhodopsin (R*) binds to a multisubunit membrane protein called transducin (T) and stimulates the exchange of a bound GDP molecule for GTP.	Guanosine Diphosphate	130-133	rhodopsin	Homo sapiens	13-22
6090950-2	1984	Photoexcited rhodopsin (R*) binds to a multisubunit membrane protein called transducin (T) and stimulates the exchange of a bound GDP molecule for GTP.	Guanosine Triphosphate	147-150	rhodopsin	Homo sapiens	13-22
6086642-8	1984	When the light intensity is decreased to 8000 rhodopsins bleached per rod per s, the light-induced cGMP decrease is completed within 50 ms, with 7 X 10(5) cGMP molecules hydrolyzed per rhodopsin bleached.	Cyclic GMP	99-103	rhodopsin	Homo sapiens	46-55
6086642-8	1984	When the light intensity is decreased to 8000 rhodopsins bleached per rod per s, the light-induced cGMP decrease is completed within 50 ms, with 7 X 10(5) cGMP molecules hydrolyzed per rhodopsin bleached.	Cyclic GMP	155-159	rhodopsin	Homo sapiens	46-55
6086642-11	1984	The correlation of rapid changes in cGMP levels with changes in membrane current leave open the possibility that changes in cGMP concentration may be an obligatory step in the reaction sequence linking rhodopsin activation by light and the resultant decrease in sodium permeability of the plasma membrane.	Cyclic GMP	36-40	rhodopsin	Homo sapiens	202-211
6086642-11	1984	The correlation of rapid changes in cGMP levels with changes in membrane current leave open the possibility that changes in cGMP concentration may be an obligatory step in the reaction sequence linking rhodopsin activation by light and the resultant decrease in sodium permeability of the plasma membrane.	Cyclic GMP	124-128	rhodopsin	Homo sapiens	202-211
6086642-11	1984	The correlation of rapid changes in cGMP levels with changes in membrane current leave open the possibility that changes in cGMP concentration may be an obligatory step in the reaction sequence linking rhodopsin activation by light and the resultant decrease in sodium permeability of the plasma membrane.	Sodium	262-268	rhodopsin	Homo sapiens	202-211
6705917-1	1984	The effect of sulfhydryl modification on the light-induced interaction between rhodopsin and the peripheral GTP-binding protein of the photoreceptor membrane (G-protein) has been investigated by time-resolved near-infrared light-scattering and polyacrylamide gel electrophoresis.	polyacrylamide	244-258	rhodopsin	Homo sapiens	79-88
6705917-2	1984	It has been found that the modification of rhodopsin with the alkylating agent N-ethylmaleimide (NEM) does not affect its light-induced interaction with the G-protein.	Ethylmaleimide	79-95	rhodopsin	Homo sapiens	43-52
6705917-2	1984	It has been found that the modification of rhodopsin with the alkylating agent N-ethylmaleimide (NEM) does not affect its light-induced interaction with the G-protein.	Ethylmaleimide	97-100	rhodopsin	Homo sapiens	43-52
16593412-15	1984	The ATP effects can be rationalized within the above hypothesis as being due to ATP-dependent rhodopsin phosphorylation that adds negative charges to the membrane surface and tends to keep the membranes disaggregated.	Adenosine Triphosphate	4-7	rhodopsin	Homo sapiens	94-103
6707709-4	1984	Biochemical analysis of [3H]leucine-labelled retinas identified some of the labelled protein observed in autoradiographs of the rhabdomes as the visual pigment, rhodopsin.	Tritium	25-27	rhodopsin	Homo sapiens	161-170
6707709-4	1984	Biochemical analysis of [3H]leucine-labelled retinas identified some of the labelled protein observed in autoradiographs of the rhabdomes as the visual pigment, rhodopsin.	Leucine	28-35	rhodopsin	Homo sapiens	161-170
6707709-8	1984	Biochemical data gathered 8 h after injection of [3H]retinol indicated chromophore addition to both rhodopsin and retinochrome with retinochrome being more heavily labelled than rhodopsin.	Tritium	50-52	rhodopsin	Homo sapiens	100-109
6707709-8	1984	Biochemical data gathered 8 h after injection of [3H]retinol indicated chromophore addition to both rhodopsin and retinochrome with retinochrome being more heavily labelled than rhodopsin.	Vitamin A	53-60	rhodopsin	Homo sapiens	100-109
6707709-8	1984	Biochemical data gathered 8 h after injection of [3H]retinol indicated chromophore addition to both rhodopsin and retinochrome with retinochrome being more heavily labelled than rhodopsin.	Vitamin A	53-60	rhodopsin	Homo sapiens	178-187
16593412-15	1984	The ATP effects can be rationalized within the above hypothesis as being due to ATP-dependent rhodopsin phosphorylation that adds negative charges to the membrane surface and tends to keep the membranes disaggregated.	Adenosine Triphosphate	80-83	rhodopsin	Homo sapiens	94-103
6335935-0	1984	Suitability of retinol, retinal and retinyl palmitate for the regeneration of bleached rhodopsin in the isolated frog retina.	Vitamin A	15-22	rhodopsin	Homo sapiens	87-96
6322841-7	1984	Rhodopsin was the dominant phosphorylated protein, and the addition of adenosine cyclic 3",5"-phosphate (cAMP) or guanosine cyclic 3",5"-phosphate (cGMP) (10(-4) M) did not qualitatively alter the ROS phosphorylation pattern.	Cyclic GMP	148-152	rhodopsin	Homo sapiens	0-9
6322841-8	1984	The only cyclic nucleotide effect we could establish in these experiments was the inhibition of rhodopsin phosphorylation by cGMP.	Nucleotides, Cyclic	9-26	rhodopsin	Homo sapiens	96-105
6509940-4	1984	The recombination reaction of rhodopsin was best modeled by branched, multistep reaction schemes which included formation of noncovalent complexes, acid-base equilibria, and acid and base-catalyzed dehydration of a Schiff base intermediate.	Schiff Bases	215-226	rhodopsin	Homo sapiens	30-39
6533979-1	1984	Rhodopsin is one of those rare macromolecules whose inherent chromophore, 11-cis retinaldehyde, allows one to naturally observe triggered macromolecular changes on the timescale of picoseconds to minutes.	11-cis retinaldehyde	74-94	rhodopsin	Homo sapiens	0-9
6533983-11	1984	High resolution proton magnetic resonance spectroscopy was used to reinvestigate the structure and relative proportions of rhodopsin"s major and minor oligosaccharide chains.	Oligosaccharides	151-166	rhodopsin	Homo sapiens	123-132
6322841-8	1984	The only cyclic nucleotide effect we could establish in these experiments was the inhibition of rhodopsin phosphorylation by cGMP.	Cyclic GMP	125-129	rhodopsin	Homo sapiens	96-105
6335935-0	1984	Suitability of retinol, retinal and retinyl palmitate for the regeneration of bleached rhodopsin in the isolated frog retina.	retinol palmitate	36-53	rhodopsin	Homo sapiens	87-96
6543481-10	1984	The proportion of 11-cis retinol was frequently higher in eyes that had been protected from illumination, suggesting that IRBP plays a role in rhodopsin regeneration during dark-adaptation.	Vitamin A	18-32	rhodopsin	Homo sapiens	143-152
6313637-3	1983	Though it has been proposed that ATP mediates its effect through rapid phosphorylation of bleached rhodopsin, previous workers have found phosphorylation kinetics too slow by more than an order of magnitude to be causal in quenching of cyclic GMP phosphodiesterase activation.	Adenosine Triphosphate	33-36	rhodopsin	Homo sapiens	99-108
6313637-4	1983	In this report, we use preparations retaining more endogenous rhodopsin kinase, higher specific activity ATP, and cyclic GMP phosphodiesterase quenching conditions to show that ATP-dependent multiple phosphorylation of rhodopsin at very weak bleaches (10(-5)) is complete in less than 2 s, easily compatible with cyclic GMP phosphodiesterase quench times of 4 s measured under identical conditions.	Adenosine Triphosphate	177-180	rhodopsin	Homo sapiens	62-71
6313637-7	1983	We conclude that the speed of rhodopsin phosphorylation is, in fact, adequate to explain ATP quenching of cyclic GMP phosphodiesterase activation.	Adenosine Triphosphate	89-92	rhodopsin	Homo sapiens	30-39
6345185-3	1983	The carbohydrate groups present in the glycopeptide cleaved from purified [3H]-GlcNAc-rhodopsin by an enzyme from the retinal pigment epithelium were analyzed in terms of the size of the oligosaccharide chains, the sequence of the sugars and their anomeric linkages.	Carbohydrates	4-16	rhodopsin	Homo sapiens	86-95
6310406-3	1983	As a result of interaction with a rhodopsin photoproduct (possibly metarhodopsin II380), this GTP-binding protein exchanges a previously bound GDP for a GTP.	Guanosine Triphosphate	94-97	rhodopsin	Homo sapiens	34-43
6310406-3	1983	As a result of interaction with a rhodopsin photoproduct (possibly metarhodopsin II380), this GTP-binding protein exchanges a previously bound GDP for a GTP.	Guanosine Diphosphate	143-146	rhodopsin	Homo sapiens	34-43
6310406-3	1983	As a result of interaction with a rhodopsin photoproduct (possibly metarhodopsin II380), this GTP-binding protein exchanges a previously bound GDP for a GTP.	Guanosine Triphosphate	153-156	rhodopsin	Homo sapiens	34-43
6615501-0	1983	Lipid bilayer dynamics and rhodopsin-lipid interactions: new approach using high-resolution solid-state 13C NMR.	13c	104-107	rhodopsin	Homo sapiens	27-36
6615501-3	1983	Rotating-frame 13C relaxation times have been measured and are discussed in terms of lipid bilayer dynamics and rhodopsin-lipid interactions.	13c	15-18	rhodopsin	Homo sapiens	112-121
6345185-3	1983	The carbohydrate groups present in the glycopeptide cleaved from purified [3H]-GlcNAc-rhodopsin by an enzyme from the retinal pigment epithelium were analyzed in terms of the size of the oligosaccharide chains, the sequence of the sugars and their anomeric linkages.	Glycopeptides	39-51	rhodopsin	Homo sapiens	86-95
6345185-3	1983	The carbohydrate groups present in the glycopeptide cleaved from purified [3H]-GlcNAc-rhodopsin by an enzyme from the retinal pigment epithelium were analyzed in terms of the size of the oligosaccharide chains, the sequence of the sugars and their anomeric linkages.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	79-85	rhodopsin	Homo sapiens	86-95
6828860-2	1983	Fourier transform infrared difference spectroscopy is sensitive to conformational changes in both the protein and the retinylidene chromophore of rhodopsin.	retinylidene	118-130	rhodopsin	Homo sapiens	146-155
6835374-3	1983	It has been suggested that the initial step of this cascade, which leads to the activation of cyclic GMP phosphodiesterase (PDE), involves the interaction of a GTP-binding regulatory (G) protein with rhodopsin.	Guanosine Triphosphate	160-163	rhodopsin	Homo sapiens	200-209
6301538-0	1983	Stimulation of rhodopsin phosphorylation by guanine nucleotides in rod outer segments.	Guanine Nucleotides	44-63	rhodopsin	Homo sapiens	15-24
6301538-4	1983	GTP increased the phosphorylation of rhodopsin at concentrations as low as 100 nM, and guanosine 5"-(beta, gamma-imidotriphosphate), a relatively stable analogue of GTP, was nearly as effective as GTP.	Guanosine Triphosphate	0-3	rhodopsin	Homo sapiens	37-46
6301538-4	1983	GTP increased the phosphorylation of rhodopsin at concentrations as low as 100 nM, and guanosine 5"-(beta, gamma-imidotriphosphate), a relatively stable analogue of GTP, was nearly as effective as GTP.	Guanylyl Imidodiphosphate	87-130	rhodopsin	Homo sapiens	37-46
6301538-5	1983	Maximal stimulation of rhodopsin phosphorylation by GTP was observed at 2 microM.	Guanosine Triphosphate	52-55	rhodopsin	Homo sapiens	23-32
6301538-2	1983	The phosphorylation of rhodopsin, the major protein-staining band (Mr approximately 34 000-38 000), was markedly and specifically increased by exposure of rod outer segments to light; various guanine nucleotides (10 microM) including GMP, GDP, and GTP also specifically increased rhodopsin phosphorylation (up to 5-fold).	Guanine Nucleotides	192-211	rhodopsin	Homo sapiens	23-32
6301538-9	1983	With increasing concentrations of ROS proteins, the phosphorylation of rhodopsin was nonlinear, whereas in the presence of GTP (2 microM) linear increases in rhodopsin phosphorylation as a function of added ROS protein were observed.	Guanosine Triphosphate	123-126	rhodopsin	Homo sapiens	158-167
6301538-10	1983	These results suggest that GTP stimulates the phosphorylation of rhodopsin by ATP and that a GTP-sensitive inhibitor (or regulator) of rhodopsin phosphorylation may be present in ROS.	Guanosine Triphosphate	27-30	rhodopsin	Homo sapiens	65-74
6301538-2	1983	The phosphorylation of rhodopsin, the major protein-staining band (Mr approximately 34 000-38 000), was markedly and specifically increased by exposure of rod outer segments to light; various guanine nucleotides (10 microM) including GMP, GDP, and GTP also specifically increased rhodopsin phosphorylation (up to 5-fold).	guanosine 5'-monophosphorothioate	234-237	rhodopsin	Homo sapiens	23-32
6301538-10	1983	These results suggest that GTP stimulates the phosphorylation of rhodopsin by ATP and that a GTP-sensitive inhibitor (or regulator) of rhodopsin phosphorylation may be present in ROS.	Guanosine Triphosphate	27-30	rhodopsin	Homo sapiens	135-144
6301538-10	1983	These results suggest that GTP stimulates the phosphorylation of rhodopsin by ATP and that a GTP-sensitive inhibitor (or regulator) of rhodopsin phosphorylation may be present in ROS.	Adenosine Triphosphate	78-81	rhodopsin	Homo sapiens	65-74
6301538-10	1983	These results suggest that GTP stimulates the phosphorylation of rhodopsin by ATP and that a GTP-sensitive inhibitor (or regulator) of rhodopsin phosphorylation may be present in ROS.	Adenosine Triphosphate	78-81	rhodopsin	Homo sapiens	135-144
6601965-3	1983	These sites possess high affinity to GDP (Kd less than 10(-6) M) in dark-adapted preparations, and in the presence of bleached rhodopsin they effectively bind the non-hydrolizable analog of GTP--GPP (NH) P (Kd less than 10(-6) M).	Guanosine Diphosphate	37-40	rhodopsin	Homo sapiens	127-136
6601965-3	1983	These sites possess high affinity to GDP (Kd less than 10(-6) M) in dark-adapted preparations, and in the presence of bleached rhodopsin they effectively bind the non-hydrolizable analog of GTP--GPP (NH) P (Kd less than 10(-6) M).	gtp--gpp (nh) p	190-205	rhodopsin	Homo sapiens	127-136
6601965-4	1983	It is shown that one bleached rhodopsin molecule can induce the binding of up to 100 molecules of GPP (NH) P at low rhodopsin photolysis.	Guanylyl Imidodiphosphate	98-108	rhodopsin	Homo sapiens	30-39
6601965-4	1983	It is shown that one bleached rhodopsin molecule can induce the binding of up to 100 molecules of GPP (NH) P at low rhodopsin photolysis.	Guanylyl Imidodiphosphate	98-108	rhodopsin	Homo sapiens	116-125
6301538-10	1983	These results suggest that GTP stimulates the phosphorylation of rhodopsin by ATP and that a GTP-sensitive inhibitor (or regulator) of rhodopsin phosphorylation may be present in ROS.	Guanosine Triphosphate	93-96	rhodopsin	Homo sapiens	135-144
6301540-0	1983	Protein-phospholipid-cholesterol interaction in the photolysis of invertebrate rhodopsin.	Phospholipids	8-20	rhodopsin	Homo sapiens	79-88
6301540-0	1983	Protein-phospholipid-cholesterol interaction in the photolysis of invertebrate rhodopsin.	Cholesterol	21-32	rhodopsin	Homo sapiens	79-88
6301538-2	1983	The phosphorylation of rhodopsin, the major protein-staining band (Mr approximately 34 000-38 000), was markedly and specifically increased by exposure of rod outer segments to light; various guanine nucleotides (10 microM) including GMP, GDP, and GTP also specifically increased rhodopsin phosphorylation (up to 5-fold).	Guanosine Diphosphate	239-242	rhodopsin	Homo sapiens	23-32
6301538-2	1983	The phosphorylation of rhodopsin, the major protein-staining band (Mr approximately 34 000-38 000), was markedly and specifically increased by exposure of rod outer segments to light; various guanine nucleotides (10 microM) including GMP, GDP, and GTP also specifically increased rhodopsin phosphorylation (up to 5-fold).	Guanosine Triphosphate	248-251	rhodopsin	Homo sapiens	23-32
6830759-4	1983	(2) The accessibility of the labeled rhodopsin sites in reconstituted vesicles to N-methyl- and N-benzylpicolinium was studied in the dark and subsequent to rhodopsin bleaching.	n-methyl- and n-benzylpicolinium	82-114	rhodopsin	Homo sapiens	37-46
6830759-5	1983	Fluorescent-labeled rhodopsin was affinity purified in octyl glucoside from rod outer segments which were previously reacted with either the sulfhydryl-specific reagents, pyrenylmaleimide or monobromobimane, or reagents specific to amino groups, dansyl chloride or fluorescein isothiocyanate.	octyl-beta-D-glucoside	55-70	rhodopsin	Homo sapiens	20-29
6830759-0	1983	Rhodopsin in reconstituted phospholipid vesicles.	Phospholipids	27-39	rhodopsin	Homo sapiens	0-9
6830759-5	1983	Fluorescent-labeled rhodopsin was affinity purified in octyl glucoside from rod outer segments which were previously reacted with either the sulfhydryl-specific reagents, pyrenylmaleimide or monobromobimane, or reagents specific to amino groups, dansyl chloride or fluorescein isothiocyanate.	pyrenylmaleimide	171-187	rhodopsin	Homo sapiens	20-29
6830759-3	1983	The structure of purified rhodopsin was investigated by steady-state resonance energy transfer and fluorescence quenching techniques: (1) Fluorescence parameters and relative distances between rhodopsin sites labeled with fluorescent probes and the endogenous chromophore 11-cis-retinal were measured in micellar detergent solution and in reconstituted phospholipid vesicles.	Retinaldehyde	272-286	rhodopsin	Homo sapiens	26-35
6830759-5	1983	Fluorescent-labeled rhodopsin was affinity purified in octyl glucoside from rod outer segments which were previously reacted with either the sulfhydryl-specific reagents, pyrenylmaleimide or monobromobimane, or reagents specific to amino groups, dansyl chloride or fluorescein isothiocyanate.	monobromobimane	191-206	rhodopsin	Homo sapiens	20-29
6830759-3	1983	The structure of purified rhodopsin was investigated by steady-state resonance energy transfer and fluorescence quenching techniques: (1) Fluorescence parameters and relative distances between rhodopsin sites labeled with fluorescent probes and the endogenous chromophore 11-cis-retinal were measured in micellar detergent solution and in reconstituted phospholipid vesicles.	Phospholipids	353-365	rhodopsin	Homo sapiens	26-35
6830759-5	1983	Fluorescent-labeled rhodopsin was affinity purified in octyl glucoside from rod outer segments which were previously reacted with either the sulfhydryl-specific reagents, pyrenylmaleimide or monobromobimane, or reagents specific to amino groups, dansyl chloride or fluorescein isothiocyanate.	dansyl chloride	246-261	rhodopsin	Homo sapiens	20-29
6830759-5	1983	Fluorescent-labeled rhodopsin was affinity purified in octyl glucoside from rod outer segments which were previously reacted with either the sulfhydryl-specific reagents, pyrenylmaleimide or monobromobimane, or reagents specific to amino groups, dansyl chloride or fluorescein isothiocyanate.	Fluorescein-5-isothiocyanate	265-291	rhodopsin	Homo sapiens	20-29
6830760-0	1983	Rhodopsin in reconstituted phospholipid vesicles.	Phospholipids	27-39	rhodopsin	Homo sapiens	0-9
6830760-3	1983	The interactions between rhodopsin molecules in a micellar detergent solution (octyl glucoside) and in reconstituted phospholipid vesicles were studied in the dark and after bleaching.	octyl-beta-D-glucoside	79-94	rhodopsin	Homo sapiens	25-34
6830760-5	1983	Reactive sulfhydryl groups of rhodopsin were labeled with pyrenylmaleimide (donor) or monobromobimane (acceptor), whereas amino groups were labeled with dansyl chloride (donor) or fluorescein isothiocyanate (acceptor).	pyrenylmaleimide	58-74	rhodopsin	Homo sapiens	30-39
6830760-5	1983	Reactive sulfhydryl groups of rhodopsin were labeled with pyrenylmaleimide (donor) or monobromobimane (acceptor), whereas amino groups were labeled with dansyl chloride (donor) or fluorescein isothiocyanate (acceptor).	monobromobimane	86-101	rhodopsin	Homo sapiens	30-39
6830760-8	1983	Rhodopsin reconstituted in phospholipid vesicles appeared aggregated both in the dark and after bleaching.	Phospholipids	27-39	rhodopsin	Homo sapiens	0-9
6327179-5	1983	About 500 T alpha- GTPs are produced per photoexcited rhodopsin at low light levels.	alpha- gtps	12-23	rhodopsin	Homo sapiens	54-63
6303466-3	1983	The Schiff-base linkage between opsin and retinal in rhodopsin was not always necessary for the phosphodiesterase activation.	Schiff Bases	4-15	rhodopsin	Homo sapiens	53-62
6293577-1	1982	Activation of guanosine 3",5"-cyclic monophosphate (cGMP) phosphodiesterase (EC 3.1.4.35) in frog rod outer segment membrane by rhodopsin analogues has been investigated.	Cyclic GMP	14-50	rhodopsin	Homo sapiens	128-137
6293577-1	1982	Activation of guanosine 3",5"-cyclic monophosphate (cGMP) phosphodiesterase (EC 3.1.4.35) in frog rod outer segment membrane by rhodopsin analogues has been investigated.	Cyclic GMP	52-56	rhodopsin	Homo sapiens	128-137
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	beta-ionone	82-93	rhodopsin	Homo sapiens	110-119
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	Schiff Bases	37-48	rhodopsin	Homo sapiens	2-11
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	n-retinyl-opsin	58-73	rhodopsin	Homo sapiens	2-11
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	retinylidene	128-140	rhodopsin	Homo sapiens	2-11
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	retinylidene	128-140	rhodopsin	Homo sapiens	110-119
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	retinylidene	128-140	rhodopsin	Homo sapiens	110-119
6293577-6	1982	Consequently, it is suggested that the necessary portion of rhodopsin chromophore for the activation of the enzyme is the rigid conjugate double-bond system between the beta-ionone ring and the Schiff-base linkage in its all-trans form.	beta-ionone	169-180	rhodopsin	Homo sapiens	60-69
6293577-6	1982	Consequently, it is suggested that the necessary portion of rhodopsin chromophore for the activation of the enzyme is the rigid conjugate double-bond system between the beta-ionone ring and the Schiff-base linkage in its all-trans form.	Schiff Bases	194-205	rhodopsin	Homo sapiens	60-69
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	beta-ionone	82-93	rhodopsin	Homo sapiens	2-11
6295447-1	1982	Rotational diffusion of rhodopsin in reconstituted membranes of phosphatidylcholines of various alkyl chain lengths has been measured by using saturation-transfer electron spin resonance spectroscopy as a function of temperature and lipid/rhodopsin mole ratio.	Phosphatidylcholines	64-84	rhodopsin	Homo sapiens	24-33
6293577-2	1982	A rhodopsin analogue modified at the Schiff-base linkage (N-retinyl-opsin) or the beta-ionone ring (3-dehydro-rhodopsin) in the retinylidene chromophore of rhodopsin has some ability in activation of the enzyme.	beta-ionone	82-93	rhodopsin	Homo sapiens	110-119
7171574-0	1982	Rhodopsin-phospholipid reconstitution by dialysis removal of octyl glucoside.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
7171574-0	1982	Rhodopsin-phospholipid reconstitution by dialysis removal of octyl glucoside.	octyl-beta-D-glucoside	61-76	rhodopsin	Homo sapiens	0-9
7171574-5	1982	These results can be explained in terms of a lower stability of the OG-phospholipid micelles relative to the OG-phospholipid-rhodopsin micelles.	og-phospholipid	109-124	rhodopsin	Homo sapiens	125-134
6125514-8	1982	This modification of the guanine nucleotide-binding subunit of transducin is markedly enhanced by the bleaching of rhodopsin and by the addition of guanosine-5"-(beta, gamma-imino)triphosphate.	Guanine Nucleotides	25-43	rhodopsin	Homo sapiens	115-124
7138888-0	1982	The effect of phospholipid structure on the thermal stability of rhodopsin.	Phospholipids	14-26	rhodopsin	Homo sapiens	65-74
7138888-1	1982	The effect of the major headgroup classes of phospholipids on the conformational stability of rhodopsin is investigated.	Phospholipids	45-58	rhodopsin	Homo sapiens	94-103
6286681-3	1982	Photoexcitation of rhodopsin results in the formation of hundreds of molecules of GTP-transducin, which in turn activate many molecules of phosphodiesterase.	Guanosine Triphosphate	82-85	rhodopsin	Homo sapiens	19-28
6284715-3	1982	One of these kanamycin-sensitive RP4 derivatives, pVS1, was used as a mobilization vector in conjugation experiments on complex media where chromosomal Tn5 transfer to the recipient was selected.	Kanamycin	13-22	rhodopsin	Homo sapiens	33-36
6291601-0	1982	Effect of hydrogen ion concentration on rhodopsin-lipid interactions.	Hydrogen	10-18	rhodopsin	Homo sapiens	40-49
7107162-5	1982	In two patients with very low (less than 7 micrograms/dl) initial retinol levels and elevated thresholds, decreased rhodopsin densities were observed; rhodopsin density and thresholds returned to normal after treatment with oral vitamin A.	Vitamin A	66-73	rhodopsin	Homo sapiens	116-125
7107162-5	1982	In two patients with very low (less than 7 micrograms/dl) initial retinol levels and elevated thresholds, decreased rhodopsin densities were observed; rhodopsin density and thresholds returned to normal after treatment with oral vitamin A.	Vitamin A	229-238	rhodopsin	Homo sapiens	116-125
7107162-5	1982	In two patients with very low (less than 7 micrograms/dl) initial retinol levels and elevated thresholds, decreased rhodopsin densities were observed; rhodopsin density and thresholds returned to normal after treatment with oral vitamin A.	Vitamin A	229-238	rhodopsin	Homo sapiens	151-160
7107162-7	1982	Only marked decreased in plasma retinol were associated with elevations of dark-adapted threshold and decreases in rhodopsin density, suggesting that the tissues of patients with CF sequester vitamin A to maintain retinal function.	Vitamin A	32-39	rhodopsin	Homo sapiens	115-124
7076416-4	1982	By measuring rhodopsin regeneration in retinal homogenates incubated with 11-cis retinal, we estimated that the amount of vitamin A in the RPE-Ch of fully dark-adapted eyes would represent 2.5 mole equivalents of the retinal rhodopsin, a value similar to that found in the frog.	Vitamin A	122-131	rhodopsin	Homo sapiens	13-22
6979541-0	1982	Re-examination of rhodopsin structure by hydrogen exchange.	Hydrogen	41-49	rhodopsin	Homo sapiens	18-27
6979541-1	1982	The hydrogen exchange behavior of rhodopsin was re-examined by studies of the protein in the disc membrane and after solubilization in octyl glucoside.	Hydrogen	4-12	rhodopsin	Homo sapiens	34-43
6979541-1	1982	The hydrogen exchange behavior of rhodopsin was re-examined by studies of the protein in the disc membrane and after solubilization in octyl glucoside.	octyl-beta-D-glucoside	135-150	rhodopsin	Homo sapiens	34-43
7076416-4	1982	By measuring rhodopsin regeneration in retinal homogenates incubated with 11-cis retinal, we estimated that the amount of vitamin A in the RPE-Ch of fully dark-adapted eyes would represent 2.5 mole equivalents of the retinal rhodopsin, a value similar to that found in the frog.	Vitamin A	122-131	rhodopsin	Homo sapiens	225-234
6279759-7	1982	Rhodopsin phosphorylation is not stimulated by cyclic nucleotides, but is inhibited by calcium, with 50% inhibition being observed as the Ca++ concentration is increased from 10(-9) to 10(-3) M. A nucleotide binding site appears to regulate rhodopsin phosphorylation.	Calcium	87-94	rhodopsin	Homo sapiens	0-9
6285360-4	1982	Both effects of p[NH]ppG were completely dependent on the presence of bleached rhodopsin.	Guanylyl Imidodiphosphate	16-24	rhodopsin	Homo sapiens	79-88
7061462-0	1982	Evidence for protein-associated lipids from deuterium nuclear magnetic resonance studies of rhodopsin-dimyristoylphosphatidylcholine recombinants.	Dimyristoylphosphatidylcholine	102-132	rhodopsin	Homo sapiens	92-101
7061462-1	1982	The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated.	Dimyristoylphosphatidylcholine	124-154	rhodopsin	Homo sapiens	185-194
7061462-1	1982	The technique of deuterium magnetic resonance was used to study the orientational order of the perdeuterated acyl chains of dimyristoylphosphatidylcholine (DMPC-d54) reconstituted with rhodopsin between 0 and 23 degrees C. This range includes the gel to liquid crystalline phase transition of DMPC-d54 at 20 degrees C. Molar lipid/protein (L/P) ratios of L/P = infinity, 150, 50, 30, and 12 were investigated.	Dimyristoylphosphatidylcholine	156-160	rhodopsin	Homo sapiens	185-194
7074076-0	1982	Photoinduced calcium release from rhodopsin-phospholipid membrane vesicles.	Calcium	13-20	rhodopsin	Homo sapiens	34-43
7074076-0	1982	Photoinduced calcium release from rhodopsin-phospholipid membrane vesicles.	Phospholipids	44-56	rhodopsin	Homo sapiens	34-43
7074076-1	1982	Brief blue-green light exposure of rhodopsin-phospholipid membrane vesicles that contained divalent cations released the cations from the vesicles.	Phospholipids	45-57	rhodopsin	Homo sapiens	35-44
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	Phosphatidylcholines	96-115	rhodopsin	Homo sapiens	82-91
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	Phosphatidylcholines	96-115	rhodopsin	Homo sapiens	170-179
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	Cobalt(2+)	235-239	rhodopsin	Homo sapiens	82-91
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	Manganese(2+)	241-245	rhodopsin	Homo sapiens	82-91
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	Nickel(2+)	247-251	rhodopsin	Homo sapiens	82-91
7074076-4	1982	At 37 degrees C and an internal concentration of 30 mM Ca2+, the initial flux for rhodopsin-egg phosphatidylcholine membrane vesicles was 0.25 +/- 0.11 Ca2+ per bleached rhodopsin per s. Similar fluxes were observed for the release of Co2+, Mn2+, Ni2+, and Mg2+.	magnesium ion	257-261	rhodopsin	Homo sapiens	82-91
7074076-5	1982	The addition of proton uncouplers and lipophilic anions accelerated the rate to approximately Ca2+ per bleached rhodopsin per s. The flux was independent of the concentration of rhodopsin in the membranes and sensitive to the head-group composition of the rhodopsin-phospholipid vesicles.	Phospholipids	266-278	rhodopsin	Homo sapiens	112-121
6279759-7	1982	Rhodopsin phosphorylation is not stimulated by cyclic nucleotides, but is inhibited by calcium, with 50% inhibition being observed as the Ca++ concentration is increased from 10(-9) to 10(-3) M. A nucleotide binding site appears to regulate rhodopsin phosphorylation.	Calcium	87-94	rhodopsin	Homo sapiens	241-250
6978738-0	1982	Orientational changes of the absorbing dipole or retinal upon the conversion of rhodopsin to bathorhodopsin, lumirhodopsin, and isorhodopsin.	dipole	39-45	rhodopsin	Homo sapiens	80-89
6978738-1	1982	The orientational change of the absorbing dipole of the retinal chromophore in vertebrate rhodopsin (rhodo) upon photo-excitation to bathorhodopsin (batho), lumirhodopsin (lumi) and isorhodopsin (iso), has been studied by polarized absorption and linear dichroism measurements on magnetically oriented frog rod suspensions that were blocked at liquid nitrogen temperature.	dipole	42-48	rhodopsin	Homo sapiens	90-99
6978738-1	1982	The orientational change of the absorbing dipole of the retinal chromophore in vertebrate rhodopsin (rhodo) upon photo-excitation to bathorhodopsin (batho), lumirhodopsin (lumi) and isorhodopsin (iso), has been studied by polarized absorption and linear dichroism measurements on magnetically oriented frog rod suspensions that were blocked at liquid nitrogen temperature.	Nitrogen	351-359	rhodopsin	Homo sapiens	90-99
7098871-0	1982	Cyanoborohydride reduction of rhodopsin.	cyanoborohydride	0-16	rhodopsin	Homo sapiens	30-39
6175962-1	1982	Two-dimensional crystals of rhodopsin have been prepared from purified frog disk membranes by using the detergent Tween 80.	Polysorbates	114-122	rhodopsin	Homo sapiens	28-37
7074022-0	1982	Assignment and interpretation of hydrogen out-of-plane vibrations in the resonance Raman spectra of rhodopsin and bathorhodopsin.	Hydrogen	33-41	rhodopsin	Homo sapiens	100-109
19431520-0	1982	Rhodopsin-Phospholipid Reconstitution from Octyl Glucoside-solubilized Samples.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
19431520-0	1982	Rhodopsin-Phospholipid Reconstitution from Octyl Glucoside-solubilized Samples.	octyl-beta-D-glucoside	43-58	rhodopsin	Homo sapiens	0-9
7098896-0	1982	Detection and properties of rapid calcium release from binding sites in isolated rod outer segments upon photoexcitation of rhodopsin.	Calcium	34-41	rhodopsin	Homo sapiens	124-133
7098911-0	1982	13C NMR spectroscopy of the chromophore of rhodopsin.	13c	0-3	rhodopsin	Homo sapiens	43-52
6101134-1	1982	Relatively high proportions of long-chain, polyunsaturated fatty acids seem to be required in rod photoreceptor membranes in order to provide the precise microenvironment for the proper function of the visual pigment rhodopsin.	Fatty Acids, Unsaturated	43-70	rhodopsin	Homo sapiens	217-226
6983179-5	1982	In vitro regeneration experiments in which bleached rod outer segment fragments were added to 11-cis retinal showed that preincubation of retinal with MS-222 in ethanol prevents rhodopsin regeneration.	tricaine	151-157	rhodopsin	Homo sapiens	178-187
6212737-0	1982	Purification of rhodopsin on Agarose.	Sepharose	29-36	rhodopsin	Homo sapiens	16-25
6212743-0	1982	Borane dimethylamine reduction of the retinal--opsin linkage in rhodopsin.	dimethylamine	7-20	rhodopsin	Homo sapiens	64-73
6285125-0	1982	Purification of rhodopsin on hydroxyapatite columns, detergent exchange, and recombination with phospholipids.	Durapatite	29-43	rhodopsin	Homo sapiens	16-25
7123857-2	1982	Digitonin extracts made at 0 degrees contain two rhodopsin-like pigments, P562 and P512, in a ratio of about 5:4.	Digitonin	0-9	rhodopsin	Homo sapiens	49-58
6983179-5	1982	In vitro regeneration experiments in which bleached rod outer segment fragments were added to 11-cis retinal showed that preincubation of retinal with MS-222 in ethanol prevents rhodopsin regeneration.	Ethanol	161-168	rhodopsin	Homo sapiens	178-187
6983179-7	1982	We propose that the formation of a Schiff"s base between these two compounds blocks the recombination of rhodopsin, and in situ, leads to the inhibition of dark-adaptation.	schiff"s base	35-48	rhodopsin	Homo sapiens	105-114
6457631-3	1981	We have applied the formalism developed in this paper to the reaction describing the formation of rhodopsin from its apoprotein and 11-cis-retinal.	formalism	20-29	rhodopsin	Homo sapiens	98-107
7182999-0	1982	Rhodopsin-phospholipid complexes in apolar solvents: characteristics and mechanism of extraction.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
6305023-1	1982	About 2000 PDE molecules are gradually activated by one bleached rhodopsin molecule, R* on a toad disk membrane to yield a final enzyme velocity of about 2.5 x 10(6) cGMP hydrolyzed sec-1 bleached rhodopsin-1.	Cyclic GMP	166-170	rhodopsin	Homo sapiens	65-74
6305023-1	1982	About 2000 PDE molecules are gradually activated by one bleached rhodopsin molecule, R* on a toad disk membrane to yield a final enzyme velocity of about 2.5 x 10(6) cGMP hydrolyzed sec-1 bleached rhodopsin-1.	Cyclic GMP	166-170	rhodopsin	Homo sapiens	197-206
7306517-0	1981	Interaction of rhodopsin with two unsaturated phosphatidylcholines: a deuterium nuclear magnetic resonance study.	unsaturated phosphatidylcholines	34-66	rhodopsin	Homo sapiens	15-24
7306517-0	1981	Interaction of rhodopsin with two unsaturated phosphatidylcholines: a deuterium nuclear magnetic resonance study.	Deuterium	70-79	rhodopsin	Homo sapiens	15-24
7295672-1	1981	Phospholipid-free rhodopsin has been purified in the detergents sodium cholate and octaethylene glycol n-dodecyl ether (C12E8).	Phospholipids	0-12	rhodopsin	Homo sapiens	18-27
7295672-1	1981	Phospholipid-free rhodopsin has been purified in the detergents sodium cholate and octaethylene glycol n-dodecyl ether (C12E8).	Sodium Cholate	64-78	rhodopsin	Homo sapiens	18-27
7295672-1	1981	Phospholipid-free rhodopsin has been purified in the detergents sodium cholate and octaethylene glycol n-dodecyl ether (C12E8).	octaethylene glycol n-dodecyl ether	83-118	rhodopsin	Homo sapiens	18-27
7295672-1	1981	Phospholipid-free rhodopsin has been purified in the detergents sodium cholate and octaethylene glycol n-dodecyl ether (C12E8).	dodecyloctaethyleneglycol monoether	120-125	rhodopsin	Homo sapiens	18-27
7295672-5	1981	In sodium cholate, the smallest species present was found to be a trimer of the rhodopsin polypeptide chain, and this association was unaffected by exposure to light.	Sodium Cholate	3-17	rhodopsin	Homo sapiens	80-89
6457631-4	1981	Qualitatively, the results demonstrate that a significant portion of the observed decrease in the extent of recombination for rhodopsin solubilized in either sodium cholate or Tween 80 may be attributed to the partition of retinal into detergent micelles and that a detergent-induced protein denaturation need not be invoked to explain the data.	Sodium Cholate	158-172	rhodopsin	Homo sapiens	126-135
6457631-4	1981	Qualitatively, the results demonstrate that a significant portion of the observed decrease in the extent of recombination for rhodopsin solubilized in either sodium cholate or Tween 80 may be attributed to the partition of retinal into detergent micelles and that a detergent-induced protein denaturation need not be invoked to explain the data.	Polysorbates	176-184	rhodopsin	Homo sapiens	126-135
6457631-5	1981	We also discuss results for rhodopsin solubilized in a nonionic detergent (octaethylene glycol n-dodecyl ether) in which the detergent is clearly causing irreversible loss of the capability to recombine with 11-cis-retinal.	octaethylene glycol n-dodecyl ether	75-110	rhodopsin	Homo sapiens	28-37
6268183-0	1981	Activation of phosphodiesterase in frog rod outer segment by an intermediate of rhodopsin photolysis I. Guanosine 3",5"-cyclic monophosphate phosphodiesterase (EC 3.1.4.1) in frog rod outer segment prepared by a sucrose stepwise density gradient method was activated by light in the presence of GTP.	Sucrose	212-219	rhodopsin	Homo sapiens	80-89
6269656-3	1981	A decrease of rotational mobility of rhodopsin in ROS induced by prolonged illumination is shown to result from irreversible protein aggregation caused by disulfide bond formation between "hydrophobic" SH-groups of rhodopsin.	Disulfides	155-164	rhodopsin	Homo sapiens	37-46
6269656-3	1981	A decrease of rotational mobility of rhodopsin in ROS induced by prolonged illumination is shown to result from irreversible protein aggregation caused by disulfide bond formation between "hydrophobic" SH-groups of rhodopsin.	Disulfides	155-164	rhodopsin	Homo sapiens	215-224
6268183-0	1981	Activation of phosphodiesterase in frog rod outer segment by an intermediate of rhodopsin photolysis I. Guanosine 3",5"-cyclic monophosphate phosphodiesterase (EC 3.1.4.1) in frog rod outer segment prepared by a sucrose stepwise density gradient method was activated by light in the presence of GTP.	Guanosine Triphosphate	295-298	rhodopsin	Homo sapiens	80-89
6268183-1	1981	Rhodopsin in rod outer segment was solubilized with sucrose laurylmonoester and then purified by concanavalin A-Sepharose column.	Sucrose	52-59	rhodopsin	Homo sapiens	0-9
6268183-1	1981	Rhodopsin in rod outer segment was solubilized with sucrose laurylmonoester and then purified by concanavalin A-Sepharose column.	Sepharose	112-121	rhodopsin	Homo sapiens	0-9
6268183-2	1981	Addition of photo-bleached preparation of the purified rhodopsin to the crude rod outer segment, which had been prepared by 43% (w/w) sucrose floatation, caused the activation of phosphodiesterase in the dark, while each component of the photo-product eluted from the column (all-trans retinal and opsin) did not.	Sucrose	134-141	rhodopsin	Homo sapiens	55-64
6974654-2	1981	The maximal release (8--10 M Ca++/M bleached rhodopsin) occurred in monovalent cations--free medium (100 MM tris--HCl, 5 mM MgCl2, 5 mM ATP, pH--7.5), when at least 50% of visual pigment was bleached.	tris--hcl	108-117	rhodopsin	Homo sapiens	45-54
6456145-5	1981	The most effective inhibitors of rhodopsin regeneration were molecules whose structure could be superimposed on 9-cis or 11-cis retinal up to carbon atom 11.	Carbon	142-148	rhodopsin	Homo sapiens	33-42
7284342-3	1981	A large quantity of 7-cis-retinal was found in the photoproduct of rhodopsin irradiated at solid carbon dioxide temperature, but not at 15 degrees C and liquid N2 temperature.	Carbon Dioxide	97-111	rhodopsin	Homo sapiens	67-76
7280048-0	1981	The circular dichroism of sodium cholate solubilized rhodopsin.	Sodium Cholate	26-40	rhodopsin	Homo sapiens	53-62
6973361-5	1981	Photooxidation systems of lipids and rhodopsin also react differently to oxygen content in the incubation medium.	Oxygen	73-79	rhodopsin	Homo sapiens	37-46
7236611-4	1981	When [3H]AP-rhodopsin is digested with thermolysin in the disk membrane, both membrane-bound fragments of rhodopsin, F1 and F2, are found to contain [3H]AP.	Tritium	6-8	rhodopsin	Homo sapiens	12-21
7236611-4	1981	When [3H]AP-rhodopsin is digested with thermolysin in the disk membrane, both membrane-bound fragments of rhodopsin, F1 and F2, are found to contain [3H]AP.	Tritium	6-8	rhodopsin	Homo sapiens	106-115
7236611-4	1981	When [3H]AP-rhodopsin is digested with thermolysin in the disk membrane, both membrane-bound fragments of rhodopsin, F1 and F2, are found to contain [3H]AP.	Tritium	150-152	rhodopsin	Homo sapiens	12-21
7236611-4	1981	When [3H]AP-rhodopsin is digested with thermolysin in the disk membrane, both membrane-bound fragments of rhodopsin, F1 and F2, are found to contain [3H]AP.	Tritium	150-152	rhodopsin	Homo sapiens	106-115
7236611-5	1981	Reaction of the reagent appears to be restricted to the lipophilic surface of rhodopsin inasmuch as the presence of the nitrene scavenger glutathione in the aqueous medium does not significantly reduce 3H incorporation into rhodopsin.	phenylnitrene	120-127	rhodopsin	Homo sapiens	78-87
7236611-5	1981	Reaction of the reagent appears to be restricted to the lipophilic surface of rhodopsin inasmuch as the presence of the nitrene scavenger glutathione in the aqueous medium does not significantly reduce 3H incorporation into rhodopsin.	Glutathione	138-149	rhodopsin	Homo sapiens	78-87
7236611-7	1981	A factor of 4.4-fold in specific radioactivities of peptide pools was found, which suggests that some specificity has been shown in the reaction of [3H]AP toward different surfaces of rhodopsin.	Tritium	149-151	rhodopsin	Homo sapiens	184-193
6974654-2	1981	The maximal release (8--10 M Ca++/M bleached rhodopsin) occurred in monovalent cations--free medium (100 MM tris--HCl, 5 mM MgCl2, 5 mM ATP, pH--7.5), when at least 50% of visual pigment was bleached.	Magnesium Chloride	124-129	rhodopsin	Homo sapiens	45-54
6974654-2	1981	The maximal release (8--10 M Ca++/M bleached rhodopsin) occurred in monovalent cations--free medium (100 MM tris--HCl, 5 mM MgCl2, 5 mM ATP, pH--7.5), when at least 50% of visual pigment was bleached.	Adenosine Triphosphate	136-139	rhodopsin	Homo sapiens	45-54
7260134-0	1981	[Release of calcium ions from native outer segments rods after partial rhodopsin bleaching].	Calcium	12-19	rhodopsin	Homo sapiens	71-80
7255554-0	1981	The involvement of water at the retinal binding site in rhodopsin and early light-induced intramolecular proton transfer.	Water	19-24	rhodopsin	Homo sapiens	56-65
7252476-1	1981	The bleaching of rhodopsin by short-duration flashes of a xenon discharge lamp was studied in vivo in the cat retina with the aid of a rapid, spectral-scan fundus reflectometer.	Xenon	58-63	rhodopsin	Homo sapiens	17-26
7213599-0	1981	Rhodopsin-phospholipid interactions: dependence of rate of the meta I to meta II transition on the level of associated disk phospholipid.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
7213599-0	1981	Rhodopsin-phospholipid interactions: dependence of rate of the meta I to meta II transition on the level of associated disk phospholipid.	Phospholipids	124-136	rhodopsin	Homo sapiens	0-9
7213599-1	1981	Solubilization of retinal rod outer segment disk membranes in octyl glucoside was employed to prepare rhodopsin samples with varying amounts of associated disk phospholipid.	octyl-beta-D-glucoside	62-77	rhodopsin	Homo sapiens	102-111
7213599-3	1981	The rate constant for the formation of meta II increased from 6.9 X 10(3) to 19.5 X 10(3) s-1 as the molar ratio of phospholipid per rhodopsin fell from 35 to 5.	Phospholipids	116-128	rhodopsin	Homo sapiens	133-142
7213599-4	1981	The activation free energy for this process had a linear dependence on the level of phospholipid, with a slope of 24 cal/mol of rhodopsin-associated phospholipid.	Phospholipids	84-96	rhodopsin	Homo sapiens	128-137
7213599-4	1981	The activation free energy for this process had a linear dependence on the level of phospholipid, with a slope of 24 cal/mol of rhodopsin-associated phospholipid.	Phospholipids	149-161	rhodopsin	Homo sapiens	128-137
6278004-1	1981	A specific protein associated with rod-outer-segment disc membranes binds GTP only in the presence of bleached rhodopsin.	Guanosine Triphosphate	74-77	rhodopsin	Homo sapiens	111-120
7470492-2	1981	The shift of the absorption maximum od the pigment from that of the protonated Schiff base of the chromophore for 5,6-dihydrobacteriorhodopsin is small compared to that of the native pigment, suggesting that negative charges similar to those controlling the lambda max of visual pigment rhodopsin exist near the cyclohexyl ring.	Schiff Bases	79-90	rhodopsin	Homo sapiens	133-142
6259273-3	1981	The dark levels of cyclic GMP also can be suppressed to approximately 0.007 mol/mol of rhodopsin by increasing the concentration of calcium from 10(-9) M to 2 x 10(-9) M, and they remain at this level as calcium concentration is raised to 10(-3) M. The final level to which illumination reduces cyclic GMP in unaffected by the calcium concentration between 10(-9) and 10(-3) M. The maximal light-induced decrease in cyclic GMP occurs within 1 s from the onset of illumination at all calcium concentrations.	Calcium	204-211	rhodopsin	Homo sapiens	87-96
6259273-3	1981	The dark levels of cyclic GMP also can be suppressed to approximately 0.007 mol/mol of rhodopsin by increasing the concentration of calcium from 10(-9) M to 2 x 10(-9) M, and they remain at this level as calcium concentration is raised to 10(-3) M. The final level to which illumination reduces cyclic GMP in unaffected by the calcium concentration between 10(-9) and 10(-3) M. The maximal light-induced decrease in cyclic GMP occurs within 1 s from the onset of illumination at all calcium concentrations.	Calcium	132-139	rhodopsin	Homo sapiens	87-96
7213657-0	1980	Effect of phospholipid and detergent on the Schiff base of cephalopod rhodopsin and metarhodopsin.	Phospholipids	10-22	rhodopsin	Homo sapiens	70-79
6259273-3	1981	The dark levels of cyclic GMP also can be suppressed to approximately 0.007 mol/mol of rhodopsin by increasing the concentration of calcium from 10(-9) M to 2 x 10(-9) M, and they remain at this level as calcium concentration is raised to 10(-3) M. The final level to which illumination reduces cyclic GMP in unaffected by the calcium concentration between 10(-9) and 10(-3) M. The maximal light-induced decrease in cyclic GMP occurs within 1 s from the onset of illumination at all calcium concentrations.	Calcium	204-211	rhodopsin	Homo sapiens	87-96
6259273-3	1981	The dark levels of cyclic GMP also can be suppressed to approximately 0.007 mol/mol of rhodopsin by increasing the concentration of calcium from 10(-9) M to 2 x 10(-9) M, and they remain at this level as calcium concentration is raised to 10(-3) M. The final level to which illumination reduces cyclic GMP in unaffected by the calcium concentration between 10(-9) and 10(-3) M. The maximal light-induced decrease in cyclic GMP occurs within 1 s from the onset of illumination at all calcium concentrations.	Calcium	204-211	rhodopsin	Homo sapiens	87-96
6264430-1	1981	Photolyzed rhodopsin catalyzes the exchange of GTP for FDP bound to a protein in retinal rod outer segments.	Guanosine Triphosphate	47-50	rhodopsin	Homo sapiens	11-20
6264430-8	1981	Reconstituted membranes containing transducin and rhodopsin but no phosphodiesterase exhibit GTPase activity and amplified binding of guanosine 5"[beta, gamma-imido]triphosphate (p[NH]ppG), a nonhydrolyzable analog of GTP, on illumination.	Guanylyl Imidodiphosphate	134-177	rhodopsin	Homo sapiens	50-59
6264430-8	1981	Reconstituted membranes containing transducin and rhodopsin but no phosphodiesterase exhibit GTPase activity and amplified binding of guanosine 5"[beta, gamma-imido]triphosphate (p[NH]ppG), a nonhydrolyzable analog of GTP, on illumination.	Guanylyl Imidodiphosphate	179-187	rhodopsin	Homo sapiens	50-59
6264430-8	1981	Reconstituted membranes containing transducin and rhodopsin but no phosphodiesterase exhibit GTPase activity and amplified binding of guanosine 5"[beta, gamma-imido]triphosphate (p[NH]ppG), a nonhydrolyzable analog of GTP, on illumination.	Guanosine Triphosphate	93-96	rhodopsin	Homo sapiens	50-59
6264430-9	1981	A single photolyzed rhodopsin molecule led to the uptake of p[NH]ppG by 71 molecules of transducin.	Guanylyl Imidodiphosphate	60-68	rhodopsin	Homo sapiens	20-29
7314483-0	1981	Effects of products of phospholipid hydrolysis by phospholipases on rhodopsin thermal stability in photoreceptor membranes.	Phospholipids	23-35	rhodopsin	Homo sapiens	68-77
7213657-0	1980	Effect of phospholipid and detergent on the Schiff base of cephalopod rhodopsin and metarhodopsin.	Schiff Bases	44-55	rhodopsin	Homo sapiens	70-79
6935647-0	1980	Wavelength regulation in rhodopsin: effects of dipoles and amino acid side chains.	dipoles	47-54	rhodopsin	Homo sapiens	25-34
6935647-1	1980	The effects of dipoles and aromatic amino acid side-chain models on the absorption and optical activity of the rhodopsin chromophore were calculated by using perturbation theory, and the results were compared with those of a Pariser-Parr-Pople calculation for the unperturbed system.	dipoles	15-22	rhodopsin	Homo sapiens	111-120
6935647-1	1980	The effects of dipoles and aromatic amino acid side-chain models on the absorption and optical activity of the rhodopsin chromophore were calculated by using perturbation theory, and the results were compared with those of a Pariser-Parr-Pople calculation for the unperturbed system.	Amino Acids, Aromatic	27-46	rhodopsin	Homo sapiens	111-120
6935647-4	1980	However, the charge separation in tyrosine is sufficient to cause substantial electrostatic perturbation; in fact, the effect of tyrosine is large enough to approximately many of the spectral properties of rhodopsin quantitatively.	Tyrosine	34-42	rhodopsin	Homo sapiens	206-215
6935647-4	1980	However, the charge separation in tyrosine is sufficient to cause substantial electrostatic perturbation; in fact, the effect of tyrosine is large enough to approximately many of the spectral properties of rhodopsin quantitatively.	Tyrosine	129-137	rhodopsin	Homo sapiens	206-215
7378347-7	1980	The remaining 10% of the rhodopsin amino groups are inaccessible to either type of imidate and are largely accounted for by the single lysine residue which specifically binds the chromophore retinal.	Lysine	135-141	rhodopsin	Homo sapiens	25-34
7429764-1	1980	Retinas of postmortem human donor eyes retained the high-affinity mechanism for uptake of 3H-taurine, the capacity to synthesize rhodopsin from 14C-amino acids, and the ability to incorporate inorganic 32P-phosphate into rhodopsin with exposure to light for 4 to 4 1/2 hr.	14c-amino acids	144-159	rhodopsin	Homo sapiens	129-138
7454849-0	1980	Rhodopsin-phospholipid interaction in detergent and in the disk.	Phospholipids	10-22	rhodopsin	Homo sapiens	0-9
6772971-1	1980	The hypothesis of Yoshikami and Hagins that calcium ions act as diffusible transmitter molecules between the photochemistry of rhodopsin and the subsequent electrical events at the outer plasma membrane of rods initiated many investigations on light-stimulated calcium release in vertebrate photoreceptor cells (see refs 2, 3).	Calcium	44-51	rhodopsin	Homo sapiens	127-136
7417541-1	1980	The interaction between rhodopsin SH-groups in the photoreceptor membrane suspension with different titrating reagents (Ag HOGM, DTNB) was studied.	Dithionitrobenzoic Acid	129-133	rhodopsin	Homo sapiens	24-33
7396520-0	1980	Effect of tunicamycin on the glycosylation of rhodopsin.	Tunicamycin	10-21	rhodopsin	Homo sapiens	46-55
6930647-0	1980	Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments.	Guanosine Triphosphate	47-50	rhodopsin	Homo sapiens	11-20
6930647-0	1980	Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments.	Guanosine Diphosphate	61-64	rhodopsin	Homo sapiens	11-20
6930647-9	1980	This corresponds to the catalyzed exchange of 500 p[NH]ppG for bound GDP per photolyzed rhodopsin.	[nh]ppg	51-58	rhodopsin	Homo sapiens	88-97
6930647-9	1980	This corresponds to the catalyzed exchange of 500 p[NH]ppG for bound GDP per photolyzed rhodopsin.	Guanosine Diphosphate	69-72	rhodopsin	Homo sapiens	88-97
6930647-15	1980	GTP per photolyzed rhodopsin may be the first stage of amplification in visual excitation.	Guanosine Triphosphate	0-3	rhodopsin	Homo sapiens	19-28
7370104-3	1980	Rhodopsin, minor membrane proteins, and lipids all incorporate the (nitrophenyl)[35S]taurine (NPT) label.	(nitrophenyl)[35s]taurine	67-92	rhodopsin	Homo sapiens	0-9
7370104-6	1980	NAPT modifies rhodopsin in the membrane in a selective manner; some cyanogen bromide peptides of NPT-rhodopsin contain appreciable NPT label and some contain essentially none.	Cyanogen Bromide	68-84	rhodopsin	Homo sapiens	101-110
7370104-8	1980	Rhodopsin"s carboxyl-terminal cyanogen bromide peptides are well labeled when the protein is modified in disk membranes but the amino-terminal peptide is poorly labeled.	Cyanogen Bromide	30-46	rhodopsin	Homo sapiens	0-9
7260258-3	1980	The anisotropy of the volume susceptibilities of frog rhodopsin is calculated to be 4.4 X 10(-8) cgs unit/cm3, which corresponds to 1.5 X 10(-27) cgs unit/molecule, or 9.0 X 10(-4) cgs unit/mol.	cysteinylglycine	97-100	rhodopsin	Homo sapiens	54-63
7260258-3	1980	The anisotropy of the volume susceptibilities of frog rhodopsin is calculated to be 4.4 X 10(-8) cgs unit/cm3, which corresponds to 1.5 X 10(-27) cgs unit/molecule, or 9.0 X 10(-4) cgs unit/mol.	cysteinylglycine	146-149	rhodopsin	Homo sapiens	54-63
7260258-3	1980	The anisotropy of the volume susceptibilities of frog rhodopsin is calculated to be 4.4 X 10(-8) cgs unit/cm3, which corresponds to 1.5 X 10(-27) cgs unit/molecule, or 9.0 X 10(-4) cgs unit/mol.	cysteinylglycine	146-149	rhodopsin	Homo sapiens	54-63
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	Carbon	144-145	rhodopsin	Homo sapiens	37-46
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	Carbon	144-145	rhodopsin	Homo sapiens	203-212
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	Carbon	148-149	rhodopsin	Homo sapiens	37-46
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	Carbon	148-149	rhodopsin	Homo sapiens	203-212
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	n-retinylidene schiff base	173-199	rhodopsin	Homo sapiens	37-46
7388122-3	1980	The application of our method to the rhodopsin/Meta II transition reveals signals which can tentatively be ascribed to the disappearance of the C = C-band of the protonated N-retinylidene Schiff base in rhodopsin.	n-retinylidene schiff base	173-199	rhodopsin	Homo sapiens	203-212
20487742-5	1980	Phosphorylation of rhodopsin in single rod outer segments may occur at a rate of 2 moles of phosphate incorporated per mol rhodopsin per minute with a half-time of less than 30 seconds.	Phosphates	92-101	rhodopsin	Homo sapiens	123-132
497178-0	1979	Rhodopsin--phospholipid complexes in apolar environments: photochemical characterization.	Phospholipids	11-23	rhodopsin	Homo sapiens	0-9
20487725-0	1980	The lipid intermediate pathway in the retina for the activation of carbohydrates involved in the glycosylation of rhodopsin.	Carbohydrates	67-80	rhodopsin	Homo sapiens	114-123
20487725-4	1980	The participation of the dolichol pathway in the glycosylation of rhodopsin was demonstrated by the inhibition of core-region glycosylation of this glycoprotein by the antibiotic, tunicamycin.	Dolichols	25-33	rhodopsin	Homo sapiens	66-75
20487725-4	1980	The participation of the dolichol pathway in the glycosylation of rhodopsin was demonstrated by the inhibition of core-region glycosylation of this glycoprotein by the antibiotic, tunicamycin.	Tunicamycin	180-191	rhodopsin	Homo sapiens	66-75
20487742-2	1980	The even distribution of label in totally bleached rod outer segments and partial labeling of rod outer segments after local illumination indicates that the light induced transfer of (32)P from exogenous (?-(32)P) ATP to rhodopsin is not restricted to particular parts of the outer segment.	Adenosine Triphosphate	214-217	rhodopsin	Homo sapiens	221-230
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	69-74	rhodopsin	Homo sapiens	35-44
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	69-74	rhodopsin	Homo sapiens	129-138
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	69-74	rhodopsin	Homo sapiens	129-138
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	193-198	rhodopsin	Homo sapiens	35-44
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	193-198	rhodopsin	Homo sapiens	129-138
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Phosphorus-32	193-198	rhodopsin	Homo sapiens	129-138
20487742-3	1980	Light activated phosphorylation of rhodopsin in retinas incubated in (32)P(i) starts with the formation of a gradient of labeled rhodopsin suggesting that either light affects the formation of (32)P labeled ATP or that outer segments contain a gradient of a diffusable metabolite involved in the phosphorylation of rhodopsin.	Adenosine Triphosphate	207-210	rhodopsin	Homo sapiens	35-44
20487742-5	1980	Phosphorylation of rhodopsin in single rod outer segments may occur at a rate of 2 moles of phosphate incorporated per mol rhodopsin per minute with a half-time of less than 30 seconds.	Phosphates	92-101	rhodopsin	Homo sapiens	19-28
6444752-4	1980	The oligosaccharide moieties of rhodopsin also appear localized within the disks.	Oligosaccharides	4-19	rhodopsin	Homo sapiens	32-41
6444752-6	1980	Rhodopsin oligosaccharides as well as some fraction of the intradisk polysaccharide appear to have extended saccharide chains preferentially oriented perpendicular to the surface of the disk membrane.	Carbohydrates	15-25	rhodopsin	Homo sapiens	0-9
317090-1	1979	Frog rod outer segments contain approximately 0.25 mol of GTP and 0.25 mol of ATP per mol of rhodopsin 3 min after their isolation from the retina.	Adenosine Triphosphate	78-81	rhodopsin	Homo sapiens	93-102
317090-3	1979	Concentrations of GTP and ATP decline in parallel over the next 4 min to reach relatively stable levels of 0.1 mol per mol of rhodopsin.	Guanosine Triphosphate	18-21	rhodopsin	Homo sapiens	126-135
317090-3	1979	Concentrations of GTP and ATP decline in parallel over the next 4 min to reach relatively stable levels of 0.1 mol per mol of rhodopsin.	Adenosine Triphosphate	26-29	rhodopsin	Homo sapiens	126-135
317090-19	1979	Known light-dependent reactions involving cyclic nucleotide transformations and rhodopsin phosphorylation appear to account for only a small fraction of the light-induced GTP decrease.	Guanosine Triphosphate	171-174	rhodopsin	Homo sapiens	80-89
518847-0	1979	Proton and carbon-13 nuclear magnetic resonance studies of rhodopsin-phospholipid interactions.	Carbon-13	11-20	rhodopsin	Homo sapiens	59-68
518847-0	1979	Proton and carbon-13 nuclear magnetic resonance studies of rhodopsin-phospholipid interactions.	Phospholipids	69-81	rhodopsin	Homo sapiens	59-68
518847-1	1979	Proton and carbon-13 nuclear magnetic resonance (1H and 13C NMR) spectra of rhodopsin-phospholipid membrane vesicles and sonicated disk membranes are presented and discussed.	Carbon	11-17	rhodopsin	Homo sapiens	76-85
518847-1	1979	Proton and carbon-13 nuclear magnetic resonance (1H and 13C NMR) spectra of rhodopsin-phospholipid membrane vesicles and sonicated disk membranes are presented and discussed.	Hydrogen	49-51	rhodopsin	Homo sapiens	76-85
518847-1	1979	Proton and carbon-13 nuclear magnetic resonance (1H and 13C NMR) spectra of rhodopsin-phospholipid membrane vesicles and sonicated disk membranes are presented and discussed.	Carbon-13	56-59	rhodopsin	Homo sapiens	76-85
518847-1	1979	Proton and carbon-13 nuclear magnetic resonance (1H and 13C NMR) spectra of rhodopsin-phospholipid membrane vesicles and sonicated disk membranes are presented and discussed.	Phospholipids	86-98	rhodopsin	Homo sapiens	76-85
518847-4	1979	The proton NMR data indicate the phospholipid molecules exchange rapidly (less than 10(-3) s) between the bulk membrane lipid and the lipid in the immediate proximity of the rhodopsin.	Phospholipids	33-45	rhodopsin	Homo sapiens	174-183
497189-1	1979	Visual pigment extracts prepared from rhabdomeric membranes of vitamin A deficient blowflies contain a 5-10 times lower concentration of rhodopsin than extracts from flies which were raised on a vitamin A rich diet.	Vitamin A	63-72	rhodopsin	Homo sapiens	137-146
497189-2	1979	Spectrophotometry showed that digitonin-solubilized rhodopsin from blowfly photoreceptors R1-6 has an absorbance maximum at about 490 nm, but no unusually enhanced beta-band in the ultraviolet.	Digitonin	30-39	rhodopsin	Homo sapiens	52-61
447724-4	1979	The unusual features of the sugar chains of rhodopsin molecule seem to support the proposed processing pathway for the biosynthesis of asparagine-linked sugar chains of glycoproteins.	Sugars	28-33	rhodopsin	Homo sapiens	44-53
512631-1	1979	Mosquito rhodopsin is a digitonin-soluble membrane protein of molecular weight 39,000 daltons, as determined by sodium dodecyl sulfate gel electrophoresis.	Digitonin	24-33	rhodopsin	Homo sapiens	9-18
512631-1	1979	Mosquito rhodopsin is a digitonin-soluble membrane protein of molecular weight 39,000 daltons, as determined by sodium dodecyl sulfate gel electrophoresis.	Sodium Dodecyl Sulfate	112-134	rhodopsin	Homo sapiens	9-18
447724-4	1979	The unusual features of the sugar chains of rhodopsin molecule seem to support the proposed processing pathway for the biosynthesis of asparagine-linked sugar chains of glycoproteins.	Asparagine	135-145	rhodopsin	Homo sapiens	44-53
447724-4	1979	The unusual features of the sugar chains of rhodopsin molecule seem to support the proposed processing pathway for the biosynthesis of asparagine-linked sugar chains of glycoproteins.	Sugars	153-158	rhodopsin	Homo sapiens	44-53
311826-2	1979	Aspartate-isolated photoresponses of the frog"s rods to weak and strong flashes have been recorded during dark-adaptation after bleaching a fraction of rhodopsin (generally 4--30%).	Aspartic Acid	0-9	rhodopsin	Homo sapiens	152-161
223156-1	1979	The microviscosity of rhodopsin boundary lipids was studied with a spin-labeled fatty acid covalently attached to rhodopsin, in rhodopsin-egg lecithin vesicles.	Fatty Acids	80-90	rhodopsin	Homo sapiens	22-31
223156-1	1979	The microviscosity of rhodopsin boundary lipids was studied with a spin-labeled fatty acid covalently attached to rhodopsin, in rhodopsin-egg lecithin vesicles.	Fatty Acids	80-90	rhodopsin	Homo sapiens	114-123
223156-1	1979	The microviscosity of rhodopsin boundary lipids was studied with a spin-labeled fatty acid covalently attached to rhodopsin, in rhodopsin-egg lecithin vesicles.	Fatty Acids	80-90	rhodopsin	Homo sapiens	114-123
451006-0	1979	Rhodopsin: its molecular substructure and phospholipid interactions.	Phospholipids	42-54	rhodopsin	Homo sapiens	0-9
451007-0	1979	Light-regulated permeability of rhodopsin-phospholipid membrane vesicles.	Phospholipids	42-54	rhodopsin	Homo sapiens	32-41
284349-3	1979	These effects show that the strength of the C=N bond and the degree of protonation of the Schiff base nitrogen are the same in bathorhodopsin, rhodopsin, and isorhodopsin.	Carbon	44-45	rhodopsin	Homo sapiens	132-141
284349-3	1979	These effects show that the strength of the C=N bond and the degree of protonation of the Schiff base nitrogen are the same in bathorhodopsin, rhodopsin, and isorhodopsin.	Nitrogen	46-47	rhodopsin	Homo sapiens	132-141
284349-3	1979	These effects show that the strength of the C=N bond and the degree of protonation of the Schiff base nitrogen are the same in bathorhodopsin, rhodopsin, and isorhodopsin.	Schiff Bases	90-101	rhodopsin	Homo sapiens	132-141
284349-3	1979	These effects show that the strength of the C=N bond and the degree of protonation of the Schiff base nitrogen are the same in bathorhodopsin, rhodopsin, and isorhodopsin.	Nitrogen	102-110	rhodopsin	Homo sapiens	132-141
728379-0	1978	A vibrational analysis of rhodopsin and bacteriorhodopsin chromophore analogues: resonance Raman and infrared spectroscopy of chemically modified retinals and Schiff bases.	Schiff Bases	159-171	rhodopsin	Homo sapiens	26-35
728379-4	1978	Band assignments were made to specific vibrational motions, and these assignments have led to a detailed understanding of the spectral features observed in the resonance raman spectra of the retinylidene chromophore in rhodopsin and bacteriorhodopsin.	retinylidene	191-203	rhodopsin	Homo sapiens	219-228
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	Fatty Acids	48-65	rhodopsin	Homo sapiens	6-15
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	Sucrose	69-76	rhodopsin	Homo sapiens	6-15
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	monolaurate	78-89	rhodopsin	Homo sapiens	6-15
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	monostearate	94-106	rhodopsin	Homo sapiens	6-15
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	DEAE-Cellulose	124-138	rhodopsin	Homo sapiens	6-15
708776-2	1978	Squid rhodopsin was extracted with solutions of fatty acid esters of sucrose (monolaurate and monostearate) and purified by DEAE-cellulose and concanavalin A-Sepharose affinity chromatography.	Sepharose	158-167	rhodopsin	Homo sapiens	6-15
708776-3	1978	The purified rhodopsin (A280/A480 = 2.5) contained 2.3 mol of glucosamine and 1.2 mol of phospholipid per mol of rhodopsin.	Glucosamine	62-73	rhodopsin	Homo sapiens	13-22
708776-3	1978	The purified rhodopsin (A280/A480 = 2.5) contained 2.3 mol of glucosamine and 1.2 mol of phospholipid per mol of rhodopsin.	Phospholipids	89-101	rhodopsin	Homo sapiens	13-22
26397-0	1978	Kinetic study of photoregeneration process of digitonin-solubilized squid rhodopsin.	Digitonin	46-55	rhodopsin	Homo sapiens	74-83
26397-1	1978	In the photoregeneration process of squid rhodopsin, an intermediate has been found at neutral pH values (phosphate buffer) with a flash light (lambda greater than 540 nm).	Phosphates	106-115	rhodopsin	Homo sapiens	42-51
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Guanosine Triphosphate	18-40	rhodopsin	Homo sapiens	288-297
77856-2	1978	These components included (1) an acidic polysaccharide texture, (2) free aldehyde groups which arise during formalin fixation and (3) the oligosaccharide chains of rhodopsin.	Oligosaccharides	138-153	rhodopsin	Homo sapiens	164-173
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Guanosine Triphosphate	42-45	rhodopsin	Homo sapiens	288-297
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Guanosine Diphosphate	79-100	rhodopsin	Homo sapiens	288-297
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Guanosine Diphosphate	102-105	rhodopsin	Homo sapiens	288-297
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Phosphates	31-40	rhodopsin	Homo sapiens	288-297
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	p1	122-124	rhodopsin	Homo sapiens	288-297
209180-2	1978	The hydrolysis of guanosine triphosphate (GTP) and the consequent formation of guanosine diphosphate (GDP) and phosphate (P1) are activated by light in a suspension of broken retinal rods: the hydrolysis rate with GTP in the micrometer concentration range is 2.5-3.5 n-mole/min per mg of rhodopsin in the preparation.	Guanosine Triphosphate	214-217	rhodopsin	Homo sapiens	288-297
743909-0	1978	[Role of lipids in the thermostability of rhodopsin in photoreceptor membranes by the technic of 1H NMR spectroscopy].	Hydrogen	97-99	rhodopsin	Homo sapiens	42-51
642003-0	1978	Resonance Raman spectroscopy of chemically modified retinals: assigning the carbon--methyl vibrations in the resonance Raman spectrum of rhodopsin.	Carbon	76-82	rhodopsin	Homo sapiens	137-146
6297939-5	1983	The molar ratio of phospholipid to cholesterol to rhodopsin is about 55:24:1.	Phospholipids	19-31	rhodopsin	Homo sapiens	50-59
6297939-5	1983	The molar ratio of phospholipid to cholesterol to rhodopsin is about 55:24:1.	Cholesterol	35-46	rhodopsin	Homo sapiens	50-59
598499-0	1977	The hydrophobic heart of rhodopsin revealed by an infrared 1H-2H exchange study.	Hydrogen	59-61	rhodopsin	Homo sapiens	25-34
228156-1	1978	The thermal stability of lipid-free rhodopsin in solutions of a homologous series of alkyltrimethylammonium bromide detergents and one nonionic detergent, dodecyl-beta-maltoside, has been studied as a function of detergent concentration.	tetradecyltrimethylammonium	85-115	rhodopsin	Homo sapiens	36-45
563922-0	1977	Formation, structure, and spectrophotometry of air-water interface films containing rhodopsin.	Water	51-56	rhodopsin	Homo sapiens	84-93
598499-0	1977	The hydrophobic heart of rhodopsin revealed by an infrared 1H-2H exchange study.	Deuterium	62-64	rhodopsin	Homo sapiens	25-34
302859-6	1977	As soon as 1 sec after illumination, a substantial decrease of the luminescent yield has been detected in a range of light bleaching from 0.007 to 20% of the rhodopsin, indicating an early reduction of the high-energy phosphate esters.4.	Phosphates	218-234	rhodopsin	Homo sapiens	158-167
21190-0	1977	Hydrogen exchange study of membrane-bound rhodopsin.	Hydrogen	0-8	rhodopsin	Homo sapiens	42-51
21190-3	1977	Hydrogen exchange studies of rhodopsin in disc membranes demonstrated that photolysis induces changes in the protein itself.	Hydrogen	0-8	rhodopsin	Homo sapiens	29-38
21190-8	1977	The unusually large fraction of exposed peptide hydrogens observed previously for rhodopsin is unaltered in the photolyzed forms.	Hydrogen	48-57	rhodopsin	Homo sapiens	82-91
890046-1	1977	Arguments are presented which support the possibility that the unfolding of the rhodopsin molecule during photolysis up to the stage of metarhodopsin II is followed by a spontaneous refolding  of the protein, once the isomerized retinaldehyde has left its original binding site.	Retinaldehyde	229-242	rhodopsin	Homo sapiens	80-89
271947-0	1977	Light-regulated permeability of rhodopsin:egg phosphatidylcholine recombinant membranes.	Phosphatidylcholines	46-65	rhodopsin	Homo sapiens	32-41
271947-1	1977	Purified rhodopsin was incorporated into phospholipid bilayers of egg phosphatidylcholine to give recombinant membrane vesicles, which were examined by proton and phosphorus nuclear magnetic resonance spectroscopy.	Phospholipids	41-53	rhodopsin	Homo sapiens	9-18
271947-1	1977	Purified rhodopsin was incorporated into phospholipid bilayers of egg phosphatidylcholine to give recombinant membrane vesicles, which were examined by proton and phosphorus nuclear magnetic resonance spectroscopy.	Phosphatidylcholines	70-89	rhodopsin	Homo sapiens	9-18
271947-2	1977	Increased rhodopsin content in the membranes appears to progressively inhibit the molecular motions of the methyl, methylene, and phosphate groups of the phospholipid molecules.	Phosphates	130-139	rhodopsin	Homo sapiens	10-19
271947-2	1977	Increased rhodopsin content in the membranes appears to progressively inhibit the molecular motions of the methyl, methylene, and phosphate groups of the phospholipid molecules.	Phospholipids	154-166	rhodopsin	Homo sapiens	10-19
271947-3	1977	This indicates that regions of the rhodopsin molecule interact in a manner that affects the phospholipids from the aqueous interface to the bilayer midline.	Phospholipids	92-105	rhodopsin	Homo sapiens	35-44
271947-6	1977	Light changed the membrane permeability, and the gradient in chemical potential resulted in a net ion movement across the rhodopsin:phospholipid recombinant membrane.	Phospholipids	132-144	rhodopsin	Homo sapiens	122-131
890049-2	1977	The properties of an air-water interface film of spectroscopically intact and chemically regenerable rhodopsin are presented, and results of studies of ion binding to these films are reported.	Water	25-30	rhodopsin	Homo sapiens	101-110
301481-0	1977	Rhodopsin regeneration in rod outer segments: utilization of 11-cis retinal and retinol.	Retinaldehyde	61-75	rhodopsin	Homo sapiens	0-9
71143-0	1977	Light increases the ion and non-electrolyte permeability of rhodopsin-phospholipid vesicles.	Phospholipids	70-82	rhodopsin	Homo sapiens	60-69
301481-0	1977	Rhodopsin regeneration in rod outer segments: utilization of 11-cis retinal and retinol.	Vitamin A	80-87	rhodopsin	Homo sapiens	0-9
557336-0	1977	Photochemical functionality of rhodopsin-phospholipid recombinant membranes.	Phospholipids	41-53	rhodopsin	Homo sapiens	31-40
557336-1	1977	Purified rhodopsin was incorporated into phospholipid bilayers to give recombinant membranes.	Phospholipids	41-53	rhodopsin	Homo sapiens	9-18
557336-3	1977	Changes in the absorption spectra of glycerol-water mixtures of rhodopsin-egg phosphatidylcholine and rhodopsin-asolectin recombinants were monitored after the sample was cooled to -196 degrees C, presented with light of wavelength greater than 440 nm, and then warmed gradually to room temperature.	Glycerol	37-45	rhodopsin	Homo sapiens	64-73
557336-3	1977	Changes in the absorption spectra of glycerol-water mixtures of rhodopsin-egg phosphatidylcholine and rhodopsin-asolectin recombinants were monitored after the sample was cooled to -196 degrees C, presented with light of wavelength greater than 440 nm, and then warmed gradually to room temperature.	Water	46-51	rhodopsin	Homo sapiens	64-73
557336-3	1977	Changes in the absorption spectra of glycerol-water mixtures of rhodopsin-egg phosphatidylcholine and rhodopsin-asolectin recombinants were monitored after the sample was cooled to -196 degrees C, presented with light of wavelength greater than 440 nm, and then warmed gradually to room temperature.	Phosphatidylcholines	78-97	rhodopsin	Homo sapiens	64-73
557336-8	1977	The photochemical functionality of rhodopsin-phospholipid recombinants is dependent upon the presence of phospholipid unsaturation and the fluidity of the phospholipid hydrocarbon chains, and is independent of the polar head group of the phospholipid.	Phospholipids	45-57	rhodopsin	Homo sapiens	35-44
557336-8	1977	The photochemical functionality of rhodopsin-phospholipid recombinants is dependent upon the presence of phospholipid unsaturation and the fluidity of the phospholipid hydrocarbon chains, and is independent of the polar head group of the phospholipid.	Phospholipids	105-117	rhodopsin	Homo sapiens	35-44
557336-8	1977	The photochemical functionality of rhodopsin-phospholipid recombinants is dependent upon the presence of phospholipid unsaturation and the fluidity of the phospholipid hydrocarbon chains, and is independent of the polar head group of the phospholipid.	phospholipid hydrocarbon	155-179	rhodopsin	Homo sapiens	35-44
557336-8	1977	The photochemical functionality of rhodopsin-phospholipid recombinants is dependent upon the presence of phospholipid unsaturation and the fluidity of the phospholipid hydrocarbon chains, and is independent of the polar head group of the phospholipid.	Phospholipids	105-117	rhodopsin	Homo sapiens	35-44
867862-0	1977	The effect of MS-222 on rhodopsin regeneration in the frog.	tricaine	14-20	rhodopsin	Homo sapiens	24-33
321787-2	1977	In reconstituted liposomes containing rhodopsin as the only protein, the presence of cholesterol lowers by 10-fold or more the amount of negericin required to eliminate the light-driven proton gradient.	Cholesterol	85-96	rhodopsin	Homo sapiens	38-47
321787-2	1977	In reconstituted liposomes containing rhodopsin as the only protein, the presence of cholesterol lowers by 10-fold or more the amount of negericin required to eliminate the light-driven proton gradient.	negericin	137-146	rhodopsin	Homo sapiens	38-47
11812-1	1976	The kinetics of recombination of 11-cis-retinal with bleached rod outer segments and sodium cholate solubilized rhodopsin have been investigated.	Sodium Cholate	85-99	rhodopsin	Homo sapiens	112-121
188474-1	1977	Sulfhydryl groups of membrane-bound rhodopsin are studied with the spin label technique by using five maleimide derivative probes of different lengths.	maleimide	102-111	rhodopsin	Homo sapiens	36-45
592816-0	1977	Accessibility of the carbohydrate moiety of membrane-boound rhodopsin to enzymatic and chemical modification.	Carbohydrates	21-33	rhodopsin	Homo sapiens	60-69
592816-1	1977	Galactose was specifically inserted into the carbohydrate moiety of rhodopsin by incubating retinal disk membranes with UDP-galactose: N-acetylglucosamine galactosyltransferase.	Galactose	0-9	rhodopsin	Homo sapiens	68-77
592816-1	1977	Galactose was specifically inserted into the carbohydrate moiety of rhodopsin by incubating retinal disk membranes with UDP-galactose: N-acetylglucosamine galactosyltransferase.	Carbohydrates	45-57	rhodopsin	Homo sapiens	68-77
592816-1	1977	Galactose was specifically inserted into the carbohydrate moiety of rhodopsin by incubating retinal disk membranes with UDP-galactose: N-acetylglucosamine galactosyltransferase.	Uridine Diphosphate Galactose	120-133	rhodopsin	Homo sapiens	68-77
592816-2	1977	The stoichiometry of labeling ranged from 1.2 to 1.8 (average = 1.5) residues of galactose per molecule of rhodopsin, indicating that some or all of the oligosaccharide chains of membrane-bound rhodopsin are readily accessible to enzymatic modification.	Oligosaccharides	153-168	rhodopsin	Homo sapiens	194-203
878346-0	1977	Isolation of three isochromic forms of rhodopsin in digitonin.	Digitonin	52-61	rhodopsin	Homo sapiens	39-48
133581-5	1976	In Triton X-100 extracts from membrane fractions, significant enrichment in rhodopsin content was observed.	Octoxynol	3-15	rhodopsin	Homo sapiens	76-85
1086346-7	1976	The KRG decrease has the rhodopsin action spectrum, is maximal in the photoreceptor layer, persists after aspartate treatment, and has an increment threshold curve which saturates at moderate background intensities.	Aspartic Acid	106-115	rhodopsin	Homo sapiens	25-34
962470-4	1976	Since it has been shown by others that lightdriven ATP synthesis can occur under anaerobic conditions, it is postulated that rhodopsin-mediated photophosphorylation is of survival value for this organism in the brines in which it lives, especially because the solubility of oxygen is low in highly saline waters and anaerobic conditions can often develop.	Adenosine Triphosphate	51-54	rhodopsin	Homo sapiens	125-134
962470-4	1976	Since it has been shown by others that lightdriven ATP synthesis can occur under anaerobic conditions, it is postulated that rhodopsin-mediated photophosphorylation is of survival value for this organism in the brines in which it lives, especially because the solubility of oxygen is low in highly saline waters and anaerobic conditions can often develop.	Oxygen	274-280	rhodopsin	Homo sapiens	125-134
962470-4	1976	Since it has been shown by others that lightdriven ATP synthesis can occur under anaerobic conditions, it is postulated that rhodopsin-mediated photophosphorylation is of survival value for this organism in the brines in which it lives, especially because the solubility of oxygen is low in highly saline waters and anaerobic conditions can often develop.	Sodium Chloride	298-304	rhodopsin	Homo sapiens	125-134
8077-9	1976	We suggest that this group is the Schiff base lysine of the chromophore binding site of rhodopsin which becomes exposed on photolysis.	Schiff Bases	34-45	rhodopsin	Homo sapiens	88-97
8077-9	1976	We suggest that this group is the Schiff base lysine of the chromophore binding site of rhodopsin which becomes exposed on photolysis.	Lysine	46-52	rhodopsin	Homo sapiens	88-97
8077-11	1976	This leads to a model involving intramolecular protonation of the Schiff base nitrogen in the retinal-opsin linkage of rhodopsin, which is consistent with the thermodynamic and spectroscopic properties of the system.	Schiff Bases	66-77	rhodopsin	Homo sapiens	119-128
8077-11	1976	This leads to a model involving intramolecular protonation of the Schiff base nitrogen in the retinal-opsin linkage of rhodopsin, which is consistent with the thermodynamic and spectroscopic properties of the system.	Nitrogen	78-86	rhodopsin	Homo sapiens	119-128
955101-0	1976	Hydrogen-tritium exchange of rhodopsin: effect of solvent on the incorporation of slowly exchanging tritium atoms.	Hydrogen	0-8	rhodopsin	Homo sapiens	29-38
955101-0	1976	Hydrogen-tritium exchange of rhodopsin: effect of solvent on the incorporation of slowly exchanging tritium atoms.	Tritium	9-16	rhodopsin	Homo sapiens	29-38
955101-0	1976	Hydrogen-tritium exchange of rhodopsin: effect of solvent on the incorporation of slowly exchanging tritium atoms.	Tritium	100-107	rhodopsin	Homo sapiens	29-38
971805-3	1976	All exconjugants retained the arginine auxotrophy of the recipient strain, and were resistant to ampicillin and kanamycin, drugs to which RP4 confers resistance.	Ampicillin	97-107	rhodopsin	Homo sapiens	138-141
971805-3	1976	All exconjugants retained the arginine auxotrophy of the recipient strain, and were resistant to ampicillin and kanamycin, drugs to which RP4 confers resistance.	Kanamycin	112-121	rhodopsin	Homo sapiens	138-141
976363-0	1976	Rhodopsin as a glycoprotein: a possible role for the oligosaccharide in phagocytosis.	Oligosaccharides	53-68	rhodopsin	Homo sapiens	0-9
1196384-0	1975	Existence of a beta-ionone ring-binding site in the rhodopsin molecule.	beta-ionone	15-26	rhodopsin	Homo sapiens	52-61
1082548-0	1976	11-Cis vitamin A in dark-adapted rod outer segments is a probable source of prosthetic groups for rhodopsin biosynthesis.	11-cis vitamin a	0-16	rhodopsin	Homo sapiens	98-107
960587-0	1976	Oxidation states of four sulfurs of rhodopsin before and after bleaching.	Sulfur	25-32	rhodopsin	Homo sapiens	36-45
1247456-0	1976	Reactivity of tryptophans in rhodopsin.	Tryptophan	14-25	rhodopsin	Homo sapiens	29-38
1079805-10	1975	The isolated rod outer segment which contains regenerated rhodopsin thus differs from one that is dark adapted in that phosphate can remain bound and the phosphorylation reaction remains activated.	Phosphates	119-128	rhodopsin	Homo sapiens	58-67
1215428-0	1975	Effect of the physical state of phospholipid on rhodopsin regeneration from retinylidene phospholipid.	Phospholipids	32-44	rhodopsin	Homo sapiens	48-57
1215428-0	1975	Effect of the physical state of phospholipid on rhodopsin regeneration from retinylidene phospholipid.	retinylidene phospholipid	76-101	rhodopsin	Homo sapiens	48-57
453-11	1975	(3) In the outer segments of vertebrate receptors, absorption of light by rhodopsin causes the plasma membrane to hyperpolarize due to a decrease in sodium conductance, possibly mediated by calcium ions.	Sodium	149-155	rhodopsin	Homo sapiens	74-83
453-11	1975	(3) In the outer segments of vertebrate receptors, absorption of light by rhodopsin causes the plasma membrane to hyperpolarize due to a decrease in sodium conductance, possibly mediated by calcium ions.	Calcium	190-197	rhodopsin	Homo sapiens	74-83
1081883-2	1975	As a result of this extraction of rhodopsin with anion detergent (sodium cholate) in the concentrations not exceeding the critical concentration of micelloformation increases, and spontaneous release of rhodopsin into water phase is observed.	Sodium Cholate	66-80	rhodopsin	Homo sapiens	34-43
1081883-2	1975	As a result of this extraction of rhodopsin with anion detergent (sodium cholate) in the concentrations not exceeding the critical concentration of micelloformation increases, and spontaneous release of rhodopsin into water phase is observed.	Water	218-223	rhodopsin	Homo sapiens	34-43
1081883-2	1975	As a result of this extraction of rhodopsin with anion detergent (sodium cholate) in the concentrations not exceeding the critical concentration of micelloformation increases, and spontaneous release of rhodopsin into water phase is observed.	Water	218-223	rhodopsin	Homo sapiens	203-212
1081883-3	1975	At the same time the number of phospholipid molecules extracted in lipoprotein rhodopsin complex from the membranes of outer segments decreases 3-4-fold.	Phospholipids	31-43	rhodopsin	Homo sapiens	79-88
1081884-4	1975	The structural organization of photoreceptor membranes is the factor which controls the reaction rate of peroxide oxidation; and reconstructions in membrane organization (at rhodopsin photolysis) result in the changes of autooxidation rate of phospholipids in the membrane.	Peroxides	105-113	rhodopsin	Homo sapiens	174-183
1081884-4	1975	The structural organization of photoreceptor membranes is the factor which controls the reaction rate of peroxide oxidation; and reconstructions in membrane organization (at rhodopsin photolysis) result in the changes of autooxidation rate of phospholipids in the membrane.	Phospholipids	243-256	rhodopsin	Homo sapiens	174-183
1151790-2	1975	Human rhodopsin in vivo was flash bleached by a 600 musec xenon flash which could deliver to the retina up to 15 rod-equivalent quanta per rhodopsin molecule, and the fraction bleached measured by fundus reflexion densitometry.	Xenon	58-63	rhodopsin	Homo sapiens	6-15
238616-7	1975	The intermediate in the photoregeneration process of cephalopod rhodopsin, P380, has a positive CD band at the main peak, 380 nm, and also a large positive CD band in the ultraviolet region like lumirhodopsin.	Cadmium	96-98	rhodopsin	Homo sapiens	64-73
238616-7	1975	The intermediate in the photoregeneration process of cephalopod rhodopsin, P380, has a positive CD band at the main peak, 380 nm, and also a large positive CD band in the ultraviolet region like lumirhodopsin.	Cadmium	156-158	rhodopsin	Homo sapiens	64-73
1151790-2	1975	Human rhodopsin in vivo was flash bleached by a 600 musec xenon flash which could deliver to the retina up to 15 rod-equivalent quanta per rhodopsin molecule, and the fraction bleached measured by fundus reflexion densitometry.	Xenon	58-63	rhodopsin	Homo sapiens	139-148
166698-0	1975	[Interaction of rhodopsin with quinone].	quinone	31-38	rhodopsin	Homo sapiens	16-25
48337-3	1975	Laser Raman spectroscopy has been used to probe specific molecular interactions inside two models of transport membrane proteins, valinomycin and gramicidin A. Conformational changes of these molecules, as well as specific interactions with ions, can be detected and may help elucidate how membrane transport proteins such as Na+ minus K+ ATPase and rhodopsin function.	Valinomycin	130-141	rhodopsin	Homo sapiens	350-359
1080056-3	1975	Reversible phototransformations of rhodopsin of the frog in vitro (in digitonine extracts) at -22 degrees C under the effect of light with gamma 579 and 435 nm are reversible processes.	Digitonin	70-80	rhodopsin	Homo sapiens	35-44
4433516-0	1974	The characterization of sodium cholate solubilized rhodopsin.	Sodium Cholate	24-38	rhodopsin	Homo sapiens	51-60
4472013-2	1974	Binding site and migration of retinaldehyde during rhodopsin photolysis.	Retinaldehyde	30-43	rhodopsin	Homo sapiens	51-60
4473959-0	1974	Hydrogen ion changes of rhodopsin.	Hydrogen	0-8	rhodopsin	Homo sapiens	24-33
4134491-0	1974	Optical polarisation indicates linear arrangement of rhodopsin oligosaccharide chain in rod disk membranes of frog retina.	Oligosaccharides	63-78	rhodopsin	Homo sapiens	53-62
4546017-0	1974	Proceedings: Autoradiographic and radiobiochemical studies on the incorporation of (6-3H)glucosamine into frog rhodopsin.	(6-3h)glucosamine	83-100	rhodopsin	Homo sapiens	111-120
4544648-0	1974	Incorporation of (3H)vitamin A into rhodopsin in light- and dark-adapted frogs.	(3h)vitamin a	17-30	rhodopsin	Homo sapiens	36-45
4823461-0	1974	Letter: Ellipsoid models for rotational diffusion of rhodopsin in a digitonin micelle and in the visual receptor membrane.	Digitonin	68-77	rhodopsin	Homo sapiens	53-62
4609125-0	1974	Transposition of ampicillin resistance from RP4 to other replicons.	Ampicillin	17-27	rhodopsin	Homo sapiens	44-47
19397002-8	1974	In the change from P380 to rhodopsin, a small change in the conformation of the protein part and the protonation of the Schiff base, the primary retinal-opsin link, occur.	Schiff Bases	120-131	rhodopsin	Homo sapiens	27-36
4584801-1	1973	Transformation of R-factor RP4 specifying resistance to ampicillin, kanamycin, and tetracycline from Escherichia coli to Rhizobium trifolii is reported.	Ampicillin	56-66	rhodopsin	Homo sapiens	27-30
4584801-1	1973	Transformation of R-factor RP4 specifying resistance to ampicillin, kanamycin, and tetracycline from Escherichia coli to Rhizobium trifolii is reported.	Kanamycin	68-77	rhodopsin	Homo sapiens	27-30
4361169-0	1973	The carbohydrate moiety of rhodopsin: lectin-binding, chemical modification and fluorescence studies.	Carbohydrates	4-16	rhodopsin	Homo sapiens	27-36
4584801-1	1973	Transformation of R-factor RP4 specifying resistance to ampicillin, kanamycin, and tetracycline from Escherichia coli to Rhizobium trifolii is reported.	Tetracycline	83-95	rhodopsin	Homo sapiens	27-30
4584801-2	1973	Partially purified RP4 deoxyribonucleic acid (DNA) of the donor strain E. coli J5-3 that carried the R-factor was prepared by the lysozyme-ethylenediaminetetraacetic acid-Triton X-100 procedure and was used in transformation experiments with R. trifolii as recipient.	acid-triton x-100	166-183	rhodopsin	Homo sapiens	19-22
4584801-4	1973	Dye buoyant density and sucrose gradient centrifugation of R. trifolii DNA showed that the expression of the specified drug resistance of RP4 by R. trifolii was accompanied by the acquisition of an extrachromosomal, satellite DNA component which has indistinguishable physical properties from the R-factor in the donor strain.	Sucrose	24-31	rhodopsin	Homo sapiens	138-141
4736806-0	1973	Extraction, regeneration after bleaching, and ion-exchange chromatography of rhodopsin in Tween 80.	Polysorbates	90-98	rhodopsin	Homo sapiens	77-86
4706718-0	1973	Iodate poisoning: early effect on regeneration of rhodopsin and the ERG.	Iodates	0-6	rhodopsin	Homo sapiens	50-59
4699981-0	1973	Accessibility of the carbohydrate moiety of rhodopsin.	Carbohydrates	21-33	rhodopsin	Homo sapiens	44-53
4692264-0	1973	Evidence for the involvement of a reduced flavin isomerization catalyst in the regeneration of bleached rhodopsin.	4,6-dinitro-o-cresol	42-48	rhodopsin	Homo sapiens	104-113
4642314-0	1972	[Artificial phospholipid membrane with rhodopsin as a model of a photoreceptor].	Phospholipids	12-24	rhodopsin	Homo sapiens	39-48
5079248-0	1972	Flash bleaching of rhodopsin in cetyltrimethylammonium bromide.	Cetrimonium	32-62	rhodopsin	Homo sapiens	19-28
4636730-0	1972	A rhodopsin-lipid-water lamellar system: its characterisation by x-ray diffraction and electron microscopy.	Water	18-23	rhodopsin	Homo sapiens	2-11
4341702-0	1972	Preparation and properties of phospholipid bilayers containing rhodopsin.	Phospholipids	30-42	rhodopsin	Homo sapiens	63-72
4341702-1	1972	Purified rhodopsin has been prepared containing less than 1.1 mol of phosphate per mol of protein.	Phosphates	69-78	rhodopsin	Homo sapiens	9-18
4341702-2	1972	The purified rhodopsin has been incorporated into phosphatidylcholine bilayers, and the molecular interactions within the bilayers were investigated by the use of spin-labeled phosphatidylcholines.	Phosphatidylcholines	50-69	rhodopsin	Homo sapiens	13-22
4341702-2	1972	The purified rhodopsin has been incorporated into phosphatidylcholine bilayers, and the molecular interactions within the bilayers were investigated by the use of spin-labeled phosphatidylcholines.	Phosphatidylcholines	176-196	rhodopsin	Homo sapiens	13-22
4341702-3	1972	Rhodopsin appears to inhibit segmental motions of the hydrocarbon chains, an effect similar to that of cholesterol on phospholipid bilayers.	Hydrocarbons	54-65	rhodopsin	Homo sapiens	0-9
5044516-0	1972	Removal of amino group containing phospholipids from rhodopsin.	Phospholipids	34-47	rhodopsin	Homo sapiens	53-62
5029868-0	1972	Aqueous cyanohydridoborate reduction of the rhodopsin chromophore.	cyanohydridoborate	8-26	rhodopsin	Homo sapiens	44-53
5034101-0	1972	The fluorescence from the tryptophans of rhodopsin.	Tryptophan	26-37	rhodopsin	Homo sapiens	41-50
5031930-0	1972	Absorption spectra of TCA-denatured rhodopsin and of a Schiff base compound of retinal.	Trichloroacetic Acid	22-25	rhodopsin	Homo sapiens	36-45
4110154-11	1972	A wet paste of rhodopsin-digitonin micelles, sheared between glass slides, becomes highly oriented, the rhodopsin chromophores lining up in the direction of shear, the retinal oxime produced by bleaching orienting more perpendicularly to the shear.	Digitonin	25-34	rhodopsin	Homo sapiens	15-24
4110154-11	1972	A wet paste of rhodopsin-digitonin micelles, sheared between glass slides, becomes highly oriented, the rhodopsin chromophores lining up in the direction of shear, the retinal oxime produced by bleaching orienting more perpendicularly to the shear.	Digitonin	25-34	rhodopsin	Homo sapiens	104-113
4110154-11	1972	A wet paste of rhodopsin-digitonin micelles, sheared between glass slides, becomes highly oriented, the rhodopsin chromophores lining up in the direction of shear, the retinal oxime produced by bleaching orienting more perpendicularly to the shear.	Oximes	176-181	rhodopsin	Homo sapiens	15-24
4110154-11	1972	A wet paste of rhodopsin-digitonin micelles, sheared between glass slides, becomes highly oriented, the rhodopsin chromophores lining up in the direction of shear, the retinal oxime produced by bleaching orienting more perpendicularly to the shear.	Oximes	176-181	rhodopsin	Homo sapiens	104-113
11946367-0	1972	Light dependent phosphorylation of rhodopsin by ATP.	Adenosine Triphosphate	48-51	rhodopsin	Homo sapiens	35-44
5132498-0	1971	Rotational diffusion of rhodopsin-digitonin micelles studied by transient photodichroism.	Digitonin	34-43	rhodopsin	Homo sapiens	24-33
5132498-3	1971	When the rhodopsin-digitonin micelles are assumed to be rotationally symmetric it was found from the observed relaxation time that the axial ratio is probably less than 2.	Digitonin	19-28	rhodopsin	Homo sapiens	9-18
5132474-0	1971	The reduction of rhodopsin with sodium borohydride under non-bleaching conditions.	sodium borohydride	32-50	rhodopsin	Homo sapiens	17-26
4399287-2	1971	Measurements on rhodopsin digitonin solutions and fragments of rod outer segments.	Digitonin	26-35	rhodopsin	Homo sapiens	16-25
5123142-2	1971	The binding site of retinaldehyde in rhodopsin studied with model aldimines.	Retinaldehyde	20-33	rhodopsin	Homo sapiens	37-46
5123142-2	1971	The binding site of retinaldehyde in rhodopsin studied with model aldimines.	aldimines	66-75	rhodopsin	Homo sapiens	37-46
5279513-5	1971	This difference of efficiencies seems to imply a large movement of the chromophore away from the tryptophans of the opsin after rhodopsin is bleached.	Tryptophan	97-108	rhodopsin	Homo sapiens	128-137
5543686-0	1971	Properties of rhodopsin dependent on associated phospholipid.	Phospholipids	48-60	rhodopsin	Homo sapiens	14-23
5495148-13	1970	The photobleaching of rhodopsin sensitized by flavin is also demonstrated.	4,6-dinitro-o-cresol	46-52	rhodopsin	Homo sapiens	22-31
5533197-1	1970	Digitonin solutions of labelled rhodopsin, containing (3)H in the retinyl moiety, were prepared by two related methods.	Digitonin	0-9	rhodopsin	Homo sapiens	32-41
5533197-2	1970	Labelled rhodopsin was also prepared for the first time in cetyltrimethylammonium bromide and purified by column chromatography.	Cetrimonium	59-89	rhodopsin	Homo sapiens	9-18
5533197-3	1970	It was shown that only certain rhodopsin preparations on denaturation in the dark and the reduction with sodium borohydride gave up to 60% of the radioactivity in a fraction characterized as N-retinylphosphatidylethanolamine.	n-retinylphosphatidylethanolamine	191-224	rhodopsin	Homo sapiens	31-40
5533197-7	1970	The only firmly established aspect of the rhodopsin active site remains the demonstration in our previous work that at the metarhodopsin-II stage the retinyl moiety is linked to an in-amino group of lysine.	Lysine	199-205	rhodopsin	Homo sapiens	42-51
5449000-0	1970	Is retinal-phosphatidyl ethanolamine the chromophore of rhodopsin?	retinal-phosphatidyl ethanolamine	3-36	rhodopsin	Homo sapiens	56-65
5466209-0	1970	[Effects of lipoperoxides on rhodopsin and its regeneration].	Lipid Peroxides	12-25	rhodopsin	Homo sapiens	29-38
5461289-0	1970	[Effects of degenerative agents to the retina, SH inhibitor and lipoperoxide upon the rhodopsin model].	Lipid Peroxides	64-76	rhodopsin	Homo sapiens	86-95
5435016-0	1970	Thermal stability of rhodopsin extracted with Triton X-100 surfactant.	Octoxynol	46-58	rhodopsin	Homo sapiens	21-30
5307435-0	1969	Hydrogen ion uptake by oxygen atoms released from rhodopsin molecules on illumination.	Hydrogen	0-8	rhodopsin	Homo sapiens	50-59
5307435-0	1969	Hydrogen ion uptake by oxygen atoms released from rhodopsin molecules on illumination.	Oxygen	23-29	rhodopsin	Homo sapiens	50-59
5786900-0	1969	On the behavior of the phospholipids in rhodopsin during photolysis.	Phospholipids	23-36	rhodopsin	Homo sapiens	40-49
5704817-4	1968	Irradiation of labelled rhodopsin in the presence of sodium borohydride resulted in the irreversible binding of the retinyl moiety to the active site.	sodium borohydride	53-71	rhodopsin	Homo sapiens	24-33
5704817-5	1968	Degradative studies established that the retinyl moiety in this reduced derivative of rhodopsin was attached to the in-amino group of lysine.	Lysine	134-140	rhodopsin	Homo sapiens	86-95
5704817-9	1968	It is suggested that the involvement of a charge-transfer interaction between the retinylidene chromophore and a suitable group -X or -X.H on the opsin best explains the spectroscopic properties of rhodopsin and other visual proteins.	retinylidene	82-94	rhodopsin	Homo sapiens	198-207
5713206-0	1968	N-retinylidene-1-amino-2-propanol: a Schiff base analog for rhodopsin.	n-retinylidene-1-amino-2-propanol	0-33	rhodopsin	Homo sapiens	60-69
5713206-0	1968	N-retinylidene-1-amino-2-propanol: a Schiff base analog for rhodopsin.	Schiff Bases	37-48	rhodopsin	Homo sapiens	60-69
5747789-0	1968	[Spectral studies of ATP-ase activity of digitonin extract of rhodopsin].	Digitonin	41-50	rhodopsin	Homo sapiens	62-71
5663804-2	1968	By the isolation and purification of visual pigment from retinas of adult frogs after injection of tritiated leucine and phenylalanine, it has been shown that at least part of this labeled protein consists of visual pigment (rhodopsin).	tritiated leucine	99-116	rhodopsin	Homo sapiens	225-234
5663804-2	1968	By the isolation and purification of visual pigment from retinas of adult frogs after injection of tritiated leucine and phenylalanine, it has been shown that at least part of this labeled protein consists of visual pigment (rhodopsin).	Phenylalanine	121-134	rhodopsin	Homo sapiens	225-234
5623652-0	1967	[Lactate dehydrogenase activity of external segments of the retina and digitonin extracts of rhodopsin].	Digitonin	71-80	rhodopsin	Homo sapiens	93-102
5945249-2	1966	Flash illumination of a suspension of frog rod outer segments or rhodopsin solution in contact with a platinum electrode produces a rapidly developing negative displacement of potential of the electrode (with respect to a reversible electrode).2.	Platinum	102-110	rhodopsin	Homo sapiens	65-74
5945249-4	1966	It is inferred that the response is due to an uptake of H(+) by the rod outer segments or rhodopsin, with the platinum surface acting as a pH electrode.3.	Platinum	110-118	rhodopsin	Homo sapiens	90-99
4224761-0	1965	[Enzymatic (ATPase) activity of digitonin extracts of rhodopsin (visual purple), and its variation under the influence of visual light].	Digitonin	32-41	rhodopsin	Homo sapiens	54-63
14270706-0	1965	REACTION OF THE RHODOPSIN CHROMOPHORE WITH SODIUM BOROHYDRIDE.	sodium borohydride	43-61	rhodopsin	Homo sapiens	16-25
14080814-1	1963	Light isomerizes the chromophore of rhodopsin, 11-cis retinal (formerly retinene), to the all-trans configuration.	Retinaldehyde	72-80	rhodopsin	Homo sapiens	36-45
14465191-3	1962	This is identified with the 502 mmu frog rhodopsin of digitonin extracts.	Digitonin	54-63	rhodopsin	Homo sapiens	41-50
14450351-0	1962	Monolayer film of rhodopsin at the air/water interface.	Water	39-44	rhodopsin	Homo sapiens	18-27
13738465-0	1961	The cis-trans isomerization of conjugated polyenes and the occurrence of a hindered cis-isomer of retinene in the rhodopsin system.	Retinaldehyde	98-106	rhodopsin	Homo sapiens	114-123
13628655-0	1959	Purification of rhodopsin using columns containing calcium triphosphate.	calcium triphosphate	51-71	rhodopsin	Homo sapiens	16-25
13622675-0	1959	Does rhodopsin contain a trace metal.	Metals	31-36	rhodopsin	Homo sapiens	5-14
13534735-0	1958	Rhodopsin bleaching in the presence of hydroxylamine.	Hydroxylamine	39-52	rhodopsin	Homo sapiens	0-9
13525671-6	1958	The conductance change is regarded as an essential property of rhodopsin, because it occurs in aqueous suspension as well as in digitonin solution; it may be caused by hydrogen or hydroxyl ions and some other conductive substances.	Digitonin	128-137	rhodopsin	Homo sapiens	63-72
13525671-6	1958	The conductance change is regarded as an essential property of rhodopsin, because it occurs in aqueous suspension as well as in digitonin solution; it may be caused by hydrogen or hydroxyl ions and some other conductive substances.	Hydrogen	168-176	rhodopsin	Homo sapiens	63-72
13525671-6	1958	The conductance change is regarded as an essential property of rhodopsin, because it occurs in aqueous suspension as well as in digitonin solution; it may be caused by hydrogen or hydroxyl ions and some other conductive substances.	Hydroxyl Radical	180-188	rhodopsin	Homo sapiens	63-72
13495499-8	1958	This is much faster than the synthesis of rhodopsin in the living human eye, and faster than human rod dark-adaptation; the rate of both processes in vivo must be limited by reactions which precede the union of neo-b retinene with opsin, the final step in rhodopsin synthesis.	neo-b retinene	211-225	rhodopsin	Homo sapiens	42-51
13495499-8	1958	This is much faster than the synthesis of rhodopsin in the living human eye, and faster than human rod dark-adaptation; the rate of both processes in vivo must be limited by reactions which precede the union of neo-b retinene with opsin, the final step in rhodopsin synthesis.	neo-b retinene	211-225	rhodopsin	Homo sapiens	256-265
13491819-1	1958	Squid rhodopsin (lambda(max) 493 mmicro)-like vertebrate rhodopsins-contains a retinene chromophore linked to a protein, opsin.	Retinaldehyde	79-87	rhodopsin	Homo sapiens	6-15
13491819-6	1958	Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene.	neo-b (11-cis) retinene	140-163	rhodopsin	Homo sapiens	15-24
13491819-6	1958	Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene.	neo-b (11-cis) retinene	140-163	rhodopsin	Homo sapiens	32-41
13491819-6	1958	Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene.	metarhodopsin all-trans retinene	165-197	rhodopsin	Homo sapiens	15-24
13491819-6	1958	Irradiation of rhodopsin or metarhodopsin produces a steady state by promoting the reactions, See PDF for Equation Squid rhodopsin contains neo-b (11-cis) retinene; metarhodopsin all-trans retinene.	metarhodopsin all-trans retinene	165-197	rhodopsin	Homo sapiens	32-41
13491819-10	1958	In both forms, retinene is attached to opsin at the same site as in rhodopsin.	Retinaldehyde	15-23	rhodopsin	Homo sapiens	68-77
13491819-11	1958	However, metarhodopsin decomposes more readily than rhodopsin into retinene and opsin.	Retinaldehyde	67-75	rhodopsin	Homo sapiens	13-22
13475700-1	1957	Hubbard has found that the photoisomerization of retinene was important for the regeneration of rhodopsin in vitro, and the object of the present investigation was to find whether this was also true for regeneration in the living human eye.	Retinaldehyde	49-57	rhodopsin	Homo sapiens	96-105
13475700-4	1957	Therefore if retinene isomerization is important for rhodopsin regeneration, blue light should cause a more rapid regeneration after bleaching, and during bleaching the equilibrium level attained should be less profound.	Retinaldehyde	13-21	rhodopsin	Homo sapiens	53-62
13385449-7	1956	The occurrence of this retinene(1) pigment, intermediate in spectral position between rhodopsin and iodopsin, is interpreted in support of the transmutation theory of Walls.	Retinaldehyde	23-31	rhodopsin	Homo sapiens	86-95
13118107-7	1954	The metabolism of the outer limb is probably adequate to provide the DPN required for the maintenance of the rhodopsin concentration necessary for vision.	NAD	69-72	rhodopsin	Homo sapiens	109-118
13034375-0	1952	Studies on the rhodopsin of liber extirpated animals and effects of choline on rhodopsin regeneration.	Choline	68-75	rhodopsin	Homo sapiens	79-88
16588965-0	1950	The Synthesis of Rhodopsin from Retinene(1).	Retinaldehyde	32-40	rhodopsin	Homo sapiens	17-26
16588966-0	1950	The Synthesis of Rhodopsin from Vitamin A(1).	Vitamin A	32-41	rhodopsin	Homo sapiens	17-26
18108501-1	1949	In the surviving vertebrate retina the retinene(1) liberated by bleaching rhodopsin is converted quantitatively to vitamin A(1).	Retinaldehyde	39-47	rhodopsin	Homo sapiens	74-83
18108501-1	1949	In the surviving vertebrate retina the retinene(1) liberated by bleaching rhodopsin is converted quantitatively to vitamin A(1).	Vitamin A	115-124	rhodopsin	Homo sapiens	74-83
18108501-17	1949	This action of DPN brings a member of the vitamin B complex, nicotinic acid amide, into an auxiliary position in the rhodopsin system.	NAD	15-18	rhodopsin	Homo sapiens	117-126
18108501-17	1949	This action of DPN brings a member of the vitamin B complex, nicotinic acid amide, into an auxiliary position in the rhodopsin system.	Niacinamide	42-51	rhodopsin	Homo sapiens	117-126
18108501-17	1949	This action of DPN brings a member of the vitamin B complex, nicotinic acid amide, into an auxiliary position in the rhodopsin system.	Niacinamide	61-81	rhodopsin	Homo sapiens	117-126
18108501-19	1949	Yet this reduction must be balanced by an oxidative process elsewhere in the rhodopsin cycle, since through rhodopsin as intermediate vitamin A(1) regenerates retinene(1).	Vitamin A	134-143	rhodopsin	Homo sapiens	77-86
18108501-19	1949	Yet this reduction must be balanced by an oxidative process elsewhere in the rhodopsin cycle, since through rhodopsin as intermediate vitamin A(1) regenerates retinene(1).	Vitamin A	134-143	rhodopsin	Homo sapiens	108-117
18108501-19	1949	Yet this reduction must be balanced by an oxidative process elsewhere in the rhodopsin cycle, since through rhodopsin as intermediate vitamin A(1) regenerates retinene(1).	Retinaldehyde	159-167	rhodopsin	Homo sapiens	77-86
18108501-19	1949	Yet this reduction must be balanced by an oxidative process elsewhere in the rhodopsin cycle, since through rhodopsin as intermediate vitamin A(1) regenerates retinene(1).	Retinaldehyde	159-167	rhodopsin	Homo sapiens	108-117
19873462-7	1946	Rhodopsin was an inevitable contaminant in most methods of extraction, but could be reduced to about 10 per cent of the absorption due to iodopsin by extraction of unhardened retinas with 4 per cent Merck"s saponin in (3/4) saturated magnesium sulfate for about 1 hour.	Saponins	207-214	rhodopsin	Homo sapiens	0-9
19873462-7	1946	Rhodopsin was an inevitable contaminant in most methods of extraction, but could be reduced to about 10 per cent of the absorption due to iodopsin by extraction of unhardened retinas with 4 per cent Merck"s saponin in (3/4) saturated magnesium sulfate for about 1 hour.	Magnesium Sulfate	234-251	rhodopsin	Homo sapiens	0-9
19873463-2	1946	The lipids released by the action of light on rhodopsin and iodopsin are found to be similar and to possess a labile absorption spectrum in chloroform, with a rising peak at about 390 mmicro and a declining peak in the region of 470 mmicro.	Chloroform	140-150	rhodopsin	Homo sapiens	46-55
33870657-2	2021	Here, we report the environmental concentrations of rhodopsin along the Subtropical Frontal Zone off New Zealand, where Subtropical waters encounter the iron-limited Subantarctic High Nutrient Low Chlorophyll (HNLC) region.	Iron	23-27	rhodopsin	Homo sapiens	52-61
33870657-2	2021	Here, we report the environmental concentrations of rhodopsin along the Subtropical Frontal Zone off New Zealand, where Subtropical waters encounter the iron-limited Subantarctic High Nutrient Low Chlorophyll (HNLC) region.	Chlorophyll	197-208	rhodopsin	Homo sapiens	52-61
33870657-3	2021	Rhodopsin concentrations were highest in HNLC waters where chlorophyll-a concentrations were lowest.	chlorophyll a	59-72	rhodopsin	Homo sapiens	0-9
34031444-6	2021	Here, we use small-angle scattering (SAS) to show that detergent-solubilized sensory rhodopsin II in complex with its cognate transducer forms dimers at low salt concentration, which associate into trimers of dimers at higher buffer molarities.	Salts	157-161	rhodopsin	Homo sapiens	85-94
34022241-0	2021	Functional Integrity of Membrane Protein Rhodopsin Solubilized by Styrene-Maleic Acid Copolymer.	styrene-maleic acid copolymer	66-95	rhodopsin	Homo sapiens	41-50
34022241-2	2021	In this study, the functional properties of the membrane protein rhodopsin in its native lipid environment were investigated after being solubilized with styrene-maleic acid (SMA) copolymer.	styrene-maleic acid	154-173	rhodopsin	Homo sapiens	65-74
34022241-2	2021	In this study, the functional properties of the membrane protein rhodopsin in its native lipid environment were investigated after being solubilized with styrene-maleic acid (SMA) copolymer.	sma	175-178	rhodopsin	Homo sapiens	65-74
34019877-0	2021	Real-Time Identification of Two Substrate-Binding Intermediates for the Light-Driven Sodium Pump Rhodopsin.	Sodium	85-91	rhodopsin	Homo sapiens	97-106
34026400-1	2021	Marine bacterial TAT rhodopsin possesses the pKa of the retinal Schiff base, the chromophore, at neutral pH, and photoexcitation of the visible protonated state forms the isomerized 13-cis state, but reverts to the original state within 10-5 sec.	Schiff Bases	64-75	rhodopsin	Homo sapiens	21-30
4798981-0	1973	[Relationship between rhodopsin and phospholipid (author"s transl)].	Phospholipids	36-48	rhodopsin	Homo sapiens	22-31
33903621-3	2021	To broaden the operating range of photoreceptors, mammalian rod photoresponse recovery is accelerated mainly by two calcium sensor proteins: recoverin, modulating the lifetime of activated rhodopsin, and guanylate cyclase-activating proteins (GCAPs), regulating the cGMP synthesis.	Calcium	116-123	rhodopsin	Homo sapiens	189-198
4799902-1	1973	Release of sodium ions from the surface of rhodopsin molecules on illumination (author"s transl)].	Sodium	11-17	rhodopsin	Homo sapiens	43-52
34026400-2	2021	To understand the origin of these unique molecular properties of TAT rhodopsin, we mutated Thr82 into Asp, because many microbial rhodopsins contain Asp at the corresponding position as the Schiff base counterion.	Aspartic Acid	102-105	rhodopsin	Homo sapiens	69-78
34026400-4	2021	It was thus concluded that T82 is the origin of the neutral pKa of the Schiff base in TAT rhodopsin.	Schiff Bases	71-82	rhodopsin	Homo sapiens	90-99
33920057-4	2021	The diversity of rhodopsin-containing bacteria in neuston and plankton of Lake Baikal was comparable to other studied water bodies.	Water	118-123	rhodopsin	Homo sapiens	17-26
33920057-6	2021	The number of rhodopsin sequences unclassified to the phylum level was rather high: 29% in the water microbiomes and 22% in the epilithon.	Water	95-100	rhodopsin	Homo sapiens	14-23
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	1-palmitoyl-2-oleoyl-sn-glycero	126-157	rhodopsin	Homo sapiens	7-16
33453187-2	2021	Light absorption by rhodopsin leads to the activation of transducin as a result of the exchange of its GDP for GTP.	Guanosine Diphosphate	103-106	rhodopsin	Homo sapiens	20-29
33453187-2	2021	Light absorption by rhodopsin leads to the activation of transducin as a result of the exchange of its GDP for GTP.	Guanosine Triphosphate	111-114	rhodopsin	Homo sapiens	20-29
33721993-4	2021	Here we studied the molecular properties of the protonated and unprotonated forms of the Schiff base in TAT rhodopsin.	Schiff Bases	89-100	rhodopsin	Homo sapiens	108-117
33753488-0	2021	Early-stage dynamics of chloride ion-pumping rhodopsin revealed by a femtosecond X-ray laser.	Chlorides	24-32	rhodopsin	Homo sapiens	45-54
33753488-1	2021	Chloride ion-pumping rhodopsin (ClR) in some marine bacteria utilizes light energy to actively transport Cl- into cells.	Chlorides	0-8	rhodopsin	Homo sapiens	21-30
33730052-6	2021	In this regard, the histamine H1 receptor, which belongs to the family of rhodopsin-like G-protein-coupled receptors and is activated by the biogenic amine histamine, was found to be the most important node in the centrality of input-degrees.	Amines	24-29	rhodopsin	Homo sapiens	74-83
33730052-6	2021	In this regard, the histamine H1 receptor, which belongs to the family of rhodopsin-like G-protein-coupled receptors and is activated by the biogenic amine histamine, was found to be the most important node in the centrality of input-degrees.	Histamine	20-29	rhodopsin	Homo sapiens	74-83
33662383-4	2021	Very long chain PUFAs (VLC-PUFAs,n-3, >= 28 carbons) are at the sn-1 of this PC molecular species and interact with rhodopsin.	Carbon	44-51	rhodopsin	Homo sapiens	116-125
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	1,2-dioleoyl-sn-glycerophospholipids	163-199	rhodopsin	Homo sapiens	7-16
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	Phosphorylcholine	205-219	rhodopsin	Homo sapiens	7-16
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	Phosphorylcholine	221-223	rhodopsin	Homo sapiens	7-16
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	phosphorylethanolamine	228-247	rhodopsin	Homo sapiens	7-16
33217383-3	2021	Visual rhodopsin was recombined with lipids varying in their degree of acyl chain unsaturation and polar headgroup size using 1-palmitoyl-2-oleoyl-sn-glycero- and 1,2-dioleoyl-sn-glycerophospholipids with phosphocholine (PC) or phosphoethanolamine (PE) headgroups.	phosphorylethanolamine	249-251	rhodopsin	Homo sapiens	7-16
33217383-11	2021	Spontaneous negative monolayer curvature towards water is mediated by unsaturated, small-headgroup lipids and couples directly to GPCR activation upon light absorption by rhodopsin.	Water	49-54	rhodopsin	Homo sapiens	171-180
33495354-8	2021	Reducing rhodopsin levels by raising animals in a carotenoid-free medium not only attenuates rhodopsin accumulation, but also retinal degeneration.	Carotenoids	50-60	rhodopsin	Homo sapiens	9-18
32596956-0	2021	Activation of the G-Protein-Coupled Receptor Rhodopsin by Water.	Water	58-63	rhodopsin	Homo sapiens	45-54
32596956-2	2021	Here we show experimentally for the first time that ~80 water molecules flood rhodopsin upon light absorption to form a solvent-swollen active state.	Water	56-61	rhodopsin	Homo sapiens	78-87
33281496-4	2021	We discovered that phosphatidylcholine bound to rhodopsin with a greater affinity than phosphatidylserine or phosphatidylethanolamine, and that binding of all lipids was influenced by zinc but with different effects.	Phosphatidylcholines	19-38	rhodopsin	Homo sapiens	48-57
33495354-8	2021	Reducing rhodopsin levels by raising animals in a carotenoid-free medium not only attenuates rhodopsin accumulation, but also retinal degeneration.	Carotenoids	50-60	rhodopsin	Homo sapiens	93-102
33215912-4	2020	Experimental works indicate the loss of thermostability of the rhodopsin protein, subjected to the combination of-typical for the disease-mutations and increased quantity of Zn2+.	Zinc	174-178	rhodopsin	Homo sapiens	63-72
33441566-9	2021	The results indicate that the color-tuning mechanism of type-I rhodopsin can be applied to understand the color-tuning of heliorhodopsin.	heliorhodopsin	122-136	rhodopsin	Homo sapiens	63-72
33453993-2	2020	Rhodopsin becomes activated when light isomerizes 11-cis-retinal into an agonist, all-trans-retinal (ATR), which enables the receptor to activate its G protein.	Retinaldehyde	50-64	rhodopsin	Homo sapiens	0-9
32757375-1	2020	Evaluating the availability of molecular oxygen (O2 ) and energy of excited states in the retinal binding site of rhodopsin is a crucial challenging first step to understand photosensitizing reactions in wild-type (WT) and mutant rhodopsins by absorbing visible light.	Oxygen	41-47	rhodopsin	Homo sapiens	114-123
32818733-4	2020	The mechanisms of ARB and ARGs removal, and conjugation transfer of RP4 plasmids by UV, chlorine and synergistic UV/chlorine disinfection was revealed.	beta-L-Arabinose	18-21	rhodopsin	Homo sapiens	68-71
32818733-4	2020	The mechanisms of ARB and ARGs removal, and conjugation transfer of RP4 plasmids by UV, chlorine and synergistic UV/chlorine disinfection was revealed.	Chlorine	88-96	rhodopsin	Homo sapiens	68-71
32818733-4	2020	The mechanisms of ARB and ARGs removal, and conjugation transfer of RP4 plasmids by UV, chlorine and synergistic UV/chlorine disinfection was revealed.	Chlorine	116-124	rhodopsin	Homo sapiens	68-71
32818733-12	2020	The risk of RP4 plasmid conjugation transfer was significantly reduced with UV/chlorine (UV >= 4 mJ/cm2, chlorine >= 1 mg/L).	Chlorine	79-87	rhodopsin	Homo sapiens	12-15
32818733-12	2020	The risk of RP4 plasmid conjugation transfer was significantly reduced with UV/chlorine (UV >= 4 mJ/cm2, chlorine >= 1 mg/L).	Chlorine	105-113	rhodopsin	Homo sapiens	12-15
32931266-1	2020	We report an in-depth analysis of the photo-induced isomerization of the 2-cis- penta-2,4-dieniminium cation: a minimal model of the 11-cis retinal protonated Schiff base chromophore of the dim-light photoreceptor rhodopsin.	2-cis- penta-2,4-dieniminium	73-101	rhodopsin	Homo sapiens	214-223
32931266-6	2020	In particular, a recently reported vibrational phase relationship between double-bond torsion and hydrogen-out-of-plane modes critical for rhodopsin isomerization efficiency is correctly reproduced.	Hydrogen	98-106	rhodopsin	Homo sapiens	139-148
33038622-5	2020	The decreased abundance of two mobile genetic elements and impaired conjugative transfer of RP4 plasmid in the presence of PA, F2 and F3 demonstrated that the weakened horizontal gene transfer (HGT) contributed to the reduced ARG level.	pyroligneous acid	123-125	rhodopsin	Homo sapiens	92-95
33038622-5	2020	The decreased abundance of two mobile genetic elements and impaired conjugative transfer of RP4 plasmid in the presence of PA, F2 and F3 demonstrated that the weakened horizontal gene transfer (HGT) contributed to the reduced ARG level.	Arginine	226-229	rhodopsin	Homo sapiens	92-95
32757375-1	2020	Evaluating the availability of molecular oxygen (O2 ) and energy of excited states in the retinal binding site of rhodopsin is a crucial challenging first step to understand photosensitizing reactions in wild-type (WT) and mutant rhodopsins by absorbing visible light.	Oxygen	49-51	rhodopsin	Homo sapiens	114-123
32194062-1	2020	Krokinobacter rhodopsin 2 (KR2) was discovered as the first light-driven sodium pumping rhodopsin (NaR) in 2013, which contains unique amino acid residues on C-helix (N112, D116, and Q123), referred to as an NDQ motif.	Sodium	73-79	rhodopsin	Homo sapiens	14-23
32844642-3	2020	We report successfully achieving this for the light-driven Na+ pump rhodopsin (NaR).	nar	79-82	rhodopsin	Homo sapiens	68-77
32470317-0	2020	A Conserved Proline Hinge Mediates Helix Dynamics and Activation of Rhodopsin.	Proline	12-19	rhodopsin	Homo sapiens	68-77
32470317-2	2020	Here, we use solid-state NMR and Fourier transform infrared spectroscopy on rhodopsin to show that Trp2656.48 within the CWxP motif on transmembrane helix H6 constrains a proline hinge in the inactive state, suggesting that activation results in unraveling of the H6 backbone within this motif, a local change in dynamics that allows helix H6 to swing outward.	Proline	171-178	rhodopsin	Homo sapiens	76-85
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Nitric Oxide	79-91	rhodopsin	Homo sapiens	150-156
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Nitric Oxide	79-91	rhodopsin	Homo sapiens	158-162
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Nitric Oxide	79-91	rhodopsin	Homo sapiens	187-191
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Peroxynitrous Acid	102-115	rhodopsin	Homo sapiens	150-156
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Peroxynitrous Acid	102-115	rhodopsin	Homo sapiens	158-162
32992650-7	2020	Fluorescence measurements revealed that UVB increased intracellular free Ca2+, nitric oxide (NO), and peroxynitrite contents, which were inhibited by Opsin2 (OPN2) siRNA, suggesting that OPN2 functions as a UVB sensor.	Peroxynitrous Acid	102-115	rhodopsin	Homo sapiens	187-191
32814821-0	2020	The chirality origin of retinal-carotenoid complex in gloeobacter rhodopsin: a temperature-dependent excitonic coupling.	Carotenoids	32-42	rhodopsin	Homo sapiens	66-75
32588871-0	2020	Quercetin protects ARPE-19 cells against photic stress mediated by the products of rhodopsin photobleaching.	Quercetin	0-9	rhodopsin	Homo sapiens	83-92
32588871-9	2020	Cytotoxicity measurements and MMP analyses confirmed that supplementation with quercetin protected ARPE-19 cells against photic stress mediated by rhodopsin-rich POS.	Quercetin	79-88	rhodopsin	Homo sapiens	147-156
32194062-1	2020	Krokinobacter rhodopsin 2 (KR2) was discovered as the first light-driven sodium pumping rhodopsin (NaR) in 2013, which contains unique amino acid residues on C-helix (N112, D116, and Q123), referred to as an NDQ motif.	2-[3-[(4-azanyl-2-methoxy-pyrimidin-5-yl)methyl]-4-methyl-1,3-thiazol-5-yl]ethyl phosphono hydrogen phosphate	208-211	rhodopsin	Homo sapiens	14-23
33062188-1	2020	GPR18 is a rhodopsin-like orphan G-protein-coupled receptor (GPCR) that is activated by the natural cannabinoid (CB) Delta9-tetrahydrocannabinol (THC).	Cannabinoids	100-111	rhodopsin	Homo sapiens	11-20
33062188-1	2020	GPR18 is a rhodopsin-like orphan G-protein-coupled receptor (GPCR) that is activated by the natural cannabinoid (CB) Delta9-tetrahydrocannabinol (THC).	Dronabinol	117-144	rhodopsin	Homo sapiens	11-20
33062188-1	2020	GPR18 is a rhodopsin-like orphan G-protein-coupled receptor (GPCR) that is activated by the natural cannabinoid (CB) Delta9-tetrahydrocannabinol (THC).	Dronabinol	146-149	rhodopsin	Homo sapiens	11-20
33173715-1	2020	Microbial rhodopsin is a large family of membrane proteins having seven transmembrane helices (TM1-7) with an all-trans retinal (ATR) chromophore that is covalently bound to Lys in the TM7.	Lysine	174-177	rhodopsin	Homo sapiens	10-19
32035313-5	2020	The aim and natural bond orbital analysis identified key contribution of individual hydrogen/halogen bonds that contribute for the binding strength through stabilization energy, rho and  2rho values.	Hydrogen	84-92	rhodopsin	Homo sapiens	178-188
32374610-2	2020	This system, based on the cellular retinoic acid binding protein, is structurally different from natural rhodopsin systems; but exhibits a similar isomerization upon light irradiation.	Tretinoin	35-48	rhodopsin	Homo sapiens	105-114
32035313-5	2020	The aim and natural bond orbital analysis identified key contribution of individual hydrogen/halogen bonds that contribute for the binding strength through stabilization energy, rho and  2rho values.	Halogens	93-100	rhodopsin	Homo sapiens	178-188
31846310-7	2020	Interestingly, our comparative analysis of non-phosphorylated and phosphorylated rhodopsin structure demonstrated enhanced receptor stability upon phosphorylation at the C-terminal region that leads to the opening of the extracellular part of the transmembrane helices.	Carbon	170-171	rhodopsin	Homo sapiens	81-90
32326322-1	2020	Most G protein-coupled receptors that bind the hydrophobic ligands (lipid receptors and steroid receptors) belong to the most populated class A (rhodopsin-like) of these receptors.	Steroids	88-95	rhodopsin	Homo sapiens	145-154
32065378-4	2020	As cofactors bound with their animal and microbial rhodopsin (seven transmembrane alpha-helices) environments, 11-cis and all-trans retinal undergo photoisomerization into all-trans and 13-cis retinal forms as part of their functional cycle.	13-cis-retinal	186-200	rhodopsin	Homo sapiens	51-60
31740780-1	2020	H1 histamine receptor (H1HR) belongs to the family of rhodopsin-like G-protein-coupled receptors.	Histamine	3-12	rhodopsin	Homo sapiens	54-63
31887021-0	2020	Allosteric Communication to the Retinal Chromophore upon Ion Binding in a Light-driven Sodium Ion Pumping Rhodopsin.	Retinaldehyde	32-39	rhodopsin	Homo sapiens	106-115
31887021-0	2020	Allosteric Communication to the Retinal Chromophore upon Ion Binding in a Light-driven Sodium Ion Pumping Rhodopsin.	Sodium	87-93	rhodopsin	Homo sapiens	106-115
31887021-1	2020	Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence of sodium ion and works as a proton pump in the presence of larger monovalent cations such as potassium ion, rubidium ion, and cesium ion.	Sodium	57-63	rhodopsin	Homo sapiens	14-23
31887021-1	2020	Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence of sodium ion and works as a proton pump in the presence of larger monovalent cations such as potassium ion, rubidium ion, and cesium ion.	Sodium	92-98	rhodopsin	Homo sapiens	14-23
31887021-1	2020	Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence of sodium ion and works as a proton pump in the presence of larger monovalent cations such as potassium ion, rubidium ion, and cesium ion.	Potassium	183-192	rhodopsin	Homo sapiens	14-23
31887021-1	2020	Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence of sodium ion and works as a proton pump in the presence of larger monovalent cations such as potassium ion, rubidium ion, and cesium ion.	Rubidium	198-206	rhodopsin	Homo sapiens	14-23
31887021-1	2020	Krokinobacter rhodopsin 2 (KR2) serves as a light-driven sodium ion pump in the presence of sodium ion and works as a proton pump in the presence of larger monovalent cations such as potassium ion, rubidium ion, and cesium ion.	Cesium	216-222	rhodopsin	Homo sapiens	14-23
31669405-13	2020	Both dexamethasone and progesterone increased retinal rhodopsin stores, suggesting a link between photoreceptor protection and transduction pathways.	Dexamethasone	5-18	rhodopsin	Homo sapiens	54-63
31669405-13	2020	Both dexamethasone and progesterone increased retinal rhodopsin stores, suggesting a link between photoreceptor protection and transduction pathways.	Progesterone	23-35	rhodopsin	Homo sapiens	54-63
31264415-0	2019	CpHMD-Then-QM/MM Identification of the Amino Acids Responsible for the Anabaena Sensory Rhodopsin pH-Dependent Electronic Absorption Spectrum.	cphmd-then	0-10	rhodopsin	Homo sapiens	88-97
31857914-1	2019	Purpose: Mutations in RHO, the gene for a rhodopsin, are a leading cause of autosomal dominant retinitis pigmentosa.	RHO rhodopsin protein, chicken	22-25	rhodopsin	Homo sapiens	42-51
31835521-6	2019	Alternatively, focus on discovering of non-retinoid small molecules beneficial in retinopathies associated with mutations in rhodopsin is currently a fast-growing pharmacological field.	Retinoids	43-51	rhodopsin	Homo sapiens	125-134
31835521-7	2019	In this review, we summarize the accumulated knowledge on retinoid ligands and non-retinoid modulators of the light-sensing GPCR, rhodopsin and their potential in combating the specific vision-related pathologies.	Retinoids	58-66	rhodopsin	Homo sapiens	130-139
31835521-7	2019	In this review, we summarize the accumulated knowledge on retinoid ligands and non-retinoid modulators of the light-sensing GPCR, rhodopsin and their potential in combating the specific vision-related pathologies.	Retinoids	83-91	rhodopsin	Homo sapiens	130-139
31720623-3	2019	However, a recent ultrafast spectroscopic study on a sodium-pumping rhodopsin suggested that such a complex decay may originate from the heterogeneity in the ground state due to the acid-base equilibrium of the counterion of the protonated retinal Schiff base (PRSB).	Schiff Bases	248-259	rhodopsin	Homo sapiens	68-77
31652065-0	2019	Induced Night-Vision by Singlet-Oxygen-Mediated Activation of Rhodopsin.	Oxygen	32-38	rhodopsin	Homo sapiens	62-71
31697785-0	2019	Correction: Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin.	IS 23	75-79	rhodopsin	Homo sapiens	116-125
31624206-5	2019	The colonies rapidly invert their curvature in response to changing light levels, which they detect through a rhodopsin-cyclic guanosine monophosphate pathway.	Cyclic GMP	120-150	rhodopsin	Homo sapiens	110-119
32016894-7	2020	Two major regions of interaction were identified: at the C-terminal tail of rhodopsin (D330-S343) and where the "finger loop" (G69-T79) of arrestin directly inserts into rhodopsin active core.	Carbon	57-58	rhodopsin	Homo sapiens	76-85
32016894-7	2020	Two major regions of interaction were identified: at the C-terminal tail of rhodopsin (D330-S343) and where the "finger loop" (G69-T79) of arrestin directly inserts into rhodopsin active core.	Carbon	57-58	rhodopsin	Homo sapiens	170-179
32016894-7	2020	Two major regions of interaction were identified: at the C-terminal tail of rhodopsin (D330-S343) and where the "finger loop" (G69-T79) of arrestin directly inserts into rhodopsin active core.	chloroamide S-330	87-96	rhodopsin	Homo sapiens	76-85
31920544-6	2019	Analysis of single-cell Ca2+ signaling profiles revealed unique Ca2+ signaling responses exist in cells expressing WT or P23H rhodopsin, consistent with the idea that second messenger signaling is affected by cell stress.	Calcium	24-28	rhodopsin	Homo sapiens	126-135
31920544-6	2019	Analysis of single-cell Ca2+ signaling profiles revealed unique Ca2+ signaling responses exist in cells expressing WT or P23H rhodopsin, consistent with the idea that second messenger signaling is affected by cell stress.	Calcium	64-68	rhodopsin	Homo sapiens	126-135
31685893-4	2019	We have developed Ace-mScarlet, a red fluorescent GEVI that fuses Ace2N, a voltage-sensitive inhibitory rhodopsin, with mScarlet, a bright red fluorescent protein (FP).	ace2n	66-71	rhodopsin	Homo sapiens	104-113
31300275-1	2019	Rhodopsin (Rho), a prototypical G-protein-coupled receptor (GPCR) in vertebrate vision, activates the G-protein transducin (GT) by catalyzing GDP-GTP exchange on its alpha subunit (GalphaT).	gdp-gtp	142-149	rhodopsin	Homo sapiens	0-9
30698921-5	2019	The esters are the substrate for RPE65, an enzyme that produces 11-cis retinol, which is converted to 11-cis retinaldehyde for transport to the photoreceptors to form rhodopsin.	Esters	4-10	rhodopsin	Homo sapiens	167-176
31457093-4	2019	The highest rhodopsin concentrations were observed above the deep chlorophyll-a maxima, and their geographical distribution tended to be inversely related to that of chlorophyll-a.	chlorophyll a	66-79	rhodopsin	Homo sapiens	12-21
31457093-4	2019	The highest rhodopsin concentrations were observed above the deep chlorophyll-a maxima, and their geographical distribution tended to be inversely related to that of chlorophyll-a.	chlorophyll a	166-179	rhodopsin	Homo sapiens	12-21
30954887-3	2019	Among these, histidine kinase rhodopsins (HKR) are photo-regulated two-component-like signaling systems that trigger a phosphorylation cascade, whereas rhodopsin phosphodiesterase (RhoPDE) or rhodopsin guanylyl cyclase (RhGC) show either light-activated hydrolysis or production of cyclic nucleotides.	Nucleotides, Cyclic	282-300	rhodopsin	Homo sapiens	30-39
30954887-3	2019	Among these, histidine kinase rhodopsins (HKR) are photo-regulated two-component-like signaling systems that trigger a phosphorylation cascade, whereas rhodopsin phosphodiesterase (RhoPDE) or rhodopsin guanylyl cyclase (RhGC) show either light-activated hydrolysis or production of cyclic nucleotides.	Nucleotides, Cyclic	282-300	rhodopsin	Homo sapiens	152-161
30698921-5	2019	The esters are the substrate for RPE65, an enzyme that produces 11-cis retinol, which is converted to 11-cis retinaldehyde for transport to the photoreceptors to form rhodopsin.	Vitamin A	64-78	rhodopsin	Homo sapiens	167-176
30698921-5	2019	The esters are the substrate for RPE65, an enzyme that produces 11-cis retinol, which is converted to 11-cis retinaldehyde for transport to the photoreceptors to form rhodopsin.	11-cis retinaldehyde	102-122	rhodopsin	Homo sapiens	167-176
31100078-4	2019	The in vitro biochemical properties of these two rhodopsin proteins, expressed in stably transfected tetracycline-inducible HEK293S cells, their UV-visible absorption, their Fourier transform infrared, circular dichroism and Metarhodopsin II fluorescence spectroscopy properties were characterized.	Tetracycline	101-113	rhodopsin	Homo sapiens	49-58
31061086-13	2019	This study uncovers a hitherto uncharacterized consequence of rhodopsin mislocalization: the activation of the lysosomal pathway, which negatively regulates the amount of the sodium-potassium ATPase (NKAalpha) on the inner segment plasma membrane.	Sodium	175-181	rhodopsin	Homo sapiens	62-71
31061086-13	2019	This study uncovers a hitherto uncharacterized consequence of rhodopsin mislocalization: the activation of the lysosomal pathway, which negatively regulates the amount of the sodium-potassium ATPase (NKAalpha) on the inner segment plasma membrane.	Potassium	182-191	rhodopsin	Homo sapiens	62-71
31050413-0	2019	Rhodopsin-Like Ionic Gate Fabricated with Graphene Oxide and Isomeric DNA Switch for Efficient Photocontrol of Ion Transport.	graphene oxide	42-56	rhodopsin	Homo sapiens	0-9
31050413-2	2019	Inspired by rhodopsin, we have fabricated a light-regulated ionic gate on the basis of the design of a graphene oxide (GO)-biomimetic DNA-nanochannel architecture.	graphene oxide	103-117	rhodopsin	Homo sapiens	12-21
31050413-2	2019	Inspired by rhodopsin, we have fabricated a light-regulated ionic gate on the basis of the design of a graphene oxide (GO)-biomimetic DNA-nanochannel architecture.	graphene oxide	119-121	rhodopsin	Homo sapiens	12-21
30948514-3	2019	Human rhodopsin is N-glycosylated on Asn2 and Asn15, whereas human (h) red and green cone opsins (hOPSR and hOPSG, respectively) are N-glycosylated at Asn34 Here, utilizing a monoclonal antibody (7G8 mAB), we demonstrate that hOPSR and hOPSG from human retina also are O-glycosylated with full occupancy.	Nitrogen	19-20	rhodopsin	Homo sapiens	6-15
31100078-7	2019	As described previously for WT rhodopsin, addition of the cytoplasmic allosteric modulator chlorin e6 stabilizes especially the P23H protein, suggesting that chlorin e6 may be generally beneficial in the rescue of those ADRP rhodopsin proteins whose stability is affected by amino acid replacement.	phytochlorin	91-101	rhodopsin	Homo sapiens	31-40
31044640-3	2019	Bleaching of rhodopsin-rich POS with green light resulted in the formation of retinoid products exhibiting distinct absorption spectra in the near-UV.	Retinoids	78-86	rhodopsin	Homo sapiens	13-22
30995409-0	2019	Bile Acid Binding Protein Functionalization Leads to a Fully Synthetic Rhodopsin Mimic.	Bile Acids and Salts	0-9	rhodopsin	Homo sapiens	71-80
30995409-3	2019	More specifically, we conjugate a bile acid binding protein with a synthetic mimic of the rhodopsin protonated Schiff base chromophore to achieve a covalent complex featuring an unnatural protein host, photoswitch, and photoswitch-protein linkage with a reverse orientation.	Bile Acids and Salts	34-43	rhodopsin	Homo sapiens	90-99
30995409-3	2019	More specifically, we conjugate a bile acid binding protein with a synthetic mimic of the rhodopsin protonated Schiff base chromophore to achieve a covalent complex featuring an unnatural protein host, photoswitch, and photoswitch-protein linkage with a reverse orientation.	Schiff Bases	111-122	rhodopsin	Homo sapiens	90-99
31098413-0	2019	The counterion-retinylidene Schiff base interaction of an invertebrate rhodopsin rearranges upon light activation.	counterion-retinylidene schiff base	4-39	rhodopsin	Homo sapiens	71-80
31098413-4	2019	Here, we demonstrate that in a spider visual rhodopsin, orthologue of mammal melanopsins relevant to circadian rhythms, the Glu181 counterion functions likely by forming a hydrogen-bonding network, where Ser186 is a key mediator of the Glu181-SB interaction.	Hydrogen	172-180	rhodopsin	Homo sapiens	45-54
31098413-4	2019	Here, we demonstrate that in a spider visual rhodopsin, orthologue of mammal melanopsins relevant to circadian rhythms, the Glu181 counterion functions likely by forming a hydrogen-bonding network, where Ser186 is a key mediator of the Glu181-SB interaction.	Schiff Bases	243-245	rhodopsin	Homo sapiens	45-54
30872581-1	2019	The retinal protonated Schiff-base (RPSB) in its all-trans form is found in bacterial rhodopsins, whereas visual rhodopsin proteins host 11-cis RPSB.	Schiff Bases	23-34	rhodopsin	Homo sapiens	86-95
30721054-4	2019	In the present work we benchmark the more affordable multiconfiguration pair-density functional theory (MC-PDFT) method whose accuracy has been recently validated for retinal chromophores in the gas phase, indicating that MC-PDFT could potentially be used to analyze large (e.g., few hundreds) sets of rhodopsin proteins.	Methylcholanthrene	104-106	rhodopsin	Homo sapiens	302-311
30463023-3	2019	A novel potential radiosensitizer 1,8-Dihydroxy -3-(2"-(4""-methylpiperazin-1""-yl) ethyl-9,10-anthraquinone -3-carboxylate (RP-4) was designed and synthesized based on molecular docking technology, which was expected to regulate the radiosensitivity of tumor cells through targeting Rac1.	1,8-dihydroxy -3-(2"-(4""-methylpiperazin-1""-yl) ethyl-9,10-anthraquinone -3-carboxylate	34-123	rhodopsin	Homo sapiens	125-129
30742765-0	2019	Point Mutation of Anabaena Sensory Rhodopsin Enhances Ground-State Hydrogen Out-of-Plane Wag Raman Activity.	Hydrogen	67-75	rhodopsin	Homo sapiens	35-44
30713705-7	2019	45, 335-341], is then shown to improve the indexing rate and quality of merged serial femtosecond crystallography data from two membrane proteins, the human delta-opioid receptor in complex with a bi-functional peptide ligand DIPP-NH2 and the NTQ chloride-pumping rhodopsin (CIR).	2',6'-dimethyltyrosyl-1,2,3,4-tetrahydro-3-isoquinolinecarbonyl-phenylalanyl-phenylalaninamide	226-234	rhodopsin	Homo sapiens	264-273
30525616-0	2019	Retinal-Salinixanthin Interactions in a Thermophilic Rhodopsin.	salinixanthin	8-21	rhodopsin	Homo sapiens	53-62
30525616-3	2019	In this paper, we present the formation of a novel antenna complex between thermophilic rhodopsin (TR) and the carotenoid salinixanthin (Sal).	Carotenoids	111-121	rhodopsin	Homo sapiens	88-97
30525616-3	2019	In this paper, we present the formation of a novel antenna complex between thermophilic rhodopsin (TR) and the carotenoid salinixanthin (Sal).	salinixanthin	122-135	rhodopsin	Homo sapiens	88-97
30525616-3	2019	In this paper, we present the formation of a novel antenna complex between thermophilic rhodopsin (TR) and the carotenoid salinixanthin (Sal).	salinixanthin	137-140	rhodopsin	Homo sapiens	88-97
30666186-0	2018	Light-Induced Thiol Oxidation of Recoverin Affects Rhodopsin Desensitization.	Sulfhydryl Compounds	14-19	rhodopsin	Homo sapiens	51-60
30321592-5	2019	Interestingly, the CCR2 receptor isoforms are identical up to arginine 313 (R313) that is part of the putative 8th helix in CCR2 receptors, and the 8th helix has been implicated in the interaction of rhodopsin-like G protein-coupled receptors with Galphaq.	Arginine	62-70	rhodopsin	Homo sapiens	200-209
30679635-2	2019	Via a multi-dimensional screening setup, we identified and combined arrestin-1 mutants that form lasting complexes with light-activated and phosphorylated rhodopsin in harsh conditions, such as high ionic salt concentration.	ionic salt	199-209	rhodopsin	Homo sapiens	155-164
30489081-6	2018	Upon light exposure, rhodopsin is swollen by the penetration of water into the protein core, allowing interactions with effector proteins in the visual signaling mechanism.	Water	64-69	rhodopsin	Homo sapiens	21-30
30969409-2	2019	The molecular dynamics (MD) simulations are powerful computational tools to investigate molecular behavior of proteins and internal water molecules which are related to the function of proteins; however, the MD simulations of the rhodopsin require several technical setups for accurate calculations.	Water	132-137	rhodopsin	Homo sapiens	230-239
30484447-2	2018	Anabaena Sensory Rhodopsin (ASR) is a microbial retinal protein that comprises a retinal chromophore in two ground state (GS) conformations: all-trans, 15-anti (AT) and 13-cis, 15-syn (13C).	13c	185-188	rhodopsin	Homo sapiens	17-26
29990597-1	2018	The neuronal calcium sensor protein recoverin is expressed in retinal rod and cone cells and is involved in the calcium-dependent control of receptor (rhodopsin) phosphorylation and receptor inactivation.	Calcium	13-20	rhodopsin	Homo sapiens	151-160
29990597-1	2018	The neuronal calcium sensor protein recoverin is expressed in retinal rod and cone cells and is involved in the calcium-dependent control of receptor (rhodopsin) phosphorylation and receptor inactivation.	Calcium	112-119	rhodopsin	Homo sapiens	151-160
29863983-10	2018	Both H1299 rho0 and rho+ cells had higher ROS levels after irradiation, however, the radiation-induced ROS production in rho0 cells was significantly lower than in rho+ cells.	ros	42-45	rhodopsin	Homo sapiens	5-23
30120952-8	2018	Hydrogen-deuterium exchange studies revealed the footprint of the light-activated rhodopsin on sArr.	Hydrogen	0-8	rhodopsin	Homo sapiens	82-91
30120952-8	2018	Hydrogen-deuterium exchange studies revealed the footprint of the light-activated rhodopsin on sArr.	Deuterium	9-18	rhodopsin	Homo sapiens	82-91
29863983-10	2018	Both H1299 rho0 and rho+ cells had higher ROS levels after irradiation, however, the radiation-induced ROS production in rho0 cells was significantly lower than in rho+ cells.	ros	103-106	rhodopsin	Homo sapiens	5-23
29750864-1	2018	Rhodopsin is widely distributed in organisms as a membrane-embedded photoreceptor protein, consisting of the apoprotein opsin and vitamin-A aldehyde retinal, A1-retinal and A2-retinal being the natural chromophores.	Vitamin A	130-139	rhodopsin	Homo sapiens	0-9
29915394-1	2018	A new microbial rhodopsin class that actively transports sodium out of the cell upon illumination was described in 2013.	Sodium	57-63	rhodopsin	Homo sapiens	16-25
29750864-1	2018	Rhodopsin is widely distributed in organisms as a membrane-embedded photoreceptor protein, consisting of the apoprotein opsin and vitamin-A aldehyde retinal, A1-retinal and A2-retinal being the natural chromophores.	Aldehydes	140-148	rhodopsin	Homo sapiens	0-9
29626443-0	2018	Effect of dietary docosahexaenoic acid on rhodopsin content and packing in photoreceptor cell membranes.	Docosahexaenoic Acids	18-38	rhodopsin	Homo sapiens	42-51
29555765-4	2018	Chemical modification of S-RS1 and further structural analysis revealed the core binding motif of this class of rhodopsin stabilizers bound at the orthosteric binding site.	s-rs1	25-30	rhodopsin	Homo sapiens	112-121
29454859-0	2018	Tauroursodeoxycholic acid binds to the G-protein site on light activated rhodopsin.	ursodoxicoltaurine	0-25	rhodopsin	Homo sapiens	73-82
29454859-2	2018	Tauroursodeoxycholic acid bears structural resemblance to several compounds that were previously identified to specifically bind to the light-activated form of the visual receptor rhodopsin and to inhibit its activation of transducin.	ursodoxicoltaurine	0-25	rhodopsin	Homo sapiens	180-189
29454859-3	2018	We show that TUDCA stabilizes the active form of rhodopsin, metarhodopsin II, and does not display the detergent-like effects of common amphiphilic compounds that share the cholesterol scaffold structure, such as deoxycholic acid.	ursodoxicoltaurine	13-18	rhodopsin	Homo sapiens	49-58
29454859-6	2018	The results show that TUDCA interacts specifically with rhodopsin, which may contribute to its wide-ranging effects on retina physiology and as a potential therapeutic compound for retina degenerative diseases.	ursodoxicoltaurine	22-27	rhodopsin	Homo sapiens	56-65
29401731-8	2018	That is, dopaminergic neuron-like cells, cholinergic neuron-like cells, GABAnergic neuron-like cells or rhodopsin-positive neuron-like cells were induced by different NDD peptides.	ndd peptides	167-179	rhodopsin	Homo sapiens	104-113
29174700-6	2018	We found that the sub-MIC of Cip or Lev enhanced the expression of several genes on the RP4 plasmid, which was consistent with the conjugation efficiency.	Levamisole	36-39	rhodopsin	Homo sapiens	88-91
29057415-0	2018	Molecular details of the unique mechanism of chloride transport by a cyanobacterial rhodopsin.	Chlorides	45-53	rhodopsin	Homo sapiens	84-93
29057415-5	2018	Here, we studied the chloride-transporting photocycle of a representative of this new group, Mastigocladopsis repens rhodopsin (MastR), using time-resolved spectroscopy in the infrared and visible ranges and site-directed mutagenesis.	Chlorides	21-29	rhodopsin	Homo sapiens	117-126
30178379-3	2018	Published experimental work with rhodopsin and bacteriorhodopsin has led to the hypothesis that integral proteins lessen membrane oxygen permeability, as well as the permeability of the lipid region.	Oxygen	130-136	rhodopsin	Homo sapiens	33-42
29111729-0	2017	Retinal Binding to Apo-Gloeobacter Rhodopsin: The Role of pH and Retinal-Carotenoid Interaction.	Carotenoids	73-83	rhodopsin	Homo sapiens	35-44
29025970-3	2017	Rhodopsin and Arf4 bind the regulatory N-terminal dimerization and cyclophillin-binding (DCB)-homology upstream of Sec7 (HUS) domain of GBF1.	dcb	89-92	rhodopsin	Homo sapiens	0-9
28569420-0	2017	Rhodopsin T17M Mutant Inhibits Complement C3 Secretion in Retinal Pigment Epithelium via ROS Induced Downregulation of TWIST1.	ros	89-92	rhodopsin	Homo sapiens	0-9
28569420-9	2017	The overexpression of T17M rhodopsin significantly induced ROS and reduced C3 secretion and transcription in ARPE-19 cells, but ROS scavengers could partially rescue reduced C3 secretion and transcription.	ros	59-62	rhodopsin	Homo sapiens	27-36
28569420-11	2017	In conclusion, our data provide the first evidence that T17M rhodopsin mutant disrupts C3 secretion via the induction of ROS and the suppression of TWIST1.	ros	121-124	rhodopsin	Homo sapiens	61-70
28787707-7	2017	After adjusting for confounding factors (the age of pregnant mothers, education level, monthly household income, parity, and sex of the newborns), we found marginally significant inverse associations of cord plasma measurements of  hexachlorcyclohexanes ( HCHs), 1,1-dichloro-2,2-di(4-chlorophenyl)ethylene (rho,rho"-DDE) and methoxychlor with FT4 levels, but not with FT3 and TSH levels.	hchs	256-260	rhodopsin	Homo sapiens	308-320
28731695-3	2017	Key events of rhodopsin activation are the initial cis-trans photoisomerization of the covalently bound retinal moiety followed by conformational rearrangements and deprotonation of the chromophore"s protonated Schiff base (PSB), which ultimately lead to full activation in the meta II state.	Schiff Bases	211-222	rhodopsin	Homo sapiens	14-23
29117518-3	2017	In this kinetic scheme, the human rhodopsin exhibited more Schiff base deprotonation than bovine rhodopsin, which could arise from the ~7% sequence difference between the two proteins, or from the difference between their membrane lipid environments.	Schiff Bases	59-70	rhodopsin	Homo sapiens	34-43
28731695-3	2017	Key events of rhodopsin activation are the initial cis-trans photoisomerization of the covalently bound retinal moiety followed by conformational rearrangements and deprotonation of the chromophore"s protonated Schiff base (PSB), which ultimately lead to full activation in the meta II state.	psb	224-227	rhodopsin	Homo sapiens	14-23
28731695-9	2017	The study shows that, compared to the inactive 11-cis-retinal case, trans-retinal rhodopsin is able to undergo PSB deprotonation due to a change in the conformation of the retinal and a consequent alteration in the hydrogen-bond (HB) network in which PSB and the counterion Glu113 are embedded.	Hydrogen	215-223	rhodopsin	Homo sapiens	82-91
28894166-0	2017	Flavonoid allosteric modulation of mutated visual rhodopsin associated with retinitis pigmentosa.	Flavonoids	0-9	rhodopsin	Homo sapiens	50-59
28894166-4	2017	We have analyzed the effect of the flavonoid quercetin on the conformation, stability and function of the G protein-coupled receptor rhodopsin, and the G90V mutant associated with the retinal degenerative disease retinitis pigmentosa.	Flavonoids	35-44	rhodopsin	Homo sapiens	133-142
28894166-4	2017	We have analyzed the effect of the flavonoid quercetin on the conformation, stability and function of the G protein-coupled receptor rhodopsin, and the G90V mutant associated with the retinal degenerative disease retinitis pigmentosa.	Quercetin	45-54	rhodopsin	Homo sapiens	133-142
28655769-1	2017	The visual photo-transduction cascade is a prototypical G protein-coupled receptor (GPCR) signaling system, in which light-activated rhodopsin (Rho*) is the GPCR catalyzing the exchange of GDP for GTP on the heterotrimeric G protein transducin (GT).	Guanosine Diphosphate	189-192	rhodopsin	Homo sapiens	133-142
28752953-4	2017	Despite their abundance in marine and fresh-water systems, the presence of functional rhodopsin systems in edaphic habitats has never been reported.	Water	44-49	rhodopsin	Homo sapiens	86-95
28655769-1	2017	The visual photo-transduction cascade is a prototypical G protein-coupled receptor (GPCR) signaling system, in which light-activated rhodopsin (Rho*) is the GPCR catalyzing the exchange of GDP for GTP on the heterotrimeric G protein transducin (GT).	Guanosine Triphosphate	197-200	rhodopsin	Homo sapiens	133-142
28700926-1	2017	The visual photoreceptor rhodopsin is a prototypical G-protein-coupled receptor (GPCR) that stabilizes its inverse agonist ligand, 11-cis-retinal (11CR), by a covalent, protonated Schiff base linkage.	Schiff Bases	180-191	rhodopsin	Homo sapiens	25-34
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Cysteine	86-95	rhodopsin	Homo sapiens	28-37
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Cysteine	86-95	rhodopsin	Homo sapiens	235-244
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Serine	101-107	rhodopsin	Homo sapiens	28-37
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Serine	101-107	rhodopsin	Homo sapiens	235-244
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Valine	121-127	rhodopsin	Homo sapiens	28-37
28536260-6	2017	Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations.	Valine	121-127	rhodopsin	Homo sapiens	235-244
28700926-6	2017	We utilized genetic code expansion and site-specific bioorthogonal labeling of rhodopsin with Alexa488 to enable, to our knowledge, a novel fluorescence resonance energy transfer-based measurement of the binding kinetics between opsin and 11CR.	alexa488	94-102	rhodopsin	Homo sapiens	79-88
28700926-8	2017	We show that the dissociation reaction of rhodopsin to 11CR and opsin has a 25-pM equilibrium dissociation constant, which corresponds to only 0.3 kcal/mol stabilization compared to the noncovalent, tightly bound antagonist-GPCR complex of iodopindolol and beta-adrenergic receptor.	Iodopindolol	240-252	rhodopsin	Homo sapiens	42-51
28483278-8	2017	Subsequent treatment of mature 3T3-L1 adipocytes at a specific VR wavelength induced rhodopsin- and beta3-adrenergic receptor (AR)-dependent lipolytic responses that consequently led to increases in intracellular cAMP and phosphorylated HSL protein levels.	Cyclic AMP	213-217	rhodopsin	Homo sapiens	85-95
28969095-7	2017	Other mechanisms involving the retinal ganglion cells or ultraweak biophoton emission and rhodopsin bleaching after exposure to free radicals are also likely to be involved.	Free Radicals	128-141	rhodopsin	Homo sapiens	90-99
28302718-1	2017	Photoactivated adenylyl cyclase (PAC) and guanylyl cyclase rhodopsin increase the concentrations of intracellular cyclic nucleotides upon illumination, serving as promising second-generation tools in optogenetics.	Nucleotides, Cyclic	114-132	rhodopsin	Homo sapiens	59-68
28484015-5	2017	In this study, we determined whether amphibian blue-sensitive cone pigments in green rods exhibit low thermal isomerization rates to act as rhodopsin-like pigments for scotopic vision.	amphibian blue	37-51	rhodopsin	Homo sapiens	140-149
28493967-0	2017	Water permeation through the internal water pathway in activated GPCR rhodopsin.	Water	0-5	rhodopsin	Homo sapiens	70-79
28493967-0	2017	Water permeation through the internal water pathway in activated GPCR rhodopsin.	Water	38-43	rhodopsin	Homo sapiens	70-79
28493967-2	2017	Internal water molecules mediate activation of the receptor in a rhodopsin cascade reaction and contribute to conformational stability of the receptor.	Water	9-14	rhodopsin	Homo sapiens	65-74
28493967-9	2017	These findings revealed a total water flux between the bulk and the protein inside in the Meta II state, and suggested that these pathways provide water molecules to the crucial sites of the activated rhodopsin.	Water	32-37	rhodopsin	Homo sapiens	201-210
28493967-9	2017	These findings revealed a total water flux between the bulk and the protein inside in the Meta II state, and suggested that these pathways provide water molecules to the crucial sites of the activated rhodopsin.	Water	147-152	rhodopsin	Homo sapiens	201-210
28518188-3	2017	Applied to the case of the photochromic Anabaena sensory rhodopsin protein, the model succeeds in reproducing qualitatively the reported experimental data, confirming the importance of aspartic acid 217 in the observed blue shift in the lambdamax of ASR at neutral pH.	Aspartic Acid	185-198	rhodopsin	Homo sapiens	57-66
28518188-3	2017	Applied to the case of the photochromic Anabaena sensory rhodopsin protein, the model succeeds in reproducing qualitatively the reported experimental data, confirming the importance of aspartic acid 217 in the observed blue shift in the lambdamax of ASR at neutral pH.	asr	250-253	rhodopsin	Homo sapiens	57-66
28240904-1	2017	Rhodopsin is a G-protein coupled receptor functioning as a photoreceptor for vision through photoactivation of a covalently bound ligand of a retinal protonated Schiff base chromophore.	Schiff Bases	161-172	rhodopsin	Homo sapiens	0-9
28212859-0	2017	Docosahexaenoic acid phospholipid differentially modulates the conformation of G90V and N55K rhodopsin mutants associated with retinitis pigmentosa.	docosahexaenoic acid phospholipid	0-33	rhodopsin	Homo sapiens	93-102
28212859-3	2017	Docosahexaenoic acid has been shown to interact with native rhodopsin but no direct evidence has been established on the effect of such lipid on the stability and regeneration of rhodopsin mutants associated with retinal diseases.	Docosahexaenoic Acids	0-20	rhodopsin	Homo sapiens	60-69
28373559-2	2017	Here conformational substates of the GPCR rhodopsin are investigated in micelles of dodecyl maltoside (DDM) and in phospholipid nanodiscs by monitoring the spatial positions of transmembrane helices 6 and 7 at the cytoplasmic surface using site-directed spin labeling and double electron-electron resonance spectroscopy.	dodecyl maltoside	84-101	rhodopsin	Homo sapiens	42-51
28373559-2	2017	Here conformational substates of the GPCR rhodopsin are investigated in micelles of dodecyl maltoside (DDM) and in phospholipid nanodiscs by monitoring the spatial positions of transmembrane helices 6 and 7 at the cytoplasmic surface using site-directed spin labeling and double electron-electron resonance spectroscopy.	Phospholipids	115-127	rhodopsin	Homo sapiens	42-51
28065882-0	2017	Rescue of mutant rhodopsin traffic by metformin-induced AMPK activation accelerates photoreceptor degeneration.	Metformin	38-47	rhodopsin	Homo sapiens	17-26
28089451-5	2017	The 2.0-A structure of an alpha-helical seven-transmembrane microbial rhodopsin thus obtained is of high quality and virtually identical to the 2.2-A structure obtained from traditional detergent-based purification and subsequent LCP crystallization.	Perchloric Acid	230-233	rhodopsin	Homo sapiens	70-79
27836700-3	2017	The 9-cis counterpart of rhodopsin, dubbed isorhodopsin, has a much lower quantum yield (0.26+-0.03), which, however, can be markedly enhanced by modification of the retinal chromophore (7,8-dihydro and 9-cyclopropyl derivatives).	7,8-dihydro and 9-cyclopropyl derivatives	187-228	rhodopsin	Homo sapiens	25-34
28065882-2	2017	Here, we tested whether the AMPK activator metformin could affect the P23H rhodopsin synthesis and folding.	Metformin	43-52	rhodopsin	Homo sapiens	75-84
28065882-3	2017	In cell models, metformin treatment improved P23H rhodopsin folding and traffic.	Metformin	16-25	rhodopsin	Homo sapiens	50-59
28065882-5	2017	The metformin-rescued P23H rhodopsin was still intrinsically unstable and led to increased structural instability of the rod outer segments.	Metformin	4-13	rhodopsin	Homo sapiens	27-36
28129424-10	2017	Results: Two-photon excited fluorescence resulting from retinol production corresponded to the fraction of rhodopsin bleached.	Vitamin A	56-63	rhodopsin	Homo sapiens	107-116
28076806-1	2017	The vertebrate visual photoreceptor rhodopsin (Rho) is a unique G protein-coupled receptor as it utilizes a covalently tethered inverse agonist (11-cis-retinal) as the native ligand.	Retinaldehyde	145-159	rhodopsin	Homo sapiens	36-45
27900815-0	2017	Selective [3+1] Fragmentations of P4 by "P" Transfer from a Lewis Acid Stabilized [RP4 ]- Butterfly Anion.	Lewis Acids	60-70	rhodopsin	Homo sapiens	83-86
28129424-15	2017	Moreover, TPEF generated due to retinol can be used as a measure of rhodopsin depletion, similar to densitometry.	Vitamin A	32-39	rhodopsin	Homo sapiens	68-77
27935291-6	2016	The comparison of bovine and human rhodopsins shows that the initial Schiff base deprotonation equilibrium is more forward shifted in human rhodopsin, and more of the reaction flows through the metarhodopsin I380 intermediate in human rhodopsin than in the bovine protein.	Schiff Bases	69-80	rhodopsin	Homo sapiens	35-44
27995922-4	2017	Here, we test this hypothesis by investigating the degree of achievable control over the photoisomerization of the retinal protonated Schiff-base in bacteriorhodopsin, isorhodopsin and rhodopsin, all of which exhibit similar chromophores but different isomerization yields and excited-state lifetimes.	Schiff Bases	134-145	rhodopsin	Homo sapiens	157-166
27935291-6	2016	The comparison of bovine and human rhodopsins shows that the initial Schiff base deprotonation equilibrium is more forward shifted in human rhodopsin, and more of the reaction flows through the metarhodopsin I380 intermediate in human rhodopsin than in the bovine protein.	Schiff Bases	69-80	rhodopsin	Homo sapiens	140-149
27628201-3	2016	Our results reveal a broadly distributed relaxation of hydrogen atom dynamics of rhodopsin on a picosecond-nanosecond time scale, crucial for protein function, as only observed for globular proteins previously.	Hydrogen	55-63	rhodopsin	Homo sapiens	81-90
27812022-0	2016	The mutation p.E113K in the Schiff base counterion of rhodopsin is associated with two distinct retinal phenotypes within the same family.	Schiff Bases	28-39	rhodopsin	Homo sapiens	54-63
27842163-7	2016	Results: Plasma mRNA levels of retinoschisin were negatively associated with visual acuity, and plasma mRNA levels of rhodopsin were positively associated with visual acuity in patients with DME (P < 0.01 and P < 0.05, respectively).	dme	191-194	rhodopsin	Homo sapiens	118-127
27842163-9	2016	Conclusions: This prospective, multicenter study found that circulating mRNA levels of retinoschisin and rhodopsin are associated with visual acuity and changes in central subfield thickness during anti-VEGF therapy in patients with DME.	dme	233-236	rhodopsin	Homo sapiens	105-114
27723349-6	2016	As an illustrative application, powdered rhodopsin was prepared with and without the cofactor 11-cis-retinal to enable partial rehydration of the protein with D2O in a controlled manner.	Deuterium Oxide	159-162	rhodopsin	Homo sapiens	41-50
27548480-7	2016	This first report of melanopsin and rhodopsin contributions to the early phase PIPR is in line with the electrophysiological findings of ipRGC and rod signalling after the cessation of light stimuli and provides a cut-off time for isolating photoreceptor specific function in healthy and diseased eyes.	pipr	79-83	rhodopsin	Homo sapiens	36-45
27630250-4	2016	The ubiquity of marine rhodopsin photosystems now challenges prior understanding of the nature and contributions of "heterotrophic" bacteria to biogeochemical carbon cycling and energy fluxes.	Carbon	159-165	rhodopsin	Homo sapiens	23-32
27216754-9	2016	The high cholesterol found in the plasma membrane and in newly synthesized disks inhibits the activation of rhodopsin.	Cholesterol	9-20	rhodopsin	Homo sapiens	108-117
27216754-10	2016	As disks are apically displaced and cholesterol is depleted rhodopsin becomes more responsive to light.	Cholesterol	36-47	rhodopsin	Homo sapiens	60-69
27216754-11	2016	This effect of cholesterol on rhodopsin activation has been shown in both native and reconstituted membranes.	Cholesterol	15-26	rhodopsin	Homo sapiens	30-39
27216754-13	2016	Cholesterol decreases the partial free volume of the hydrocarbon region of the bilayer and thereby inhibits rhodopsin conformational changes required for activation.	Cholesterol	0-11	rhodopsin	Homo sapiens	108-117
27216754-13	2016	Cholesterol decreases the partial free volume of the hydrocarbon region of the bilayer and thereby inhibits rhodopsin conformational changes required for activation.	Hydrocarbons	53-64	rhodopsin	Homo sapiens	108-117
27216754-14	2016	However, cholesterol binds to rhodopsin and may directly affect the protein also.	Cholesterol	9-20	rhodopsin	Homo sapiens	30-39
27216754-15	2016	Furthermore, cholesterol stabilizes rhodopsin to thermal denaturation.	Cholesterol	13-24	rhodopsin	Homo sapiens	36-45
27216754-17	2016	Cholesterol thus plays a complex role in modulating the activity and stability of rhodopsin, which have implications for other G-protein coupled receptors.	Cholesterol	0-11	rhodopsin	Homo sapiens	82-91
27458239-5	2016	Our results indicate that both the charged G90D2.57 and the hydrophobic T94I2.61 mutation alter the dark state by weakening the interaction between the Schiff base (SB) and its counterion E1133.28 We propose that this interference with the tight regulation of the dim light photoreceptor rhodopsin increases background noise in the visual system and causes the loss of night vision characteristic for CSNB patients.	Schiff Bases	152-163	rhodopsin	Homo sapiens	288-297
27458239-5	2016	Our results indicate that both the charged G90D2.57 and the hydrophobic T94I2.61 mutation alter the dark state by weakening the interaction between the Schiff base (SB) and its counterion E1133.28 We propose that this interference with the tight regulation of the dim light photoreceptor rhodopsin increases background noise in the visual system and causes the loss of night vision characteristic for CSNB patients.	Schiff Bases	165-167	rhodopsin	Homo sapiens	288-297
26642989-1	2015	As a minimal model of the chromophore of rhodopsin proteins, the penta-2,4-dieniminium cation (PSB3) poses a challenging test system for the assessment of electronic-structure methods for the exploration of ground- and excited-state potential-energy surfaces, the topography of conical intersections, and the dimensionality (topology) of the branching space.	penta-2,4-dieniminium	65-86	rhodopsin	Homo sapiens	41-50
27068978-6	2016	Focus is put on the ENM-NMA-based strategy applied to the crystallographic structures of rhodopsin in its inactive (dark) and signalling active (meta II (MII)) states, highlighting changes in structure network and centrality of the retinal chromophore in differentiating the inactive and active states of the receptor.	nma	24-27	rhodopsin	Homo sapiens	89-98
27009873-3	2016	We site-specifically label a genetically-encoded azido group in the visual photoreceptor rhodopsin to demonstrate the utility of the strategy.	3',5-diazido-2',3'-dideoxyuridine	49-54	rhodopsin	Homo sapiens	89-98
26416182-9	2016	Treatment of cells with Wortmannin, an inhibitor of NMD, eliminated the degradation of Y136X, W161X, and E249X rhodopsin mRNAs.	Wortmannin	24-34	rhodopsin	Homo sapiens	111-120
26750104-2	2016	This novel approach allows controlled P-C bond formation using the bulky DmpLi (Dmp = 2,6-Mes2C6H3) and the unencumbered MesLi, giving sterically diverse doubly complexed RP4 butterfly derivatives in a single step.	dmpli	73-78	rhodopsin	Homo sapiens	171-174
26750104-2	2016	This novel approach allows controlled P-C bond formation using the bulky DmpLi (Dmp = 2,6-Mes2C6H3) and the unencumbered MesLi, giving sterically diverse doubly complexed RP4 butterfly derivatives in a single step.	Unithiol	73-76	rhodopsin	Homo sapiens	171-174
26750104-2	2016	This novel approach allows controlled P-C bond formation using the bulky DmpLi (Dmp = 2,6-Mes2C6H3) and the unencumbered MesLi, giving sterically diverse doubly complexed RP4 butterfly derivatives in a single step.	2,6-mes2c6h3	86-98	rhodopsin	Homo sapiens	171-174
26860474-9	2016	Global fit analysis yielded lifetimes and spectral features of bleaching intermediates, revealing remarkably altered kinetics: whereas the slowest process of wild-type rhodopsin and of bleached and 11-cis retinal assembled rhodopsin takes place with lifetimes of 7 and 3.8 s, respectively, this process for 10-methyl-13-demethyl retinal was nearly 10 h (34670 s), coming to completion only after ca.	10-methyl-13-demethyl retinal	307-336	rhodopsin	Homo sapiens	168-177
26860474-9	2016	Global fit analysis yielded lifetimes and spectral features of bleaching intermediates, revealing remarkably altered kinetics: whereas the slowest process of wild-type rhodopsin and of bleached and 11-cis retinal assembled rhodopsin takes place with lifetimes of 7 and 3.8 s, respectively, this process for 10-methyl-13-demethyl retinal was nearly 10 h (34670 s), coming to completion only after ca.	10-methyl-13-demethyl retinal	307-336	rhodopsin	Homo sapiens	223-232
26671371-2	2015	These data illustrate the ability of field enhanced photoemission (FEP) to determine V0(rho) accurately in strongly absorbing fluids (e.g., O2) and fluids with extremely low critical temperatures (e.g., H2 and D2).	Oxygen	140-142	rhodopsin	Homo sapiens	85-92
27185384-1	2016	Fusion of a palladium-binding peptide to an archaeal rhodopsin promotes intimate integration of the lipid-embedded membrane protein with a palladium hydride protonic contact.	palladium hydride	139-156	rhodopsin	Homo sapiens	53-62
27233115-3	2016	In particular, both aspartate residues that occupy the positions of the chromophore Schiff base proton acceptor and donor, a hallmark of rhodopsin proton pumps, are conserved in these cryptophyte proteins.	Aspartic Acid	20-29	rhodopsin	Homo sapiens	137-146
27233115-3	2016	In particular, both aspartate residues that occupy the positions of the chromophore Schiff base proton acceptor and donor, a hallmark of rhodopsin proton pumps, are conserved in these cryptophyte proteins.	Schiff Bases	84-95	rhodopsin	Homo sapiens	137-146
26803268-2	2016	In this study, the conjugative gene transfer of RP4 plasmid after disinfection including ultraviolet (UV) irradiation and low-level chlorine treatment was investigated.	Chlorine	132-140	rhodopsin	Homo sapiens	48-51
26803268-6	2016	The RP4 plasmid transfer frequency was not significantly affected by chlorine treatment at dosages ranging from 0.05 to 0.2 mg/l, but treatment with 0.3-0.5 mg/l chlorine induced a decrease in conjugative transfer to 4.40 x 10(-5) or below the detection limit.	Chlorine	162-170	rhodopsin	Homo sapiens	4-7
26343933-3	2016	The mGluR1 mutagenesis data, conserved amino acid sequences across class A and class C GPCRs, and previously reported multiple sequence alignments of class C GPCRs to the rhodopsin template, were employed for the sequence alignment to overcome difficulties of model generation with low sequence identity of mGluR1 and dopamine D3.	Dopamine	318-326	rhodopsin	Homo sapiens	171-180
26248892-5	2015	Using molecular dynamics simulations, we examined the behavior of rhodopsin in the Meta-II conformation (active) under Meta-I conditions (inactive), and discovered that the retinal binding pocket is flexible enough to allow a 180  rotation along the long axis of the retinal polyene chain.	Polyenes	275-282	rhodopsin	Homo sapiens	66-75
26654369-1	2015	A candidate gene approach has finally identified the 3,4-dehydrogenase that converts vitamin A1 into vitamin A2 to supply the chromophore for rhodopsin that freshwater vertebrates need for long-wavelength vision.	vitamin A2	101-111	rhodopsin	Homo sapiens	142-151
26526852-4	2015	Comparison of this extensive solvent-mediated hydrogen-bonding network with the positions of ordered solvent in earlier crystallographic structures of rhodopsin photointermediates reveals both static structural and dynamic functional water-protein interactions present during the activation process.	Hydrogen	46-54	rhodopsin	Homo sapiens	151-160
26526852-4	2015	Comparison of this extensive solvent-mediated hydrogen-bonding network with the positions of ordered solvent in earlier crystallographic structures of rhodopsin photointermediates reveals both static structural and dynamic functional water-protein interactions present during the activation process.	Water	234-239	rhodopsin	Homo sapiens	151-160
26526852-5	2015	When considered along with observations that solvent occupies similar positions in the structures of other GPCRs, these analyses strongly support an integral role for this dynamic ordered water network in both rhodopsin and GPCR activation.	Water	188-193	rhodopsin	Homo sapiens	210-219
26179029-0	2015	Phospholipid scrambling by rhodopsin.	Phospholipids	0-12	rhodopsin	Homo sapiens	27-36
26179029-2	2015	We recently discovered that it also functions as an ATP-independent phospholipid scramblase: when reconstituted into large unilamellar vesicles, rhodopsin accelerates the normally sluggish transbilayer translocation of common phospholipids by more than 1000-fold, to rates in excess of 10 000 phospholipids transported per rhodopsin per second.	Adenosine Triphosphate	52-55	rhodopsin	Homo sapiens	145-154
26179029-2	2015	We recently discovered that it also functions as an ATP-independent phospholipid scramblase: when reconstituted into large unilamellar vesicles, rhodopsin accelerates the normally sluggish transbilayer translocation of common phospholipids by more than 1000-fold, to rates in excess of 10 000 phospholipids transported per rhodopsin per second.	Phospholipids	226-239	rhodopsin	Homo sapiens	145-154
26179029-2	2015	We recently discovered that it also functions as an ATP-independent phospholipid scramblase: when reconstituted into large unilamellar vesicles, rhodopsin accelerates the normally sluggish transbilayer translocation of common phospholipids by more than 1000-fold, to rates in excess of 10 000 phospholipids transported per rhodopsin per second.	Phospholipids	293-306	rhodopsin	Homo sapiens	145-154
26179029-3	2015	Here we summarize the work leading to this discovery and speculate on the mechanism by which rhodopsin scrambles phospholipids.	Phospholipids	113-126	rhodopsin	Homo sapiens	93-102
26179029-4	2015	We also present a hypothesis that rhodopsin"s scramblase activity is necessary for the function of the ABC transporter ABCA4 that is responsible for mitigating the toxic accumulation of 11-cis-retinal and bis-retinoids in the retina.	Retinaldehyde	186-200	rhodopsin	Homo sapiens	34-43
26179029-4	2015	We also present a hypothesis that rhodopsin"s scramblase activity is necessary for the function of the ABC transporter ABCA4 that is responsible for mitigating the toxic accumulation of 11-cis-retinal and bis-retinoids in the retina.	bis-retinoids	205-218	rhodopsin	Homo sapiens	34-43
26375013-1	2015	Invertebrate visual opsins are G protein-coupled receptors coupled to retinoid chromophores that isomerize reversibly between inactive rhodopsin and active metarhodopsin upon absorption of photons of light.	Retinoids	70-78	rhodopsin	Homo sapiens	135-144
26590321-5	2015	Indeed, we demonstrated that guanylate cyclase-1, producing the cGMP second messenger in photoreceptors, requires rhodopsin for intracellular stability and outer segment delivery.	Cyclic GMP	64-68	rhodopsin	Homo sapiens	114-123
26257274-0	2015	The role of the non-covalent beta-ionone-ring binding site in rhodopsin: historical and physiological perspective.	beta-ionone	29-40	rhodopsin	Homo sapiens	62-71
26257274-1	2015	Bleached rhodopsin regenerates by way of the Schiff base formation between the 11-cis retinal and opsin.	Schiff Bases	45-56	rhodopsin	Homo sapiens	9-18
26257274-2	2015	Recovery of human vision from light adapted states follows biphasic kinetics and each adaptive phase is assigned to two distinct classes of visual pigments in cones and rods, respectively, suggesting that the speed of Schiff base formation differs between iodopsin and rhodopsin.	Schiff Bases	218-229	rhodopsin	Homo sapiens	269-278
26257274-3	2015	Matsumoto and Yoshizawa predicted the existence of a beta-ionone ring-binding site in rhodopsin, which has been proven by structural studies.	beta-ionone	53-64	rhodopsin	Homo sapiens	86-95
26257274-4	2015	They postulated that rhodopsin regeneration starts with a non-covalent binding of the beta-ionone ring moiety of 11-cis-retinal, followed by the Schiff base formation.	beta-ionone	86-97	rhodopsin	Homo sapiens	21-30
26257274-4	2015	They postulated that rhodopsin regeneration starts with a non-covalent binding of the beta-ionone ring moiety of 11-cis-retinal, followed by the Schiff base formation.	Schiff Bases	145-156	rhodopsin	Homo sapiens	21-30
26248892-9	2015	These findings are significant in developing our understanding of the retinoid cycle and how ligand-receptor interactions in rhodopsin relate to G protein-coupled receptor activation.	Retinoids	70-78	rhodopsin	Homo sapiens	125-134
26257274-6	2015	In order to understand the role of non-covalent binding of 11-cis-retinal to opsin during regeneration, we studied the kinetics of rhodopsin regeneration from opsin and 11-cis-retinal and found that the Schiff base formation is accelerated ~10(7) times compared to that between retinal and free amine.	Schiff Bases	203-214	rhodopsin	Homo sapiens	131-140
26257274-6	2015	In order to understand the role of non-covalent binding of 11-cis-retinal to opsin during regeneration, we studied the kinetics of rhodopsin regeneration from opsin and 11-cis-retinal and found that the Schiff base formation is accelerated ~10(7) times compared to that between retinal and free amine.	Amines	295-300	rhodopsin	Homo sapiens	131-140
26181234-0	2015	Phospholipid Bicelles Improve the Conformational Stability of Rhodopsin Mutants Associated with Retinitis Pigmentosa.	Phospholipids	0-12	rhodopsin	Homo sapiens	62-71
26488656-5	2015	Conservation of the arginine component of the ionic lock among Rhodopsin-like G-protein-coupled receptors suggests that intracellular lipid ingression between receptor helices H6 and H7 may be a general mechanism for active-state stabilization.	Arginine	20-28	rhodopsin	Homo sapiens	63-72
26365012-1	2015	Anabaena Sensory Rhodopsin (ASR) stands out among the microbial retinal proteins in that, under light-adaptation (LA) conditions, it binds both the 13-cis isomer and the all-trans isomer of the protonated Schiff base of retinal (PSBR).	Schiff Bases	205-216	rhodopsin	Homo sapiens	17-26
26365012-5	2015	Even though this recalls the record isomerization time and the coherent reaction scenario of 11-cis PSBR in rhodopsin, the photoisomerization quantum yield (QY) is much lower, actually the lowest value ever reported for retinal proteins (<15%).	11-cis psbr	93-104	rhodopsin	Homo sapiens	108-117
26412387-3	2015	Here we show that a chimeric rhodopsin/beta2 adrenergic receptor (opto-beta2AR) is similar in dynamics to endogenous beta2AR in terms of: cAMP generation, MAP kinase activation and receptor internalization.	Cyclic AMP	138-142	rhodopsin	Homo sapiens	29-38
26258638-2	2015	We generated these maps by measuring the effects of alanine mutations on the stability of Galphai1 and the rhodopsin-Galphai1 complex.	Alanine	52-59	rhodopsin	Homo sapiens	107-116
26510463-1	2015	Binding mechanism of arrestin requires photoactivation and phosphorylation of the receptor protein rhodopsin, where the receptor bound phosphate groups cause displacement of the long C-tail "activating" arrestin.	Phosphates	135-144	rhodopsin	Homo sapiens	99-108
26472483-2	2015	Comparison of the recently solved high-resolution structures of the sodium-translocating bacterial rhodopsin and various Na(+)-binding GPCRs revealed striking similarity of their sodium-binding sites.	Sodium	68-74	rhodopsin	Homo sapiens	99-108
26181234-6	2015	We find that DMPC/DHPC bicelles dramatically increase the thermal stability of the rhodopsin mutants G90V and N55K.	Dimyristoylphosphatidylcholine	13-17	rhodopsin	Homo sapiens	83-92
26181234-6	2015	We find that DMPC/DHPC bicelles dramatically increase the thermal stability of the rhodopsin mutants G90V and N55K.	1,2-dihexadecyl-sn-glycero-3-phosphocholine	18-22	rhodopsin	Homo sapiens	83-92
25781680-6	2015	Over 95% of contaminating membrane protein and his-tagged MSP could be removed from the rhodopsin-nanodiscs using a single Ni2+-affinity chromatography step.	Nickel(2+)	123-127	rhodopsin	Homo sapiens	88-97
25781680-3	2015	This is exemplified with recombinant his-tagged rhodopsin, which is rapidly extracted from its host membrane and directly assembled into membrane scaffold protein (MSP) nanodiscs.	Histidine	1-4	rhodopsin	Homo sapiens	48-57
25910054-0	2015	C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor.	Threonine	11-21	rhodopsin	Homo sapiens	80-89
25910054-0	2015	C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor.	Serine	26-33	rhodopsin	Homo sapiens	80-89
25910054-3	2015	Rhodopsin phosphorylation has been measured biochemically at C-terminal serine residues, suggesting that these residues are critical for producing fast, low-noise responses.	Serine	72-78	rhodopsin	Homo sapiens	0-9
25910054-6	2015	Contrary to expectation, serine-only rhodopsin generated prolonged step-like single-photon responses that terminated abruptly and randomly, whereas threonine-only rhodopsin generated responses that were only modestly slower than normal.	Serine	25-31	rhodopsin	Homo sapiens	37-46
25910054-7	2015	We show that the step-like responses of serine-only rhodopsin reflect slow and stochastic arrestin binding.	Serine	40-46	rhodopsin	Homo sapiens	52-61
25910054-8	2015	Thus, threonine sites play a privileged role in promoting timely arrestin binding and rhodopsin desensitization.	Threonine	6-15	rhodopsin	Homo sapiens	86-95
25821414-1	2015	The penta-2,4-dieniminium cation (PSB3) displays similar ground state and first excited state potential energy features as those of the retinal protonated Schiff base (RPSB) chromophore in rhodopsin.	penta-2,4-dieniminium	4-25	rhodopsin	Homo sapiens	189-198
25769401-0	2015	The kinetics of regeneration of rhodopsin under enzyme-limited availability of 11-cis retinoid.	11-cis retinoid	79-94	rhodopsin	Homo sapiens	32-41
26579769-0	2015	Opsin Effect on the Electronic Structure of the Retinylidene Chromophore in Rhodopsin.	retinylidene	48-60	rhodopsin	Homo sapiens	76-85
25821414-1	2015	The penta-2,4-dieniminium cation (PSB3) displays similar ground state and first excited state potential energy features as those of the retinal protonated Schiff base (RPSB) chromophore in rhodopsin.	Schiff Bases	155-166	rhodopsin	Homo sapiens	189-198
26579769-1	2015	Direct examination of experimental NMR parameters combined with electronic structure analysis was used to provide a first-principle interpretation of NMR experiments and give a precise evaluation of how the electronic perturbation of the protein environment affects the electronic properties of the retinylidene chromophere in rhodopsin.	retinylidene	299-311	rhodopsin	Homo sapiens	327-336
25614992-2	2015	Following its activation by light, rhodopsin activates the G-protein transducin causing the dissociation of its GTP-bound alpha-subunit, which in turn activates phosphodiesterase 6 (PDE6) leading to the hyperpolarization of photoreceptor cells.	Guanosine Triphosphate	112-115	rhodopsin	Homo sapiens	35-44
25734540-6	2015	Identifying a rhodopsin gene fragment in Erythropsidinium ESTs that is expressed in the retinal body by in situ hybridization, we also show that ocelloids are actually light sensitive photoreceptors.	erythropsidinium	41-57	rhodopsin	Homo sapiens	14-23
25144664-0	2015	Efficient femtosecond energy transfer from carotenoid to retinal in gloeobacter rhodopsin-salinixanthin complex.	Carotenoids	43-53	rhodopsin	Homo sapiens	80-89
25144664-0	2015	Efficient femtosecond energy transfer from carotenoid to retinal in gloeobacter rhodopsin-salinixanthin complex.	salinixanthin	90-103	rhodopsin	Homo sapiens	80-89
26055054-2	2015	Because the OSs are incapable of protein synthesis, rhodopsin must first be synthesized in the inner segments (ISs) and subsequently trafficked across the connecting cilia to the OSs where it participates in the phototransduction cascade.	OSS	12-15	rhodopsin	Homo sapiens	52-61
25326165-3	2015	Carotenoids are the precursors for the visual pigment rhodopsin, and lutein and zeaxanthin must be accumulated in the yellow eye spot to protect the retina from excess light and ultraviolet damage.	Carotenoids	0-11	rhodopsin	Homo sapiens	54-63
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	8-azidoguanosine triphosphate	46-75	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	8-azidoguanosine triphosphate	77-84	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	8-azidoguanosine triphosphate	198-205	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	talpha	229-235	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	8-azidoguanosine triphosphate	198-205	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	tbeta	275-280	rhodopsin	Homo sapiens	35-44
25450251-2	2015	In the presence of light-activated rhodopsin, 8-azidoguanosine triphosphate (8-N3GTP) was covalently incorporated into T in a UV-light photodependent manner, with a low stoichiometry of 0.02 mol of 8-N3GTP per mol of T. Although Talpha was preferentially labeled by 8-N3GTP, Tbeta and Tgamma were also modified.	tgamma	285-291	rhodopsin	Homo sapiens	35-44
25450251-4	2015	This was consistent with the observation that the photoaffinity probe was completely hydrolyzed to 8-N3GDP by T activated by illuminated rhodopsin.	8-azidoguanosine-3',5'-diphosphate	99-106	rhodopsin	Homo sapiens	137-146
25697516-2	2015	This imaging method has proven especially useful for rhodopsin, because of the dependence of rhodopsin"s fluorescence spectra on the isomerization state of its intrinsic chromophore (retinylidene) and, as such, it can provide additional information about the identity and functional state of rhodopsin in crystals.	retinylidene	183-195	rhodopsin	Homo sapiens	53-62
25697516-2	2015	This imaging method has proven especially useful for rhodopsin, because of the dependence of rhodopsin"s fluorescence spectra on the isomerization state of its intrinsic chromophore (retinylidene) and, as such, it can provide additional information about the identity and functional state of rhodopsin in crystals.	retinylidene	183-195	rhodopsin	Homo sapiens	93-102
25697516-2	2015	This imaging method has proven especially useful for rhodopsin, because of the dependence of rhodopsin"s fluorescence spectra on the isomerization state of its intrinsic chromophore (retinylidene) and, as such, it can provide additional information about the identity and functional state of rhodopsin in crystals.	retinylidene	183-195	rhodopsin	Homo sapiens	93-102
25697517-3	2015	Like all transmembrane proteins, rhodopsin is embedded within a phospholipid bilayer.	Phospholipids	64-76	rhodopsin	Homo sapiens	33-42
25697519-0	2015	Detection of structural waters and their role in structural dynamics of rhodopsin activation.	Water	24-30	rhodopsin	Homo sapiens	72-81
25697519-2	2015	Radiolysis-based hydroxyl radical footprinting (HRF) strategies coupled to mass spectrometry have been used to explore the structural waters within rhodopsin in multiple signaling states.	Hydroxyl Radical	17-33	rhodopsin	Homo sapiens	148-157
25697519-2	2015	Radiolysis-based hydroxyl radical footprinting (HRF) strategies coupled to mass spectrometry have been used to explore the structural waters within rhodopsin in multiple signaling states.	Water	134-140	rhodopsin	Homo sapiens	148-157
25697520-0	2015	Probing conformational changes in rhodopsin using hydrogen-deuterium exchange coupled to mass spectrometry.	Hydrogen	50-58	rhodopsin	Homo sapiens	34-43
25697520-0	2015	Probing conformational changes in rhodopsin using hydrogen-deuterium exchange coupled to mass spectrometry.	Deuterium	59-68	rhodopsin	Homo sapiens	34-43
25697521-0	2015	Analysis of conformational changes in rhodopsin by histidine hydrogen-deuterium exchange.	Histidine	51-60	rhodopsin	Homo sapiens	38-47
25697521-0	2015	Analysis of conformational changes in rhodopsin by histidine hydrogen-deuterium exchange.	Hydrogen	61-69	rhodopsin	Homo sapiens	38-47
25697521-0	2015	Analysis of conformational changes in rhodopsin by histidine hydrogen-deuterium exchange.	Deuterium	70-79	rhodopsin	Homo sapiens	38-47
25697521-5	2015	Herein we describe an experimental protocol to characterize rhodopsin by His-HDX-MS.	Histidine	73-76	rhodopsin	Homo sapiens	60-69
25697522-0	2015	Investigation of rhodopsin dynamics in its signaling state by solid-state deuterium NMR spectroscopy.	Deuterium	74-83	rhodopsin	Homo sapiens	17-26
25697523-3	2015	We first outline the methods for large-scale production of stable, functional rhodopsin containing (13)C- and (15)N-labeled amino acids.	Carbon	103-104	rhodopsin	Homo sapiens	78-87
25697523-3	2015	We first outline the methods for large-scale production of stable, functional rhodopsin containing (13)C- and (15)N-labeled amino acids.	Nitrogen	114-115	rhodopsin	Homo sapiens	78-87
25250790-2	2014	Subsequent alkylation of the nucleophilic site of the RP4 anion gives access to non-symmetrical disubstituted bicyclic tetraphosphorus compounds.	bicyclic tetraphosphorus	110-134	rhodopsin	Homo sapiens	54-57
25530840-0	2014	Chemical chaperone 4-phenylbutyrate prevents endoplasmic reticulum stress induced by T17M rhodopsin.	4-phenylbutyric acid	19-35	rhodopsin	Homo sapiens	90-99
25530840-3	2014	This study aimed to examine whether chemical chaperone 4-phenylbutyrate prevents ER stress induced by rhodopsin T17M.	4-phenylbutyric acid	55-71	rhodopsin	Homo sapiens	102-111
25530840-5	2014	Turnover of WT and T17M rhodopsin was measured by cycloheximide chase analysis.	Cycloheximide	50-63	rhodopsin	Homo sapiens	24-33
25530840-9	2014	Moreover, chemical chaperone 4-phenylbutyrate facilitated the turnover of T17M rhodopsin and prevented apoptosis and ER stress induced by T17M rhodopsin.	4-phenylbutyric acid	29-45	rhodopsin	Homo sapiens	79-88
25530840-9	2014	Moreover, chemical chaperone 4-phenylbutyrate facilitated the turnover of T17M rhodopsin and prevented apoptosis and ER stress induced by T17M rhodopsin.	4-phenylbutyric acid	29-45	rhodopsin	Homo sapiens	143-152
25268658-3	2014	One-dimensional 1H NMR spectra confirm a progressive increase in flexibility of resonances in rhodopsin with increasing denaturant concentrations.	Hydrogen	16-18	rhodopsin	Homo sapiens	94-103
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	Hydrogen	16-18	rhodopsin	Homo sapiens	66-75
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	15n	19-22	rhodopsin	Homo sapiens	66-75
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	Lysine	45-57	rhodopsin	Homo sapiens	66-75
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	Lysine	45-57	rhodopsin	Homo sapiens	200-209
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	15n	40-43	rhodopsin	Homo sapiens	66-75
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	15n	40-43	rhodopsin	Homo sapiens	200-209
25268658-4	2014	Two-dimensional 1H-15N HSQC spectra of [15N]-alpha-lysine-labeled rhodopsin in which signals arise primarily from residues in the cytoplasmic (CP) domain and of [15N]-alpha,epsilon-tryptophan-labeled rhodopsin in which signals arise only from transmembrane (TM) and extracellular (EC) residues indicate qualitatively that EC and CP domains may be differentially affected by denaturation.	epsilon-tryptophan	173-191	rhodopsin	Homo sapiens	66-75
25255466-0	2014	Initial excited-state dynamics of an N-alkylated indanylidene-pyrroline (NAIP) rhodopsin analog.	Nitrogen	37-38	rhodopsin	Homo sapiens	79-88
25381497-4	2014	Specifically, we show that experimental data for dye molecules in several solvents, amino acid proteins in water, and some photochemical systems (e.g., rhodopsin and green fluorescence proteins), are well described by a three-parameter family of sub-Ohmic spectral densities that are characterized by a fast initial Gaussian-like decay followed by a slow algebraic-like decay rate at long times.	Water	107-112	rhodopsin	Homo sapiens	152-161
25316345-2	2014	Introducing the N-oxides into the azacubanes could improve their detonation performance significantly due to the increase of the OB and rho but would also increase the sensitivity to some extent.	n-oxides	16-24	rhodopsin	Homo sapiens	129-139
25316345-2	2014	Introducing the N-oxides into the azacubanes could improve their detonation performance significantly due to the increase of the OB and rho but would also increase the sensitivity to some extent.	azacubanes	34-44	rhodopsin	Homo sapiens	129-139
25255466-0	2014	Initial excited-state dynamics of an N-alkylated indanylidene-pyrroline (NAIP) rhodopsin analog.	alkylated indanylidene-pyrroline	39-71	rhodopsin	Homo sapiens	79-88
25255466-0	2014	Initial excited-state dynamics of an N-alkylated indanylidene-pyrroline (NAIP) rhodopsin analog.	naip	73-77	rhodopsin	Homo sapiens	79-88
25255466-1	2014	N-Alkylated indanylidene-pyrroline-based molecular switches mimic different aspects of the light-induced retinal chromophore isomerization in rhodopsin: the vertebrate dim-light visual pigment.	n-alkylated indanylidene-pyrroline	0-34	rhodopsin	Homo sapiens	142-151
25296113-1	2014	Opsin, the rhodopsin apoprotein, was recently shown to be an ATP-independent flippase (or scramblase) that equilibrates phospholipids across photoreceptor disc membranes in mammalian retina, a process required for disc homoeostasis.	Adenosine Triphosphate	61-64	rhodopsin	Homo sapiens	11-20
25338686-7	2014	Rhodopsin, which is activated by photoisomerization of its 11-cis-retinylidene chromophore, is a prototypical member of a large family of membrane-bound proteins called G protein-coupled receptors (GPCRs).	11-cis-retinylidene	59-78	rhodopsin	Homo sapiens	0-9
25296113-1	2014	Opsin, the rhodopsin apoprotein, was recently shown to be an ATP-independent flippase (or scramblase) that equilibrates phospholipids across photoreceptor disc membranes in mammalian retina, a process required for disc homoeostasis.	Phospholipids	120-133	rhodopsin	Homo sapiens	11-20
25296113-3	2014	Upon reconstitution into vesicles, discrete conformational states of the protein (rhodopsin, a metarhodopsin II-mimic, and two forms of opsin) facilitated rapid (>10,000 phospholipids per protein per second) scrambling of phospholipid probes.	Phospholipids	173-186	rhodopsin	Homo sapiens	82-91
25296113-3	2014	Upon reconstitution into vesicles, discrete conformational states of the protein (rhodopsin, a metarhodopsin II-mimic, and two forms of opsin) facilitated rapid (>10,000 phospholipids per protein per second) scrambling of phospholipid probes.	Phospholipids	173-185	rhodopsin	Homo sapiens	82-91
25045132-5	2014	In contrast, the strain-promoted [3+2] azide-alkyne cycloaddition (SpAAC) with dibenzocyclooctyne (DIBO) reagents yielded stoichiometric conjugates with azF-rhodopsin while undergoing negligible background reactions.	[3+2] azide-alkyne	33-51	rhodopsin	Homo sapiens	157-166
25166739-0	2014	Functional water molecules in rhodopsin activation.	Water	11-16	rhodopsin	Homo sapiens	30-39
25166739-2	2014	Studies of rhodopsin, a prototype GPCR, have suggested that water plays an important role in mediating the activation of family A GPCRs.	Water	60-65	rhodopsin	Homo sapiens	11-20
25166739-4	2014	Using all-atom molecular dynamics simulations in combination with inhomogeneous fluid theory, we identify in this work the positioning of functional water molecules in the inactive state, the Meta II state, and the constitutive active state of rhodopsin, basing on the thermodynamic signatures of the water molecules.	Water	149-154	rhodopsin	Homo sapiens	244-253
25166739-4	2014	Using all-atom molecular dynamics simulations in combination with inhomogeneous fluid theory, we identify in this work the positioning of functional water molecules in the inactive state, the Meta II state, and the constitutive active state of rhodopsin, basing on the thermodynamic signatures of the water molecules.	Water	301-306	rhodopsin	Homo sapiens	244-253
25166739-5	2014	We find that one hydration site likely functions as a switch to regulate the distance between Glu181 and the Schiff base in the rhodopsin activation.	Schiff Bases	109-120	rhodopsin	Homo sapiens	128-137
25166739-7	2014	We thereby propose a hypothesis of the water-mediated rhodopsin activation pathway.	Water	39-44	rhodopsin	Homo sapiens	54-63
25045132-5	2014	In contrast, the strain-promoted [3+2] azide-alkyne cycloaddition (SpAAC) with dibenzocyclooctyne (DIBO) reagents yielded stoichiometric conjugates with azF-rhodopsin while undergoing negligible background reactions.	spaac	67-72	rhodopsin	Homo sapiens	157-166
25045132-5	2014	In contrast, the strain-promoted [3+2] azide-alkyne cycloaddition (SpAAC) with dibenzocyclooctyne (DIBO) reagents yielded stoichiometric conjugates with azF-rhodopsin while undergoing negligible background reactions.	dibenzocyclooctyne	79-97	rhodopsin	Homo sapiens	157-166
25045132-5	2014	In contrast, the strain-promoted [3+2] azide-alkyne cycloaddition (SpAAC) with dibenzocyclooctyne (DIBO) reagents yielded stoichiometric conjugates with azF-rhodopsin while undergoing negligible background reactions.	dibo	99-103	rhodopsin	Homo sapiens	157-166
24694997-4	2014	The performed calculations revealed that the nu(NH2) stretching, rho(NH2) rocking and tau(CH3) torsional modes are very sensitive to formation of the hydrogen bond between the DMA(+) cation and Ni-formate framework.	Hydrogen	150-158	rhodopsin	Homo sapiens	65-72
24694997-4	2014	The performed calculations revealed that the nu(NH2) stretching, rho(NH2) rocking and tau(CH3) torsional modes are very sensitive to formation of the hydrogen bond between the DMA(+) cation and Ni-formate framework.	N-myristoyl-alaninol	176-179	rhodopsin	Homo sapiens	65-72
24694997-4	2014	The performed calculations revealed that the nu(NH2) stretching, rho(NH2) rocking and tau(CH3) torsional modes are very sensitive to formation of the hydrogen bond between the DMA(+) cation and Ni-formate framework.	ni-formate	194-204	rhodopsin	Homo sapiens	65-72
24692562-0	2014	Intramolecular interactions that induce helical rearrangement upon rhodopsin activation: light-induced structural changes in metarhodopsin IIa probed by cysteine S-H stretching vibrations.	Cysteine	153-161	rhodopsin	Homo sapiens	67-76
24724832-6	2014	We mapped these sites using a novel tryptophan-induced quenching method, in which we introduced Trp residues into arrestin and measured their ability to quench the fluorescence of bimane probes attached to cysteine residues on TM6 of rhodopsin (T242C and T243C).	Tryptophan	36-46	rhodopsin	Homo sapiens	234-243
24724832-6	2014	We mapped these sites using a novel tryptophan-induced quenching method, in which we introduced Trp residues into arrestin and measured their ability to quench the fluorescence of bimane probes attached to cysteine residues on TM6 of rhodopsin (T242C and T243C).	Tryptophan	96-99	rhodopsin	Homo sapiens	234-243
24724832-6	2014	We mapped these sites using a novel tryptophan-induced quenching method, in which we introduced Trp residues into arrestin and measured their ability to quench the fluorescence of bimane probes attached to cysteine residues on TM6 of rhodopsin (T242C and T243C).	Cysteine	206-214	rhodopsin	Homo sapiens	234-243
24960425-0	2014	Contribution of glutamic acid in the conserved E/DRY triad to the functional properties of rhodopsin.	Glutamic Acid	16-29	rhodopsin	Homo sapiens	91-100
24960425-1	2014	Rhodopsin is a G protein-coupled receptor specialized for photoreception and contains a light-absorbing chromophore retinal that binds to the lysine residue of opsin through a protonated Schiff base linkage.	Lysine	142-148	rhodopsin	Homo sapiens	0-9
24960425-1	2014	Rhodopsin is a G protein-coupled receptor specialized for photoreception and contains a light-absorbing chromophore retinal that binds to the lysine residue of opsin through a protonated Schiff base linkage.	Schiff Bases	187-198	rhodopsin	Homo sapiens	0-9
24960425-2	2014	Light converts rhodopsin to an equilibrium mixture of the active state metarhodopsin II (MII) and its precursor, metarhodopsin I (MI), which have deprotonated and protonated Schiff base chromophores, respectively.	Schiff Bases	174-185	rhodopsin	Homo sapiens	15-24
25279248-1	2014	Aspects of our discovery of lateral diffusion of the G protein coupled receptor (GPCR) rhodopsin and that a single activated rhodopsin can non-covalently catalyze GTP binding to thousands of GTPases per second on rod disk membranes via this diffusion are summarized herein.	Guanosine Triphosphate	163-166	rhodopsin	Homo sapiens	125-134
24613493-2	2014	Indeed, it is responsible for the esterification of all-trans retinol into all-trans retinyl esters, which can then be stored in microsomes or further metabolized to produce the chromophore of rhodopsin.	Vitamin A	52-69	rhodopsin	Homo sapiens	193-202
24613493-2	2014	Indeed, it is responsible for the esterification of all-trans retinol into all-trans retinyl esters, which can then be stored in microsomes or further metabolized to produce the chromophore of rhodopsin.	trans retinyl esters	79-99	rhodopsin	Homo sapiens	193-202
24692562-2	2014	To investigate the mechanism by which rhodopsin adopts the transducin-activating conformation, the local environmental changes in the transmembrane region were probed using the cysteine S-H group, whose stretching frequency is well isolated from the other protein vibrational modes.	Cysteine	177-185	rhodopsin	Homo sapiens	38-47
24723847-2	2014	Photoexcited rhodopsin initiates a biochemical cascade that leads to a drop in the intracellular level of cyclic GMP and closure of cyclic nucleotide gated ion channels.	Nucleotides, Cyclic	132-149	rhodopsin	Homo sapiens	13-22
24505031-3	2014	Milligram quantities of alpha,epsilon-(15)N-labeled tryptophan rhodopsin were produced in stably transfected HEK293 cells.	alpha,epsilon-(15)n	24-43	rhodopsin	Homo sapiens	63-72
24512648-1	2014	A combined strategy based on the computation of absorption energies, using the ZINDO/S semiempirical method, for a statistically relevant number of thermally sampled configurations extracted from QM/MM trajectories is used to establish a one-to-one correspondence between the structures of the different early intermediates (dark, batho, BSI, lumi) involved in the initial steps of the rhodopsin photoactivation mechanism and their optical spectra.	Sulfur	85-86	rhodopsin	Homo sapiens	386-395
24505031-3	2014	Milligram quantities of alpha,epsilon-(15)N-labeled tryptophan rhodopsin were produced in stably transfected HEK293 cells.	Tryptophan	52-62	rhodopsin	Homo sapiens	63-72
24449856-6	2014	Interaction of phosphates in the rhodopsin C terminus with Arg29 controls a C-tail exchange mechanism in which the C tail of arrestin is released and exposes several charged amino acids (Lys14, Lys15, Arg18, Lys20, Lys110, and Lys300) for binding of the phosphorylated receptor C terminus.	Phosphates	15-25	rhodopsin	Homo sapiens	33-42
24559994-3	2014	Here, we monitored conformational changes of rhodopsin using a fluorescent probe Alexa594 at the cytoplasmic surface, which shows fluorescence increase upon the generation of active state, by single-molecule measurements.	Alexa594	81-89	rhodopsin	Homo sapiens	45-54
24158802-0	2014	Coarse-grained molecular dynamics provides insight into the interactions of lipids and cholesterol with rhodopsin.	Cholesterol	87-98	rhodopsin	Homo sapiens	104-113
27493492-4	2014	We validated the sensitivity of this method using bathorhodopsin, a photoproduct of rhodopsin trapped at liquid nitrogen temperature, which undergoes little conformational changes from the dark state as shown by the X-ray crystallography.	Nitrogen	112-120	rhodopsin	Homo sapiens	55-64
27493492-5	2014	The cysteine residues were individually introduced into 15 positions of Helix III, which contains several key amino acid residues for the light-induced conformational changes of rhodopsin.	Cysteine	4-12	rhodopsin	Homo sapiens	178-187
24328127-10	2014	We show here that the purified complex in Nanodiscs contains an activated rhodopsin with a covalently bound all-trans-retinal chromophore, that transducin has an empty nucleotide-binding pocket, that the isolated complex is active and dissociates upon addition of guanine nucleotide, and that the stoichiometry corresponds to exactly one molecule of rhodopsin and one molecule of transducin.	Guanine Nucleotides	264-282	rhodopsin	Homo sapiens	74-83
24158802-3	2014	It has been well documented that lipid headgroups, polyunsaturated tails, and the concentration of cholesterol in membranes all play a role in the function of rhodopsin.	Cholesterol	99-110	rhodopsin	Homo sapiens	159-168
24158802-6	2014	Accordingly, we present here 32 independent 1.6 mus coarse-grained simulations exploring lipids and cholesterols surrounding rhodopsin and opsin, in lipid bilayers mimicking those found naturally.	Cholesterol	100-112	rhodopsin	Homo sapiens	125-134
24189072-1	2013	Recoverin, a 23-kDa Ca(2+)-binding protein of the neuronal calcium sensing (NCS) family, inhibits rhodopsin kinase, a Ser/Thr kinase responsible for termination of photoactivated rhodopsin in rod photoreceptor cells.	Calcium	59-66	rhodopsin	Homo sapiens	98-107
24077848-3	2014	Both rhodopsin families share the seven transmembrane alpha-helix GPCR fold and a Schiff base linkage from a conserved lysine to retinal in helix G. Nevertheless, rhodopsins are widely cited as a striking example of evolutionary convergence, largely because the two families lack detectable sequence similarity and differ in many structural and mechanistic details.	Schiff Bases	82-93	rhodopsin	Homo sapiens	5-14
24077848-3	2014	Both rhodopsin families share the seven transmembrane alpha-helix GPCR fold and a Schiff base linkage from a conserved lysine to retinal in helix G. Nevertheless, rhodopsins are widely cited as a striking example of evolutionary convergence, largely because the two families lack detectable sequence similarity and differ in many structural and mechanistic details.	Lysine	119-125	rhodopsin	Homo sapiens	5-14
25621306-1	2014	Three active-site components in rhodopsin play a key role in the stability and function of the protein: 1) the counter-ion residues which stabilize the protonated Schiff base, 2) water molecules, and 3) the hydrogen-bonding network.	Schiff Bases	163-174	rhodopsin	Homo sapiens	32-41
25621306-1	2014	Three active-site components in rhodopsin play a key role in the stability and function of the protein: 1) the counter-ion residues which stabilize the protonated Schiff base, 2) water molecules, and 3) the hydrogen-bonding network.	Water	179-184	rhodopsin	Homo sapiens	32-41
25621306-1	2014	Three active-site components in rhodopsin play a key role in the stability and function of the protein: 1) the counter-ion residues which stabilize the protonated Schiff base, 2) water molecules, and 3) the hydrogen-bonding network.	Hydrogen	207-215	rhodopsin	Homo sapiens	32-41
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Glutamic Acid	22-25	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Hydrogen	64-72	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Serine	94-97	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Tyrosine	103-106	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Tyrosine	112-115	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Water	129-134	rhodopsin	Homo sapiens	171-180
25621306-2	2014	The ionizable residue Glu-181, which is involved in an extended hydrogen-bonding network with Ser-186, Tyr-268, Tyr-192, and key water molecules within the active site of rhodopsin, has been shown to be involved in a complex counter-ion switch mechanism with Glu-113 during the photobleaching sequence of the protein.	Glutamic Acid	259-262	rhodopsin	Homo sapiens	171-180
25621306-3	2014	Herein, we examine the photobleaching sequence of the E181Q rhodopsin mutant by using cryogenic UV-visible spectroscopy to further elucidate the role of Glu-181 during photoactivation of the protein.	Glutamic Acid	153-156	rhodopsin	Homo sapiens	60-69
25621306-8	2014	We conclude that the substitution of Glu-181 with Gln-181 results in a significant perturbation of the hydrogen-bonding network within the active site of rhodopsin.	Hydrogen	103-111	rhodopsin	Homo sapiens	154-163
25621306-10	2014	The observed destabilization upon this substitution further supports that Glu-181 is negatively charged in the early intermediates of the photobleaching sequence of rhodopsin.	Glutamic Acid	74-77	rhodopsin	Homo sapiens	165-174
23942379-8	2013	Interestingly, the abundance of the RP4 plasmid in total DNA remained at high levels and relatively stable at 104 copies/mg of biosolids, suggesting that ARGs were transferred from donor strains to activated sludge bacteria in our study.	args	154-158	rhodopsin	Homo sapiens	36-39
24106275-4	2013	As a complementary approach, we superimposed this panel of ADRP mutants onto a rhodopsin background containing a juxtaposed cysteine pair (N2C/D282C) that forms a disulfide bond.	Cysteine	124-132	rhodopsin	Homo sapiens	79-88
24106275-4	2013	As a complementary approach, we superimposed this panel of ADRP mutants onto a rhodopsin background containing a juxtaposed cysteine pair (N2C/D282C) that forms a disulfide bond.	Disulfides	163-172	rhodopsin	Homo sapiens	79-88
24111668-2	2013	This study demonstrated that a combination of low doses of kanamycin and streptomycin, which inhibited the growth of recipient and donor cells, respectively, had positive effects on the transmission of the conjugation plasmids pRK2013, pSU2007, and RP4 from Escherichia coli DH5alpha to HB101 at their minimum inhibitory concentrations (MICs).	Kanamycin	59-68	rhodopsin	Homo sapiens	249-252
24111668-2	2013	This study demonstrated that a combination of low doses of kanamycin and streptomycin, which inhibited the growth of recipient and donor cells, respectively, had positive effects on the transmission of the conjugation plasmids pRK2013, pSU2007, and RP4 from Escherichia coli DH5alpha to HB101 at their minimum inhibitory concentrations (MICs).	Streptomycin	73-85	rhodopsin	Homo sapiens	249-252
22983928-0	2013	Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin.	13c	16-19	rhodopsin	Homo sapiens	108-117
22983928-0	2013	Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin.	15n	24-27	rhodopsin	Homo sapiens	108-117
23754968-8	2013	In addition, the loss of Osiris 21 function shifts the membrane balance between late endosomes and lysosomes as evidenced by smaller late endosomes and the proliferation of lysosomal compartments, thus facilitating the degradation of endocytosed rhodopsin.	osiris	25-31	rhodopsin	Homo sapiens	246-255
24069221-3	2013	Furthermore, the photopigment rhodopsin is expressed in human melanocytes and is involved in ultraviolet A phototransduction which induces early melanin synthesis.	Melanins	145-152	rhodopsin	Homo sapiens	30-39
23701524-0	2013	Retinal conformation governs pKa of protonated Schiff base in rhodopsin activation.	Schiff Bases	47-58	rhodopsin	Homo sapiens	62-71
23701524-1	2013	We have explored the relationship between conformational energetics and the protonation state of the Schiff base in retinal, the covalently bound ligand responsible for activating the G protein-coupled receptor rhodopsin, using quantum chemical calculations.	Schiff Bases	101-112	rhodopsin	Homo sapiens	211-220
23625926-4	2013	To assess thermal stability, we measured the rate of two thermal reactions contributing to the thermal decay of rhodopsin as follows: thermal isomerization of 11-cis-retinal and hydrolysis of the protonated Schiff base linkage between the 11-cis-retinal chromophore and opsin protein.	Schiff Bases	207-218	rhodopsin	Homo sapiens	112-121
23625926-6	2013	Compared with WT rhodopsin and the D190N mutant, the S186W mutation dramatically increases the rates of both thermal isomerization and dark state hydrolysis of the Schiff base by 1-2 orders of magnitude.	Schiff Bases	164-175	rhodopsin	Homo sapiens	17-26
23625926-7	2013	The results suggest that the S186W mutant thermally destabilizes rhodopsin by disrupting a hydrogen bond network at the receptor"s active site.	Hydrogen	91-99	rhodopsin	Homo sapiens	65-74
23980892-2	2013	In this mini-review, we briefly examine the basic experimental data on the role of Zn2+ in the retina and photoreceptors, binding of endogenous Zn2+ by zinc-binding sites of differing affinities in rhodopsin, the influence of the exogenous Zn2+ on various properties of rhodopsin, including its ability for phosphorylation and activation of transducin, as well as its thermal stability and regeneration.	Zinc	144-148	rhodopsin	Homo sapiens	198-207
23980892-2	2013	In this mini-review, we briefly examine the basic experimental data on the role of Zn2+ in the retina and photoreceptors, binding of endogenous Zn2+ by zinc-binding sites of differing affinities in rhodopsin, the influence of the exogenous Zn2+ on various properties of rhodopsin, including its ability for phosphorylation and activation of transducin, as well as its thermal stability and regeneration.	Zinc	144-148	rhodopsin	Homo sapiens	198-207
23579341-4	2013	The mutant thus interferes with the E113Q-K296 activation switch and the covalent binding of the inverse agonist 11-cis-retinal, two interactions that are crucial for the deactivation of rhodopsin.	Retinaldehyde	113-127	rhodopsin	Homo sapiens	187-196
23841875-2	2013	In rhodopsin (Rh), this process is coupled to a change in the protonation state of a key residue, E134, whose exact role in activation is not well understood.	e134	98-102	rhodopsin	Homo sapiens	3-12
23088961-6	2013	Rhodopsin distribution within the DCN was determined to be within several cell types identified based on morphology and location within the DCN.	dcn	34-37	rhodopsin	Homo sapiens	0-9
23693153-4	2013	In particular, we have improved the model by implementing a more detailed representation of the recoverin (Rec)-mediated calcium feedback on rhodopsin kinase and including a dynamic arrestin (Arr) oligomerization mechanism.	Calcium	121-128	rhodopsin	Homo sapiens	141-150
23088961-6	2013	Rhodopsin distribution within the DCN was determined to be within several cell types identified based on morphology and location within the DCN.	dcn	140-143	rhodopsin	Homo sapiens	0-9
23458690-1	2013	Upon illumination the visual receptor rhodopsin (Rho) transitions to the activated form Rho(*), which binds the heterotrimeric G protein, transducin (Gt) causing GDP to GTP exchange and Gt dissociation.	Guanosine Triphosphate	169-172	rhodopsin	Homo sapiens	38-47
23140223-1	2013	Photochemistry of bacteriorhodopsin (bR), anabaena sensory rhodopsin (ASR), and all-trans retinal protonated Schiff base (RPSB) in ethanol is followed with femtosecond pump-hyperspectral near-IR (NIR) probe spectroscopy.	Ethanol	131-138	rhodopsin	Homo sapiens	26-35
23458690-1	2013	Upon illumination the visual receptor rhodopsin (Rho) transitions to the activated form Rho(*), which binds the heterotrimeric G protein, transducin (Gt) causing GDP to GTP exchange and Gt dissociation.	Guanosine Diphosphate	162-165	rhodopsin	Homo sapiens	38-47
23420844-3	2013	Homology modeling of mGluR8 transmembrane domain with rhodopsin as a template suggested the presence of a conserved water-mediated hydrogen-bonding network between helices VI and VII, which presumably constrains the receptor in an inactive conformation.	Water	116-121	rhodopsin	Homo sapiens	54-63
23420844-3	2013	Homology modeling of mGluR8 transmembrane domain with rhodopsin as a template suggested the presence of a conserved water-mediated hydrogen-bonding network between helices VI and VII, which presumably constrains the receptor in an inactive conformation.	Hydrogen	131-139	rhodopsin	Homo sapiens	54-63
23313943-0	2013	Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation.	Histidine	29-32	rhodopsin	Homo sapiens	60-69
23477373-0	2013	Large spectral change due to amide modes of a beta-sheet upon the formation of an early photointermediate of middle rhodopsin.	Amides	29-34	rhodopsin	Homo sapiens	116-125
23447332-0	2013	Improved conformational stability of the visual G protein-coupled receptor rhodopsin by specific interaction with docosahexaenoic acid phospholipid.	docosahexaenoic acid phospholipid	114-147	rhodopsin	Homo sapiens	75-84
23447332-5	2013	In this work, rhodopsin reconstituted in docosahexaenoic acid (DHA) liposomes is shown to have more thermal stability than when it is solubilised with the neutral detergent dodecyl maltoside.	Docosahexaenoic Acids	41-61	rhodopsin	Homo sapiens	14-23
23447332-5	2013	In this work, rhodopsin reconstituted in docosahexaenoic acid (DHA) liposomes is shown to have more thermal stability than when it is solubilised with the neutral detergent dodecyl maltoside.	Docosahexaenoic Acids	63-66	rhodopsin	Homo sapiens	14-23
23447332-5	2013	In this work, rhodopsin reconstituted in docosahexaenoic acid (DHA) liposomes is shown to have more thermal stability than when it is solubilised with the neutral detergent dodecyl maltoside.	dodecyl maltoside	173-190	rhodopsin	Homo sapiens	14-23
23447332-6	2013	Moreover, the specific interaction between rhodopsin and DHA was followed by means of Langmuir experiments with insertion of rhodopsin into lipid monolayers; this showed high affinity for the lipid-receptor interaction.	Docosahexaenoic Acids	57-60	rhodopsin	Homo sapiens	43-52
23447332-6	2013	Moreover, the specific interaction between rhodopsin and DHA was followed by means of Langmuir experiments with insertion of rhodopsin into lipid monolayers; this showed high affinity for the lipid-receptor interaction.	Docosahexaenoic Acids	57-60	rhodopsin	Homo sapiens	125-134
23313943-0	2013	Salt bridge in the conserved His-Asp cluster in Gloeobacter rhodopsin contributes to trimer formation.	Aspartic Acid	33-36	rhodopsin	Homo sapiens	60-69
23313943-1	2013	Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate.	Histidine	82-91	rhodopsin	Homo sapiens	12-21
23313943-1	2013	Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate.	Retinaldehyde	101-108	rhodopsin	Homo sapiens	12-21
23313943-1	2013	Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate.	Schiff Bases	109-120	rhodopsin	Homo sapiens	12-21
23313943-1	2013	Gloeobacter rhodopsin (GR) is a eubacterial proton pump having a highly conserved histidine near the retinal Schiff base counter-ion, aspartate.	Aspartic Acid	134-143	rhodopsin	Homo sapiens	12-21
23095117-14	2012	The photoinduced proton release (possibly by the decrease in the pK(a) of the secondary counterion) in acidic media was also observed in other microbial rhodopsins with the exception of the Anabaena sensory rhodopsin, which lacks the dissociable residue at the position of Asp212 of BR or Asp227 of PR and halorhodopsin.	Bromine	283-285	rhodopsin	Homo sapiens	153-162
23086229-2	2013	The crystal structure of rhodopsin revealed a salt bridge between R135(3.50) and another conserved residue, E247(6.30), in helix 6.	3-Nitrocinnamic acid	66-70	rhodopsin	Homo sapiens	25-34
23086229-2	2013	The crystal structure of rhodopsin revealed a salt bridge between R135(3.50) and another conserved residue, E247(6.30), in helix 6.	e247	108-112	rhodopsin	Homo sapiens	25-34
24143971-5	2013	Focus is put on the ENM-NMA-based strategy applied to the crystallographic structures of rhodopsin in its inactive (dark) and signaling active (meta II (MII)) states, highlighting clear changes in the PSN and the centrality of the retinal chromophore in differentiating the inactive and active states of the receptor.	nma	24-27	rhodopsin	Homo sapiens	89-98
23114546-0	2012	Solution mediated phase transformation (RHO to SOD) in porous Co-imidazolate based zeolitic frameworks with high water stability.	co-imidazolate	62-76	rhodopsin	Homo sapiens	40-50
23114546-0	2012	Solution mediated phase transformation (RHO to SOD) in porous Co-imidazolate based zeolitic frameworks with high water stability.	Water	113-118	rhodopsin	Homo sapiens	40-50
23192733-5	2013	In surprising contrast to these findings, a recombinant virus (RP4) containing the VP16N deletion was capable of modest forskolin-induced reactivation whereas a recombinant (RP3) containing a deletion of VP16C was incapable of stress-induced reactivation from QIF-PC12 cells.	Colforsin	120-129	rhodopsin	Homo sapiens	63-66
22729505-12	2012	CONCLUSION: Shorter T1(rho) and T2 values after running suggest alteration in the water content and collagen fiber orientation of the articular cartilage.	Water	82-87	rhodopsin	Homo sapiens	20-27
22865888-0	2012	Factors that differentiate the H-bond strengths of water near the Schiff bases in bacteriorhodopsin and Anabaena sensory rhodopsin.	Water	51-56	rhodopsin	Homo sapiens	90-99
22865888-0	2012	Factors that differentiate the H-bond strengths of water near the Schiff bases in bacteriorhodopsin and Anabaena sensory rhodopsin.	Schiff Bases	66-78	rhodopsin	Homo sapiens	90-99
22428905-3	2012	Photoactivated rhodopsin releases all-trans-RAL, which is subsequently transported by ATP-binding cassette transporter 4 and reduced to all-trans-retinol by all-trans-retinol dehydrogenases located in photoreceptor cells.	Vitamin A	136-153	rhodopsin	Homo sapiens	15-24
23083739-0	2012	Calcium feedback to cGMP synthesis strongly attenuates single-photon responses driven by long rhodopsin lifetimes.	Calcium	0-7	rhodopsin	Homo sapiens	94-103
23083739-0	2012	Calcium feedback to cGMP synthesis strongly attenuates single-photon responses driven by long rhodopsin lifetimes.	Cyclic GMP	20-24	rhodopsin	Homo sapiens	94-103
22874131-9	2012	Our results show that with respect to hydroxylamine sensitivity and retinal release, the wild-type echidna rhodopsin displays major differences to all previously characterized mammalian rhodopsins and appears more similar to other nonmammalian vertebrate rhodopsins such as chicken and anole.	Hydroxylamine	38-51	rhodopsin	Homo sapiens	107-116
22700873-5	2012	Inhibition of stathmin activity by small interfering RNA-based knockdown or cAMP-mediated phosphorylation abrogated thrombin-induced F-actin remodeling and Rho-dependent EC hyperpermeability, while expression of a phosphorylation-deficient stathmin mutant exacerbated thrombin-induced EC barrier disruption.	Cyclic AMP	76-80	rhodopsin	Homo sapiens	133-159
22842041-1	2012	We have determined the spatial arrangement of rhodopsin in the retinal rod outer segment (ROS) membrane by measuring the distances between rhodopsin molecules in which native cysteines were spin-labeled at ~1.0 mol/mol rhodopsin.	Cysteine	175-184	rhodopsin	Homo sapiens	46-55
22482865-2	2012	We designed a benzylidene-pyrroline chromophore that mimics the Schiff base of rhodopsin and can be used to introduce light-switchable intramolecular cross-links in peptides and proteins.	benzylidene-pyrroline	14-35	rhodopsin	Homo sapiens	79-88
22435481-0	2012	Vibrational coupling between helices influences the amide I infrared absorption of proteins: application to bacteriorhodopsin and rhodopsin.	Amides	52-57	rhodopsin	Homo sapiens	116-125
22448927-4	2012	Here we show that GDP-GTP exchange on alphaT*(G56P), in the presence of the light-activated GPCR, rhodopsin (R*), is less sensitive to the beta1gamma1 subunit complex than to wild-type alphaT*.	gdp-gtp	18-25	rhodopsin	Homo sapiens	98-107
22639195-1	2012	Double-quantum magic-angle-spinning NMR experiments were performed on 11,12-(13)C(2)-retinylidene-rhodopsin under illumination at low temperature, in order to characterize torsional angle changes at the C11-C12 photoisomerization site.	(2)-retinylidene	81-97	rhodopsin	Homo sapiens	98-107
22482865-2	2012	We designed a benzylidene-pyrroline chromophore that mimics the Schiff base of rhodopsin and can be used to introduce light-switchable intramolecular cross-links in peptides and proteins.	Schiff Bases	64-75	rhodopsin	Homo sapiens	79-88
22431612-1	2012	In the retinal binding pocket of rhodopsin, a Schiff base links the retinal ligand covalently to the Lys296 side chain.	Schiff Bases	46-57	rhodopsin	Homo sapiens	33-42
22409209-1	2012	Recent experimental and theoretical studies on N-alkylated indanylidene pyrroline Schiff bases (NAIP) show that these compounds exhibit biomimetic photoisomerization analogous to that in the chromophore of rhodopsin.	n-alkylated indanylidene pyrroline schiff bases	47-94	rhodopsin	Homo sapiens	206-215
22275358-3	2012	The interaction of rhodopsin-attached phosphates with Lys-14 and Lys-15 in beta-strand I was shown to disrupt the interaction of alpha-helix I, beta-strand I, and the C-tail of visual arrestin-1, facilitating its transition into an active receptor-binding state.	Phosphates	38-48	rhodopsin	Homo sapiens	19-28
22275358-3	2012	The interaction of rhodopsin-attached phosphates with Lys-14 and Lys-15 in beta-strand I was shown to disrupt the interaction of alpha-helix I, beta-strand I, and the C-tail of visual arrestin-1, facilitating its transition into an active receptor-binding state.	Lysine	54-57	rhodopsin	Homo sapiens	19-28
22275358-3	2012	The interaction of rhodopsin-attached phosphates with Lys-14 and Lys-15 in beta-strand I was shown to disrupt the interaction of alpha-helix I, beta-strand I, and the C-tail of visual arrestin-1, facilitating its transition into an active receptor-binding state.	Lysine	65-68	rhodopsin	Homo sapiens	19-28
22260165-2	2012	The functional role of water molecules has been discussed for rhodopsin, the light sensor for twilight vision, on the basis of X-ray crystallography, Fourier transform infrared (FTIR) spectroscopy, and a radiolytic labeling method, but nothing is known about the protein-bound waters in our color visual pigments.	Water	23-28	rhodopsin	Homo sapiens	62-71
22352709-2	2012	To probe the intradimeric proximity of helix 8 (H8), we conducted chemical cross-linking of endogenous cysteines in rhodopsin in disk membranes.	Cysteine	103-112	rhodopsin	Homo sapiens	116-125
22260165-6	2012	The absence of strongly hydrogen-bonded water molecules (O-D stretch at <2400 cm(-1)) is common between rhodopsin and color pigments, which greatly contrasts with the case of proton-pumping microbial rhodopsins.	Hydrogen	24-32	rhodopsin	Homo sapiens	107-116
22260165-6	2012	The absence of strongly hydrogen-bonded water molecules (O-D stretch at <2400 cm(-1)) is common between rhodopsin and color pigments, which greatly contrasts with the case of proton-pumping microbial rhodopsins.	Water	40-45	rhodopsin	Homo sapiens	107-116
22260165-7	2012	On the other hand, two important differences are observed in water signal between rhodopsin and color pigments.	Water	61-66	rhodopsin	Homo sapiens	82-91
21761071-4	2011	As an application to a realistic protein, carbon chemical shifts are calculated for the retinal chromophore in visual rhodopsin.	Carbon	42-48	rhodopsin	Homo sapiens	118-127
22011645-5	2012	Our results show that a novel, double tyrosine mutant of AAV9 significantly enhanced gene delivery to the CNS and retina, and that gene expression can be restricted to rod photoreceptor cells by incorporating a rhodopsin promoter.	Tyrosine	38-46	rhodopsin	Homo sapiens	211-220
22074921-2	2012	A photon of visible light carries a sufficient amount of energy to cause, when absorbed, a cis,trans-geometric isomerization of the 11-cis-retinal chromophore, a vitamin A derivative bound to rhodopsin and cone opsins of retinal photoreceptors.	Vitamin A	162-171	rhodopsin	Homo sapiens	192-201
22368384-0	2012	Docking of human rhodopsin mutant (Gly90 Asp) with beta-arrestin and cyanidin 3-rutinoside to cure night blindness.	cyanidin 3-rutinoside	69-90	rhodopsin	Homo sapiens	17-26
22261069-0	2011	Salt effects on the conformational stability of the visual G-protein-coupled receptor rhodopsin.	Salts	0-4	rhodopsin	Homo sapiens	86-95
22261069-4	2011	Under high salt concentrations, rhodopsin significantly increased its activation enthalpy change for thermal bleaching, whereas acid denaturation affected the formation of a denatured loose-bundle state for both the active and inactive conformations.	Salts	11-15	rhodopsin	Homo sapiens	32-41
22261069-6	2011	However, chromophore regeneration with the 11-cis-retinal chromophore and MetarhodopsinII decay kinetics were slower only in the presence of sodium chloride, suggesting that in this case, the underlying phenomenon may be linked to the activation of rhodopsin and the retinal release processes.	Sodium Chloride	141-156	rhodopsin	Homo sapiens	78-87
22261069-8	2011	The observed effects on rhodopsin could indicate that salts favor electrostatic interactions in the retinal binding pocket and indirectly favor hydrophobic interactions at the membrane protein receptor core.	Salts	54-59	rhodopsin	Homo sapiens	24-33
21801333-12	2011	After induced differentiation, IPE-derived cells showed only partial neuronal differentiation expressing beta-III-tubulin, Map-2 and Rhodopsin, whereas no mature glial markers were found.	ipe	31-34	rhodopsin	Homo sapiens	133-142
21741231-4	2011	The production of ROS was significantly different between ASTC-a-1 and rho(0)ASTC-a-1 cells after an identical PDT treatment.	Reactive Oxygen Species	18-21	rhodopsin	Homo sapiens	58-74
21741231-7	2011	Moreover, we found that the difference in intracellular ROS productions between ASTC-a-1 and rho(0)ASTC-a-1 cells started during a PDT treatment, while the irradiation was still being delivered.	Reactive Oxygen Species	56-59	rhodopsin	Homo sapiens	80-96
21940625-0	2011	Molecular mechanisms of disease for mutations at Gly-90 in rhodopsin.	Glycine	49-52	rhodopsin	Homo sapiens	59-68
21940625-1	2011	Two different mutations at Gly-90 in the second transmembrane helix of the photoreceptor protein rhodopsin have been proposed to lead to different phenotypes.	Glycine	27-30	rhodopsin	Homo sapiens	97-106
21940625-4	2011	The G90V and G90D mutants have a similar conformation around the Schiff base linkage region in the dark state and same regeneration kinetics with 11-cis-retinal, but G90V has dramatically reduced thermal stability when compared with the G90D mutant rhodopsin.	Schiff Bases	65-76	rhodopsin	Homo sapiens	249-258
21921035-0	2011	Chemical kinetic analysis of thermal decay of rhodopsin reveals unusual energetics of thermal isomerization and hydrolysis of Schiff base.	Schiff Bases	126-137	rhodopsin	Homo sapiens	46-55
21921035-2	2011	To understand thermal decay quantitatively, we propose a kinetic model consisting of two pathways: 1) thermal isomerization of 11-cis-retinal followed by hydrolysis of Schiff base (SB) and 2) hydrolysis of SB in dark state rhodopsin followed by opsin-catalyzed isomerization of free 11-cis-retinal.	Retinaldehyde	127-141	rhodopsin	Homo sapiens	223-232
21921035-2	2011	To understand thermal decay quantitatively, we propose a kinetic model consisting of two pathways: 1) thermal isomerization of 11-cis-retinal followed by hydrolysis of Schiff base (SB) and 2) hydrolysis of SB in dark state rhodopsin followed by opsin-catalyzed isomerization of free 11-cis-retinal.	Schiff Bases	206-208	rhodopsin	Homo sapiens	223-232
21921035-2	2011	To understand thermal decay quantitatively, we propose a kinetic model consisting of two pathways: 1) thermal isomerization of 11-cis-retinal followed by hydrolysis of Schiff base (SB) and 2) hydrolysis of SB in dark state rhodopsin followed by opsin-catalyzed isomerization of free 11-cis-retinal.	Retinaldehyde	283-297	rhodopsin	Homo sapiens	223-232
21921035-3	2011	We solve the kinetic model mathematically and use it to analyze kinetic data from four experiments that we designed to assay thermal decay, isomerization, hydrolysis of SB using dark state rhodopsin, and hydrolysis of SB using photoactivated rhodopsin.	Schiff Bases	169-171	rhodopsin	Homo sapiens	189-198
21921035-4	2011	We apply the model to WT rhodopsin and E181Q and S186A mutants at 55  C, as well as WT rhodopsin in H(2)O and D(2)O at 59  C. The results show that the hydrogen-bonding network strongly restrains thermal isomerization but is less important in opsin and activated rhodopsin.	Hydrogen	152-160	rhodopsin	Homo sapiens	25-34
21921035-4	2011	We apply the model to WT rhodopsin and E181Q and S186A mutants at 55  C, as well as WT rhodopsin in H(2)O and D(2)O at 59  C. The results show that the hydrogen-bonding network strongly restrains thermal isomerization but is less important in opsin and activated rhodopsin.	Hydrogen	152-160	rhodopsin	Homo sapiens	87-96
21921035-4	2011	We apply the model to WT rhodopsin and E181Q and S186A mutants at 55  C, as well as WT rhodopsin in H(2)O and D(2)O at 59  C. The results show that the hydrogen-bonding network strongly restrains thermal isomerization but is less important in opsin and activated rhodopsin.	Hydrogen	152-160	rhodopsin	Homo sapiens	87-96
21873336-4	2011	The alpha subunits of G12 or G13 have been shown to interact with members of the RH domain containing guanine nucleotide exchange factors for Rho (RH-RhoGEF) family of proteins to directly connect G protein-mediated signalling and RhoGTPase signalling.	Guanine Nucleotides	102-120	rhodopsin	Homo sapiens	147-156
21924236-2	2012	It has been well established that lipid bilayers that are under negative curvature elastic stress from incorporation of lipids like phosphatidylethanolamines (PE) favor formation of MII, the rhodopsin photointermediate that is capable of activating G protein.	Phosphatidylethanolamines	132-157	rhodopsin	Homo sapiens	191-200
21924236-2	2012	It has been well established that lipid bilayers that are under negative curvature elastic stress from incorporation of lipids like phosphatidylethanolamines (PE) favor formation of MII, the rhodopsin photointermediate that is capable of activating G protein.	Phosphatidylethanolamines	159-161	rhodopsin	Homo sapiens	191-200
22976031-5	2012	Specifically, quantification of the strong proline-induced distortions in the transmembrane bundle of rhodopsin shows that they are not standard proline kinks.	Proline	43-50	rhodopsin	Homo sapiens	102-111
22192505-0	2011	Vitamin A activates rhodopsin and sensitizes it to ultraviolet light.	Vitamin A	0-9	rhodopsin	Homo sapiens	20-29
22192505-5	2011	Rod and cone photoreceptors contain vast amounts of rhodopsin, so after exposure to bright light, the concentration of vitamin A can reach relatively high levels within their outer segments.	Vitamin A	119-128	rhodopsin	Homo sapiens	52-61
22192505-9	2011	Microspectrophotometric measurements showed that vitamin A accumulated in the outer segments and binding of vitamin A to rhodopsin was confirmed in in vitro assays.	Vitamin A	108-117	rhodopsin	Homo sapiens	121-130
22192505-11	2011	Apparently, the energy of a UV photon absorbed by vitamin A transferred by a radiationless process to the 11-cis retinal chromophore of rhodopsin, which subsequently isomerized.	Vitamin A	50-59	rhodopsin	Homo sapiens	136-145
22192505-12	2011	Therefore, our results suggest that vitamin A binds to rhodopsin at an allosteric binding site distinct from the chromophore binding pocket for 11-cis retinal to activate the rhodopsin, and that it serves as a sensitizing chromophore for UV light.	Vitamin A	36-45	rhodopsin	Homo sapiens	55-64
22192505-12	2011	Therefore, our results suggest that vitamin A binds to rhodopsin at an allosteric binding site distinct from the chromophore binding pocket for 11-cis retinal to activate the rhodopsin, and that it serves as a sensitizing chromophore for UV light.	Vitamin A	36-45	rhodopsin	Homo sapiens	175-184
21906602-2	2011	Unlike vertebrate rhodopsin, which interacts with Gt-type G-protein to stimulate the cyclic GMP signaling pathway, invertebrate rhodopsin interacts with Gq-type G-protein to stimulate a signaling pathway that is based on inositol 1,4,5-triphosphate.	Inositol 1,4,5-Trisphosphate	221-248	rhodopsin	Homo sapiens	128-137
21906602-3	2011	Since the inositol 1,4,5-triphosphate signaling pathway is utilized by mammalian nonvisual pigments and a large number of G-protein-coupled receptors, it is important to elucidate how the activation mechanism of invertebrate rhodopsin differs from that of vertebrate rhodopsin.	Inositol 1,4,5-Trisphosphate	10-37	rhodopsin	Homo sapiens	225-234
21906602-3	2011	Since the inositol 1,4,5-triphosphate signaling pathway is utilized by mammalian nonvisual pigments and a large number of G-protein-coupled receptors, it is important to elucidate how the activation mechanism of invertebrate rhodopsin differs from that of vertebrate rhodopsin.	Inositol 1,4,5-Trisphosphate	10-37	rhodopsin	Homo sapiens	267-276
21906602-8	2011	Our results suggest that the light energy absorbed by squid rhodopsin is mostly converted into the distortion energy of the retinal polyene chain and surrounding residues.	Polyenes	132-139	rhodopsin	Homo sapiens	60-69
21640147-4	2011	We demonstrate this process with the Poly(DL-lactic-co-glycolic acid) system encapsulating amphiphilic agents such as doxorubicin (DOX), Rhodamine B (RHO(B)) and Rhodamine B octadecyl ester perchlorate (RHO(BOEP)).	Polyglactin 910	37-69	rhodopsin	Homo sapiens	162-212
21471193-5	2011	We show that alanine substitution of these residues blocks the binding of arrestin-1 to rhodopsin in vitro and of arrestin-2 and -3 to beta2-adrenergic, M2 muscarinic cholinergic, and D2 dopamine receptors in intact cells, suggesting that these elements critically contribute to the energy of the interaction.	Alanine	13-20	rhodopsin	Homo sapiens	88-97
21766795-0	2011	Alkylated hydroxylamine derivatives eliminate peripheral retinylidene Schiff bases but cannot enter the retinal binding pocket of light-activated rhodopsin.	alkylated hydroxylamine	0-23	rhodopsin	Homo sapiens	146-155
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	Hydroxylamine	26-39	rhodopsin	Homo sapiens	96-105
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	eha	195-198	rhodopsin	Homo sapiens	96-105
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	O-tert-butylhydroxylamine	201-226	rhodopsin	Homo sapiens	96-105
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	t-bha	228-233	rhodopsin	Homo sapiens	96-105
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	Aminooxyacetic Acid	240-270	rhodopsin	Homo sapiens	96-105
21766795-3	2011	We discovered that, while hydroxylamine can enter the retinal binding pocket of light-activated rhodopsin, the modified hydroxylamine compounds o-methylhydroxylamine (mHA), o-ethylhydroxylamine (eHA), o-tert-butylhydroxylamine (t-bHA), and o-(carboxymethyl)hydroxylamine (cmHA) are excluded.	Aminooxyacetic Acid	272-276	rhodopsin	Homo sapiens	96-105
21766795-5	2011	We further investigated how t-bHA affects light-activated rhodopsin and its interaction with binding partners.	t-bha	28-33	rhodopsin	Homo sapiens	58-67
21766795-8	2011	We believe that alkylated hydroxylamines will prove to be extremely useful reagents for the investigation of rhodopsin activation and decay mechanisms.	alkylated hydroxylamines	16-40	rhodopsin	Homo sapiens	109-118
21806918-2	2011	We used this technique for the site-specific detection of light-induced hydrogen-deuterium exchange in the lipid-embedded heptahelical transmembrane photosensor Anabaena sensory rhodopsin to pinpoint the location of its conformational changes upon activation.	Hydrogen	72-80	rhodopsin	Homo sapiens	178-187
21806918-2	2011	We used this technique for the site-specific detection of light-induced hydrogen-deuterium exchange in the lipid-embedded heptahelical transmembrane photosensor Anabaena sensory rhodopsin to pinpoint the location of its conformational changes upon activation.	Deuterium	81-90	rhodopsin	Homo sapiens	178-187
21659526-3	2011	We studied the thermal stability of rhodopsin at 55  C with single point mutations (E181Q and S186A) that perturb the hydrogen-bonding network at the active site.	Hydrogen	118-126	rhodopsin	Homo sapiens	36-45
21659526-5	2011	Our results illustrate the importance of the intact hydrogen-bonding network for dim-light detection, revealing the functional roles of water molecules in rhodopsin.	Hydrogen	52-60	rhodopsin	Homo sapiens	155-164
21659526-5	2011	Our results illustrate the importance of the intact hydrogen-bonding network for dim-light detection, revealing the functional roles of water molecules in rhodopsin.	Water	136-141	rhodopsin	Homo sapiens	155-164
21506561-1	2011	Rhodopsin, a seven transmembrane helix (TM) receptor, binds its ligand 11-cis-retinal via a protonated Schiff base.	Retinaldehyde	71-85	rhodopsin	Homo sapiens	0-9
21527723-0	2011	Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.	Deuterium	12-14	rhodopsin	Homo sapiens	108-117
21527723-5	2011	Surprisingly, we find the retinylidene methyl groups exhibit site-specific differences in dynamics that change upon light excitation--even more striking, the C9-methyl group is a dynamical hotspot that corresponds to a crucial functional hotspot of rhodopsin.	retinylidene	26-38	rhodopsin	Homo sapiens	249-258
21555003-15	2011	Inhibition of FPPS prevents the biosynthesis of isoprenoid compounds (notably farnesol and geranylgeraniol) that are required for the post-translational prenylation of small GTP-binding proteins (which are also GTPases) such as rab, rho and rac, which are essential for intracellular signalling events within osteoclasts.	Terpenes	48-58	rhodopsin	Homo sapiens	233-244
21555003-15	2011	Inhibition of FPPS prevents the biosynthesis of isoprenoid compounds (notably farnesol and geranylgeraniol) that are required for the post-translational prenylation of small GTP-binding proteins (which are also GTPases) such as rab, rho and rac, which are essential for intracellular signalling events within osteoclasts.	Farnesol	78-86	rhodopsin	Homo sapiens	233-244
21555003-15	2011	Inhibition of FPPS prevents the biosynthesis of isoprenoid compounds (notably farnesol and geranylgeraniol) that are required for the post-translational prenylation of small GTP-binding proteins (which are also GTPases) such as rab, rho and rac, which are essential for intracellular signalling events within osteoclasts.	geranylgeraniol	91-106	rhodopsin	Homo sapiens	233-244
21460218-0	2011	Role of bulk water in hydrolysis of the rhodopsin chromophore.	Water	13-18	rhodopsin	Homo sapiens	40-49
21506561-1	2011	Rhodopsin, a seven transmembrane helix (TM) receptor, binds its ligand 11-cis-retinal via a protonated Schiff base.	Schiff Bases	103-114	rhodopsin	Homo sapiens	0-9
20713020-5	2011	The arginine of the conserved E/DRY motif, R3.50, is not involved in the communication paths but participates in the structure network as a stable hub, being linked to both D3.49 and E6.30 like in the inactive states of rhodopsin.	Arginine	4-12	rhodopsin	Homo sapiens	220-229
21243153-0	2011	Product formation in rhodopsin by fast hydrogen motions.	Hydrogen	39-47	rhodopsin	Homo sapiens	21-30
21319741-0	2011	Glutamic acid 181 is negatively charged in the bathorhodopsin photointermediate of visual rhodopsin.	Glutamic Acid	0-13	rhodopsin	Homo sapiens	52-61
21319741-1	2011	Assignment of the protonation state of the residue Glu-181 is important to our understanding of the primary event, activation processes and wavelength selection in rhodopsin.	Glutamic Acid	51-54	rhodopsin	Homo sapiens	164-173
21319741-7	2011	Because the primary event in rhodopsin does not include a proton translocation or disruption of the hydrogen-bonding network within the binding pocket, we may conclude that the Glu-181 residue in rhodopsin is also charged.	Glutamic Acid	177-180	rhodopsin	Homo sapiens	29-38
21319741-7	2011	Because the primary event in rhodopsin does not include a proton translocation or disruption of the hydrogen-bonding network within the binding pocket, we may conclude that the Glu-181 residue in rhodopsin is also charged.	Glutamic Acid	177-180	rhodopsin	Homo sapiens	196-205
21389983-8	2011	Comparison with the structure of ground-state rhodopsin suggests how translocation of the retinal beta-ionone ring leads to a rotation of transmembrane helix 6, which is the critical conformational change on activation.	beta-ionone	98-109	rhodopsin	Homo sapiens	46-55
21389988-2	2011	The photoreceptor rhodopsin couples to transducin and bears its ligand 11-cis-retinal covalently bound via a protonated Schiff base to the opsin apoprotein.	Schiff Bases	120-131	rhodopsin	Homo sapiens	18-27
21254762-1	2011	Symmetrically disubstituted diacetylenes, X-C C-C C-X, were studied computationally by using the DFT B3LYP/aug-cc-pVDZ method.	diacetylenes	28-40	rhodopsin	Homo sapiens	44-47
21149645-5	2011	The presence of PCs containing polyunsaturated fatty acids in the OS layer implied that these phospholipids form flexible lipid bilayers, which facilitate phototransduction process occurring in the rhodopsin rich OS layer.	Phosphatidylcholines	16-19	rhodopsin	Homo sapiens	198-207
21149645-5	2011	The presence of PCs containing polyunsaturated fatty acids in the OS layer implied that these phospholipids form flexible lipid bilayers, which facilitate phototransduction process occurring in the rhodopsin rich OS layer.	Fatty Acids, Unsaturated	31-58	rhodopsin	Homo sapiens	198-207
21149645-5	2011	The presence of PCs containing polyunsaturated fatty acids in the OS layer implied that these phospholipids form flexible lipid bilayers, which facilitate phototransduction process occurring in the rhodopsin rich OS layer.	Phospholipids	94-107	rhodopsin	Homo sapiens	198-207
21254762-1	2011	Symmetrically disubstituted diacetylenes, X-C C-C C-X, were studied computationally by using the DFT B3LYP/aug-cc-pVDZ method.	diacetylenes	28-40	rhodopsin	Homo sapiens	48-51
21050017-2	2010	Here we report the first successful use of solution NMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimic phosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin.	Phytic Acid	200-222	rhodopsin	Homo sapiens	189-198
21254762-5	2011	The electron density of the C-X bond critical point decreases linearly with an increase of the sigma-electron donating properties, whereas the Laplacian of electron density in the C C bond critical point increases as the sEDA descriptor i.e., sigma-electron donating properties of the substituent, are increased.	seda	221-225	rhodopsin	Homo sapiens	180-183
21295282-10	2011	DHDDS is a key enzyme in the pathway of dolichol, which plays an important role in N-glycosylation of many glycoproteins, including rhodopsin.	Dolichols	40-48	rhodopsin	Homo sapiens	132-141
21295282-10	2011	DHDDS is a key enzyme in the pathway of dolichol, which plays an important role in N-glycosylation of many glycoproteins, including rhodopsin.	Nitrogen	83-84	rhodopsin	Homo sapiens	132-141
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	ros	358-361	rhodopsin	Homo sapiens	115-124
21161517-9	2011	The uneven distribution of saturated and polyunsaturated chain densities and the cholesterol-induced balancing of chain distributions may have important implications for the function and integrity of membrane receptors, such as rhodopsin.	Cholesterol	81-92	rhodopsin	Homo sapiens	228-237
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	carbonyl sulfide	215-218	rhodopsin	Homo sapiens	42-51
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	carbonyl sulfide	215-218	rhodopsin	Homo sapiens	115-124
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	carbonyl sulfide	215-218	rhodopsin	Homo sapiens	115-124
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	carbonyl sulfide	215-218	rhodopsin	Homo sapiens	115-124
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	ros	358-361	rhodopsin	Homo sapiens	115-124
21268073-6	2011	The results revealed all of the truncated rhodopsin fragments except for the C-terminal domain and the full-length rhodopsin which had some plasma membrane localization, formed aggregates nearby or within the ER in COS-1 cells; however, the N-terminally truncated rhodopsin fragment, the C-terminal domain, and the full-length rhodopsin could traffic to the ROS in the zebrafish.	ros	358-361	rhodopsin	Homo sapiens	115-124
21146498-6	2011	We report here the presence of CRAC motifs in three representative GPCRs, namely, rhodopsin, the beta(2)-adrenergic receptor, and the serotonin(1A) receptor.	crac	31-35	rhodopsin	Homo sapiens	82-91
21050017-2	2010	Here we report the first successful use of solution NMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimic phosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin.	Phytic Acid	224-227	rhodopsin	Homo sapiens	189-198
21050017-2	2010	Here we report the first successful use of solution NMR in mapping the binding sites in arrestin-1 (visual arrestin) for two polyanionic compounds that mimic phosphorylated light-activated rhodopsin: inositol hexaphosphate (IP6) and heparin.	Heparin	233-240	rhodopsin	Homo sapiens	189-198
21041664-0	2010	Highly conserved tyrosine stabilizes the active state of rhodopsin.	Tyrosine	17-25	rhodopsin	Homo sapiens	57-66
20967340-6	2010	Then, I will discuss how SDL studies were carried out on rhodopsin, and how they were used to identify a key structural change that occurs in rhodopsin upon activation--movement of transmembrane helix 6 (TM6).	loxoribine	25-28	rhodopsin	Homo sapiens	57-66
20939497-0	2010	Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange.	Histidine	79-88	rhodopsin	Homo sapiens	57-66
20939497-0	2010	Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange.	Hydrogen	89-97	rhodopsin	Homo sapiens	57-66
20939497-0	2010	Conformational changes in the g protein-coupled receptor rhodopsin revealed by histidine hydrogen-deuterium exchange.	Deuterium	98-107	rhodopsin	Homo sapiens	57-66
20939497-2	2010	Utilizing His residues found spaced throughout the GPCR, rhodopsin, we used His hydrogen-deuterium exchange (His-HDX) to monitor long-time scale structural rearrangements previously inaccessible by other means.	Hydrogen	80-88	rhodopsin	Homo sapiens	57-66
20939497-2	2010	Utilizing His residues found spaced throughout the GPCR, rhodopsin, we used His hydrogen-deuterium exchange (His-HDX) to monitor long-time scale structural rearrangements previously inaccessible by other means.	Deuterium	89-98	rhodopsin	Homo sapiens	57-66
20939497-3	2010	The half-lives of His-HDX indicate clear differences in the solvent accessibility of three His residues in rhodopsin/opsin and Zn2+-dependent changes in the pKa for His195.	Histidine	18-21	rhodopsin	Homo sapiens	107-116
20967340-6	2010	Then, I will discuss how SDL studies were carried out on rhodopsin, and how they were used to identify a key structural change that occurs in rhodopsin upon activation--movement of transmembrane helix 6 (TM6).	loxoribine	25-28	rhodopsin	Homo sapiens	142-151
20395291-2	2010	Molecular dynamics simulations showed that, although the fewer water molecules in rhodopsin were relatively movable, the hydrogen bond network of the beta2-adrenergic receptor was fully loaded with water molecules that were surprisingly immobilized between the two rotamer switches, both apparently being in their closed conformation.	Water	63-68	rhodopsin	Homo sapiens	82-91
20923654-0	2010	Coupling of retinal, protein, and water dynamics in squid rhodopsin.	Water	34-39	rhodopsin	Homo sapiens	58-67
20923668-6	2010	Using SEIRA spectroscopy, we followed specific binding of rhodopsin-loaded NABB particles to the surface and formation of a membrane protein monolayer.	seira	6-11	rhodopsin	Homo sapiens	58-67
20923668-6	2010	Using SEIRA spectroscopy, we followed specific binding of rhodopsin-loaded NABB particles to the surface and formation of a membrane protein monolayer.	nabb	75-79	rhodopsin	Homo sapiens	58-67
20805032-0	2010	Retinobenzaldehydes as proper-trafficking inducers of folding-defective P23H rhodopsin mutant responsible for retinitis pigmentosa.	retinobenzaldehydes	0-19	rhodopsin	Homo sapiens	77-86
21073427-1	2010	Staining by antibodies to rhodopsin (Rh) and fluorescence of N-retinylopsin (RO) have shown that digitonin (DIG)- , dodecyl-beta-D-maltoside (DM)- , and sodium dodecyl sulfate (SDS)-solubilized frog Rh after BN- and HRCN-PAGE is situated in the gradient gel in the state of dimer with a slight content of higher oligomers (trimer, tetramer, etc.).	Digitonin	97-106	rhodopsin	Homo sapiens	26-35
21073427-1	2010	Staining by antibodies to rhodopsin (Rh) and fluorescence of N-retinylopsin (RO) have shown that digitonin (DIG)- , dodecyl-beta-D-maltoside (DM)- , and sodium dodecyl sulfate (SDS)-solubilized frog Rh after BN- and HRCN-PAGE is situated in the gradient gel in the state of dimer with a slight content of higher oligomers (trimer, tetramer, etc.).	Digitonin	108-111	rhodopsin	Homo sapiens	26-35
21073427-1	2010	Staining by antibodies to rhodopsin (Rh) and fluorescence of N-retinylopsin (RO) have shown that digitonin (DIG)- , dodecyl-beta-D-maltoside (DM)- , and sodium dodecyl sulfate (SDS)-solubilized frog Rh after BN- and HRCN-PAGE is situated in the gradient gel in the state of dimer with a slight content of higher oligomers (trimer, tetramer, etc.).	dodecyl maltoside	142-144	rhodopsin	Homo sapiens	26-35
21254535-7	2010	Similarly to other GPCR-cascades, one may suggest that there are multiple signalling pathways that start from photoactivated rhodopsin and rely on different secondary messengers (e.g. cAMP vs. cGMP).	Cyclic AMP	184-188	rhodopsin	Homo sapiens	125-134
21254535-7	2010	Similarly to other GPCR-cascades, one may suggest that there are multiple signalling pathways that start from photoactivated rhodopsin and rely on different secondary messengers (e.g. cAMP vs. cGMP).	Cyclic GMP	193-197	rhodopsin	Homo sapiens	125-134
21254535-8	2010	We also show that rhodopsin in retinal rods may form areas of paracristalline organization, and that the oligomerization might be a mechanism for controlling the amplification of the signalling cascade.	paracristalline	62-77	rhodopsin	Homo sapiens	18-27
20600126-7	2010	Additionally, Met292 (TM7) equivalent to Lys(7.45) (Ballesteros numbering scheme) involved in covalently attaching retinal in rhodopsin is shown to be in close proximity to Trp(9).	Lysine	41-44	rhodopsin	Homo sapiens	126-135
20600126-7	2010	Additionally, Met292 (TM7) equivalent to Lys(7.45) (Ballesteros numbering scheme) involved in covalently attaching retinal in rhodopsin is shown to be in close proximity to Trp(9).	Tryptophan	173-176	rhodopsin	Homo sapiens	126-135
20695526-6	2010	TOAC and Proxyl spin-labels in this GPCR-G-protein alpha-peptide system provide unique biophysical probes that can be used to explore the structure and conformational changes at the rhodopsin-G-protein interface.	2,2,6,6-tetramethylpiperidine-N-oxide-4-amino-4-carboxylic acid	0-4	rhodopsin	Homo sapiens	182-191
20575534-6	2010	We investigated the effects of the chemical denaturants sodium dodecyl sulfate (SDS), urea, guanidine hydrochloride (GuHCl), and trifluoroacetic acid (TFA) on rhodopsin"s secondary structure and propensity for aggregation.	Sodium Dodecyl Sulfate	56-78	rhodopsin	Homo sapiens	159-168
20575534-6	2010	We investigated the effects of the chemical denaturants sodium dodecyl sulfate (SDS), urea, guanidine hydrochloride (GuHCl), and trifluoroacetic acid (TFA) on rhodopsin"s secondary structure and propensity for aggregation.	Guanidine	92-115	rhodopsin	Homo sapiens	159-168
20575534-6	2010	We investigated the effects of the chemical denaturants sodium dodecyl sulfate (SDS), urea, guanidine hydrochloride (GuHCl), and trifluoroacetic acid (TFA) on rhodopsin"s secondary structure and propensity for aggregation.	Guanidine	117-122	rhodopsin	Homo sapiens	159-168
20575534-6	2010	We investigated the effects of the chemical denaturants sodium dodecyl sulfate (SDS), urea, guanidine hydrochloride (GuHCl), and trifluoroacetic acid (TFA) on rhodopsin"s secondary structure and propensity for aggregation.	Trifluoroacetic Acid	129-149	rhodopsin	Homo sapiens	159-168
20575534-12	2010	Thus, 30% SDS and 3% SDS + 8 M urea are the denaturing conditions of choice to study maximally unfolded rhodopsin without aggregation.	Sodium Dodecyl Sulfate	10-13	rhodopsin	Homo sapiens	104-113
20575534-12	2010	Thus, 30% SDS and 3% SDS + 8 M urea are the denaturing conditions of choice to study maximally unfolded rhodopsin without aggregation.	Sodium Dodecyl Sulfate	21-24	rhodopsin	Homo sapiens	104-113
20575534-12	2010	Thus, 30% SDS and 3% SDS + 8 M urea are the denaturing conditions of choice to study maximally unfolded rhodopsin without aggregation.	Urea	31-35	rhodopsin	Homo sapiens	104-113
20575562-2	2010	The SDS-unfolded states of rhodopsin.	Sodium Dodecyl Sulfate	4-7	rhodopsin	Homo sapiens	27-36
20575562-4	2010	A screen of chemical denaturants to maximally unfold the mammalian membrane protein and prototypic G protein coupled receptor rhodopsin, without interference from aggregation, described in an accompanying paper (DOI 10.1021/bi100338e ), identified sodium dodecyl sulfate (SDS), alone or in combination with other chemicals, as the most suitable denaturant.	Sodium Dodecyl Sulfate	248-270	rhodopsin	Homo sapiens	126-135
20575562-4	2010	A screen of chemical denaturants to maximally unfold the mammalian membrane protein and prototypic G protein coupled receptor rhodopsin, without interference from aggregation, described in an accompanying paper (DOI 10.1021/bi100338e ), identified sodium dodecyl sulfate (SDS), alone or in combination with other chemicals, as the most suitable denaturant.	Sodium Dodecyl Sulfate	272-275	rhodopsin	Homo sapiens	126-135
20575562-5	2010	Here, we initiate the biophysical characterization of SDS-denatured states of rhodopsin.	Sodium Dodecyl Sulfate	54-57	rhodopsin	Homo sapiens	78-87
20510285-1	2010	The regeneration of the 11-cis-retinyl imine chromophore of rhodopsin during the visual cycle and mechanisms that control this process are central questions in the field of vision research.	11-cis-retinyl imine	24-44	rhodopsin	Homo sapiens	60-69
20407846-2	2010	This article describes recent studies that link the photoactivation of rhodopsin to tyrosine phosphorylation of the IR and subsequent activation of phosphoinositide 3-kinase, a neuron survival factor.	Tyrosine	84-92	rhodopsin	Homo sapiens	71-80
20383122-4	2010	We used site-directed non-natural amino acid mutagenesis to engineer rhodopsin with p-azido-l-phenylalanine residues incorporated at selected sites, and monitored the azido vibrational signatures using infrared spectroscopy as rhodopsin proceeded along its activation pathway.	4-Azido-L-phenylalanine	84-107	rhodopsin	Homo sapiens	69-78
20382160-3	2010	Photoreceptor-associated retinol dehydrogenase (prRDH) is evolutionarily closely related to 17beta-HSD1 but reduces all-trans retinal to all-trans retinol, contributing to rhodopsin regeneration in the visual cycle.	Vitamin A	25-32	rhodopsin	Homo sapiens	172-181
20532191-1	2010	Q344ter is a naturally occurring rhodopsin mutation in humans that causes autosomal dominant retinal degeneration through mechanisms that are not fully understood, but are thought to involve an early termination that removed the trafficking signal, QVAPA, leading to its mislocalization in the rod photoreceptor cell.	qvapa	249-254	rhodopsin	Homo sapiens	33-42
20299456-9	2010	Analysis suggested that a lid conformation similar to that of ECL2 in rhodopsin was induced upon binding both agonist and antagonist, but exposing different accessible segments delimited by the highly conserved disulfide bond.	Disulfides	211-220	rhodopsin	Homo sapiens	70-79
20102149-3	2010	Recent in vitro studies demonstrate that anthocyanins and other flavonoids interact directly with rhodopsin and modulate visual pigment function.	Anthocyanins	41-53	rhodopsin	Homo sapiens	98-107
20184892-3	2010	In this study, we used all-atom molecular dynamics simulations of a transmembrane protein complex between rhodopsin and the heterotrimeric transducin (G alpha beta gamma) in an all-atom DOPC (1,2-dioleoylsn-glycero-3-phosphocholine) membrane-water environment.	1,2-oleoylphosphatidylcholine	186-190	rhodopsin	Homo sapiens	106-115
20184892-3	2010	In this study, we used all-atom molecular dynamics simulations of a transmembrane protein complex between rhodopsin and the heterotrimeric transducin (G alpha beta gamma) in an all-atom DOPC (1,2-dioleoylsn-glycero-3-phosphocholine) membrane-water environment.	1,2-oleoylphosphatidylcholine	192-231	rhodopsin	Homo sapiens	106-115
20184892-3	2010	In this study, we used all-atom molecular dynamics simulations of a transmembrane protein complex between rhodopsin and the heterotrimeric transducin (G alpha beta gamma) in an all-atom DOPC (1,2-dioleoylsn-glycero-3-phosphocholine) membrane-water environment.	Water	242-247	rhodopsin	Homo sapiens	106-115
20102149-3	2010	Recent in vitro studies demonstrate that anthocyanins and other flavonoids interact directly with rhodopsin and modulate visual pigment function.	Flavonoids	64-74	rhodopsin	Homo sapiens	98-107
21355205-3	2010	Improve visual function by increasing rhodopsin regeneration and ocular health is the earliest reported bioactivities of anthocyanin.	Anthocyanins	121-132	rhodopsin	Homo sapiens	38-47
20659113-4	2010	A short tetrazole peptidomimetic based on the photoactivated state of rhodopsin-bound structure of Gt(alpha)(340-350) was previously designed and shown to stabilize the photoactivated state of rhodopsin, the G-protein coupled receptor involved in vision.	1H-tetrazole	8-17	rhodopsin	Homo sapiens	70-79
20170125-2	2010	However, we recently found that replacement of Ala178 with Arg in the E-F loop of proteorhodopsin (PR), an archaeal-type rhodopsin in marine bacteria, shifts the lambda(max) from 525 to 545 nm at neutral pH [Yoshitsugu, M., Shibata, M., Ikeda, D., Furutani, Y., and Kandori, H. (2008) Angew.	furutani	248-256	rhodopsin	Homo sapiens	88-97
20053991-5	2010	Mutational analyses of agonist-binding rhodopsin showed that replacement of Ala-269, one of the residues constituting the antagonist-binding site, with bulky amino acids resulted in a large spectral shift in its active state and a great reduction in G protein activity, whereas these were rescued by subsequent replacement of Phe-208 with smaller amino acids.	Alanine	76-79	rhodopsin	Homo sapiens	39-48
20053991-5	2010	Mutational analyses of agonist-binding rhodopsin showed that replacement of Ala-269, one of the residues constituting the antagonist-binding site, with bulky amino acids resulted in a large spectral shift in its active state and a great reduction in G protein activity, whereas these were rescued by subsequent replacement of Phe-208 with smaller amino acids.	Phenylalanine	326-329	rhodopsin	Homo sapiens	39-48
20053991-7	2010	Therefore, the agonist is located close to Ala-269 in the agonist-binding rhodopsin, but not in vertebrate rhodopsins, and Ala-269 with Phe-208 acts as a pivot for the formation of the G protein-activating state in both rhodopsins.	Alanine	43-46	rhodopsin	Homo sapiens	74-83
20659113-4	2010	A short tetrazole peptidomimetic based on the photoactivated state of rhodopsin-bound structure of Gt(alpha)(340-350) was previously designed and shown to stabilize the photoactivated state of rhodopsin, the G-protein coupled receptor involved in vision.	1H-tetrazole	8-17	rhodopsin	Homo sapiens	193-202
19933196-0	2010	The dependence of retinal degeneration caused by the rhodopsin P23H mutation on light exposure and vitamin a deprivation.	Vitamin A	99-108	rhodopsin	Homo sapiens	53-62
19933196-7	2010	Vitamin A deprivation also induced retinal degeneration associated with defects in P23H rhodopsin biosynthesis.	Vitamin A	0-9	rhodopsin	Homo sapiens	88-97
20126799-3	2010	H8 runs parallel to the membrane surface and extends from transmembrane helix 7 whose highly conserved NPxxY(x)F motif connects that region of rhodopsin with the retinal binding pocket.	N-(2-(methylamino)ethyl)-5-isoquinolinesulfonamide	0-2	rhodopsin	Homo sapiens	143-152
19666736-2	2010	Rearrangement of phospholipids in the bilayer accompanies the formation of the active intermediates of rhodopsin following photon absorption.	Phospholipids	17-30	rhodopsin	Homo sapiens	103-112
20004206-3	2010	The simulations yield a working model for how photoisomerization of the 11-cis retinylidene chromophore bound within the interior of rhodopsin is coupled to transmembrane helix motion and receptor activation.	11-cis retinylidene	72-91	rhodopsin	Homo sapiens	133-142
19892132-13	2010	Vitamin A: In 1913, Ishihara proposed that a "fatty substance" in blood is necessary for synthesis of both rhodopsin and the surface layer of the cornea, and that night blindness and keratomalacia develop when this substance is deficient.	Vitamin A	0-9	rhodopsin	Homo sapiens	107-116
20396622-1	2010	Engineering squid rhodopsin with modified retinal analogues is essential for understanding the conserved steric and electrostatic interaction networks that govern the architecture of the Schiff base binding site.	Schiff Bases	187-198	rhodopsin	Homo sapiens	18-27
19892132-13	2010	Vitamin A: In 1913, Ishihara proposed that a "fatty substance" in blood is necessary for synthesis of both rhodopsin and the surface layer of the cornea, and that night blindness and keratomalacia develop when this substance is deficient.	fatty	46-51	rhodopsin	Homo sapiens	107-116
20552425-3	2010	In rod photoreceptor outer segments, all-trans-retinol is generated after light exposure from the reduction of all-trans-retinal that is released from bleached rhodopsin.	Vitamin A	37-54	rhodopsin	Homo sapiens	160-169
19941040-3	2010	We have recently shown that ATP pre-binding to the KHD in ROS-GC drastically enhances its GCAP-stimulated activity, and that rhodopsin illumination, as the outside signal, is required for the ATP pre-binding.	Adenosine Triphosphate	192-195	rhodopsin	Homo sapiens	125-134
20552432-1	2010	The retinoid (visual) cycle is a complex enzymatic pathway essential for regeneration of the visual chromophore, 11-cis-retinal, a component of rhodopsin that undergoes activation by light in vertebrate eyes.	Retinoids	4-12	rhodopsin	Homo sapiens	144-153
20552433-1	2010	Vertebrate vision is maintained by the retinoid (visual) cycle, a complex enzymatic pathway that operates in the retina to regenerate the visual chromophore, 11-cis-retinal, a prosthetic group of rhodopsin that undergoes activation by light.	Retinoids	39-47	rhodopsin	Homo sapiens	196-205
19941040-4	2010	These results indicate that illuminated rhodopsin is involved in ROS-GC activation in two ways: to initiate ATP binding to ROS-GC for preparation of its activation and to reduce [Ca(2+)] through activation of cGMP phosphodiesterase.	Adenosine Triphosphate	108-111	rhodopsin	Homo sapiens	40-49
19941040-6	2010	These results also suggest that the ECD receives the signal for ATP binding from illuminated rhodopsin.	Adenosine Triphosphate	64-67	rhodopsin	Homo sapiens	93-102
19995077-0	2009	Fluoro derivatives of retinal illuminate the decisive role of the C(12)-H element in photoisomerization and rhodopsin activation.	c(12)	66-71	rhodopsin	Homo sapiens	108-117
19910672-2	2009	In order to perform their function, most of them need energy, e.g. either in the form of a photon, as in the case of the visual pigment rhodopsin, or through the breaking of a chemical bond, as in the presence of adenosine triphosphate (ATP).	Adenosine Triphosphate	237-240	rhodopsin	Homo sapiens	136-145
19934058-2	2009	When the corresponding cysteine is mutated in rhodopsin, it disrupts proper folding of the pigment, causing severe, early onset retinitis pigmentosa.	Cysteine	23-31	rhodopsin	Homo sapiens	46-55
19173312-0	2009	Structural and dynamic effects of cholesterol at preferred sites of interaction with rhodopsin identified from microsecond length molecular dynamics simulations.	Cholesterol	34-45	rhodopsin	Homo sapiens	85-94
19653674-1	2009	Nonadiabatic photodynamical simulations are presented for the all-trans and 5-cis isomers of the hepta-3,5,7-trieniminium cation (PSB4) with the goal of characterizing the types of torsional modes occurring in the cis-trans isomerization processes in retinal protonated Schiff base (RPSB), the rhodopsin and bacteriorhodopsin chropomhore.	hepta-3,5,7-trieniminium	97-121	rhodopsin	Homo sapiens	294-303
19795853-1	2009	The visual pigment rhodopsin is unique among the G protein-coupled receptors in having an 11-cis retinal chromophore covalently bound to the protein through a protonated Schiff base linkage.	Schiff Bases	170-181	rhodopsin	Homo sapiens	19-28
19671662-6	2009	Subsequent treatment with retinoic acid and taurine induces photoreceptors that express recoverin, rhodopsin and genes involved in phototransduction.	Tretinoin	26-39	rhodopsin	Homo sapiens	99-108
19671662-6	2009	Subsequent treatment with retinoic acid and taurine induces photoreceptors that express recoverin, rhodopsin and genes involved in phototransduction.	Taurine	44-51	rhodopsin	Homo sapiens	99-108
19706523-0	2009	Structural waters define a functional channel mediating activation of the GPCR, rhodopsin.	Water	11-17	rhodopsin	Homo sapiens	80-89
19454479-0	2009	Syntaxin 3 and SNAP-25 pairing, regulated by omega-3 docosahexaenoic acid, controls the delivery of rhodopsin for the biogenesis of cilia-derived sensory organelles, the rod outer segments.	omega-3 docosahexaenoic acid	45-73	rhodopsin	Homo sapiens	100-109
19247721-11	2009	After induction by taurine, 80.5 +/- 16.2% of the cell population expressed NSE, 36.8 +/- 9.6% expressed RHOS, and 29.6 +/- 9.3% expressed Nestin, while only 7.9 +/- 3.5% expressed NSE in the control group.	Taurine	19-26	rhodopsin	Homo sapiens	105-109
19795787-6	2009	This suggests that the rhodopsin molecule with its twisted chromophore will possess a considerably lower activation energy than the rhodopsin molecule where the beta-ionone ring is in a planar orientation to the retinal polyene chain.	beta-ionone	161-172	rhodopsin	Homo sapiens	23-32
19795787-6	2009	This suggests that the rhodopsin molecule with its twisted chromophore will possess a considerably lower activation energy than the rhodopsin molecule where the beta-ionone ring is in a planar orientation to the retinal polyene chain.	beta-ionone	161-172	rhodopsin	Homo sapiens	132-141
19795787-6	2009	This suggests that the rhodopsin molecule with its twisted chromophore will possess a considerably lower activation energy than the rhodopsin molecule where the beta-ionone ring is in a planar orientation to the retinal polyene chain.	Polyenes	220-227	rhodopsin	Homo sapiens	23-32
19795787-6	2009	This suggests that the rhodopsin molecule with its twisted chromophore will possess a considerably lower activation energy than the rhodopsin molecule where the beta-ionone ring is in a planar orientation to the retinal polyene chain.	Polyenes	220-227	rhodopsin	Homo sapiens	132-141
19505100-0	2009	Thermal decay of rhodopsin: role of hydrogen bonds in thermal isomerization of 11-cis retinal in the binding site and hydrolysis of protonated Schiff base.	Hydrogen	36-44	rhodopsin	Homo sapiens	17-26
19505100-0	2009	Thermal decay of rhodopsin: role of hydrogen bonds in thermal isomerization of 11-cis retinal in the binding site and hydrolysis of protonated Schiff base.	Schiff Bases	143-154	rhodopsin	Homo sapiens	17-26
19505100-2	2009	Using UV-vis spectroscopy and HPLC analysis, we have demonstrated that the thermal decay of rhodopsin involves both hydrolysis of the protonated Schiff base and thermal isomerization of 11-cis to all-trans retinal.	Schiff Bases	145-156	rhodopsin	Homo sapiens	92-101
19505100-5	2009	These results provide insight into understanding the critical role of an extensive hydrogen-bonding network on stabilizing the inactive state of rhodopsin and contribute to our current understanding of the low dark noise level of rhodopsin, which enables this specialized protein to function as an extremely sensitive biological light detector.	Hydrogen	83-91	rhodopsin	Homo sapiens	145-154
19505100-5	2009	These results provide insight into understanding the critical role of an extensive hydrogen-bonding network on stabilizing the inactive state of rhodopsin and contribute to our current understanding of the low dark noise level of rhodopsin, which enables this specialized protein to function as an extremely sensitive biological light detector.	Hydrogen	83-91	rhodopsin	Homo sapiens	230-239
19113950-10	2009	Photoreceptor differentiation in these cultures is confirmed by significant upregulation of rhodopsin and AaNat, an enzyme implicated in melatonin synthesis (immunohistochemistry and Western blot analysis).	Melatonin	137-146	rhodopsin	Homo sapiens	92-101
32688665-4	2009	Retinal, a beta-carotene derivative that is the chromophore of rhodopsin, acts not only as a sensory pigment, but also as an ion-pumping photochemical transducer.	beta Carotene	11-24	rhodopsin	Homo sapiens	63-72
19645663-0	2009	Aggregation of frog rhodopsin to oligomers and their dissociation to monomer: application of BN- and SDS-PAGE.	6-bromo-2-naphthyl sulfate	93-96	rhodopsin	Homo sapiens	20-29
19645663-0	2009	Aggregation of frog rhodopsin to oligomers and their dissociation to monomer: application of BN- and SDS-PAGE.	Sodium Dodecyl Sulfate	101-104	rhodopsin	Homo sapiens	20-29
19396177-1	2009	We demonstrate the site-directed incorporation of an IR-active amino acid, p-azido-L-phenylalanine (azidoF, 1), into the G protein-coupled receptor rhodopsin using amber codon suppression technology.	4-Azido-L-phenylalanine	75-98	rhodopsin	Homo sapiens	148-157
19396177-1	2009	We demonstrate the site-directed incorporation of an IR-active amino acid, p-azido-L-phenylalanine (azidoF, 1), into the G protein-coupled receptor rhodopsin using amber codon suppression technology.	azidof	100-106	rhodopsin	Homo sapiens	148-157
19334675-2	2009	However, we recently found that replacement of Ala178 with Arg in the E-F loop of proteorhodopsin (PR), an archaeal-type rhodopsin in marine bacteria, shifts the lambda(max) from 525 to 545 nm at neutral pH [Yoshitsugu, M., Shibata, M., Ikeda, D., Furutani, Y., and Kandori, H. (2008) Angew.	furutani	248-256	rhodopsin	Homo sapiens	88-97
19222791-1	2009	For the first time to our knowledge, X-ray absorption spectroscopy (XAS) has been used to investigate the environment of putative Zn(2+) binding sites in rhodopsin.	Zinc	130-136	rhodopsin	Homo sapiens	154-163
19348742-0	2009	Dynamics of the internal water molecules in squid rhodopsin.	Water	25-30	rhodopsin	Homo sapiens	50-59
19348742-5	2009	The crystal structure of the visual rhodopsin from squid solved recently suggests that a chain of water molecules extending from the retinal toward the cytoplasmic side of the protein may play a role in the signal transduction from the all-trans retinal geometry to the activated receptor.	Water	98-103	rhodopsin	Homo sapiens	36-45
19348742-6	2009	As a first step toward understanding the role of water in rhodopsin function, we performed a molecular dynamics simulation of squid rhodopsin embedded in a hydrated bilayer of polyunsaturated lipid molecules.	Water	49-54	rhodopsin	Homo sapiens	58-67
19190096-1	2009	KorA is a global repressor in RP4 which regulates cooperatively the expression of plasmid genes whose products are involved in replication, conjugative transfer and stable inheritance.	kora	0-4	rhodopsin	Homo sapiens	30-33
19090684-7	2009	In contrast, solvation in methanol retards the quenching process of the retinal protonated Schiff base (RPSB), the rhodopsin chromophore.	Methanol	26-34	rhodopsin	Homo sapiens	115-124
19090684-7	2009	In contrast, solvation in methanol retards the quenching process of the retinal protonated Schiff base (RPSB), the rhodopsin chromophore.	Schiff Bases	91-102	rhodopsin	Homo sapiens	115-124
19267871-0	2009	pH-dependent interaction of rhodopsin with cyanidin-3-glucoside.	cyanidin-3-o-glucoside	43-63	rhodopsin	Homo sapiens	28-37
19343351-2	2009	The RPE is responsible for a continuous supply of rhodopsin by the retinol cycle and blocking of light by its pigmentation to minimize light-induced oxidation of retinal lipids and proteins.	Vitamin A	67-74	rhodopsin	Homo sapiens	50-59
19192199-0	2009	pH-dependent interaction of rhodopsin with cyanidin-3-glucoside.	cyanidin-3-o-glucoside	43-63	rhodopsin	Homo sapiens	28-37
19192210-0	2009	Water-mediated spectral shifts in rhodopsin and bathorhodopsin.	Water	0-5	rhodopsin	Homo sapiens	34-43
19222791-4	2009	Our results demonstrate that Zn(2+) is intrinsically bound to rhodopsin and are compatible with the existence of an octahedral coordination involving six oxygen atoms in the first shell (average Zn-O distance of 2.08 A), and with a second coordination shell containing one or two phosphorus or sulfur atoms at an average distance of 2.81 A.	Zinc	29-31	rhodopsin	Homo sapiens	62-71
19267872-0	2009	Additive effects of chlorin e6 and metal ion binding on the thermal stability of rhodopsin in vitro.	phytochlorin	20-30	rhodopsin	Homo sapiens	81-90
19267872-0	2009	Additive effects of chlorin e6 and metal ion binding on the thermal stability of rhodopsin in vitro.	Metals	35-40	rhodopsin	Homo sapiens	81-90
19222795-9	2009	We found that in fluorescently labeled bR and rhodopsin the intensity of fluorescein and Atto647 increased upon formation of the key intermediates M and metarhodopsin-II, respectively, suggesting different surface properties compared to the dark state.	Fluorescein	73-84	rhodopsin	Homo sapiens	46-55
19267872-2	2009	Because Zn(2+) binds directly to the photoreceptor rhodopsin and alters its stability, the stabilization of rhodopsin may be key to prevention and treatment of retinal dysfunctions.	Zinc	8-10	rhodopsin	Homo sapiens	51-60
19222795-9	2009	We found that in fluorescently labeled bR and rhodopsin the intensity of fluorescein and Atto647 increased upon formation of the key intermediates M and metarhodopsin-II, respectively, suggesting different surface properties compared to the dark state.	atto647	89-96	rhodopsin	Homo sapiens	46-55
19267872-2	2009	Because Zn(2+) binds directly to the photoreceptor rhodopsin and alters its stability, the stabilization of rhodopsin may be key to prevention and treatment of retinal dysfunctions.	Zinc	8-10	rhodopsin	Homo sapiens	108-117
19267873-0	2009	Structural coupling of 11-cis-7-methyl-retinal and amino acids at the ligand binding pocket of rhodopsin.	7-methylretinal	23-46	rhodopsin	Homo sapiens	95-104
18643908-1	2009	Rhodopsin is one of the members of the G protein-coupled receptor family that can catalyze a GDP-GTP exchange reaction on the retinal G protein transducin (Gt) upon photon absorption.	gdp-gtp	93-100	rhodopsin	Homo sapiens	0-9
19325074-5	2009	Trace amines have been shown to act on one of a novel group of mammalian seven transmembrane spanning G protein-coupled receptors belonging to the rhodopsin superfamily, cloned in 2001.	Amines	6-12	rhodopsin	Homo sapiens	147-156
18827025-1	2009	Transitory binding between photoactivated rhodopsin (Rho* or Meta II) and the G protein transducin (Gt-GDP) is the first step in the visual signaling cascade.	gt-gdp	100-106	rhodopsin	Homo sapiens	42-51
18827025-2	2009	Light causes photoisomerization of the 11-cis-retinylidene chromophore in rhodopsin (Rho) to all-trans-retinylidene, which induces conformational changes that allow Gt-GDP to dock onto the Rho* surface.	11-cis-retinylidene	39-58	rhodopsin	Homo sapiens	74-83
18827025-2	2009	Light causes photoisomerization of the 11-cis-retinylidene chromophore in rhodopsin (Rho) to all-trans-retinylidene, which induces conformational changes that allow Gt-GDP to dock onto the Rho* surface.	all-trans-retinylidene	93-115	rhodopsin	Homo sapiens	74-83
18827025-2	2009	Light causes photoisomerization of the 11-cis-retinylidene chromophore in rhodopsin (Rho) to all-trans-retinylidene, which induces conformational changes that allow Gt-GDP to dock onto the Rho* surface.	gt-gdp	165-171	rhodopsin	Homo sapiens	74-83
19182802-1	2009	The second extracellular loop (EL2) of rhodopsin forms a cap over the binding site of its photoreactive 11-cis retinylidene chromophore.	11-cis retinylidene	104-123	rhodopsin	Homo sapiens	39-48
18819016-9	2009	The Special TRIPLE spectra were pH dependent, and at pH 8, the introduction of aspartate at L170 increased the spin density ratio, rho (L)/rho (M), to 6.1 while an aspartate at the symmetry related position, M199, decreased the ratio to 0.7 compared to the value of 2.1 for wild type.	Aspartic Acid	79-88	rhodopsin	Homo sapiens	131-142
19420982-0	2009	Lysophosphatidic acid stimulates cell growth by different mechanisms in SKOV-3 and Caov-3 ovarian cancer cells: distinct roles for Gi- and Rho-dependent pathways.	lysophosphatidic acid	0-21	rhodopsin	Homo sapiens	131-142
19035639-0	2008	Glutamic acid 181 is uncharged in dark-adapted visual rhodopsin.	Glutamic Acid	0-13	rhodopsin	Homo sapiens	54-63
19194506-1	2009	The G protein coupled receptor rhodopsin contains a pocket within its seven-transmembrane helix (TM) structure, which bears the inactivating 11-cis-retinal bound by a protonated Schiff-base to Lys296 in TM7.	Schiff Bases	178-189	rhodopsin	Homo sapiens	31-40
18997017-8	2008	In light of the conservation of the E(D)RY motif in rhodopsin-like GPCRs, protonation of this carboxylate also may serve a similar function in signal transduction of other members of this receptor family.	carboxylate	94-105	rhodopsin	Homo sapiens	52-61
18821775-3	2008	However, although carazolol and the 11- cis-retinylidene moiety of rhodopsin are situated in the same general binding pocket, the second extracellular (E2) loop structures are quite distinct.	11- cis-retinylidene	36-56	rhodopsin	Homo sapiens	67-76
19004797-2	2008	Here, we focus on a molecular switch designed by merging a conformationally locked diarylidene skeleton with a retinal-like Schiff base and capable of mimicking, in solution, different aspects of the transduction of the visual pigment Rhodopsin.	diarylidene	83-94	rhodopsin	Homo sapiens	235-244
19004797-2	2008	Here, we focus on a molecular switch designed by merging a conformationally locked diarylidene skeleton with a retinal-like Schiff base and capable of mimicking, in solution, different aspects of the transduction of the visual pigment Rhodopsin.	Schiff Bases	124-135	rhodopsin	Homo sapiens	235-244
18775703-2	2008	By combining sequence alignment, the rhodopsin crystal structure, and point mutation data on the beta2 adrenoreceptor (b2ar), we predict a (-)-epinephrine-bound computational model of the beta2 adrenoreceptor.	Epinephrine	139-154	rhodopsin	Homo sapiens	37-46
18487375-5	2008	The ability of mutant rhodopsin to activate transducin constitutively was monitored by measuring the catalytic exchange of bound GDP for radiolabeled [(35)S]GTPgammaS in transducin.	Guanosine Diphosphate	129-132	rhodopsin	Homo sapiens	22-31
18729405-9	2008	This ansatz is employed to study the influence of the protein polarizability on calculated optical properties of the protonated Schiff base of retinal in rhodopsin (Rh), bacterio-rhodopsin (bR), and pharaonis sensory rhodopsin II (psRII).	Schiff Bases	128-139	rhodopsin	Homo sapiens	154-163
18729405-9	2008	This ansatz is employed to study the influence of the protein polarizability on calculated optical properties of the protonated Schiff base of retinal in rhodopsin (Rh), bacterio-rhodopsin (bR), and pharaonis sensory rhodopsin II (psRII).	Schiff Bases	128-139	rhodopsin	Homo sapiens	179-188
18729405-9	2008	This ansatz is employed to study the influence of the protein polarizability on calculated optical properties of the protonated Schiff base of retinal in rhodopsin (Rh), bacterio-rhodopsin (bR), and pharaonis sensory rhodopsin II (psRII).	Schiff Bases	128-139	rhodopsin	Homo sapiens	179-188
18698306-3	2008	RESULTS: A probable high-penetrance disease-causing sequence variation in the rhodopsin gene, a heterozygous cytosine-to-thymine ACG>ATG nucleotide substitution resulting in a threonine to methionine (Thr17Met) amino acid change, was detected.	Cytosine	109-117	rhodopsin	Homo sapiens	78-87
18682040-1	2008	The interaction of the rod GTP binding protein, Transducin (G(t)), with bleached Rhodopsin (R(*)) was investigated by measuring radiolabeled guanine nucleotide binding to and release from soluble and/or membrane-bound G(t) by reconstituting G(t) containing bound GDP (G(t-)GDP) or the hydrolysis-resistant GTP analog guanylyl imidodiphosphate (G(t-)p[NH]ppG) with R* under physiological conditions.	Guanosine Triphosphate	27-30	rhodopsin	Homo sapiens	81-90
18682040-4	2008	When ROS containing bleached rhodopsin (R(*)) were centrifuged in low ionic strength buffer, G(t-) remained associated with the membrane fraction, whereas G(t-)GDP remained in the soluble fraction.	ros	5-8	rhodopsin	Homo sapiens	29-38
18682040-4	2008	When ROS containing bleached rhodopsin (R(*)) were centrifuged in low ionic strength buffer, G(t-) remained associated with the membrane fraction, whereas G(t-)GDP remained in the soluble fraction.	Guanosine Diphosphate	160-163	rhodopsin	Homo sapiens	29-38
18682040-6	2008	The results also suggest that G(t-), rather than G(t-)GDP, is the moiety which exhibits tight, "light-induced" binding to rhodopsin.	Guanosine Diphosphate	54-57	rhodopsin	Homo sapiens	122-131
18422873-1	2008	Rhodopsin, the visual pigment of the rod photoreceptor cell contains as its light-sensitive cofactor 11-cis retinal, which is bound by a protonated Schiff base between its aldehyde group and the Lys296 side chain of the apoprotein.	Schiff Bases	148-159	rhodopsin	Homo sapiens	0-9
18422873-1	2008	Rhodopsin, the visual pigment of the rod photoreceptor cell contains as its light-sensitive cofactor 11-cis retinal, which is bound by a protonated Schiff base between its aldehyde group and the Lys296 side chain of the apoprotein.	Aldehydes	172-180	rhodopsin	Homo sapiens	0-9
18422873-4	2008	Subsequently, rhodopsin"s dark state is regenerated by a complicated retinal metabolism, termed the retinoid cycle.	Retinoids	100-108	rhodopsin	Homo sapiens	14-23
19004627-2	2008	Perhaps one of the best studied examples is the function of the G-protein-coupled membrane receptor (GPCR) rhodopsin which is located in membranes with high content of phospholipids with polyunsaturated docosahexaenoic acid chains (DHA, 22:6n-3).	Phospholipids	168-181	rhodopsin	Homo sapiens	107-116
19004627-2	2008	Perhaps one of the best studied examples is the function of the G-protein-coupled membrane receptor (GPCR) rhodopsin which is located in membranes with high content of phospholipids with polyunsaturated docosahexaenoic acid chains (DHA, 22:6n-3).	polyunsaturated docosahexaenoic acid	187-223	rhodopsin	Homo sapiens	107-116
19004627-2	2008	Perhaps one of the best studied examples is the function of the G-protein-coupled membrane receptor (GPCR) rhodopsin which is located in membranes with high content of phospholipids with polyunsaturated docosahexaenoic acid chains (DHA, 22:6n-3).	Dihydroalprenolol	232-235	rhodopsin	Homo sapiens	107-116
19004627-3	2008	Technological advances enabled a more detailed study of structure and dynamics of DHA chains and their interaction with rhodopsin.	Dihydroalprenolol	82-85	rhodopsin	Homo sapiens	120-129
19004627-6	2008	The interface of rhodopsin has a small number of sites for tighter interaction with DHA.	Dihydroalprenolol	84-87	rhodopsin	Homo sapiens	17-26
19004627-9	2008	While some observations point at an involvement of continuum elastic properties of membranes in modulation of rhodopsin function, there is growing evidence for a role of weakly specific DHA-rhodopsin interactions.	Dihydroalprenolol	186-189	rhodopsin	Homo sapiens	190-199
18636747-6	2008	When photoreactive Tbetagamma was reconstituted with Talpha and light-activated rhodopsin (Rh*) in rod outer segment (ROS) membranes, the POG moiety interacted with not only Talpha and Tbeta but also Rh* and membrane phospholipids.	tbetagamma	19-29	rhodopsin	Homo sapiens	80-89
18636747-6	2008	When photoreactive Tbetagamma was reconstituted with Talpha and light-activated rhodopsin (Rh*) in rod outer segment (ROS) membranes, the POG moiety interacted with not only Talpha and Tbeta but also Rh* and membrane phospholipids.	tbeta	19-24	rhodopsin	Homo sapiens	80-89
18351404-11	2008	Rhodopsin has a negative torsion angle for the beta-ionone ring, whereas the change in the sign of the first peak in the experimental CD spectrum for bathorhodopsin could suggest that it has a positive torsion angle for the beta-ionone ring.	beta-ionone	47-58	rhodopsin	Homo sapiens	0-9
18351404-11	2008	Rhodopsin has a negative torsion angle for the beta-ionone ring, whereas the change in the sign of the first peak in the experimental CD spectrum for bathorhodopsin could suggest that it has a positive torsion angle for the beta-ionone ring.	beta-ionone	224-235	rhodopsin	Homo sapiens	0-9
18698306-3	2008	RESULTS: A probable high-penetrance disease-causing sequence variation in the rhodopsin gene, a heterozygous cytosine-to-thymine ACG>ATG nucleotide substitution resulting in a threonine to methionine (Thr17Met) amino acid change, was detected.	Thymine	120-128	rhodopsin	Homo sapiens	78-87
18698306-3	2008	RESULTS: A probable high-penetrance disease-causing sequence variation in the rhodopsin gene, a heterozygous cytosine-to-thymine ACG>ATG nucleotide substitution resulting in a threonine to methionine (Thr17Met) amino acid change, was detected.	acceleratory factor from growth hormone	129-132	rhodopsin	Homo sapiens	78-87
18698306-3	2008	RESULTS: A probable high-penetrance disease-causing sequence variation in the rhodopsin gene, a heterozygous cytosine-to-thymine ACG>ATG nucleotide substitution resulting in a threonine to methionine (Thr17Met) amino acid change, was detected.	Threonine	179-188	rhodopsin	Homo sapiens	78-87
18698306-3	2008	RESULTS: A probable high-penetrance disease-causing sequence variation in the rhodopsin gene, a heterozygous cytosine-to-thymine ACG>ATG nucleotide substitution resulting in a threonine to methionine (Thr17Met) amino acid change, was detected.	Methionine	192-202	rhodopsin	Homo sapiens	78-87
18511075-1	2008	Disruption of an interhelical salt bridge between the retinal protonated Schiff base linked to H7 and Glu113 on H3 is one of the decisive steps during activation of rhodopsin.	Schiff Bases	73-84	rhodopsin	Homo sapiens	165-174
18463093-3	2008	We determined the structure of squid rhodopsin at 3.7A resolution, which transduces signals through the G(q) protein to the phosphoinositol cascade.	phosphoinositol	124-139	rhodopsin	Homo sapiens	37-46
18511075-2	2008	Using previously established stabilization strategies, we engineered a stabilized E113Q counterion mutant that converted rhodopsin to a UV-absorbing photoreceptor with deprotonated Schiff base and allowed reconstitution into native-like lipid membranes.	Schiff Bases	181-192	rhodopsin	Homo sapiens	121-130
18490656-5	2008	For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain.	Hydroxylamine	84-93	rhodopsin	Homo sapiens	13-22
18490656-5	2008	For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain.	Hydroxylamine	84-93	rhodopsin	Homo sapiens	159-168
18490656-5	2008	For inactive rhodopsin, it was possible to find a globally minimized arrangement of nitroxide locations that simultaneously satisfied the crystal structure of rhodopsin (Protein Data Bank entry 1GZM), the experimentally measured distance data, and the known rotamers of the nitroxide side chain.	Hydroxylamine	274-283	rhodopsin	Homo sapiens	13-22
18067244-3	2008	The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).	Sulfhydryl Compounds	8-13	rhodopsin	Homo sapiens	79-88
18419122-0	2008	Inherent chirality dominates the visible/near-ultraviolet CD spectrum of rhodopsin.	Cadmium	58-60	rhodopsin	Homo sapiens	73-82
18419122-3	2008	We have calculated the contributions of these two mechanisms to the CD of rhodopsin.	Cadmium	68-70	rhodopsin	Homo sapiens	74-83
18419122-13	2008	Our results show that the visible/near-UV CD bands of rhodopsin are determined by the intrinsic chirality of the retPSB chromophore and that the contributions of coupling with the protein are significantly smaller for the alpha-band and negligible for the beta-band.	Cadmium	42-44	rhodopsin	Homo sapiens	54-63
17993461-5	2008	Rhodopsin containing Acp at three different sites was also purified in high yield (0.5-2 microg/10(7) cells) and reacted with fluorescein hydrazide in vitro to produce fluorescently labeled rhodopsin.	fluorescein hydrazide	126-147	rhodopsin	Homo sapiens	0-9
18067244-3	2008	The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).	Sulfhydryl Compounds	8-13	rhodopsin	Homo sapiens	90-92
18067244-3	2008	The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).	Cysteine	55-63	rhodopsin	Homo sapiens	79-88
18067244-3	2008	The new thiol-active reagents were labeled cytoplasmic cysteine 140 and 316 in rhodopsin (Rh), a G protein coupled receptor (GPCR).	Cysteine	55-63	rhodopsin	Homo sapiens	90-92
17999150-1	2008	High amino acid coverage labeling of the mammalian G protein coupled receptors (GPCR) rhodopsin was established with 15N and 15N/13C isotopes.	15n	117-120	rhodopsin	Homo sapiens	86-95
17935687-5	2008	Moreover, a few conserved interactions observed in the X-ray structure of rhodopsin, such as inter-helical sidechain-sidechain hydrogen bonds were accurately reproduced in the MD simulation.	Hydrogen	127-135	rhodopsin	Homo sapiens	74-83
17999150-1	2008	High amino acid coverage labeling of the mammalian G protein coupled receptors (GPCR) rhodopsin was established with 15N and 15N/13C isotopes.	15n	125-128	rhodopsin	Homo sapiens	86-95
17999150-1	2008	High amino acid coverage labeling of the mammalian G protein coupled receptors (GPCR) rhodopsin was established with 15N and 15N/13C isotopes.	13c	129-132	rhodopsin	Homo sapiens	86-95
17704167-6	2007	Values in the region of 50-110 A(2) are estimated for the effective cross-sectional shape changes on the insertion and conductance transitions of alamethicin, and on the activation of CTP:phosphocholine cytidylyltransferase or rhodopsin in lipid membranes.	Alamethicin	146-157	rhodopsin	Homo sapiens	227-236
17988684-1	2007	The structure in the extracellular, intradiscal domain of rhodopsin surrounding the Cys110-Cys187 disulfide bond has been shown to be important for correct folding of this receptor in vivo.	Disulfides	98-107	rhodopsin	Homo sapiens	58-67
18021739-13	2007	For rhodopsin, the strain energy and dynamics of retinal as established by 2H NMR are implicated in substituent control of activation.	Deuterium	75-77	rhodopsin	Homo sapiens	4-13
18052280-7	2007	Rhodopsin is the classic biochemical example where the protein (opsin)-bound protonated Schiff base of retinal displays a remarkable range of red-shifted absorptions modulated by the protein environment.	Schiff Bases	88-99	rhodopsin	Homo sapiens	0-9
18043798-4	2007	The large rho(X) (rho(nuc) = -3.1 to -3.4) and beta(X) (beta(nuc) = 1.1-1.2) values seem to be characteristic of the anilinolysis of phosphates and thiophosphates with the Cl leaving group.	Phosphates	133-143	rhodopsin	Homo sapiens	10-31
18043798-4	2007	The large rho(X) (rho(nuc) = -3.1 to -3.4) and beta(X) (beta(nuc) = 1.1-1.2) values seem to be characteristic of the anilinolysis of phosphates and thiophosphates with the Cl leaving group.	thiophosphoric acid	148-162	rhodopsin	Homo sapiens	10-31
18077356-2	2007	To study how these activation steps relate to each other, spin-labeled rhodopsin in solutions of dodecyl maltoside was used so that time-resolved TM6 motion and proton exchange could each be monitored as a function of pH and temperature after an activating light flash.	dodecyl maltoside	97-114	rhodopsin	Homo sapiens	71-80
17996895-5	2007	We show that opsin can also be directly purified in DMPC/DHPC bicelles to give correctly folded functional opsin, as shown by the ability to regenerate rhodopsin to approximately 70% yield.	Dimyristoylphosphatidylcholine	52-56	rhodopsin	Homo sapiens	152-161
17704167-6	2007	Values in the region of 50-110 A(2) are estimated for the effective cross-sectional shape changes on the insertion and conductance transitions of alamethicin, and on the activation of CTP:phosphocholine cytidylyltransferase or rhodopsin in lipid membranes.	Cytidine Triphosphate	184-187	rhodopsin	Homo sapiens	227-236
17918963-2	2007	The 11-cis retinoid chromophore, the inverse agonist holding rhodopsin inactive, is well-resolved.	11-cis retinoid	4-19	rhodopsin	Homo sapiens	61-70
17848565-6	2007	The complex of arrestin with hyperphosphorylated light-activated rhodopsin is less sensitive to high salt and appears to release retinal faster.	Salts	101-105	rhodopsin	Homo sapiens	65-74
17848565-7	2007	These data suggest that arrestin likely quenches rhodopsin signaling after the third phosphate is added by rhodopsin kinase.	Phosphates	85-94	rhodopsin	Homo sapiens	49-58
17918963-9	2007	However, unlike wild-type rhodopsin, the covalent linkage of the ligand can be attacked by hydroxylamine in the dark.	Hydroxylamine	91-104	rhodopsin	Homo sapiens	26-35
17719606-0	2007	Dynamic structure of retinylidene ligand of rhodopsin probed by molecular simulations.	retinylidene	21-33	rhodopsin	Homo sapiens	44-53
17825322-2	2007	The mutant was designed to form a disulfide bond between the N terminus and loop E3, which allows handling of opsin in detergent solution and increases thermal stability of rhodopsin by 10 deg.C.	Disulfides	34-43	rhodopsin	Homo sapiens	173-182
17935446-6	2007	The calculation of large systems as porphine in gas phase and a model of the complete retinal binding pocket in rhodopsin with 622 basis functions on 280 atoms at the quantum mechanical level show reliability leading to a resulting first allowed transition in 483 nm, very similar to the known experimental value of 500 nm of "dark state."	porphine	36-44	rhodopsin	Homo sapiens	112-121
17719606-4	2007	We analyzed a total of 23 independent, 100 ns all-atom molecular dynamics simulations of rhodopsin embedded in a lipid bilayer in the microcanonical (N,V,E) ensemble.	Lipid Bilayers	113-126	rhodopsin	Homo sapiens	89-98
17640664-0	2007	Structural analysis and dynamics of retinal chromophore in dark and meta I states of rhodopsin from 2H NMR of aligned membranes.	Deuterium	100-102	rhodopsin	Homo sapiens	85-94
17320349-2	2007	According to the currently prevailing model, constructed for rhodopsin and structurally related receptors, the arginine of the conserved "DRY" motif located at the cytosolic end of TM3 (R3.50) would interact with acidic residues in TM3 (D/E3.49) and TM6 (D/E6.30) at the resting state and shift out of this polar pocket upon agonist stimulation.	Arginine	111-119	rhodopsin	Homo sapiens	61-70
17693260-4	2007	Rhodopsin-laden vesicles in the OS axonemal cytoplasm fuse with nascent discs that are highly specialized with abundant phosphatidylinositol 3-phosphate (PI3P).	phosphatidylinositol 3-phosphate	120-152	rhodopsin	Homo sapiens	0-9
17880503-6	2007	Hypericin-like pigments are involved in some well-known photophobic reactions but other pigments (rhodopsin and flavins) are also involved in photoresponses in heterotrichs and other protists.	hypericin	0-9	rhodopsin	Homo sapiens	98-107
17658882-3	2007	We developed and employed coarse-grain molecular dynamics (CGMD) models to investigate the molecular basis of how the physicochemical properties of the phospholipid bilayer membrane affect self-assembly of visual rhodopsin, a prototypical GPCR.	Phospholipids	152-164	rhodopsin	Homo sapiens	213-222
17263515-8	2007	The minimum of T1(rho) assigned to the classical hopping of a hydrogen-bonded proton occurs in the same low-temperature regime in which the flattening of the temperature dependencies of T1 points to the dominance of incoherent tunneling.	Hydrogen	62-70	rhodopsin	Homo sapiens	15-22
17630977-8	2007	Based on homology with rhodopsin, Ile(104) is likely buried within inactive cAR1 and exposed to the cytoplasm upon activation.	Isoleucine	34-37	rhodopsin	Homo sapiens	23-32
17525222-0	2007	All-trans-retinol generated by rhodopsin photobleaching induces rapid recruitment of TIP47 to lipid droplets in the retinal pigment epithelium.	Vitamin A	0-17	rhodopsin	Homo sapiens	31-40
17397191-3	2007	Our results suggested a new 3D model of the rhodopsin-transducin complex that fully satisfied all available experimental data on site-directed mutagenesis of rhodopsin and Gtalphabetagamma as well as data from disulfide-linking experiments.	Disulfides	210-219	rhodopsin	Homo sapiens	44-53
17287211-2	2007	However, only in rhodopsin the retinylidene Schiff base bond to the apoprotein is eventually hydrolyzed, making a complex regeneration pathway necessary.	retinylidene schiff base	31-55	rhodopsin	Homo sapiens	17-26
17170198-3	2007	In this construct, free metal ions had no agonistic effect in accordance with the optimal geometry of the metal ion site in molecular models built over the inactive form of rhodopsin.	Metals	106-111	rhodopsin	Homo sapiens	173-182
17170198-8	2007	It is proposed that in rhodopsin-like 7TM receptors, small-molecule compounds in general act as agonists in a similar manner as here demonstrated with the artificial, metal ion site anchored chelators, by holding TM-VI bent inward.	Metals	167-172	rhodopsin	Homo sapiens	23-32
17132044-10	2007	The presence of two Alexa 633 molecules in each domain prevented binding of rhodopsin to arrestin.	alexa 633	20-29	rhodopsin	Homo sapiens	76-85
17578920-4	2007	Purified rhodopsin was prepared in dodecyl maltoside detergent solution.	dodecyl maltoside	35-52	rhodopsin	Homo sapiens	9-18
17646742-12	2007	Rhodopsin, necessary to the survival of the cell, cannot be renewed if retinol is not present, which causes a permanent bright light stimulation that is lethal for the photoreceptor.	Vitamin A	71-78	rhodopsin	Homo sapiens	0-9
17350285-7	2007	In all cases, the long chain polyoxyethylene detergent Brij78 was found to be highly effective for solubilization and milligram amounts of soluble protein could be generated in less than 24 h. Single particle analysis indicated a homogenous distribution of predominantly protein dimers of the cell-free expressed GPCR samples, with dimensions similar to the related rhodopsin.	Polyethylene Glycols	29-44	rhodopsin	Homo sapiens	366-375
17447762-1	2007	Rational redesign of the binding pocket of Cellular Retinoic Acid Binding Protein II (CRABPII) has provided a mutant that can bind retinal as a protonated Schiff base, mimicking the binding observed in rhodopsin.	Schiff Bases	155-166	rhodopsin	Homo sapiens	202-211
17576345-7	2007	As activation of native rhodopsin is known to involve deprotonation of the retinal Schiff base prior to formation of Meta II, this Meta I(SB) state may serve as a model for the structural characterization of a key transient species in the activation pathway of a prototypical G protein-coupled receptor.	Schiff Bases	83-94	rhodopsin	Homo sapiens	24-33
17176084-1	2006	Meta III is formed during the decay of rhodopsin"s active receptor state at neutral to alkaline pH by thermal isomerization of the retinal Schiff base C15=N bond, converting the ligand from all-trans 15-anti to all-trans 15-syn.	Retinaldehyde	131-138	rhodopsin	Homo sapiens	39-48
17358601-3	2007	The method is applied to the study of the photorelaxation of protonated formaldimine, a minimal model of the rhodopsin chromophore retinal.	formaldimine	72-84	rhodopsin	Homo sapiens	109-118
17173267-0	2007	The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors.	Water	21-26	rhodopsin	Homo sapiens	74-83
18051365-9	2007	The critical residue Ser86 (Asp 96 position in bacteriorhodopsin: proton donor) for the pumping activity was replaced with Asp, but it did not change the proton pumping activity of Anabaena rhodopsin.	Aspartic Acid	28-31	rhodopsin	Homo sapiens	55-64
18051365-9	2007	The critical residue Ser86 (Asp 96 position in bacteriorhodopsin: proton donor) for the pumping activity was replaced with Asp, but it did not change the proton pumping activity of Anabaena rhodopsin.	Aspartic Acid	123-126	rhodopsin	Homo sapiens	55-64
17177390-1	2006	Photoisomerization of the retinylidene chromophore of rhodopsin is the starting point in the vision cascade.	retinylidene	26-38	rhodopsin	Homo sapiens	54-63
17201384-0	2007	The role of the beta-ionone ring in the photochemical reaction of rhodopsin.	beta-ionone	16-27	rhodopsin	Homo sapiens	66-75
16800722-7	2007	Thus, the GDP-GTP exchange reaction, namely G-protein activation, by rhodopsin proceeds through at least two steps, with conformational changes in both rhodopsin and the G-protein.	gdp-gtp	10-17	rhodopsin	Homo sapiens	69-78
16800722-7	2007	Thus, the GDP-GTP exchange reaction, namely G-protein activation, by rhodopsin proceeds through at least two steps, with conformational changes in both rhodopsin and the G-protein.	gdp-gtp	10-17	rhodopsin	Homo sapiens	152-161
17176057-6	2006	We studied mutants of Leptosphaeria rhodopsin in which this aspartic acid was replaced with Glu or Asn using spectroscopy in the infrared and visible ranges.	Aspartic Acid	60-73	rhodopsin	Homo sapiens	36-45
17176057-6	2006	We studied mutants of Leptosphaeria rhodopsin in which this aspartic acid was replaced with Glu or Asn using spectroscopy in the infrared and visible ranges.	Glutamic Acid	92-95	rhodopsin	Homo sapiens	36-45
17177390-2	2006	A counterion switch mechanism that stabilizes the retinal protonated Schiff base (PSB) has been proposed to be an essential step in rhodopsin activation.	Schiff Bases	69-80	rhodopsin	Homo sapiens	132-141
17176084-1	2006	Meta III is formed during the decay of rhodopsin"s active receptor state at neutral to alkaline pH by thermal isomerization of the retinal Schiff base C15=N bond, converting the ligand from all-trans 15-anti to all-trans 15-syn.	Schiff Bases	139-150	rhodopsin	Homo sapiens	39-48
17012326-2	2006	Subsequently, all-trans retinal is released from the protein and reduced to all-trans retinol, the first step in the recycling of rhodopsin"s chromophore group through the series of reactions that constitute the visual cycle.	Vitamin A	86-93	rhodopsin	Homo sapiens	130-139
17177390-2	2006	A counterion switch mechanism that stabilizes the retinal protonated Schiff base (PSB) has been proposed to be an essential step in rhodopsin activation.	psb	82-85	rhodopsin	Homo sapiens	132-141
17012326-5	2006	Retinol produced after rhodopsin bleaching moved laterally in the disk membrane bilayer with an apparent diffusion coefficient of 2.5 +/- 0.3 micro m(2) s(-1).	Vitamin A	0-7	rhodopsin	Homo sapiens	23-32
17012328-5	2006	The fluorescence data correlate with the pK(a) for the MI-to-MII transition of rhodopsin, where deprotonation of the retinylidene Schiff base occurs in conjunction with helical movements leading to activation of the photoreceptor.	2-methyl-4-isothiazolin-3-one	55-57	rhodopsin	Homo sapiens	79-88
17167410-1	2006	PURPOSE: The purpose of our study was to determine whether arrestin residues previously predicted by computational modeling to interact with an aspartic acid substituted rhodopsin tail are actually involved in interactions with phospho-residues on the rhodopsin cytoplasmic tail.	Aspartic Acid	144-157	rhodopsin	Homo sapiens	170-179
17012328-5	2006	The fluorescence data correlate with the pK(a) for the MI-to-MII transition of rhodopsin, where deprotonation of the retinylidene Schiff base occurs in conjunction with helical movements leading to activation of the photoreceptor.	retinylidene schiff base	117-141	rhodopsin	Homo sapiens	79-88
17009319-6	2006	The model is found to correctly predict 93% of the experimentally observed effects in 119 rhodopsin mutants for which the decay rates and misfolding data have been measured, including a systematic analysis of Cys-->Ser replacements reported here.	Cysteine	209-212	rhodopsin	Homo sapiens	90-99
17177891-0	2006	Alternate binding mode of C-terminal phenethylamine analogs of G(t)alpha(340-350) to photoactivated rhodopsin.	phenethylamine	37-51	rhodopsin	Homo sapiens	100-109
17069872-2	2006	Our experiments, which employ a fluorescently labeled arrestin and rhodopsin solubilized in detergent/phospholipid micelles, indicate that arrestin can trap a population of retinal in the binding pocket with an absorbance characteristic of Meta II with the retinal Schiff-base intact.	Phospholipids	102-114	rhodopsin	Homo sapiens	67-76
17069872-2	2006	Our experiments, which employ a fluorescently labeled arrestin and rhodopsin solubilized in detergent/phospholipid micelles, indicate that arrestin can trap a population of retinal in the binding pocket with an absorbance characteristic of Meta II with the retinal Schiff-base intact.	Schiff Bases	265-276	rhodopsin	Homo sapiens	67-76
17010408-2	2006	A proposed cascade of molecular interactions, initiated by the rhodopsin C-terminal sequence VXPX-COOH during trafficking from the Golgi/TGN in retinal photoreceptors, is relayed by the small GTPase ARF4 to the downstream effectors.	Carbonic Acid	98-102	rhodopsin	Homo sapiens	63-72
17107108-1	2006	The neutral retinal Schiff base is connected to opsin in UV sensing pigments and in the blue-shifted meta-II signaling state of the rhodopsin photocycle.	Schiff Bases	20-31	rhodopsin	Homo sapiens	132-141
17010408-3	2006	One of the candidates for an ARF4 effector is the ARF-GAP ASAP1, which may function as a subunit of, or form a novel protein coat involved in trafficking from the TGN and in cytoskeletal remodeling, whose assembly is regulated by the binding of ARF4 to rhodopsin, and whose function is essential for the polarized trafficking toward the ROS.	ros	337-340	rhodopsin	Homo sapiens	253-262
17011013-1	2006	In the early steps of visual signal transduction, light-activated rhodopsin (R*) catalyzes GDP/GTP exchange in the heterotrimeric G protein (Galphabetagamma) transducin.	Guanosine Diphosphate	91-94	rhodopsin	Homo sapiens	66-75
17011013-1	2006	In the early steps of visual signal transduction, light-activated rhodopsin (R*) catalyzes GDP/GTP exchange in the heterotrimeric G protein (Galphabetagamma) transducin.	Guanosine Triphosphate	95-98	rhodopsin	Homo sapiens	66-75
17014882-2	2006	Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316.	Cysteine	163-171	rhodopsin	Homo sapiens	4-13
17014882-2	2006	Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316.	Cysteine	163-171	rhodopsin	Homo sapiens	153-162
17014882-2	2006	Metarhodopsin-II is stabilized when the N-terminus of the carboxyl (340-350) tail peptide of the alpha-subunit of transducin (Gtalpha) is crosslinked to rhodopsin cysteine 140 or the 340-350 peptide C-terminus of Gtalpha is crosslinked to rhodopsin cysteine 316.	Cysteine	249-257	rhodopsin	Homo sapiens	4-13
16968701-0	2006	Functional importance of the interhelical hydrogen bond between Thr204 and Tyr174 of sensory rhodopsin II and its alteration during the signaling process.	Hydrogen	42-50	rhodopsin	Homo sapiens	93-102
17059215-7	2006	Here, it is shown that both light-activated rhodopsin and the soluble mimic of R form trapped intermediate complexes with a GDP-released "empty pocket" state of the heterotrimer in the absence of GTP (or GTPgammaS).	Guanosine Diphosphate	124-127	rhodopsin	Homo sapiens	44-53
16553464-5	2006	The blue shift is similar to one induced by chloride ion in the E181Q rhodopsin mutant and may indicate that the ionization state of Glu181 in rhodopsin is affected by detergent.	Chlorides	44-52	rhodopsin	Homo sapiens	70-79
16553464-5	2006	The blue shift is similar to one induced by chloride ion in the E181Q rhodopsin mutant and may indicate that the ionization state of Glu181 in rhodopsin is affected by detergent.	Chlorides	44-52	rhodopsin	Homo sapiens	143-152
16906791-0	2006	Rhodopsin deactivation is affected by mutations of Tyrl91.	tyrl91	51-57	rhodopsin	Homo sapiens	0-9
17059215-7	2006	Here, it is shown that both light-activated rhodopsin and the soluble mimic of R form trapped intermediate complexes with a GDP-released "empty pocket" state of the heterotrimer in the absence of GTP (or GTPgammaS).	Guanosine 5'-O-(3-Thiotriphosphate)	196-199	rhodopsin	Homo sapiens	44-53
16925423-3	2006	Rhodopsin was regenerated using retinal that was (2)H-labeled at the C5, C9, or C13 methyl groups and was reconstituted with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine.	1-palmitoyl-2-oleoylphosphatidylcholine	125-173	rhodopsin	Homo sapiens	0-9
16962138-1	2006	The C-11=C-12 double bond of the retinylidene chromophore of rhodopsin holds a central position in its light-induced photoisomerization and hence the photosensory function of this visual pigment.	Carbon	4-5	rhodopsin	Homo sapiens	61-70
16962138-1	2006	The C-11=C-12 double bond of the retinylidene chromophore of rhodopsin holds a central position in its light-induced photoisomerization and hence the photosensory function of this visual pigment.	Carbon	9-10	rhodopsin	Homo sapiens	61-70
16962138-1	2006	The C-11=C-12 double bond of the retinylidene chromophore of rhodopsin holds a central position in its light-induced photoisomerization and hence the photosensory function of this visual pigment.	retinylidene	33-45	rhodopsin	Homo sapiens	61-70
16962138-2	2006	To probe the local environment of the HC-11=C-12H element we have prepared the 11-methyl and 12-methyl derivatives of 11-Z retinal and incorporated these into opsin to generate the rhodopsin analogs 11-methyl and 12-methyl rhodopsin.	Carbon	39-40	rhodopsin	Homo sapiens	181-190
16956299-1	2006	The low-lying excited states of a solution in alcohol of a five-double-bond model of the rhodopsin protein chromophore, the protonated 11-cis-retinal Schiff base (PSB11), are studied theoretically.	Alcohols	46-53	rhodopsin	Homo sapiens	89-98
16956299-1	2006	The low-lying excited states of a solution in alcohol of a five-double-bond model of the rhodopsin protein chromophore, the protonated 11-cis-retinal Schiff base (PSB11), are studied theoretically.	11-cis-retinal schiff base	135-161	rhodopsin	Homo sapiens	89-98
16956299-1	2006	The low-lying excited states of a solution in alcohol of a five-double-bond model of the rhodopsin protein chromophore, the protonated 11-cis-retinal Schiff base (PSB11), are studied theoretically.	8-ethyl-4-methyl-2-phenyl-4,5,7,8-tetrahydro-1H-imidazo(2,1-i)purin-5-one	163-168	rhodopsin	Homo sapiens	89-98
16895417-0	2006	Modulating rhodopsin receptor activation by altering the pKa of the retinal Schiff base.	Schiff Bases	76-87	rhodopsin	Homo sapiens	11-20
16895417-2	2006	Activation of rhodopsin involves two pH-dependent steps: proton uptake at a conserved cytoplasmic motif between TM helices 3 and 6, and disruption of a salt bridge between a protonated Schiff base (PSB) and its carboxylate counterion in the transmembrane core of the receptor.	Schiff Bases	185-196	rhodopsin	Homo sapiens	14-23
16895417-2	2006	Activation of rhodopsin involves two pH-dependent steps: proton uptake at a conserved cytoplasmic motif between TM helices 3 and 6, and disruption of a salt bridge between a protonated Schiff base (PSB) and its carboxylate counterion in the transmembrane core of the receptor.	psb	198-201	rhodopsin	Homo sapiens	14-23
16895417-2	2006	Activation of rhodopsin involves two pH-dependent steps: proton uptake at a conserved cytoplasmic motif between TM helices 3 and 6, and disruption of a salt bridge between a protonated Schiff base (PSB) and its carboxylate counterion in the transmembrane core of the receptor.	carboxylate	211-222	rhodopsin	Homo sapiens	14-23
16567806-4	2006	In molecular models built over the backbone conformation of the inactive rhodopsin structure, the heavy atoms that coordinate the metal ion were located too far away from each other to form high affinity metal ion sites in both the bidentate and potential tridentate settings.	Metals	130-135	rhodopsin	Homo sapiens	73-82
16453309-2	2006	In the photoreceptor rhodopsin, and possibly other rhodopsin-like GPCRs, protonation of a carboxylic acid in the conserved E(D)RY motif at the cytosolic end of transmembrane helix 3 (TM3) is coupled to receptor activation.	Carboxylic Acids	90-105	rhodopsin	Homo sapiens	21-30
16453309-2	2006	In the photoreceptor rhodopsin, and possibly other rhodopsin-like GPCRs, protonation of a carboxylic acid in the conserved E(D)RY motif at the cytosolic end of transmembrane helix 3 (TM3) is coupled to receptor activation.	Carboxylic Acids	90-105	rhodopsin	Homo sapiens	51-60
16675451-2	2006	It prevents premature phosphorylation of rhodopsin until the opening of cGMP-gated ion channels causes a decrease in intracellular calcium levels, signaling completion of the light response.	Cyclic GMP	72-76	rhodopsin	Homo sapiens	41-50
16675451-2	2006	It prevents premature phosphorylation of rhodopsin until the opening of cGMP-gated ion channels causes a decrease in intracellular calcium levels, signaling completion of the light response.	Calcium	131-138	rhodopsin	Homo sapiens	41-50
16675451-3	2006	This calcium depletion causes release of recoverin from rhodopsin kinase, freeing the kinase to phosphorylate rhodopsin and to terminate the light response.	Calcium	5-12	rhodopsin	Homo sapiens	56-65
16567806-4	2006	In molecular models built over the backbone conformation of the inactive rhodopsin structure, the heavy atoms that coordinate the metal ion were located too far away from each other to form high affinity metal ion sites in both the bidentate and potential tridentate settings.	Metals	204-209	rhodopsin	Homo sapiens	73-82
16731977-5	2006	Previously, we reported the development of an HEK293S tetracycline-inducible system for high-level expression of rhodopsin.	Tetracycline	54-66	rhodopsin	Homo sapiens	113-122
16756308-2	2006	The transferred NOE NMR structure of the G(t)alpha(340-350) peptide bound to photoactivated rhodopsin (R*) geometrically suggests a cation-pi interaction stabilizing the structure between the epsilon-amine of Lys341 and the aromatic ring of the C-terminal residue, Phe350.	noe	16-19	rhodopsin	Homo sapiens	92-101
16756308-2	2006	The transferred NOE NMR structure of the G(t)alpha(340-350) peptide bound to photoactivated rhodopsin (R*) geometrically suggests a cation-pi interaction stabilizing the structure between the epsilon-amine of Lys341 and the aromatic ring of the C-terminal residue, Phe350.	epsilon-amine	192-205	rhodopsin	Homo sapiens	92-101
16595170-1	2006	Most members of the large family of rhodopsin-like G-protein-coupled receptors possess an evolutionarily conserved Asp-Arg-Tyr (DRY) motif in the C-terminal region of the third transmembrane domain.	Asp-Arg-Tyr	115-126	rhodopsin	Homo sapiens	36-45
16682009-4	2006	Indeed, relative energies of the R* state were significantly lower than that of the R state for the rhodopsin mutants G90D/M257Y and E113Q/M257Y (strong CAMs), but not for G90D, E113Q, and M257Y (not CAMs).	cams	153-157	rhodopsin	Homo sapiens	100-109
16682009-4	2006	Indeed, relative energies of the R* state were significantly lower than that of the R state for the rhodopsin mutants G90D/M257Y and E113Q/M257Y (strong CAMs), but not for G90D, E113Q, and M257Y (not CAMs).	cams	200-204	rhodopsin	Homo sapiens	100-109
16565146-8	2006	In most of the receptors coupling to Gs family, the occurrence of proline on the position corresponding to the 170th residue on rhodopsin is rare.	Proline	66-73	rhodopsin	Homo sapiens	128-137
16626818-1	2006	An insertion of residues in the third extracellular loop and a disulfide bond linking this loop to the N-terminal domain were identified in a structural model of a G-protein coupled receptor specific to angiotensin II (AT1 receptor), built in homology to the seven-transmembrane-helix bundle of rhodopsin.	Disulfides	63-72	rhodopsin	Homo sapiens	295-304
16671691-1	2006	Recent NMR experiments and molecular dynamics simulations have indicated that rhodopsin is preferentially solvated by omega-3 fatty acids compared to saturated chains.	Fatty Acids, Omega-3	118-137	rhodopsin	Homo sapiens	78-87
16634635-1	2006	Nitroxide sensors were placed in rhodopsin at sites 140, 227, 250, and 316 to monitor the dynamics and conformation of the receptor at the cytoplasmic surface in solutions of dodecyl maltoside (DM), digitonin, and phospholipid bilayers of two compositions.	Hydroxylamine	0-9	rhodopsin	Homo sapiens	33-42
16414074-2	2006	We present solid-state magic angle spinning NMR measurements of rhodopsin and the metarhodopsin II intermediate that support the proposal that interaction of Trp265(6.48) with the retinal chromophore is responsible for stabilizing an inactive conformation in the dark, and that motion of the beta-ionone ring allows Trp265(6.48) and transmembrane helix H6 to adopt active conformations in the light.	beta-ionone	292-303	rhodopsin	Homo sapiens	64-73
16547139-0	2006	A role for direct interactions in the modulation of rhodopsin by omega-3 polyunsaturated lipids.	omega-3 polyunsaturated lipids	65-95	rhodopsin	Homo sapiens	52-61
16547139-1	2006	Rhodopsin, the G protein-coupled receptor primarily responsible for sensing light, is found in an environment rich in polyunsaturated lipid chains and cholesterol.	polyunsaturated lipid	118-139	rhodopsin	Homo sapiens	0-9
16547139-1	2006	Rhodopsin, the G protein-coupled receptor primarily responsible for sensing light, is found in an environment rich in polyunsaturated lipid chains and cholesterol.	Cholesterol	151-162	rhodopsin	Homo sapiens	0-9
16547139-2	2006	Biophysical experiments have shown that lipid unsaturation and cholesterol both have significant effects on rhodopsin"s stability and function; omega-3 polyunsaturated chains, such as docosahexaenoic acid (DHA), destabilize rhodopsin and enhance the kinetics of the photocycle, whereas cholesterol has the opposite effect.	Cholesterol	63-74	rhodopsin	Homo sapiens	108-117
16547139-2	2006	Biophysical experiments have shown that lipid unsaturation and cholesterol both have significant effects on rhodopsin"s stability and function; omega-3 polyunsaturated chains, such as docosahexaenoic acid (DHA), destabilize rhodopsin and enhance the kinetics of the photocycle, whereas cholesterol has the opposite effect.	Cholesterol	63-74	rhodopsin	Homo sapiens	224-233
16547139-2	2006	Biophysical experiments have shown that lipid unsaturation and cholesterol both have significant effects on rhodopsin"s stability and function; omega-3 polyunsaturated chains, such as docosahexaenoic acid (DHA), destabilize rhodopsin and enhance the kinetics of the photocycle, whereas cholesterol has the opposite effect.	omega-3	144-151	rhodopsin	Homo sapiens	108-117
16547139-2	2006	Biophysical experiments have shown that lipid unsaturation and cholesterol both have significant effects on rhodopsin"s stability and function; omega-3 polyunsaturated chains, such as docosahexaenoic acid (DHA), destabilize rhodopsin and enhance the kinetics of the photocycle, whereas cholesterol has the opposite effect.	Docosahexaenoic Acids	206-209	rhodopsin	Homo sapiens	108-117
16547139-2	2006	Biophysical experiments have shown that lipid unsaturation and cholesterol both have significant effects on rhodopsin"s stability and function; omega-3 polyunsaturated chains, such as docosahexaenoic acid (DHA), destabilize rhodopsin and enhance the kinetics of the photocycle, whereas cholesterol has the opposite effect.	Cholesterol	286-297	rhodopsin	Homo sapiens	108-117
16547139-4	2006	By analyzing the results of 26 independent 100-ns simulations of dark-adapted rhodopsin, we found that DHA routinely forms tight associations with the protein in a small number of specific locations qualitatively different from the nonspecific interactions made by saturated chains and cholesterol.	Docosahexaenoic Acids	103-106	rhodopsin	Homo sapiens	78-87
16547139-6	2006	These results are consistent with recent NMR work, which proposes that rhodopsin binds DHA, and they suggest a molecular rationale for DHA"s effects on rhodopsin stability and kinetics.	Docosahexaenoic Acids	87-90	rhodopsin	Homo sapiens	71-80
16547139-6	2006	These results are consistent with recent NMR work, which proposes that rhodopsin binds DHA, and they suggest a molecular rationale for DHA"s effects on rhodopsin stability and kinetics.	Docosahexaenoic Acids	135-138	rhodopsin	Homo sapiens	152-161
16428804-0	2006	Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent.	Phospholipids	52-65	rhodopsin	Homo sapiens	21-30
16428804-0	2006	Dynamics of arrestin-rhodopsin interactions: acidic phospholipids enable binding of arrestin to purified rhodopsin in detergent.	Phospholipids	52-65	rhodopsin	Homo sapiens	105-114
16428804-1	2006	We report that acidic phospholipids can restore the binding of visual arrestin to purified rhodopsin solubilized in n-dodecyl-beta-d-maltopyranoside.	Phospholipids	22-35	rhodopsin	Homo sapiens	91-100
16428804-1	2006	We report that acidic phospholipids can restore the binding of visual arrestin to purified rhodopsin solubilized in n-dodecyl-beta-d-maltopyranoside.	dodecyl maltopyranoside	116-148	rhodopsin	Homo sapiens	91-100
16551073-0	2006	Accurate measurements of 13C-13C J-couplings in the rhodopsin chromophore by double-quantum solid-state NMR spectroscopy.	13c	25-28	rhodopsin	Homo sapiens	52-61
16551073-0	2006	Accurate measurements of 13C-13C J-couplings in the rhodopsin chromophore by double-quantum solid-state NMR spectroscopy.	13c	29-32	rhodopsin	Homo sapiens	52-61
16551073-1	2006	A new double-quantum solid-state NMR pulse sequence is presented and used to measure one-bond 13C-13C J-couplings in a set of 13C2-labeled rhodopsin isotopomers.	13c	94-97	rhodopsin	Homo sapiens	139-148
16551073-1	2006	A new double-quantum solid-state NMR pulse sequence is presented and used to measure one-bond 13C-13C J-couplings in a set of 13C2-labeled rhodopsin isotopomers.	13c	98-101	rhodopsin	Homo sapiens	139-148
16414074-6	2006	This motion, in conjunction with the Trp-C19 contact, implies that the Trp265(6.48) side-chain moves significantly upon rhodopsin activation.	Tryptophan	37-40	rhodopsin	Homo sapiens	120-129
16038577-4	2006	Correlation of the relative conversion of the oximes with Hammett parameters shows that radical effects dominate for the meta-substituted acetophenone oximes (rho(rad)/rho(pol) = 5.4; r2 = 0.93), whereas the para-substituted oximes are influenced almost equally by radical and ionic effects (rho(rad)/rho(pol) = -1.1; r2 = 0.98).	Oximes	46-52	rhodopsin	Homo sapiens	292-316
16460036-4	2006	Here we show that illuminated rhodopsin is essential for development of the AMP-PNP incubation effect.	Adenosine Monophosphate	76-79	rhodopsin	Homo sapiens	30-39
16460036-7	2006	It is concluded that illuminated rhodopsin is involved in retGC activation in two ways: to initiate the ATP incubation effect for preparation of retGC activation as shown here and to reduce the Ca2+ concentrations through cGMP phosphodiesterase activation as already known.	Adenosine Triphosphate	104-107	rhodopsin	Homo sapiens	33-42
16430225-5	2006	From the analyses of the C=NH and C=ND stretching bands, we conclude that the displacement of the Schiff base region upon photoisomerization of the chromophore is restricted, as is the case for rhodopsin.	Schiff Bases	98-109	rhodopsin	Homo sapiens	194-203
16384706-0	2006	Cyclodextrin retinylidene: a biomimetic kinetic trap model for rhodopsin.	cyclodextrin retinylidene	0-25	rhodopsin	Homo sapiens	63-72
16384706-1	2006	All trans retinal was attached to both the primary face and the secondary face of beta-cyclodextrin via a Schiff base linkage, analogous to that in rhodopsin.	betadex	82-99	rhodopsin	Homo sapiens	148-157
16368093-2	2006	In rhodopsin, Glu113 serves as a counterion to the positively charged protonated Schiff base formed by 11-cis retinal attached to Lys296.	Schiff Bases	81-92	rhodopsin	Homo sapiens	3-12
16621670-5	2006	Since rhodopsin, the major integral protein of rod outer segments is surrounded by phospholipids highly enriched in docosahexaenoic acid, the author proposes the outer segments of photoreceptors as an excellent model to study lipid peroxidation using the chemiluminescence assay since these membranes contain the highest concentration of polyunsaturated fatty acids of any vertebrate tissue and are highly susceptible to oxidative damage.	Phospholipids	83-96	rhodopsin	Homo sapiens	6-15
16038577-4	2006	Correlation of the relative conversion of the oximes with Hammett parameters shows that radical effects dominate for the meta-substituted acetophenone oximes (rho(rad)/rho(pol) = 5.4; r2 = 0.93), whereas the para-substituted oximes are influenced almost equally by radical and ionic effects (rho(rad)/rho(pol) = -1.1; r2 = 0.98).	ODEPA	121-125	rhodopsin	Homo sapiens	292-316
16038577-4	2006	Correlation of the relative conversion of the oximes with Hammett parameters shows that radical effects dominate for the meta-substituted acetophenone oximes (rho(rad)/rho(pol) = 5.4; r2 = 0.93), whereas the para-substituted oximes are influenced almost equally by radical and ionic effects (rho(rad)/rho(pol) = -1.1; r2 = 0.98).	substituted	126-137	rhodopsin	Homo sapiens	292-316
16038577-4	2006	Correlation of the relative conversion of the oximes with Hammett parameters shows that radical effects dominate for the meta-substituted acetophenone oximes (rho(rad)/rho(pol) = 5.4; r2 = 0.93), whereas the para-substituted oximes are influenced almost equally by radical and ionic effects (rho(rad)/rho(pol) = -1.1; r2 = 0.98).	acetophenone oximes	138-157	rhodopsin	Homo sapiens	292-316
16199504-8	2005	Results of these calculations are in good agreement with the x-ray data available for the dark-adapted rhodopsin as well as with the available experimental biophysical data on the disulfide-linked mutants of rhodopsin.	Disulfides	180-189	rhodopsin	Homo sapiens	103-112
16199504-8	2005	Results of these calculations are in good agreement with the x-ray data available for the dark-adapted rhodopsin as well as with the available experimental biophysical data on the disulfide-linked mutants of rhodopsin.	Disulfides	180-189	rhodopsin	Homo sapiens	208-217
16027155-3	2005	Here, we demonstrate that cis-acyclic retinals, lacking four carbon atoms of the ring, can activate rhodopsin.	Carbon	61-67	rhodopsin	Homo sapiens	100-109
16103122-6	2005	However, surprisingly, we found that alphaT*(R238E) effectively blocked rhodopsin-catalyzed GDP-GTP exchange on alphaT*, as well as rhodopsin-stimulated phosphodiesterase activity.	gdp-gtp	92-99	rhodopsin	Homo sapiens	72-81
16285719-0	2005	Strongly hydrogen-bonded water molecule present near the retinal chromophore of Leptosphaeria rhodopsin, the bacteriorhodopsin-like proton pump from a eukaryote.	Hydrogen	9-17	rhodopsin	Homo sapiens	94-103
16285719-0	2005	Strongly hydrogen-bonded water molecule present near the retinal chromophore of Leptosphaeria rhodopsin, the bacteriorhodopsin-like proton pump from a eukaryote.	Water	25-30	rhodopsin	Homo sapiens	94-103
16129667-3	2005	Here, we show that ChiT can be functionally reconstituted with G(betagamma) as assessed by aluminum fluoride-dependent changes in intrinsic tryptophan fluorescence and light-activated rhodopsin-catalyzed guanine nucleotide exchange.	aluminum fluoride	91-108	rhodopsin	Homo sapiens	184-193
16129667-3	2005	Here, we show that ChiT can be functionally reconstituted with G(betagamma) as assessed by aluminum fluoride-dependent changes in intrinsic tryptophan fluorescence and light-activated rhodopsin-catalyzed guanine nucleotide exchange.	Guanine Nucleotides	204-222	rhodopsin	Homo sapiens	184-193
16120006-7	2005	Efficient retinoid cycle leads to rapid regeneration of rhodopsin, which may result in ATR release from the opsin "exit site" before its enzymatic reduction to all-trans-retinol.	Retinoids	10-18	rhodopsin	Homo sapiens	56-65
16120006-7	2005	Efficient retinoid cycle leads to rapid regeneration of rhodopsin, which may result in ATR release from the opsin "exit site" before its enzymatic reduction to all-trans-retinol.	Vitamin A	160-177	rhodopsin	Homo sapiens	56-65
16085771-0	2005	The hydroxylamine reaction of sensory rhodopsin II: light-induced conformational alterations with C13=C14 nonisomerizable pigment.	Hydroxylamine	4-17	rhodopsin	Homo sapiens	38-47
16085771-3	2005	Similarly to other retinal proteins, sensory rhodopsin II undergoes a bleaching reaction with hydroxylamine in the dark which is markedly catalyzed by light.	Hydroxylamine	94-107	rhodopsin	Homo sapiens	45-54
16173715-1	2005	We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR).	mono- and polyunsaturated phosphatidylcholines	30-76	rhodopsin	Homo sapiens	82-91
16170112-5	2005	RESULTS: Mutation screening identified five different rhodopsin mutations including three novel mutations: Ser176Phe, Arg314fs16, and Val20Gly and two missense mutations, Pro215Leu and Thr289Pro, that were only reported once in a mutation report.	arg314fs16	118-128	rhodopsin	Homo sapiens	54-63
16173715-1	2005	We studied the interaction of mono- and polyunsaturated phosphatidylcholines with rhodopsin by 1H NMR saturation transfer difference spectroscopy with magic angle spinning (STD-MAS NMR).	Hydrogen	95-97	rhodopsin	Homo sapiens	82-91
16173715-2	2005	The results indicate a strong preference for interaction of rhodopsin with the polyunsaturated docosahexaenoic acid.	polyunsaturated docosahexaenoic acid	79-115	rhodopsin	Homo sapiens	60-69
15840841-0	2005	Cysteine 2.59(89) in the second transmembrane domain of human CB2 receptor is accessible within the ligand binding crevice: evidence for possible CB2 deviation from a rhodopsin template.	Cysteine	0-8	rhodopsin	Homo sapiens	167-176
16110519-1	2005	The structure and dynamics of the retinal chromophore of rhodopsin are investigated systematically in different environments (vacuum, methanol solution, and protein binding pocket) and with different computational approaches (classical, quantum, and hybrid quantum mechanics/molecular mechanics (QM/MM) descriptions).	Methanol	134-142	rhodopsin	Homo sapiens	57-66
15980173-6	2005	Our results showed that increased rhodopsin packing density led to reduced membrane dynamics revealed by the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene, increased phospholipid acyl chain packing, and reduced rhodopsin activation, yet it had minimal impact on the structural stability of rhodopsin.	Diphenylhexatriene	127-156	rhodopsin	Homo sapiens	34-43
15980173-6	2005	Our results showed that increased rhodopsin packing density led to reduced membrane dynamics revealed by the fluorescent probe 1,6-diphenyl-1,3,5-hexatriene, increased phospholipid acyl chain packing, and reduced rhodopsin activation, yet it had minimal impact on the structural stability of rhodopsin.	Phospholipids	168-180	rhodopsin	Homo sapiens	34-43
16986276-1	2005	Rod photoreceptors are activated by light through activation of a cascade that includes the G protein-coupled receptor rhodopsin, the G protein transducin, its effector cyclic guanosine monophosphate (cGMP) phosphodiesterase and the second messengers cGMP and Ca2+.	Cyclic GMP	201-205	rhodopsin	Homo sapiens	119-128
16986276-1	2005	Rod photoreceptors are activated by light through activation of a cascade that includes the G protein-coupled receptor rhodopsin, the G protein transducin, its effector cyclic guanosine monophosphate (cGMP) phosphodiesterase and the second messengers cGMP and Ca2+.	Cyclic GMP	251-255	rhodopsin	Homo sapiens	119-128
16986276-6	2005	The model shows that, upon activation of a single rhodopsin, changes of the second messengers cGMP and Ca2+ are local about the particular activated disc.	Cyclic GMP	94-98	rhodopsin	Homo sapiens	50-59
16039844-0	2005	Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin.	Docosahexaenoic Acids	14-34	rhodopsin	Homo sapiens	92-101
16039844-3	2005	The G-protein-coupled receptor rhodopsin and docosahexaenoic acid, the dominant fatty acid in the retinal membrane, provide the best-studied example of protein function being influenced by lipid environment.	Fatty Acids	80-90	rhodopsin	Homo sapiens	31-40
15919078-3	2005	The resonance Raman spectrum provides evidence for a strongly hydrogen-bonded Schiff base like in mammalian rhodopsin but unlike to the homologous pSRII from Natronobacterium pharaonis.	Hydrogen	62-70	rhodopsin	Homo sapiens	108-117
15919078-3	2005	The resonance Raman spectrum provides evidence for a strongly hydrogen-bonded Schiff base like in mammalian rhodopsin but unlike to the homologous pSRII from Natronobacterium pharaonis.	Schiff Bases	78-89	rhodopsin	Homo sapiens	108-117
15855270-1	2005	Ab initio multi-reference second-order perturbation theory computations are used to explore the photochemical behavior of two ion pairs constituted by a chloride counterion interacting with either a rhodopsin or bacteriorhodopsin chromophore model (i.e., the 4-cis-gamma-methylnona-2,4,6,8-tetraeniminium and all-trans-nona-2,4,6,8-tetraeniminium cations, respectively).	Chlorides	153-161	rhodopsin	Homo sapiens	199-208
15870200-2	2005	Despite evidence that much of this fluorescent material may originate as inadvertent products of the retinoid cycle, the enzymatic pathway by which the 11-cis-retinal chromophore of rhodopsin is generated, the only fluorophores of the RPE to be characterized as yet have been A2E and its isomers.	Retinoids	101-109	rhodopsin	Homo sapiens	182-191
15722344-10	2005	As residues Leu-2.46, Asp-2.50, and Asn-7.49 are strongly conserved, this molecular mechanism of TSHr activation can be extended to other members of the rhodopsin-like family of G protein-coupled receptors.	Asparagine	36-39	rhodopsin	Homo sapiens	153-162
15796514-1	2005	We present a 118-ns molecular dynamics simulation of rhodopsin embedded in a bilayer composed of a 2:2:1 mixture of 1-stearoyl-2-docosahexaenoyl-phosphatidylcholine (SDPC), 1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine (SDPE), and cholesterol, respectively.	1-stearoyl-2-docosahexaenoyl-phosphatidylcholine	116-164	rhodopsin	Homo sapiens	53-62
15839640-6	2005	We have used SIDY to probe the ligand-protein binding surface between a uniformly isotopically labeled ligand cofactor, U-13C20-11-cis-retinal, and its binding site in rhodopsin (Rho), an unlabeled, membrane-embedded G-protein coupled receptor (GPCR).	u-13c20-11	120-130	rhodopsin	Homo sapiens	168-177
15769471-0	2005	Changes in interhelical hydrogen bonding upon rhodopsin activation.	Hydrogen	24-32	rhodopsin	Homo sapiens	46-55
15796514-1	2005	We present a 118-ns molecular dynamics simulation of rhodopsin embedded in a bilayer composed of a 2:2:1 mixture of 1-stearoyl-2-docosahexaenoyl-phosphatidylcholine (SDPC), 1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine (SDPE), and cholesterol, respectively.	sdpc	166-170	rhodopsin	Homo sapiens	53-62
15769471-1	2005	Hydrogen bonding interactions between transmembrane helices stabilize the visual pigment rhodopsin in an inactive conformation in the dark.	Hydrogen	0-8	rhodopsin	Homo sapiens	89-98
15769471-2	2005	The crystal structure of rhodopsin has previously revealed that Glu122 and Trp126 on transmembrane helix H3 form a complex hydrogen bonding network with Tyr206 and His211 on H5, while the indole nitrogen of Trp265 on H6 forms a water-mediated hydrogen bond with Asn302 on H7.	Hydrogen	123-131	rhodopsin	Homo sapiens	25-34
15769471-2	2005	The crystal structure of rhodopsin has previously revealed that Glu122 and Trp126 on transmembrane helix H3 form a complex hydrogen bonding network with Tyr206 and His211 on H5, while the indole nitrogen of Trp265 on H6 forms a water-mediated hydrogen bond with Asn302 on H7.	Nitrogen	195-203	rhodopsin	Homo sapiens	25-34
15769471-2	2005	The crystal structure of rhodopsin has previously revealed that Glu122 and Trp126 on transmembrane helix H3 form a complex hydrogen bonding network with Tyr206 and His211 on H5, while the indole nitrogen of Trp265 on H6 forms a water-mediated hydrogen bond with Asn302 on H7.	Water	228-233	rhodopsin	Homo sapiens	25-34
15796514-1	2005	We present a 118-ns molecular dynamics simulation of rhodopsin embedded in a bilayer composed of a 2:2:1 mixture of 1-stearoyl-2-docosahexaenoyl-phosphatidylcholine (SDPC), 1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine (SDPE), and cholesterol, respectively.	1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine	173-226	rhodopsin	Homo sapiens	53-62
15769471-2	2005	The crystal structure of rhodopsin has previously revealed that Glu122 and Trp126 on transmembrane helix H3 form a complex hydrogen bonding network with Tyr206 and His211 on H5, while the indole nitrogen of Trp265 on H6 forms a water-mediated hydrogen bond with Asn302 on H7.	Hydrogen	243-251	rhodopsin	Homo sapiens	25-34
15769471-3	2005	Here, we use solid-state magic angle spinning NMR spectroscopy to probe the changes in hydrogen bonding upon rhodopsin activation.	Hydrogen	87-95	rhodopsin	Homo sapiens	109-118
15796514-1	2005	We present a 118-ns molecular dynamics simulation of rhodopsin embedded in a bilayer composed of a 2:2:1 mixture of 1-stearoyl-2-docosahexaenoyl-phosphatidylcholine (SDPC), 1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine (SDPE), and cholesterol, respectively.	PE(18:0/22:6)	228-232	rhodopsin	Homo sapiens	53-62
15769471-4	2005	The NMR chemical shifts of 15N-labeled tryptophan are consistent with the indole nitrogens of Trp126 and Trp265 becoming more weakly hydrogen bonded between rhodopsin and metarhodopsin II.	15n	27-30	rhodopsin	Homo sapiens	157-166
15769471-4	2005	The NMR chemical shifts of 15N-labeled tryptophan are consistent with the indole nitrogens of Trp126 and Trp265 becoming more weakly hydrogen bonded between rhodopsin and metarhodopsin II.	Tryptophan	39-49	rhodopsin	Homo sapiens	157-166
15796514-1	2005	We present a 118-ns molecular dynamics simulation of rhodopsin embedded in a bilayer composed of a 2:2:1 mixture of 1-stearoyl-2-docosahexaenoyl-phosphatidylcholine (SDPC), 1-stearoyl-2-docosahexaenoyl-phosphatidylethanolamine (SDPE), and cholesterol, respectively.	Cholesterol	239-250	rhodopsin	Homo sapiens	53-62
15769471-4	2005	The NMR chemical shifts of 15N-labeled tryptophan are consistent with the indole nitrogens of Trp126 and Trp265 becoming more weakly hydrogen bonded between rhodopsin and metarhodopsin II.	indole	74-80	rhodopsin	Homo sapiens	157-166
15796514-3	2005	Lipids near the protein preferentially reorient such that their unsaturated chains interact with the protein, while the distribution of cholesterol in the membrane complements the variations in rhodopsin"s transverse profile.	Cholesterol	136-147	rhodopsin	Homo sapiens	194-203
15769471-4	2005	The NMR chemical shifts of 15N-labeled tryptophan are consistent with the indole nitrogens of Trp126 and Trp265 becoming more weakly hydrogen bonded between rhodopsin and metarhodopsin II.	Nitrogen	81-90	rhodopsin	Homo sapiens	157-166
15769471-4	2005	The NMR chemical shifts of 15N-labeled tryptophan are consistent with the indole nitrogens of Trp126 and Trp265 becoming more weakly hydrogen bonded between rhodopsin and metarhodopsin II.	Hydrogen	133-141	rhodopsin	Homo sapiens	157-166
15769471-6	2005	Moreover, measurements of rhodopsin containing 13C-labeled histidine show that a strong hydrogen bond between the side-chain of Glu122 and the backbone carbonyl of His211 is disrupted in metarhodopsin II.	13c	47-50	rhodopsin	Homo sapiens	26-35
15769471-6	2005	Moreover, measurements of rhodopsin containing 13C-labeled histidine show that a strong hydrogen bond between the side-chain of Glu122 and the backbone carbonyl of His211 is disrupted in metarhodopsin II.	Histidine	59-68	rhodopsin	Homo sapiens	26-35
15769471-6	2005	Moreover, measurements of rhodopsin containing 13C-labeled histidine show that a strong hydrogen bond between the side-chain of Glu122 and the backbone carbonyl of His211 is disrupted in metarhodopsin II.	Hydrogen	88-96	rhodopsin	Homo sapiens	26-35
15796514-4	2005	The latter phenomenon suggests a molecular-level mechanism for the experimental finding that cholesterol stabilizes the native dark-adapted state of rhodopsin without binding directly to the protein.	Cholesterol	93-104	rhodopsin	Homo sapiens	149-158
15766276-3	2005	In this study, we examined the molecular interaction of TFA-derived phospholipid with cholesterol and the membrane receptor rhodopsin in model membranes.	Trans Fatty Acids	56-59	rhodopsin	Homo sapiens	124-133
15766276-9	2005	TFA phospholipid membranes also exhibited a higher acyl chain packing order, which was indicated by the lower acyl chain packing free volume as determined by DPH fluorescence and the higher transition temperature for rhodopsin thermal denaturation.	Trans Fatty Acids	0-3	rhodopsin	Homo sapiens	217-226
15766276-9	2005	TFA phospholipid membranes also exhibited a higher acyl chain packing order, which was indicated by the lower acyl chain packing free volume as determined by DPH fluorescence and the higher transition temperature for rhodopsin thermal denaturation.	Phospholipids	4-16	rhodopsin	Homo sapiens	217-226
15766276-10	2005	The level of rhodopsin activation was diminished in TFA phospholipids.	tfa phospholipids	52-69	rhodopsin	Homo sapiens	13-22
15591052-2	2005	We find that two mutants, I72C and S251C, when labeled with the small, solvent-sensitive fluorophore monobromobimane, exhibit spectral changes only upon binding light-activated, phosphorylated rhodopsin.	monobromobimane	101-116	rhodopsin	Homo sapiens	193-202
15924998-12	2005	The cholesterol composition of membranes has profound consequences on the major protein, rhodopsin.	Cholesterol	4-15	rhodopsin	Homo sapiens	89-98
15924998-13	2005	Biophysical studies in both model membranes and in native membranes have demonstrated that cholesterol can modulate the activity of rhodopsin by altering the membrane hydrocarbon environment.	Cholesterol	91-102	rhodopsin	Homo sapiens	132-141
15924998-13	2005	Biophysical studies in both model membranes and in native membranes have demonstrated that cholesterol can modulate the activity of rhodopsin by altering the membrane hydrocarbon environment.	Hydrocarbons	167-178	rhodopsin	Homo sapiens	132-141
15924998-15	2005	Although rhodopsin is also the major protein of the plasma membrane, the high membrane cholesterol content inhibits rhodopsin participation in the visual transduction cascade.	Cholesterol	87-98	rhodopsin	Homo sapiens	116-125
15924998-16	2005	In addition to its effect on the hydrocarbon region, cholesterol may interact directly with rhodopsin.	Cholesterol	53-64	rhodopsin	Homo sapiens	92-101
15924998-17	2005	While high cholesterol inhibits rhodopsin activation, it also stabilizes the protein to denaturation.	Cholesterol	11-22	rhodopsin	Homo sapiens	32-41
15924998-22	2005	The effects exerted by cholesterol on rhodopsin function have far-reaching implications for the study of G-protein coupled receptors as a whole.	Cholesterol	23-34	rhodopsin	Homo sapiens	38-47
15689154-1	2005	Focusing on the similarity and divergence of GPCR subtypes and their ligand interactions, we generated dopamine D2, D3, and D4 receptor models based on the rhodopsin crystal structure and refined these with an extensive MM/MD protocol.	Dopamine	103-111	rhodopsin	Homo sapiens	156-165
15501933-0	2005	Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy.	phosphatidylethanolamine	0-24	rhodopsin	Homo sapiens	34-43
15501933-0	2005	Phosphatidylethanolamine enhances rhodopsin photoactivation and transducin binding in a solid supported lipid bilayer as determined using plasmon-waveguide resonance spectroscopy.	Lipid Bilayers	104-117	rhodopsin	Homo sapiens	34-43
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	octyl-beta-D-glucoside	0-14	rhodopsin	Homo sapiens	27-36
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	Phosphatidylcholines	129-148	rhodopsin	Homo sapiens	27-36
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	dioleoyl phosphatidylethanolamine	201-233	rhodopsin	Homo sapiens	27-36
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	dioleoyl phosphatidylethanolamine	235-239	rhodopsin	Homo sapiens	27-36
15615756-10	2005	BrdU labelling identified dividing cells from neurospheres that differentiated to express NFM and rhodopsin.	Bromodeoxyuridine	0-4	rhodopsin	Homo sapiens	98-107
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	1,2-oleoylphosphatidylcholine	281-308	rhodopsin	Homo sapiens	27-36
15501933-3	2005	Octylglucoside-solubilized rhodopsin was incorporated by detergent dilution into solid-supported bilayers composed either of egg phosphatidylcholine or various mixtures of a nonlamellar-forming lipid (dioleoylphosphatidylethanolamine; DOPE) together with a lamellar-forming lipid (dioleoylphosphatidylcholine; DOPC).	1,2-oleoylphosphatidylcholine	310-314	rhodopsin	Homo sapiens	27-36
15501933-7	2005	In addition, measurements of the G(t)/rhodopsin interaction in a DOPC/DOPE (25:75) bilayer at pH 5 demonstrated that light activation increased the affinity for G(t) from 64 nM to 0.7 nM, whereas G(t) affinity for dark-adapted rhodopsin was unchanged.	1,2-oleoylphosphatidylcholine	65-69	rhodopsin	Homo sapiens	38-47
15501933-7	2005	In addition, measurements of the G(t)/rhodopsin interaction in a DOPC/DOPE (25:75) bilayer at pH 5 demonstrated that light activation increased the affinity for G(t) from 64 nM to 0.7 nM, whereas G(t) affinity for dark-adapted rhodopsin was unchanged.	dioleoyl phosphatidylethanolamine	70-74	rhodopsin	Homo sapiens	38-47
15501933-8	2005	By contrast, in DOPC bilayers the affinity of G(t) for light-activated rhodopsin was only 18 nM at pH 5.	1,2-oleoylphosphatidylcholine	16-20	rhodopsin	Homo sapiens	71-80
15475355-0	2004	Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.	Hydrogen	20-28	rhodopsin	Homo sapiens	45-54
15475355-0	2004	Role of the retinal hydrogen bond network in rhodopsin Schiff base stability and hydrolysis.	Schiff Bases	55-66	rhodopsin	Homo sapiens	45-54
15475355-1	2004	Little is known about the molecular mechanism of Schiff base hydrolysis in rhodopsin.	Schiff Bases	49-60	rhodopsin	Homo sapiens	75-84
15475355-3	2004	We find conservative mutations in this network (T94I, E113Q, S186A, E181Q, Y192F, and Y268F) increase the activation energy (E(a)) and abolish the concave Arrhenius plot normally seen for Schiff base hydrolysis in dark state rhodopsin.	Schiff Bases	188-199	rhodopsin	Homo sapiens	225-234
15475355-4	2004	Interestingly, two mutants (T94I and E113Q) show dramatically faster rates of Schiff base hydrolysis in dark state rhodopsin, yet slower hydrolysis rates in the active MII form.	Schiff Bases	78-89	rhodopsin	Homo sapiens	115-124
15475355-5	2004	We find deuterium affects the hydrolysis process in wild-type rhodopsin, exhibiting a specific isotope effect of approximately 2.5, and proton inventory studies indicate that multiple proton transfer events occur during the process of Schiff base hydrolysis for both dark state and MII forms.	Deuterium	8-17	rhodopsin	Homo sapiens	62-71
15475355-5	2004	We find deuterium affects the hydrolysis process in wild-type rhodopsin, exhibiting a specific isotope effect of approximately 2.5, and proton inventory studies indicate that multiple proton transfer events occur during the process of Schiff base hydrolysis for both dark state and MII forms.	Schiff Bases	235-246	rhodopsin	Homo sapiens	62-71
15475355-5	2004	We find deuterium affects the hydrolysis process in wild-type rhodopsin, exhibiting a specific isotope effect of approximately 2.5, and proton inventory studies indicate that multiple proton transfer events occur during the process of Schiff base hydrolysis for both dark state and MII forms.	Methicillin	282-285	rhodopsin	Homo sapiens	62-71
15475355-6	2004	Taken together, our study demonstrates the importance of the retinal hydrogen bond network both in maintaining Schiff base integrity in dark state rhodopsin, as well as in catalyzing the hydrolysis and release of retinal from the MII form.	Hydrogen	69-77	rhodopsin	Homo sapiens	147-156
15475355-6	2004	Taken together, our study demonstrates the importance of the retinal hydrogen bond network both in maintaining Schiff base integrity in dark state rhodopsin, as well as in catalyzing the hydrolysis and release of retinal from the MII form.	Schiff Bases	111-122	rhodopsin	Homo sapiens	147-156
15506960-4	2004	For example, the 11-cis retinal chromophore of rhodopsin forms a protonated Schiff base linkage to a lysine in TM7, deep within the helical bundle, and small ligands, such as amine neurotransmitters and non-peptide analogues of peptide hormones, also bind within the corresponding region of their cognate receptors.	Schiff Bases	76-87	rhodopsin	Homo sapiens	47-56
15471866-1	2004	ABCA4, a member of the family of ATP binding cassette (ABC) proteins found in rod and cone photoreceptors, has been implicated in the transport of retinoid compounds across the outer segment disk membrane following the photoactivation of rhodopsin.	Retinoids	147-155	rhodopsin	Homo sapiens	238-247
15595835-1	2004	Site-directed mutagenesis and design of Zn(2+)-binding centers have been used to determine a set of specific tertiary interactions between the mu-opioid receptor, a rhodopsin-like G protein-coupled receptor (GPCR), and its cyclic peptide agonist ligand, Tyr(1)-c(S-Et-S)[d-Cys(2)-Phe(3)-d-Pen(4)]NH(2) (JOM6).	Zinc	40-42	rhodopsin	Homo sapiens	165-174
15595835-1	2004	Site-directed mutagenesis and design of Zn(2+)-binding centers have been used to determine a set of specific tertiary interactions between the mu-opioid receptor, a rhodopsin-like G protein-coupled receptor (GPCR), and its cyclic peptide agonist ligand, Tyr(1)-c(S-Et-S)[d-Cys(2)-Phe(3)-d-Pen(4)]NH(2) (JOM6).	Tyrosine	254-257	rhodopsin	Homo sapiens	165-174
15595835-1	2004	Site-directed mutagenesis and design of Zn(2+)-binding centers have been used to determine a set of specific tertiary interactions between the mu-opioid receptor, a rhodopsin-like G protein-coupled receptor (GPCR), and its cyclic peptide agonist ligand, Tyr(1)-c(S-Et-S)[d-Cys(2)-Phe(3)-d-Pen(4)]NH(2) (JOM6).	D-cysteine	271-276	rhodopsin	Homo sapiens	165-174
15595835-1	2004	Site-directed mutagenesis and design of Zn(2+)-binding centers have been used to determine a set of specific tertiary interactions between the mu-opioid receptor, a rhodopsin-like G protein-coupled receptor (GPCR), and its cyclic peptide agonist ligand, Tyr(1)-c(S-Et-S)[d-Cys(2)-Phe(3)-d-Pen(4)]NH(2) (JOM6).	Phenylalanine	280-283	rhodopsin	Homo sapiens	165-174
15595835-1	2004	Site-directed mutagenesis and design of Zn(2+)-binding centers have been used to determine a set of specific tertiary interactions between the mu-opioid receptor, a rhodopsin-like G protein-coupled receptor (GPCR), and its cyclic peptide agonist ligand, Tyr(1)-c(S-Et-S)[d-Cys(2)-Phe(3)-d-Pen(4)]NH(2) (JOM6).	d-pen	287-292	rhodopsin	Homo sapiens	165-174
15347651-1	2004	Photoisomerization of rhodopsin activates a heterotrimeric G-protein cascade leading to closure of cGMP-gated channels and hyperpolarization of photoreceptor cells.	Cyclic GMP	99-103	rhodopsin	Homo sapiens	22-31
15351781-4	2004	In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin.	Phosphates	50-60	rhodopsin	Homo sapiens	18-27
15351781-4	2004	In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin.	Lysine	200-206	rhodopsin	Homo sapiens	18-27
15351781-4	2004	In a model of the rhodopsin-arrestin complex, the phosphates point in the direction of arrestin and form a continuous negatively charged surface, which is stabilized by a number of positively charged lysine and arginine residues of arrestin.	Arginine	211-219	rhodopsin	Homo sapiens	18-27
15351781-6	2004	In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin.	Phosphates	100-110	rhodopsin	Homo sapiens	132-141
15351781-6	2004	In conjunction with other binding sites, the helix-loop structure provides a mechanism of shielding phosphates in the center of the rhodopsin-arrestin complex and appears critical in guiding arrestin for high affinity binding with rhodopsin.	Phosphates	100-110	rhodopsin	Homo sapiens	231-240
15609995-2	2004	Natural rhodopsin contains an 11-cis-retinylidene chromophore.	11-cis-retinylidene	30-49	rhodopsin	Homo sapiens	8-17
15609995-8	2004	They provide converging evidence for global, nonspecific steric interactions between the chromophore and protein, and contrast with the specific interactions over the entire ionone ring and its substituents detected for rhodopsin.	Norisoprenoids	174-180	rhodopsin	Homo sapiens	220-229
15506960-4	2004	For example, the 11-cis retinal chromophore of rhodopsin forms a protonated Schiff base linkage to a lysine in TM7, deep within the helical bundle, and small ligands, such as amine neurotransmitters and non-peptide analogues of peptide hormones, also bind within the corresponding region of their cognate receptors.	Lysine	101-107	rhodopsin	Homo sapiens	47-56
15506960-4	2004	For example, the 11-cis retinal chromophore of rhodopsin forms a protonated Schiff base linkage to a lysine in TM7, deep within the helical bundle, and small ligands, such as amine neurotransmitters and non-peptide analogues of peptide hormones, also bind within the corresponding region of their cognate receptors.	Amines	175-180	rhodopsin	Homo sapiens	47-56
15548806-9	2004	The overall regression model comparing solid angles of visual fields from patients with rhodopsin mutations (Pro23His, Pro347Ala, Arg135Leu) shows significant effects for age (p = 0.0005), mutation (p = 0.0014), and interaction between age and mutation (p = 0.018) with an R(2) of 0.407.	pro23his	109-117	rhodopsin	Homo sapiens	88-97
15459346-3	2004	Anabaena sensory rhodopsin exhibits light-induced interconversion between stable 13-cis and all-trans states of the retinylidene protein.	retinylidene	116-128	rhodopsin	Homo sapiens	17-26
15563129-1	2004	Light absorption by the visual pigment rhodopsin leads to vision via a complex signal transduction pathway that is initiated by the ultrafast and highly efficient photoreaction of its chromophore, the retinal protonated Schiff base (RPSB).	Schiff Bases	220-231	rhodopsin	Homo sapiens	39-48
15375171-0	2004	Involvement of the C-terminal proline-rich motif of G protein-coupled receptor kinases in recognition of activated rhodopsin.	Proline	30-37	rhodopsin	Homo sapiens	115-124
15375171-7	2004	Through a series of mutagenesis analyses, a proline-rich motif in the CC was identified as the key element involved in the interaction between the CC region and rhodopsin.	Proline	44-51	rhodopsin	Homo sapiens	161-170
15194703-3	2004	We report the identification of a high-affinity zinc coordination site within the transmembrane domain of rhodopsin, coordinated by the side chains of two highly conserved residues, Glu(122) in transmembrane helix III and His(211) in transmembrane helix V. We also demonstrate that this zinc coordination is critical for rhodopsin folding, 11-cis-retinal binding, and the stability of the chromophore-receptor interaction, defects of which are observed in retinitis pigmentosa.	Glutamic Acid	182-185	rhodopsin	Homo sapiens	106-115
15322129-0	2004	Transition of rhodopsin into the active metarhodopsin II state opens a new light-induced pathway linked to Schiff base isomerization.	Schiff Bases	107-118	rhodopsin	Homo sapiens	14-23
15322129-1	2004	Rhodopsin bears 11-cis-retinal covalently bound by a protonated Schiff base linkage.	Schiff Bases	64-75	rhodopsin	Homo sapiens	0-9
15340926-2	2004	Eleven single-point mutations associated with retinitis pigmentosa at and in the proximity to the retinal binding pocket of rhodopsin have been modeled in silico and their spectra calculated with the NDOL (Neglect of Differential Overlap accounting L azimuthal quantum number) a priori method.	ndol	200-204	rhodopsin	Homo sapiens	124-133
15340926-4	2004	Different energy balances in the case of mutants at the very molecular level, compared to native nonmutated rhodopsin, can cause permanent cellular stress and would play a role in the progression of the retine degenerative process.	retine	203-209	rhodopsin	Homo sapiens	108-117
15526430-2	2004	A digitonin extract of rhodopsin was irradiated at -155 degrees C with blue light of wavelength 436 nm.	Digitonin	2-11	rhodopsin	Homo sapiens	23-32
15465057-1	2004	The current view that the beta-ionone ring of the rhodopsin chromophore vacates its binding pocket within the protein early in the photocascade has been adopted in efforts to provide structural models of photoreceptor activation.	beta-ionone	26-37	rhodopsin	Homo sapiens	50-59
15465057-6	2004	This describes a plausible role for the ring in operating a hydrophobic switch from within the aromatic cluster of helix 6 of rhodopsin, which is coupled to electronic changes within the receptor through water-mediated, hydrogen-bonded networks between the conserved residues in G protein-coupled receptors.	Water	204-209	rhodopsin	Homo sapiens	126-135
15465057-6	2004	This describes a plausible role for the ring in operating a hydrophobic switch from within the aromatic cluster of helix 6 of rhodopsin, which is coupled to electronic changes within the receptor through water-mediated, hydrogen-bonded networks between the conserved residues in G protein-coupled receptors.	Hydrogen	220-228	rhodopsin	Homo sapiens	126-135
15271992-1	2004	The GDP-GTP exchange activity of the retinal G protein, transducin, is markedly accelerated by the photoreceptor rhodopsin in the first step of visual transduction.	gdp-gtp	4-11	rhodopsin	Homo sapiens	113-122
15366925-2	2004	Membrane preparations of unactivated (Rh) and light-activated rhodopsin (Rh*), each in the presence or absence of G(t)alpha(340-350), were acetylated with the water-soluble reagent sulfosuccinimidyl acetate, and the extent of the acetylation was determined by mass spectrometry.	Water	159-164	rhodopsin	Homo sapiens	73-76
15368571-3	2004	Glu181 and Ser186 form a network of hydrogen bonds mediated by a water molecule in the dark-state crystal structure of rhodopsin.	Hydrogen	36-44	rhodopsin	Homo sapiens	119-128
15368571-3	2004	Glu181 and Ser186 form a network of hydrogen bonds mediated by a water molecule in the dark-state crystal structure of rhodopsin.	Water	65-70	rhodopsin	Homo sapiens	119-128
15194703-3	2004	We report the identification of a high-affinity zinc coordination site within the transmembrane domain of rhodopsin, coordinated by the side chains of two highly conserved residues, Glu(122) in transmembrane helix III and His(211) in transmembrane helix V. We also demonstrate that this zinc coordination is critical for rhodopsin folding, 11-cis-retinal binding, and the stability of the chromophore-receptor interaction, defects of which are observed in retinitis pigmentosa.	Glutamic Acid	182-185	rhodopsin	Homo sapiens	321-330
15194703-3	2004	We report the identification of a high-affinity zinc coordination site within the transmembrane domain of rhodopsin, coordinated by the side chains of two highly conserved residues, Glu(122) in transmembrane helix III and His(211) in transmembrane helix V. We also demonstrate that this zinc coordination is critical for rhodopsin folding, 11-cis-retinal binding, and the stability of the chromophore-receptor interaction, defects of which are observed in retinitis pigmentosa.	Histidine	222-225	rhodopsin	Homo sapiens	106-115
15194703-3	2004	We report the identification of a high-affinity zinc coordination site within the transmembrane domain of rhodopsin, coordinated by the side chains of two highly conserved residues, Glu(122) in transmembrane helix III and His(211) in transmembrane helix V. We also demonstrate that this zinc coordination is critical for rhodopsin folding, 11-cis-retinal binding, and the stability of the chromophore-receptor interaction, defects of which are observed in retinitis pigmentosa.	Histidine	222-225	rhodopsin	Homo sapiens	321-330
15287753-2	2004	It is produced from the Meta I/Meta II photoproduct equilibrium of rhodopsin by a thermal isomerization of the protonated Schiff base C=N bond of Meta I, and its chromophore configuration is therefore all-trans 15-syn.	Schiff Bases	122-133	rhodopsin	Homo sapiens	67-76
15288992-3	2004	Mutations on both alleles of RPE65 result in absent or largely decreased formation of rhodopsin, due to a defect in all-trans retinol isomerization in the RPE.	Vitamin A	126-133	rhodopsin	Homo sapiens	86-95
15274618-0	2004	FTIR spectroscopy of the K photointermediate of Neurospora rhodopsin: structural changes of the retinal, protein, and water molecules after photoisomerization.	Water	118-123	rhodopsin	Homo sapiens	59-68
15236586-1	2004	The GTP-binding protein (G protein), transducin, serves as a key molecular switch in vertebrate vision through the tight regulation of its GTP-binding (activation)/GTP hydrolytic (deactivation) cycle by the photoreceptor rhodopsin.	Guanosine Triphosphate	4-7	rhodopsin	Homo sapiens	221-230
15552367-6	2004	It appeared that the decay of metarhodopsins controls both the time course of rod dark adaptation following small bleaches and the production of retinol that is the substrate for rhodopsin regeneration.	Vitamin A	145-152	rhodopsin	Homo sapiens	34-43
15260488-1	2004	Thermal isomerization of the retinal Schiff base C=N double bond is known to trigger the decay of rhodopsin"s Meta I/Meta II photoproduct equilibrium to the inactive Meta III state [Vogel, R., Siebert, F., Mathias, G., Tavan, P., Fan, G., and Sheves, M. (2003) Biochemistry 42, 9863-9874].	Schiff Bases	37-48	rhodopsin	Homo sapiens	98-107
15236586-1	2004	The GTP-binding protein (G protein), transducin, serves as a key molecular switch in vertebrate vision through the tight regulation of its GTP-binding (activation)/GTP hydrolytic (deactivation) cycle by the photoreceptor rhodopsin.	Guanosine Triphosphate	139-142	rhodopsin	Homo sapiens	221-230
15170322-1	2004	Glutamic acid E134 in rhodopsin is part of a highly conserved triad, D(E)RY, located near the cytoplasmic lipid/water interface in transmembrane helix 3 of G protein-coupled receptors (GPCRs).	Glutamic Acid	0-13	rhodopsin	Homo sapiens	22-31
15170322-1	2004	Glutamic acid E134 in rhodopsin is part of a highly conserved triad, D(E)RY, located near the cytoplasmic lipid/water interface in transmembrane helix 3 of G protein-coupled receptors (GPCRs).	e134	14-18	rhodopsin	Homo sapiens	22-31
15170322-1	2004	Glutamic acid E134 in rhodopsin is part of a highly conserved triad, D(E)RY, located near the cytoplasmic lipid/water interface in transmembrane helix 3 of G protein-coupled receptors (GPCRs).	Water	112-117	rhodopsin	Homo sapiens	22-31
15170322-2	2004	A large body of experimental evidence suggests that the protonation of E134 plays a role in the mechanism of activation of rhodopsin and other GPCRs as well.	e134	71-75	rhodopsin	Homo sapiens	123-132
15170322-13	2004	This sensitivity together with the location of E134 near the actual position of the lipid/water interface could be a strategic element in the mechanism of activation of rhodopsin.	e134	47-51	rhodopsin	Homo sapiens	169-178
15170322-13	2004	This sensitivity together with the location of E134 near the actual position of the lipid/water interface could be a strategic element in the mechanism of activation of rhodopsin.	Water	90-95	rhodopsin	Homo sapiens	169-178
15053840-1	2004	BACKGROUND: Early stages in the excitation cascade of Limulus photoreceptors are mediated by activation of Gq by rhodopsin, generation of inositol-1,4,5-trisphosphate by phospholipase-C and the release of Ca2+.	glycylglutamine	107-109	rhodopsin	Homo sapiens	113-122
14757760-11	2004	The interactions established by Thr-90 emerge as a general feature of archaeal rhodopsin proteins.	Threonine	32-35	rhodopsin	Homo sapiens	79-88
15041649-2	2004	A molecular dynamics model of rhodopsin in a POPC phospholipid bilayer was simulated for 15 ns, revealing a conformation significantly different from the recent crystal structures.	Phospholipids	50-62	rhodopsin	Homo sapiens	30-39
15151987-7	2004	Altogether, our results indicate that Rho/Rock acts on signaling pathways favoring nuclear translocation during tangential migration of PCN.	PREGNENOLONE CARBONITRILE	136-139	rhodopsin	Homo sapiens	38-46
15123809-2	2004	Rhodopsin dysfunction has been linked to misfolding, caused by chemical modifications that affect the naturally occurring disulfide bond between C110 and C187.	Disulfides	122-131	rhodopsin	Homo sapiens	0-9
15123809-4	2004	We simulate the thermal unfolding of rhodopsin by breaking the native-state hydrogen bonds sequentially in the order of their relative strength, using the recently developed Floppy Inclusion and Rigid Substructure Topography (FIRST) method [Jacobs, D. J., Rader, A. J., Kuhn, L. A.	Hydrogen	76-84	rhodopsin	Homo sapiens	37-46
15123809-8	2004	Fast mode analysis of rhodopsin using the Gaussian network model also identifies the disulfide bond and the retinal ligand binding pocket to be the most rigid region in rhodopsin.	Disulfides	85-94	rhodopsin	Homo sapiens	22-31
15123809-8	2004	Fast mode analysis of rhodopsin using the Gaussian network model also identifies the disulfide bond and the retinal ligand binding pocket to be the most rigid region in rhodopsin.	Disulfides	85-94	rhodopsin	Homo sapiens	169-178
15017136-0	2004	Dipolar assisted rotational resonance NMR of tryptophan and tyrosine in rhodopsin.	Tryptophan	45-55	rhodopsin	Homo sapiens	72-81
15017136-0	2004	Dipolar assisted rotational resonance NMR of tryptophan and tyrosine in rhodopsin.	Tyrosine	60-68	rhodopsin	Homo sapiens	72-81
15017136-5	2004	In rhodopsin containing 4"-(13)C-Tyr and 8,19-(13)C retinal, we observe two distinct tyrosine-to-retinal correlations in the DARR spectrum.	Tyrosine	33-36	rhodopsin	Homo sapiens	3-12
15017136-5	2004	In rhodopsin containing 4"-(13)C-Tyr and 8,19-(13)C retinal, we observe two distinct tyrosine-to-retinal correlations in the DARR spectrum.	Tyrosine	85-93	rhodopsin	Homo sapiens	3-12
15017136-9	2004	In rhodopsin containing 2-(13)C Gly121 and U-(13)C Trp265, we do not observe a Trp-Gly cross peak in the DARR spectrum despite their close proximity (3.6 A) in the crystal structure.	Glycine	32-35	rhodopsin	Homo sapiens	3-12
15177205-3	2004	Here we review the biochemical and physical processes involved in eliminating the products of light absorption from the photoreceptor outer segment, in recycling the released retinoid to its original isomeric form as 11-cis retinal, and in regenerating the visual pigment rhodopsin.	Retinoids	175-183	rhodopsin	Homo sapiens	272-281
14976207-8	2004	Last, we show that mutation of the hydrophobic residues severely diminishes phospholipid-dependent autophosphorylation of GRK5 and phosphorylation of membrane-bound rhodopsin by GRK5.	Phospholipids	76-88	rhodopsin	Homo sapiens	165-174
15469705-0	2004	Chemical modification of transducin with dansyl chloride hinders its binding to light-activated rhodopsin.	dansyl chloride	41-56	rhodopsin	Homo sapiens	96-105
15469705-5	2004	Additionally, rhodopsin completely protected against the DnsCl inactivation of T. These results demonstrated the existence of functional lysines on T that are located in the proximity of the interaction site with the photoreceptor protein.	Lysine	137-144	rhodopsin	Homo sapiens	14-23
14611935-0	2003	Assessing structural elements that influence Schiff base stability: mutants E113Q and D190N destabilize rhodopsin through different mechanisms.	Schiff Bases	45-56	rhodopsin	Homo sapiens	104-113
15471346-5	2004	This conjecture is investigated by mapping the intersection space of the rhodopsin chromophore model 2-Z-hepta-2,4,6-trieniminium cation and of the conjugated hydrocarbon 3-Z-deca-1,3,5,6,7-pentaene.	2-z-hepta-2,4,6-trieniminium	101-129	rhodopsin	Homo sapiens	73-82
15471346-5	2004	This conjecture is investigated by mapping the intersection space of the rhodopsin chromophore model 2-Z-hepta-2,4,6-trieniminium cation and of the conjugated hydrocarbon 3-Z-deca-1,3,5,6,7-pentaene.	3-z-deca-1,3,5,6,7-pentaene	171-198	rhodopsin	Homo sapiens	73-82
13679519-0	2004	Phosphoinositides, ezrin/moesin, and rac1 regulate fusion of rhodopsin transport carriers in retinal photoreceptors.	Phosphatidylinositols	0-17	rhodopsin	Homo sapiens	61-70
14611939-1	2003	In HEK293S cells expressing opsin, rhodopsin regenerates on addition of all-trans retinol.	Vitamin A	82-89	rhodopsin	Homo sapiens	35-44
14744159-9	2004	This result indicates that the distances between the phosphorylated sites on the C-terminus and the (19)F sites on helix 8 (Cys 316) and in the second cytoplasmic loop (Cys140) are greater than 12 A in phosphorylated rhodopsin.	Cysteine	124-127	rhodopsin	Homo sapiens	217-226
14717583-6	2004	Reconstitution of POG-Tbetagamma with Talpha and light-activated rhodopsin (Rh) in photoreceptor membranes resulted in cross-linking of Tgamma with a glycerophospholipid, indicating molecular interaction of the farnesyl group with cellular membranes.	tgamma	136-142	rhodopsin	Homo sapiens	65-74
14717583-6	2004	Reconstitution of POG-Tbetagamma with Talpha and light-activated rhodopsin (Rh) in photoreceptor membranes resulted in cross-linking of Tgamma with a glycerophospholipid, indicating molecular interaction of the farnesyl group with cellular membranes.	Glycerophospholipids	150-169	rhodopsin	Homo sapiens	65-74
15064451-4	2004	The attachment of rhodopsin via its extracellular carbohydrate residues provides a convenient, and universally applicable, procedure for GPCR immobilization in a form that retains full biochemical activity and ability to interact with intracellular signaling components.	Carbohydrates	50-62	rhodopsin	Homo sapiens	18-27
14611935-3	2003	Here we describe methods to determine Schiff base stability in rhodopsin, present examples of dark state and MII rhodopsin stability differences, and show that studies of mutants E113Q and D190N demonstrate different parts of rhodopsin influence Schiff base stability in different ways.	Schiff Bases	38-49	rhodopsin	Homo sapiens	63-72
14611936-1	2003	To regenerate light-sensitive rhodopsin in rods from active metarhodopsin II (Meta II), all-trans-retinal must be removed from the retinal binding pocket and metabolically supplied 11-cis-retinal has to form a new retinylidene bond in the active site.	retinylidene	214-226	rhodopsin	Homo sapiens	30-39
14641583-4	2003	However, very little is known about the diversity and distribution of rhodopsin genes in hypersaline environments.	hypersaline	89-100	rhodopsin	Homo sapiens	70-79
12958314-2	2003	Molecular dynamic simulations of the rhodopsin-based homology model of CXCR4 were performed in a solvated lipid bilayer to reproduce the microenvironment of this integral membrane protein.	Lipid Bilayers	106-119	rhodopsin	Homo sapiens	37-46
14576451-3	2003	This article, describes recent studies that link the photobleaching of rhodopsin to tyrosine phosphorylation of the insulin receptor and subsequent activation of phosphoinositide 3- kinase (PI3K).	Tyrosine	84-92	rhodopsin	Homo sapiens	71-80
14556740-6	2003	To begin to understand the nature of the efficiency of this coupling in different lipid settings, we present a molecular dynamics study of rhodopsin in an explicit dioleoyl-phosphatidylcholine bilayer.	1,2-oleoylphosphatidylcholine	164-192	rhodopsin	Homo sapiens	139-148
12944255-5	2003	The model shows that upon activation of a single rhodopsin, cGMP changes are local, and exhibit both a longitudinal and a transversal component.	Cyclic GMP	60-64	rhodopsin	Homo sapiens	49-58
12835420-1	2003	The biological function of Glu-181 in the photoactivation process of rhodopsin is explored through spectroscopic studies of site-specific mutants.	Glutamic Acid	27-30	rhodopsin	Homo sapiens	69-78
12769524-0	2003	Stimulatory effect of cyanidin 3-glycosides on the regeneration of rhodopsin.	cyanidin-3-glycoside	22-43	rhodopsin	Homo sapiens	67-76
12906790-10	2003	This activation is specifically blocked by a synthetic peptide corresponding to the Asn-Pro-X-X-Tyr motif found in rhodopsin, and Rac-1 coprecipitates with rhodopsin on Concanavalin A Sepharose.	asn-pro-x-x-tyr	84-99	rhodopsin	Homo sapiens	115-124
12906790-10	2003	This activation is specifically blocked by a synthetic peptide corresponding to the Asn-Pro-X-X-Tyr motif found in rhodopsin, and Rac-1 coprecipitates with rhodopsin on Concanavalin A Sepharose.	asn-pro-x-x-tyr	84-99	rhodopsin	Homo sapiens	156-165
12906790-10	2003	This activation is specifically blocked by a synthetic peptide corresponding to the Asn-Pro-X-X-Tyr motif found in rhodopsin, and Rac-1 coprecipitates with rhodopsin on Concanavalin A Sepharose.	Sepharose	184-193	rhodopsin	Homo sapiens	115-124
12906790-10	2003	This activation is specifically blocked by a synthetic peptide corresponding to the Asn-Pro-X-X-Tyr motif found in rhodopsin, and Rac-1 coprecipitates with rhodopsin on Concanavalin A Sepharose.	Sepharose	184-193	rhodopsin	Homo sapiens	156-165
12910240-2	2003	Opsin expressed in HEK293 cells has been reported to form rhodopsin on the addition of all-trans retinol, indicating that the machinery for retinoid isomerization is present.	Vitamin A	97-104	rhodopsin	Homo sapiens	58-67
12966076-7	2003	These results indicate that rearrangement of the C-terminal region of Gt(alpha) after the binding of a rhodopsin intermediate is necessary for the GDP-GTP exchange reaction on Gt(alpha).	gdp-gtp	147-154	rhodopsin	Homo sapiens	103-112
14521218-0	2003	Photochemical reactivity of polyenes: from dienes to rhodopsin, from microseconds to femtoseconds.	Polyenes	28-36	rhodopsin	Homo sapiens	53-62
12846569-0	2003	Active peptidic mimics of the second intracellular loop of the V(1A) vasopressin receptor are structurally related to the second intracellular rhodopsin loop: a combined 1H NMR and biochemical study.	Hydrogen	170-172	rhodopsin	Homo sapiens	143-152
12824482-3	2003	For aminergic GPCRs, the motif is composed of a conserved aspartic acid in the third transmembrane (TM) domain (rhodopsin position 117) and a conserved tryptophan in the seventh TM domain (rhodopsin position 293); the roles of each are readily justified by molecular modeling of ligand-receptor interactions.	Aspartic Acid	58-71	rhodopsin	Homo sapiens	112-121
12742390-2	2003	The signal transduction pathway can be mapped from the initial absorption of light to conformational changes within rhodopsin, through activation of the G protein transducin, and to the ultimate closure of the cation cGMP-gated channels in the plasma membrane.	Cyclic GMP	217-221	rhodopsin	Homo sapiens	116-125
12769524-2	2003	This study examined the effect of four anthocyanins in black currant fruits on the regeneration of rhodopsin using frog rod outer segment (ROS) membranes.	Anthocyanins	39-51	rhodopsin	Homo sapiens	99-108
12769524-6	2003	It was concluded that the major effect of anthocyanins in rod photoreceptors is on the regeneration of rhodopsin.	Anthocyanins	42-54	rhodopsin	Homo sapiens	103-112
12736149-6	2003	In muscle cells overexpressing the active phosphorylation site-deficient mutant Rho(A188), MLC(20) phosphorylation was partly inhibited by SNP, VIP, cBIMPS, and 8-pCPT-cGMP, suggesting the existence of an independent inhibitory mechanism downstream of RhoA.	5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole-3',5'-monophosphorothioate	149-155	rhodopsin	Homo sapiens	80-88
12787029-0	2003	N-Glycan structures of squid rhodopsin.	n-glycan	0-8	rhodopsin	Homo sapiens	29-38
12787029-4	2003	The major glycans of squid rhodopsin were shown to possess the alpha1-3 and alpha1-6 difucosylated innermost GlcNAc residue found in glycoproteins produced by insects and helminths.	Polysaccharides	10-17	rhodopsin	Homo sapiens	27-36
12787029-4	2003	The major glycans of squid rhodopsin were shown to possess the alpha1-3 and alpha1-6 difucosylated innermost GlcNAc residue found in glycoproteins produced by insects and helminths.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	109-115	rhodopsin	Homo sapiens	27-36
12736149-6	2003	In muscle cells overexpressing the active phosphorylation site-deficient mutant Rho(A188), MLC(20) phosphorylation was partly inhibited by SNP, VIP, cBIMPS, and 8-pCPT-cGMP, suggesting the existence of an independent inhibitory mechanism downstream of RhoA.	8-pcpt	161-167	rhodopsin	Homo sapiens	80-88
12736149-6	2003	In muscle cells overexpressing the active phosphorylation site-deficient mutant Rho(A188), MLC(20) phosphorylation was partly inhibited by SNP, VIP, cBIMPS, and 8-pCPT-cGMP, suggesting the existence of an independent inhibitory mechanism downstream of RhoA.	Cyclic GMP	168-172	rhodopsin	Homo sapiens	80-88
12547830-8	2003	Our results indicate that the loop E-2 ion pair is important for rhodopsin stability and thus suggest that retinitis pigmentosa observed in patients with Asp-190 mutations may in part be the result of thermally unstable rhodopsin proteins.	Aspartic Acid	154-157	rhodopsin	Homo sapiens	65-74
12547830-8	2003	Our results indicate that the loop E-2 ion pair is important for rhodopsin stability and thus suggest that retinitis pigmentosa observed in patients with Asp-190 mutations may in part be the result of thermally unstable rhodopsin proteins.	Aspartic Acid	154-157	rhodopsin	Homo sapiens	220-229
12778626-3	2003	METHODS: Two psoralen-linked triplex-forming oligonucleotides were used to inhibit the expression from a plasmid carrying the rhodopsin and green fluorescent protein fusion gene.	Ficusin	13-21	rhodopsin	Homo sapiens	126-135
12778626-3	2003	METHODS: Two psoralen-linked triplex-forming oligonucleotides were used to inhibit the expression from a plasmid carrying the rhodopsin and green fluorescent protein fusion gene.	triplex-forming oligonucleotides	29-61	rhodopsin	Homo sapiens	126-135
12778626-8	2003	Mutations at one of the triplex binding sites within the rhodopsin gene also abolished the effect of the corresponding triplex forming oligonucleotide, without diminishing the inhibition by the other oligo.	triplex forming oligonucleotide	119-150	rhodopsin	Homo sapiens	57-66
12778626-10	2003	CONCLUSION: The authors conclude, that psoralen linked triplex forming oligonucleotides are efficient and specific tools for blocking gene expression from the human rhodopsin gene.	Ficusin	39-47	rhodopsin	Homo sapiens	165-174
12509432-8	2003	The residues Val-757(5.47), Trp-798(6.48), Phe-801(6.51), Tyr-805(6.55), and Thr-815(7.39) are critical determinants of the EM-TBPC-binding pocket of the mGlu1 receptor, validating the rhodopsin crystal structure as a template for the family 3 G-protein-coupled receptors.	Threonine	77-80	rhodopsin	Homo sapiens	185-194
12778626-10	2003	CONCLUSION: The authors conclude, that psoralen linked triplex forming oligonucleotides are efficient and specific tools for blocking gene expression from the human rhodopsin gene.	triplex forming oligonucleotides	55-87	rhodopsin	Homo sapiens	165-174
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	bisretinoids	232-244	rhodopsin	Homo sapiens	149-158
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	bisretinoids	232-244	rhodopsin	Homo sapiens	197-206
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	bisretinoids	232-244	rhodopsin	Homo sapiens	197-206
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	Lysine	274-280	rhodopsin	Homo sapiens	149-158
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	Lysine	274-280	rhodopsin	Homo sapiens	197-206
12926382-2	2003	It is now shown that the presence of high exogenous concentrations of all-trans-retinal in photoreceptor outer segments leads to the formation of A2-rhodopsin (A2-Rh), an unprecedented fluorescent rhodopsin adduct which consists of bisretinoids (A2) linked to each of three lysine residues in rhodopsin (Rh) and which exhibits an emission spectrum similar to A2E.	Lysine	274-280	rhodopsin	Homo sapiens	197-206
12926382-5	2003	Examination of A2-Rh and A2-PE (the precursor of A2E) fluorescence in relation to all-trans-retinal concentration indicated that whereas A2-PE formation is favored over that of A2-Rh, for a single rhodopsin molecule only one phosphatidylethanolamine molecule is available to react with all-trans-retinal; this phosphatidylethanolamine is probably tightly associated with the protein.	phosphatidylethanolamine	225-249	rhodopsin	Homo sapiens	197-206
12926382-5	2003	Examination of A2-Rh and A2-PE (the precursor of A2E) fluorescence in relation to all-trans-retinal concentration indicated that whereas A2-PE formation is favored over that of A2-Rh, for a single rhodopsin molecule only one phosphatidylethanolamine molecule is available to react with all-trans-retinal; this phosphatidylethanolamine is probably tightly associated with the protein.	phosphatidylethanolamine	310-334	rhodopsin	Homo sapiens	197-206
12486133-6	2003	And indeed, the amino terminus of GRK2 (GRK2(1-185)) inhibited a Gbetagamma-stimulated inositol phosphate signal in cells, purified GRK2(1-185) suppressed the Gbetagamma-stimulated phosphorylation of rhodopsin, and GRK2(1-185) bound directly to purified Gbetagamma subunits.	gbetagamma	65-75	rhodopsin	Homo sapiens	200-209
12683809-0	2003	Rhodopsin exhibits a preference for solvation by polyunsaturated docosohexaenoic acid.	polyunsaturated docosohexaenoic acid	49-85	rhodopsin	Homo sapiens	0-9
12683809-6	2003	These observations are consistent with various experimental studies on rhodopsin and other G-protein coupled receptors and with the picture of extreme flexibility in polyunsaturated fatty acid chains that has arisen from recent NMR and computational work.	Fatty Acids, Unsaturated	166-192	rhodopsin	Homo sapiens	71-80
12673590-3	2003	RESULTS: A new point mutation in rhodopsin gene at codon 52 of exon 1 (TTC to TAC) that resulted in a substitution of Tyr to Phe was detected in the four affected family members, but not in the four control individuals from the same pedigree.	Tyrosine	118-121	rhodopsin	Homo sapiens	33-42
12673590-3	2003	RESULTS: A new point mutation in rhodopsin gene at codon 52 of exon 1 (TTC to TAC) that resulted in a substitution of Tyr to Phe was detected in the four affected family members, but not in the four control individuals from the same pedigree.	Phenylalanine	125-128	rhodopsin	Homo sapiens	33-42
12509432-8	2003	The residues Val-757(5.47), Trp-798(6.48), Phe-801(6.51), Tyr-805(6.55), and Thr-815(7.39) are critical determinants of the EM-TBPC-binding pocket of the mGlu1 receptor, validating the rhodopsin crystal structure as a template for the family 3 G-protein-coupled receptors.	2-(4-tert-butylphenoxy)cyclohexanol	127-131	rhodopsin	Homo sapiens	185-194
12616639-0	2003	Modelling of photointermediates suggests a mechanism of the flip of the beta-ionone moiety of the retinylidene chromophore in the rhodopsin photocascade.	beta-ionone	72-83	rhodopsin	Homo sapiens	130-139
12616639-0	2003	Modelling of photointermediates suggests a mechanism of the flip of the beta-ionone moiety of the retinylidene chromophore in the rhodopsin photocascade.	retinylidene	98-110	rhodopsin	Homo sapiens	130-139
12641706-1	2003	Recently it has been suggested that a previously undetected, rhodopsin-based, visual pigment, located in some retinal ganglion cells and having a peak sensitivity around 460 nm, may be responsible for light-induced melatonin suppression and, perhaps, maintenance of the circadian rhythm.	Melatonin	215-224	rhodopsin	Homo sapiens	61-70
12708040-3	2003	Activated rhodopsin is then inactivated and uncouples all-trans-retinal, which is metabolized to all-trans-retinol and transferred to the retinal pigment epithelium, where it is re-isomerzed to form 11-cis-retinal.	Vitamin A	107-114	rhodopsin	Homo sapiens	10-19
12590586-1	2003	This report describes the biochemical characterization of a double mutant of rhodopsin (N2C,D282C) in which Cys residues engineered into the protein at positions 2 (in the amino-terminal extracellular domain) and 282 (in the extracellular loop between transmembrane helices 6 and 7) are shown to form a disulfide bond and increase the thermal stability of the unliganded or opsin form of the protein.	Cysteine	108-111	rhodopsin	Homo sapiens	77-86
12590586-1	2003	This report describes the biochemical characterization of a double mutant of rhodopsin (N2C,D282C) in which Cys residues engineered into the protein at positions 2 (in the amino-terminal extracellular domain) and 282 (in the extracellular loop between transmembrane helices 6 and 7) are shown to form a disulfide bond and increase the thermal stability of the unliganded or opsin form of the protein.	Disulfides	303-312	rhodopsin	Homo sapiens	77-86
12465986-9	2002	The above rotation is a good example of hula-twist rotation in the process of photoisomerization of polyenes such as rhodopsin.	Polyenes	100-108	rhodopsin	Homo sapiens	117-126
12446735-7	2003	This binding pocket is distinct from that of the biogenic amine receptors and rhodopsin where the native ligands (also composed of a carbon ring and a carbon chain) are accommodated in an opposing direction.	Carbon	133-139	rhodopsin	Homo sapiens	78-87
12446735-7	2003	This binding pocket is distinct from that of the biogenic amine receptors and rhodopsin where the native ligands (also composed of a carbon ring and a carbon chain) are accommodated in an opposing direction.	Carbon	151-157	rhodopsin	Homo sapiens	78-87
12585469-0	2003	Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards.	Peptides	106-114	rhodopsin	Homo sapiens	58-67
12629973-0	2003	Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.	Sulfhydryl Compounds	112-122	rhodopsin	Homo sapiens	0-9
12629973-0	2003	Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking.	Disulfides	139-148	rhodopsin	Homo sapiens	0-9
12466267-0	2003	Unusual thermal and conformational properties of the rhodopsin congenital night blindness mutant Thr-94 --> Ile.	Threonine	97-100	rhodopsin	Homo sapiens	53-62
12427735-2	2003	Vertebrate rhodopsin consists of the apoprotein opsin and the chromophore 11-cis-retinal covalently linked via a protonated Schiff base.	Schiff Bases	124-135	rhodopsin	Homo sapiens	11-20
14526423-7	2003	A novel mutation was identified in the rhodopsin gene at codon 52 of exon 1 (TTC-TAC) that resulted in a substitution of Phe to Tyr.	ttc-tac	77-84	rhodopsin	Homo sapiens	39-48
14526423-7	2003	A novel mutation was identified in the rhodopsin gene at codon 52 of exon 1 (TTC-TAC) that resulted in a substitution of Phe to Tyr.	Phenylalanine	121-124	rhodopsin	Homo sapiens	39-48
14526423-7	2003	A novel mutation was identified in the rhodopsin gene at codon 52 of exon 1 (TTC-TAC) that resulted in a substitution of Phe to Tyr.	Tyrosine	128-131	rhodopsin	Homo sapiens	39-48
12176994-1	2002	Phototransduction is initiated by the photoisomerization of rhodopsin (Rho) chromophore 11-cis-retinylidene to all-trans-retinylidene.	11-cis-retinylidene	88-107	rhodopsin	Homo sapiens	60-69
12484764-0	2002	11-cis-retinal protonated Schiff base: influence of the protein environment on the geometry of the rhodopsin chromophore.	Schiff Bases	26-37	rhodopsin	Homo sapiens	99-108
12416988-0	2002	Structure of rhodopsin in monolayers at the air-water interface: a PM-IRRAS and X-ray reflectivity study.	Water	48-53	rhodopsin	Homo sapiens	13-22
12416988-1	2002	Monomolecular films of the membrane protein rhodopsin have been investigated in situ at the air-water interface by polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) and X-ray reflectivity in order to find conditions that retain the protein secondary structure.	Water	96-101	rhodopsin	Homo sapiens	44-53
12416988-4	2002	The amide I/amide II ratio also allowed to determine that the orientation of rhodopsin only slightly changes with surface pressure and it remains almost unchanged when the film is maintained at 20 mN m(-1) for 120 min at 4 degrees C. In addition, the PM-IRRAS spectra of rod outer segment disk membranes in monolayers suggest that rhodopsin also retained its secondary structure in these films.	Amides	4-9	rhodopsin	Homo sapiens	77-86
12176994-1	2002	Phototransduction is initiated by the photoisomerization of rhodopsin (Rho) chromophore 11-cis-retinylidene to all-trans-retinylidene.	all-trans-retinylidene	111-133	rhodopsin	Homo sapiens	60-69
12370422-0	2002	Structure and function in rhodopsin: a tetracycline-inducible system in stable mammalian cell lines for high-level expression of opsin mutants.	Tetracycline	39-51	rhodopsin	Homo sapiens	26-35
12499666-9	2002	Additional fluorescence (due to rhodopsin) was observed in the villous layer upon treatment with NaBH(4) after denaturation.	sodium borohydride	97-101	rhodopsin	Homo sapiens	32-41
12177057-1	2002	The visual pigment rhodopsin is characterized by an 11-cis retinal chromophore bound to Lys-296 via a protonated Schiff base.	Lysine	88-91	rhodopsin	Homo sapiens	19-28
12177057-1	2002	The visual pigment rhodopsin is characterized by an 11-cis retinal chromophore bound to Lys-296 via a protonated Schiff base.	Schiff Bases	113-124	rhodopsin	Homo sapiens	19-28
12370423-0	2002	Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line.	Tetracycline	125-137	rhodopsin	Homo sapiens	26-35
12370423-0	2002	Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line.	Tetracycline	125-137	rhodopsin	Homo sapiens	62-71
12370423-5	2002	Analysis of the N-glycan in rhodopsin expressed by the HEK293S GnTI(-) stable cell line showed it to be Man(5)GlcNAc(2).	n-glycan	16-24	rhodopsin	Homo sapiens	28-37
12146960-11	2002	Interaction of the resulting spin-labeled Galphabetagamma with photoactivated rhodopsin, followed by rhodopsin-catalyzed GTPgammaS binding, caused the amino-terminal domain of Galpha to revert to a dynamically disordered state similar to that of the GDP-bound form.	Guanosine Diphosphate	250-253	rhodopsin	Homo sapiens	78-87
12237324-5	2002	We have also built a molecular model of the M(2) mAChR-(S)-methacholine complex, based on the X-ray crystallographic structure of rhodopsin.	Methacholine Chloride	55-71	rhodopsin	Homo sapiens	130-139
12359230-0	2002	Retinitis pigmentosa-associated rhodopsin mutations in three membrane-located cysteine residues present three different biochemical phenotypes.	Cysteine	78-86	rhodopsin	Homo sapiens	32-41
12163076-1	2002	Halorhodopsin, a light-driven halide pump, is the second archaeal rhodopsin involved in ion pumping to be studied at high resolution by X-ray crystallography.	halide	30-36	rhodopsin	Homo sapiens	4-13
12163079-2	2002	Spectral differences between sensory rhodopsin and the light-driven proton pump bacteriorhodopsin depend largely upon the repositioning of a conserved arginine residue in the chromophore-binding pocket.	Arginine	151-159	rhodopsin	Homo sapiens	37-46
12146960-11	2002	Interaction of the resulting spin-labeled Galphabetagamma with photoactivated rhodopsin, followed by rhodopsin-catalyzed GTPgammaS binding, caused the amino-terminal domain of Galpha to revert to a dynamically disordered state similar to that of the GDP-bound form.	Guanosine Diphosphate	250-253	rhodopsin	Homo sapiens	101-110
12206508-5	2002	Interestingly, PLP modified both the alpha- and beta-subunits of T. Moreover, PLP in the presence of GDP behaved as a GTP analog, since this mixture was capable of dissociating T from T:photoactivated rhodopsin complexes.	Guanosine Diphosphate	101-104	rhodopsin	Homo sapiens	201-210
12081478-1	2002	The crystal structure of rhodopsin revealed a cytoplasmic helical segment (H8) extending from transmembrane (TM) helix seven to a pair of vicinal palmitoylated cysteine residues.	Cysteine	160-168	rhodopsin	Homo sapiens	25-34
12081478-6	2002	We conclude that H8 in rhodopsin, in addition to its role in binding the G protein transducin, acts as a membrane-dependent conformational switch domain.	N-(2-(methylamino)ethyl)-5-isoquinolinesulfonamide	17-19	rhodopsin	Homo sapiens	23-32
12065750-4	2002	The different amino acid sequence that forms helix 3 in rhodopsin (basically the conserved Gly(3.36)Glu(3.37) motif in the opsin family) and the 5-HT1A receptor (the conserved Cys(3.36)Thr(3.37) motif in the neurotransmitter family) produces these structural divergences.	Glycine	91-94	rhodopsin	Homo sapiens	56-65
12065750-4	2002	The different amino acid sequence that forms helix 3 in rhodopsin (basically the conserved Gly(3.36)Glu(3.37) motif in the opsin family) and the 5-HT1A receptor (the conserved Cys(3.36)Thr(3.37) motif in the neurotransmitter family) produces these structural divergences.	Glutamic Acid	100-103	rhodopsin	Homo sapiens	56-65
12065750-4	2002	The different amino acid sequence that forms helix 3 in rhodopsin (basically the conserved Gly(3.36)Glu(3.37) motif in the opsin family) and the 5-HT1A receptor (the conserved Cys(3.36)Thr(3.37) motif in the neurotransmitter family) produces these structural divergences.	Threonine	185-188	rhodopsin	Homo sapiens	56-65
12065750-4	2002	The different amino acid sequence that forms helix 3 in rhodopsin (basically the conserved Gly(3.36)Glu(3.37) motif in the opsin family) and the 5-HT1A receptor (the conserved Cys(3.36)Thr(3.37) motif in the neurotransmitter family) produces these structural divergences.	Cysteine	176-179	rhodopsin	Homo sapiens	56-65
12206508-5	2002	Interestingly, PLP modified both the alpha- and beta-subunits of T. Moreover, PLP in the presence of GDP behaved as a GTP analog, since this mixture was capable of dissociating T from T:photoactivated rhodopsin complexes.	Guanosine Triphosphate	118-121	rhodopsin	Homo sapiens	201-210
11889130-4	2002	Reduced cholesterol in disk membranes resulted in a higher proportion of photolyzed rhodopsin being converted to the G protein-activating metarhodopsin II (MII) conformation, whereas enrichment of cholesterol reduced the extent of MII formation.	Cholesterol	8-19	rhodopsin	Homo sapiens	84-93
12034887-1	2002	In retinal rods, light-induced isomerization of 11-cis-retinal to all-trans-retinal within rhodopsin triggers an enzyme cascade that lowers the concentration of cGMP.	Cyclic GMP	161-165	rhodopsin	Homo sapiens	91-100
11889130-7	2002	In addition, the thermal stability of rhodopsin increased with mol % of cholesterol in disk membranes.	Cholesterol	72-83	rhodopsin	Homo sapiens	38-47
11889130-9	2002	These results indicate that cholesterol mediates the function of the G protein-coupled receptor, rhodopsin, by influencing membrane lipid properties, i.e. reducing acyl chain packing free volume, rather than interacting specifically with rhodopsin.	Cholesterol	28-39	rhodopsin	Homo sapiens	97-106
11904408-0	2002	Solution NMR spectroscopy of [alpha -15N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence.	[alpha -15n]lysine	29-47	rhodopsin	Homo sapiens	56-65
12001191-5	2002	RESULTS: FAMA is a feasible procedure for prenatal molecular diagnosis of rhodopsin mutations.	fama	9-13	rhodopsin	Homo sapiens	74-83
11888268-2	2002	Influence of salts on conformational equilibria between active and Inactive states of rhodopsin.	Salts	13-18	rhodopsin	Homo sapiens	86-95
11904408-0	2002	Solution NMR spectroscopy of [alpha -15N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence.	Lysine	156-159	rhodopsin	Homo sapiens	56-65
11904408-1	2002	[alpha-(15)N]Lysine-labeled rhodopsin, prepared by expression of a synthetic gene in HEK293 cells, was investigated both by conventional and transverse relaxation optimized spectroscopy-type heteronuclear single quantum correlation spectroscopy.	[alpha-(15)n]lysine	0-19	rhodopsin	Homo sapiens	28-37
11904408-2	2002	Whereas rhodopsin contains 11 lysines, 8 in cytoplasmic loops and 1 each in the C-terminal peptide sequence and the intradiscal and transmembrane domains, only a single sharp peak was observed in dodecyl maltoside micelles.	Lysine	30-37	rhodopsin	Homo sapiens	8-17
11904408-7	2002	First, the signal is observed in HNCO spectra of rhodopsin, containing the labeled [(13)C]Ser-338/[(15)N]Lys-339 dipeptide.	Serine	90-93	rhodopsin	Homo sapiens	49-58
11904408-7	2002	First, the signal is observed in HNCO spectra of rhodopsin, containing the labeled [(13)C]Ser-338/[(15)N]Lys-339 dipeptide.	Lysine	105-108	rhodopsin	Homo sapiens	49-58
11904408-7	2002	First, the signal is observed in HNCO spectra of rhodopsin, containing the labeled [(13)C]Ser-338/[(15)N]Lys-339 dipeptide.	Dipeptides	113-122	rhodopsin	Homo sapiens	49-58
11904408-10	2002	The results indicate motion in the backbone amide groups of rhodopsin at time scales depending on their location in the sequence.	Amides	44-49	rhodopsin	Homo sapiens	60-69
11866527-0	2002	X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8.	Cysteine	106-114	rhodopsin	Homo sapiens	69-78
11866527-0	2002	X-ray diffraction of heavy-atom labelled two-dimensional crystals of rhodopsin identifies the position of cysteine 140 in helix 3 and cysteine 316 in helix 8.	Cysteine	134-142	rhodopsin	Homo sapiens	69-78
11866527-4	2002	The native cysteine residues C140 and C316 were then selectively labelled with mercury using the sulphydryl-specific reagent p-chloromercuribenzoate (1.6-2.1 mol Hg per mol rhodopsin).	p-chloromercuribenzoate	125-148	rhodopsin	Homo sapiens	173-182
12596918-5	2002	Lastly, the antibody blocks recoverin function (inhibition of rhodopsin phosphorylation in a calcium dependent manner), and enhancement of rhodopsin phosphorylation induces retinal apoptosis.	Calcium	93-100	rhodopsin	Homo sapiens	62-71
11852972-4	2002	The resulting 11-cis-retinol feeds into the visual cycle to be oxidized to 11-cis-retinal, thus replenishing the 11-cis-retinal of the rhodopsin.	Vitamin A	14-28	rhodopsin	Homo sapiens	135-144
11774337-2	2002	Photoisomerization of Limulus rhodopsin leads to phosphoinositide hydrolysis, resulting in the production of inositol trisphosphate and diacylglycerol (DAG).	Phosphatidylinositols	49-65	rhodopsin	Homo sapiens	30-39
11774337-2	2002	Photoisomerization of Limulus rhodopsin leads to phosphoinositide hydrolysis, resulting in the production of inositol trisphosphate and diacylglycerol (DAG).	inositol 1,2,3-trisphosphate	109-131	rhodopsin	Homo sapiens	30-39
11774337-2	2002	Photoisomerization of Limulus rhodopsin leads to phosphoinositide hydrolysis, resulting in the production of inositol trisphosphate and diacylglycerol (DAG).	Diglycerides	136-150	rhodopsin	Homo sapiens	30-39
11774337-2	2002	Photoisomerization of Limulus rhodopsin leads to phosphoinositide hydrolysis, resulting in the production of inositol trisphosphate and diacylglycerol (DAG).	Diglycerides	152-155	rhodopsin	Homo sapiens	30-39
11774337-5	2002	PKC activation by (-)-indolactam V in darkness induces disorganization and swelling of the rhodopsin-containing microvilli and endocytosis of rhabdomeral membrane.	indolactam V	18-34	rhodopsin	Homo sapiens	91-100
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	Guanosine Triphosphate	6-9	rhodopsin	Homo sapiens	78-87
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	Guanosine Diphosphate	10-13	rhodopsin	Homo sapiens	78-87
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	talpha	55-61	rhodopsin	Homo sapiens	78-87
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	Guanosine Triphosphate	93-96	rhodopsin	Homo sapiens	78-87
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	talpha	108-114	rhodopsin	Homo sapiens	78-87
12596920-2	2002	After GTP/GDP exchange on the a subunit of transducin (Talpha) by illuminated rhodopsin, the GTP-bound form Talpha (GTP/Talpha) interacts with the regulatory subunit (Pgamma) of PDE6 to activate cGMP hydrolytic activity.	Cyclic GMP	195-199	rhodopsin	Homo sapiens	78-87
12187497-8	2002	CONCLUSIONS: The lower than expected D for retinoids and our calculations suggest that mechanisms in addition to pure aqueous diffusion may be needed to account for normal rhodopsin regeneration rates in the mammalian retina.	Retinoids	43-52	rhodopsin	Homo sapiens	172-181
12596942-3	2002	This amplification is critically dependent upon the coupling of photoactivated rhodopsin to the phosphoinositide cascade, resulting in the release of Ca2+ from intracellular stores.	Phosphatidylinositols	96-112	rhodopsin	Homo sapiens	79-88
11820824-8	2002	These aspects are demonstrated by optimization and simulation of novel DCP and C7 based 2D N(CO)CA, N(CA)CB, and N(CA)CX MAS correlation experiments for multiple-spin clusters in ubiquitin and by simulation of PISA wheels from PISEMA spectra of uniaxially oriented bacteriorhodopsin and rhodopsin under conditions of finite RF pulses and multiple spin interactions.	dcp	71-74	rhodopsin	Homo sapiens	273-282
11853707-10	2002	Among these drugs, only betaxolol showed a recovery effect on NMDA-induced decrease of rhodopsin phosphorylation.	Betaxolol	24-33	rhodopsin	Homo sapiens	87-96
11853707-10	2002	Among these drugs, only betaxolol showed a recovery effect on NMDA-induced decrease of rhodopsin phosphorylation.	N-Methylaspartate	62-66	rhodopsin	Homo sapiens	87-96
11544259-2	2001	Rhodopsin was reconstituted into large, unilamellar phospholipid vesicles with varying acyl chain unsaturation, with and without cholesterol.	Phospholipids	52-64	rhodopsin	Homo sapiens	0-9
11747423-2	2001	Magnetic dipole-dipole interactions between the spins are analyzed to provide interspin distance distributions in both the dark and photoactivated states of rhodopsin.	dipole-dipole	9-22	rhodopsin	Homo sapiens	157-166
11747424-1	2001	Double-spin-labeled mutants of rhodopsin were prepared containing a nitroxide side chain at position 316 in the cytoplasmic surface helix H8, and a second nitroxide in the sequence of residues 60-75, which includes the cytoplasmic loop CL1 and cytoplasmic ends of helices TM1 and TM2.	Hydroxylamine	68-77	rhodopsin	Homo sapiens	31-40
11747424-1	2001	Double-spin-labeled mutants of rhodopsin were prepared containing a nitroxide side chain at position 316 in the cytoplasmic surface helix H8, and a second nitroxide in the sequence of residues 60-75, which includes the cytoplasmic loop CL1 and cytoplasmic ends of helices TM1 and TM2.	Hydroxylamine	155-164	rhodopsin	Homo sapiens	31-40
11747424-2	2001	Magnetic dipole-dipole interactions between the spins were analyzed to provide interspin distance distributions in both the dark and photoactivated states of rhodopsin.	dipole-dipole	9-22	rhodopsin	Homo sapiens	158-167
11747424-3	2001	In the dark state in solutions of dodecyl maltoside, the interspin distances are found to be consistent with structural models of the nitroxide side chain and rhodopsin, both derived from crystallography.	dodecyl maltoside	34-51	rhodopsin	Homo sapiens	159-168
11747424-3	2001	In the dark state in solutions of dodecyl maltoside, the interspin distances are found to be consistent with structural models of the nitroxide side chain and rhodopsin, both derived from crystallography.	Hydroxylamine	134-143	rhodopsin	Homo sapiens	159-168
11747424-4	2001	Photoactivation of rhodopsin shows a pattern of increases in internitroxide distance between the reference, position 316 in H8, and residues in CL1 and TM2 that suggests an outward displacement of TM2 relative to H8 by approximately 3 A.	internitroxide	61-75	rhodopsin	Homo sapiens	19-28
11720992-0	2001	Rhodopsin-transducin interface: studies with conformationally constrained peptides.	Peptides	74-82	rhodopsin	Homo sapiens	0-9
12402507-5	2002	Another distinct feature is rhodopsin"s ligand, 11-cis-retinal, which is covalently bound via a Schiff base to transmembrane seven (TM VII), allowing extensive spectroscopic studies.	Schiff Bases	96-107	rhodopsin	Homo sapiens	28-37
12408104-6	2002	As with rhodopsin, conformational signaling appears to depend on the rearrangement of key electrostatic, hydrogen-bond, and hydrophobic interactions that normally serve to stabilize the inactive LHR conformation.	Hydrogen	105-113	rhodopsin	Homo sapiens	8-17
11859928-1	2001	The conserved residues Y239 and L240 of human VPAC1 receptor are predicted to be at the same location as the asparagine and arginine in the "DRY" motif in the Rhodopsin family of G protein-coupled receptors.	Asparagine	109-119	rhodopsin	Homo sapiens	159-168
11859928-1	2001	The conserved residues Y239 and L240 of human VPAC1 receptor are predicted to be at the same location as the asparagine and arginine in the "DRY" motif in the Rhodopsin family of G protein-coupled receptors.	Arginine	124-132	rhodopsin	Homo sapiens	159-168
11544259-2	2001	Rhodopsin was reconstituted into large, unilamellar phospholipid vesicles with varying acyl chain unsaturation, with and without cholesterol.	Cholesterol	129-140	rhodopsin	Homo sapiens	0-9
11683644-1	2001	In rhodopsin, the retinal chromophore is covalently bound to the apoprotein by a protonated Schiff base, which is stabilized by the negatively charged counterion Glu113, conferring upon it a pK(a) of presumably >16.	Schiff Bases	92-103	rhodopsin	Homo sapiens	3-12
11697851-0	2001	Chemical modification of transducin with iodoacetic acid: transducin-alpha carboxymethylated at Cys(347) allows transducin binding to Light-activated rhodopsin but prevents its release in the presence of GTP.	Iodoacetic Acid	41-56	rhodopsin	Homo sapiens	150-159
11697851-0	2001	Chemical modification of transducin with iodoacetic acid: transducin-alpha carboxymethylated at Cys(347) allows transducin binding to Light-activated rhodopsin but prevents its release in the presence of GTP.	Cysteine	96-99	rhodopsin	Homo sapiens	150-159
11697851-6	2001	A comparable inactivation of T and analogous interactions between T and R* were observed when 2-nitro 5-thiocyanobenzoic acid (NTCBA) was used as the modifying reagent (J. O. Ortiz and J. Bubis, 2001, Effects of differential sulfhydryl group-specific labeling on the rhodopsin and guanine nucleotide binding activities of transducin, Arch.	2-nitro-5-thiocyanobenzoic acid	94-125	rhodopsin	Homo sapiens	267-276
11697851-6	2001	A comparable inactivation of T and analogous interactions between T and R* were observed when 2-nitro 5-thiocyanobenzoic acid (NTCBA) was used as the modifying reagent (J. O. Ortiz and J. Bubis, 2001, Effects of differential sulfhydryl group-specific labeling on the rhodopsin and guanine nucleotide binding activities of transducin, Arch.	2-nitro-5-thiocyanobenzoic acid	127-132	rhodopsin	Homo sapiens	267-276
11466416-1	2001	A dominant form of human congenital nightblindness is caused by a gly90-->asp (G90D) mutation in rhodopsin.	Aspartic Acid	77-80	rhodopsin	Homo sapiens	100-109
11724460-11	2001	DHA also has significant effects on photoreceptor membranes and neurotransmitters involved in the signal transduction process; rhodopsin activation, rod and cone development, neuronal dendritic connectivity, and functional maturation of the central nervous system.	Docosahexaenoic Acids	0-3	rhodopsin	Homo sapiens	127-136
11743870-0	2001	Internal water molecules as mobile polar groups for light-induced proton translocation in bacteriorhodopsin and rhodopsin as studied by difference FTIR spectroscopy.	Water	9-14	rhodopsin	Homo sapiens	98-107
11989623-1	2001	A computational model of the transmembrane domain of the human 5-HT4 receptorcomplexed with the GR113808 antagonist was constructed from the crystal structure of rhodopsin and the putative residues of the ligand-binding site, experimentally determined by site-directed mutagenesis.	GR 113808	96-104	rhodopsin	Homo sapiens	162-171
11601970-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.	Disulfides	139-148	rhodopsin	Homo sapiens	71-80
11601970-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.	Cysteine	194-203	rhodopsin	Homo sapiens	71-80
11601970-7	2001	The observed disulfide bond formation rates correlate well with proximity of these residues found in the crystal structure of rhodopsin in the dark.	Disulfides	13-22	rhodopsin	Homo sapiens	126-135
11601971-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4.	Disulfides	139-148	rhodopsin	Homo sapiens	71-80
11601971-0	2001	Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between cysteine pairs engineered in cytoplasmic loops 1, 3, and 4.	Cysteine	172-180	rhodopsin	Homo sapiens	71-80
11601971-6	2001	Comparisons of the results from disulfide bond formation in solution with the distances observed in the rhodopsin crystal structure showed that the rates of disulfide bond formation in most cases were consistent with the amino acid proximities as revealed in crystal structure.	Disulfides	157-166	rhodopsin	Homo sapiens	104-113
11601986-1	2001	In vertebrate photoreceptors, photoexcited rhodopsin interacts with the G protein transducin, causing it to bind GTP and stimulate the enzyme cGMP phosphodiesterase.	Guanosine Triphosphate	113-116	rhodopsin	Homo sapiens	43-52
11316815-7	2001	Modeling the locked chromophore analogs in the active site of rhodopsin suggests that the beta-ionone ring rotates but is largely confined within the binding site of the natural 11-cis-retinal chromophore.	beta-ionone	90-101	rhodopsin	Homo sapiens	62-71
11408595-3	2001	Moreover, the amino acid residues inferred to form the surface of the binding-site crevice based on our application of the substituted-cysteine accessibility method in the dopamine D(2) receptor are in remarkable agreement with the rhodopsin structure, with the notable exception of some residues in the fourth transmembrane segment.	Cysteine	135-143	rhodopsin	Homo sapiens	232-241
11423407-4	2001	The docosahexaenoic fatty acid, in particular, is fundamental for the proper function of the visual receptor rhodopsin.	docosahexaenoic fatty acid	4-30	rhodopsin	Homo sapiens	109-118
11408595-5	2001	We further propose that several of the highly unusual structural features of rhodopsin are also present in amine GPCRs, despite the absence of amino acids that might have thought to have been critical to the adoption of these features.	Amines	107-112	rhodopsin	Homo sapiens	77-86
11237604-2	2001	Using both existing and newly developed tools to analyze transmembrane segments of all available membrane protein three-dimensional structures, including that very recently elucidated for the GPCR, rhodopsin, we report here the finding of frequent non-alpha-helical components, i.e. 3(10)-helices ("tight turns"), pi-helices ("wide turns") and intrahelical kinks (often due to residues other than proline).	Proline	397-404	rhodopsin	Homo sapiens	198-207
11320236-0	2001	Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants.	Disulfides	99-108	rhodopsin	Homo sapiens	26-35
11320236-2	2001	Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin.	Cysteine	130-133	rhodopsin	Homo sapiens	171-180
11320236-2	2001	Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin.	Cysteine	138-141	rhodopsin	Homo sapiens	171-180
11320236-2	2001	Previous work has shown that misfolding is caused by the formation of a disulfide bond in the ID domain different from the native Cys-110-Cys-187 disulfide bond in native rhodopsin.	Disulfides	146-155	rhodopsin	Homo sapiens	171-180
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda >495 nm.	monocysteine	55-67	rhodopsin	Homo sapiens	68-77
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda >495 nm.	monocysteine	55-67	rhodopsin	Homo sapiens	167-176
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda >495 nm.	Disulfides	91-100	rhodopsin	Homo sapiens	68-77
11320237-4	2001	The reagent is attached to the SH group of cytoplasmic monocysteine rhodopsin mutants by a disulfide-exchange reaction with the pyridylthio group, and the derivatized rhodopsin then is complexed with T by illumination at lambda >495 nm.	Disulfides	91-100	rhodopsin	Homo sapiens	167-176
11320237-6	2001	Crosslinking was demonstrated between T and a number of single cysteine rhodopsin mutants.	Cysteine	63-71	rhodopsin	Homo sapiens	72-81
11320239-1	2001	19F nuclear Overhauser effects (NOEs) between fluorine labels on the cytoplasmic domain of rhodopsin solubilized in detergent micelles are reported.	Fluorine	46-54	rhodopsin	Homo sapiens	91-100
11320239-2	2001	Previously, high-resolution solution (19)F NMR spectra of fluorine-labeled rhodopsin in detergent micelles were described, demonstrating the applicability of this technique to studies of tertiary structure in the cytoplasmic domain.	Fluorine	58-66	rhodopsin	Homo sapiens	75-84
11284674-1	2001	In the absence of a high-resolution diffraction structure, the orientation and conformation of the protonated Schiffs base retinylidinium chromophore of rhodopsin within the opsin matrix has been the subject of much speculation.	schiffs base retinylidinium	110-137	rhodopsin	Homo sapiens	153-162
11258947-0	2001	Ultra-high-field MAS NMR assay of a multispin labeled ligand bound to its G-protein receptor target in the natural membrane environment: electronic structure of the retinylidene chromophore in rhodopsin.	retinylidene	165-177	rhodopsin	Homo sapiens	193-202
11258947-2	2001	The 13C shifts are assigned with magic angle spinning NMR dipolar correlation spectroscopy in a single experiment and compared with data of singly labeled retinylidene ligands in detergent-solubilized rhodopsin.	retinylidene	155-167	rhodopsin	Homo sapiens	201-210
11258947-4	2001	We have used the chemical shift data to analyze the electronic structure of the retinylidene ligand at three levels of understanding: (i) by specifying interactions between the 13C-labeled ligand and the G-protein-coupled receptor target, (ii) by making a charge assessment of the protonation of the Schiff base in rhodopsin, and (iii) by evaluating the total charge on the carbons of the retinylidene chromophore.	retinylidene	80-92	rhodopsin	Homo sapiens	315-324
11258947-5	2001	In this way it is shown that a conjugation defect is the predominant ground-state property governing the molecular electronics of the retinylidene chromophore in rhodopsin.	retinylidene	134-146	rhodopsin	Homo sapiens	162-171
11258947-8	2001	Since rhodopsin has the largest value of Delta(sigma)odd, the data contribute to existing and converging spectroscopic evidence for a complex counterion stabilizing the protonated Schiff base in the binding pocket.	Schiff Bases	180-191	rhodopsin	Homo sapiens	6-15
11370846-2	2001	All these compounds rapidly inhibited the [3H]GMPpNp-binding activity of transducin stimulated by photoexcited rhodopsin (R*).	[3h]gmppnp	42-52	rhodopsin	Homo sapiens	111-120
11370846-5	2001	Photoactivated rhodopsin was capable of protecting against the observed AMDA and NTCBA inhibition in transducin function, but not against the inactivation caused by VP or DM.	4-acetamido-4'-maleimidylstilbene-2,2'-disulfonic acid	72-76	rhodopsin	Homo sapiens	15-24
11394879-4	2001	Cultured NPE cells responded to treatment with phorbol ester by enhancing the expression of rhodopsin mRNA three- to fourfold.	Phorbol Esters	47-60	rhodopsin	Homo sapiens	92-101
11392621-6	2001	A model of the M1 receptor, based on the recently determined structure of rhodopsin, has the residues that have been shown to be important for gallamine binding clustered within and to one side of a cleft in the extracellular face of the receptor.	Gallamine Triethiodide	143-152	rhodopsin	Homo sapiens	74-83
11171300-2	2001	Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol.	Guanine Nucleotides	37-55	rhodopsin	Homo sapiens	16-25
11171300-2	2001	Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol.	Phosphatidylinositol 4,5-Diphosphate	140-177	rhodopsin	Homo sapiens	16-25
11171300-2	2001	Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol.	Inositol 1,4,5-Trisphosphate	181-209	rhodopsin	Homo sapiens	16-25
11171300-2	2001	Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol.	Diglycerides	214-228	rhodopsin	Homo sapiens	16-25
11171300-8	2001	Since rhodopsin, receptor kinase and phospholipase C are involved upstream of phosphatidylinositol turnover in the signal cascade, our result suggests that phosphatidylinositol turnover is important in feedback pathways in the signalling system.	Phosphatidylinositols	78-98	rhodopsin	Homo sapiens	6-15
11171300-8	2001	Since rhodopsin, receptor kinase and phospholipase C are involved upstream of phosphatidylinositol turnover in the signal cascade, our result suggests that phosphatidylinositol turnover is important in feedback pathways in the signalling system.	Phosphatidylinositols	156-176	rhodopsin	Homo sapiens	6-15
11135409-1	2001	CASSCF and GAUSSIAN CIS calculations were performed on ground and excited states of different conformations of 11-cis-retinal protonated Schiff bases, the chromophore of rhodopsin, in order to study their chiroptical properties and attempt a correlation between absolute conformation and CD-spectral data.	Schiff Bases	137-149	rhodopsin	Homo sapiens	170-179
11018024-3	2001	Using a combinatorial library we identified analogs of G(talpha)-(340-350) that bound light-activated rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996) J. Biol.	talpha	57-63	rhodopsin	Homo sapiens	102-111
10930473-2	2000	METHODS: The sequence of the seventh transmembrane segment of rhodopsin, which contains the NPxxY sequence that is highly conserved among G-protein coupled receptors and lys296 that forms the Schiff base with the retinal, was synthesized by solid phase peptide synthesis.	Schiff Bases	192-203	rhodopsin	Homo sapiens	62-71
11106502-0	2000	Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface.	Alexa594	72-80	rhodopsin	Homo sapiens	40-49
11106502-2	2000	Rhodopsin in native membranes was selectively modified with fluorescent Alexa594-maleimide at the Cys(316) position, with a large excess of the reagent Cys(140) that was also derivatized.	alexa594-maleimide	72-90	rhodopsin	Homo sapiens	0-9
11106502-2	2000	Rhodopsin in native membranes was selectively modified with fluorescent Alexa594-maleimide at the Cys(316) position, with a large excess of the reagent Cys(140) that was also derivatized.	Cysteine	98-101	rhodopsin	Homo sapiens	0-9
11106502-2	2000	Rhodopsin in native membranes was selectively modified with fluorescent Alexa594-maleimide at the Cys(316) position, with a large excess of the reagent Cys(140) that was also derivatized.	Cysteine	152-155	rhodopsin	Homo sapiens	0-9
11106502-3	2000	Modification with Alexa594 allowed the monitoring of fluorescence changes at a red excitation light wavelength of 605 nm, thus avoiding significant rhodopsin bleaching.	Alexa594	18-26	rhodopsin	Homo sapiens	148-157
11106502-4	2000	Upon absorption of a photon by rhodopsin, the fluorescence intensity increased as much as 20% at acidic pH with an apparent pK(a) of approximately 6.8 at 4 degrees C, and was sensitive to the presence of hydroxylamine.	Hydroxylamine	204-217	rhodopsin	Homo sapiens	31-40
11106502-9	2000	In the presence of arrestin, under conditions that favored the formation of metarhodopsin I or II, a phosphorylated, photolyzed rhodopsin-Alexa594 complex only slightly decreased the fluorescence intensity, suggesting that the cytoplasmic surface structure of metarhodopsin II is different in the complex with arrestin and transducin.	Alexa594	138-146	rhodopsin	Homo sapiens	80-89
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	45-53	rhodopsin	Homo sapiens	63-72
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	45-53	rhodopsin	Homo sapiens	83-92
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	45-53	rhodopsin	Homo sapiens	83-92
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	74-82	rhodopsin	Homo sapiens	63-72
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	74-82	rhodopsin	Homo sapiens	83-92
11106502-10	2000	These results demonstrate the application of Alexa594-modified rhodopsin (Alexa594-rhodopsin) to continuously monitor the conformational changes in rhodopsin during light-induced transformations and its interactions with other proteins.	Alexa594	74-82	rhodopsin	Homo sapiens	83-92
11106612-0	2000	Rhodopsin activation affects the environment of specific neighboring phospholipids: an FTIR spectroscopic study.	Phospholipids	69-82	rhodopsin	Homo sapiens	0-9
11106612-3	2000	A difference band at 1744 cm(-1) (+)/1727 cm(-1) (-) was identified in the FTIR-difference spectrum of rhodopsin mutant D83N/E122Q in which spectral difference bands arising from the carbonyl stretching frequencies of protonated carboxylic acid groups were removed by mutation.	Carboxylic Acids	229-244	rhodopsin	Homo sapiens	103-112
11106612-5	2000	Rhodopsin and the D83N/E122Q mutant were reconstituted into various (13)C-labeled 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine vesicles and probed.	Carbon-13	68-73	rhodopsin	Homo sapiens	0-9
11058128-1	2000	To explore the ability of triplex-forming oligodeoxyribonucleotides (TFOs) to inhibit genes responsible for dominant genetic disorders, we used two TFOs to block expression of the human rhodopsin gene, which encodes a G protein-coupled receptor involved in the blinding disorder autosomal dominant retinitis pigmentosa.	triplex-forming oligodeoxyribonucleotides	26-67	rhodopsin	Homo sapiens	186-195
11058128-1	2000	To explore the ability of triplex-forming oligodeoxyribonucleotides (TFOs) to inhibit genes responsible for dominant genetic disorders, we used two TFOs to block expression of the human rhodopsin gene, which encodes a G protein-coupled receptor involved in the blinding disorder autosomal dominant retinitis pigmentosa.	tfos	69-73	rhodopsin	Homo sapiens	186-195
11058128-1	2000	To explore the ability of triplex-forming oligodeoxyribonucleotides (TFOs) to inhibit genes responsible for dominant genetic disorders, we used two TFOs to block expression of the human rhodopsin gene, which encodes a G protein-coupled receptor involved in the blinding disorder autosomal dominant retinitis pigmentosa.	tfos	148-152	rhodopsin	Homo sapiens	186-195
11058128-2	2000	Psoralen-modified TFOs and UVA irradiation were used to form photoadducts at two target sites in a plasmid expressing a rhodopsin-EGFP fusion, which was then transfected into HT1080 cells.	tfos	18-22	rhodopsin	Homo sapiens	120-129
11058128-3	2000	Each TFO reduced rhodopsin-GFP expression by 70-80%, whereas treatment with both reduced expression by 90%.	tfo	5-8	rhodopsin	Homo sapiens	17-26
11058128-8	2000	Irradiation of cells after transfection with plasmid and psoralen-TFOs produced photoadducts inside the cells and also inhibited expression of rhodopsin-EGFP.	psoralen-tfos	57-70	rhodopsin	Homo sapiens	143-152
11058128-9	2000	We conclude that directing DNA damage with psoralen-TFOs is an efficient and specific means for blocking transcription from the human rhodopsin gene.	psoralen-tfos	43-56	rhodopsin	Homo sapiens	134-143
11016972-2	2000	A case is made that the Hula-Twist mechanism, postulated in 1985 as a photochemical reaction pathway for a polyene chromophore imbedded in a protein binding cavity such as those of rhodopsin and bacteriorhodopsin, is also a dominant reaction pathway for a diene, or a longer polyene confined in a rigid (relative to isomerization rate) medium.	Polyenes	107-114	rhodopsin	Homo sapiens	181-190
11016972-2	2000	A case is made that the Hula-Twist mechanism, postulated in 1985 as a photochemical reaction pathway for a polyene chromophore imbedded in a protein binding cavity such as those of rhodopsin and bacteriorhodopsin, is also a dominant reaction pathway for a diene, or a longer polyene confined in a rigid (relative to isomerization rate) medium.	diene	256-261	rhodopsin	Homo sapiens	181-190
11016972-2	2000	A case is made that the Hula-Twist mechanism, postulated in 1985 as a photochemical reaction pathway for a polyene chromophore imbedded in a protein binding cavity such as those of rhodopsin and bacteriorhodopsin, is also a dominant reaction pathway for a diene, or a longer polyene confined in a rigid (relative to isomerization rate) medium.	Polyenes	275-282	rhodopsin	Homo sapiens	181-190
10964659-6	2000	A reducing agent [dithiothreitol (DDT) or mercaptoacetic acid (MAA)] also induces retinal synthesis in the dark via a rhodopsin with a chromophore.	Dithiothreitol	18-32	rhodopsin	Homo sapiens	118-127
10964659-6	2000	A reducing agent [dithiothreitol (DDT) or mercaptoacetic acid (MAA)] also induces retinal synthesis in the dark via a rhodopsin with a chromophore.	DDT	34-37	rhodopsin	Homo sapiens	118-127
10964659-6	2000	A reducing agent [dithiothreitol (DDT) or mercaptoacetic acid (MAA)] also induces retinal synthesis in the dark via a rhodopsin with a chromophore.	2-mercaptoacetate	42-61	rhodopsin	Homo sapiens	118-127
10964659-6	2000	A reducing agent [dithiothreitol (DDT) or mercaptoacetic acid (MAA)] also induces retinal synthesis in the dark via a rhodopsin with a chromophore.	2-mercaptoacetate	63-66	rhodopsin	Homo sapiens	118-127
10964659-8	2000	We conclude that the reducing agent as well as light break a disulfide bond resulting in activation of the rhodopsin and induction of carotenogenesis.	Disulfides	61-70	rhodopsin	Homo sapiens	107-116
10944211-2	2000	This is accomplished by computing the ground state (S(0)) and the first two singlet excited-state (S(1), S(2)) energies along the rigorously determined photoisomerization coordinate of the rhodopsin chromophore model 4-cis-gamma-methylnona-2,4,6,8-tetraeniminium cation and the bacteriorhodopsin chromophore model all-trans-hepta-2,4, 6-trieniminium cation in isolated conditions.	,4,6,8-tetraeniminium	241-262	rhodopsin	Homo sapiens	189-198
10944211-2	2000	This is accomplished by computing the ground state (S(0)) and the first two singlet excited-state (S(1), S(2)) energies along the rigorously determined photoisomerization coordinate of the rhodopsin chromophore model 4-cis-gamma-methylnona-2,4,6,8-tetraeniminium cation and the bacteriorhodopsin chromophore model all-trans-hepta-2,4, 6-trieniminium cation in isolated conditions.	2,4, 6-trieniminium	330-349	rhodopsin	Homo sapiens	189-198
11139649-9	2000	RESULTS: The analyses showed that: (1) Within the context of a model with Ca++ feedback onto rhodopsin (R*) lifetime (tR), the salient features of the Murnick & Lamb data can only be accounted for if the rate-limiting step is not the Ca++-sensitive step in the early cascade reactions, i.e., if PDE* lifetime, and not tR, is rate-limiting.	Adenosine Monophosphate	160-163	rhodopsin	Homo sapiens	93-102
11094174-0	2000	Rhodopsin gene codon 106 mutation (Gly-to-Arg) in a Japanese family with autosomal dominant retinitis pigmentosa.	Glycine	35-38	rhodopsin	Homo sapiens	0-9
11094174-0	2000	Rhodopsin gene codon 106 mutation (Gly-to-Arg) in a Japanese family with autosomal dominant retinitis pigmentosa.	Arginine	42-45	rhodopsin	Homo sapiens	0-9
10956053-0	2000	Transducin-dependent protonation of glutamic acid 134 in rhodopsin.	Glutamic Acid	36-49	rhodopsin	Homo sapiens	57-66
10956053-1	2000	A highly conserved carboxylic acid residue in rhodopsin, Glu(134), modulates transducin (G(t)) interaction.	Carboxylic Acids	19-34	rhodopsin	Homo sapiens	46-55
10956053-1	2000	A highly conserved carboxylic acid residue in rhodopsin, Glu(134), modulates transducin (G(t)) interaction.	Glutamic Acid	57-60	rhodopsin	Homo sapiens	46-55
10956053-4	2000	Formation of the complex between G(t) and photoactivated rhodopsin reconstituted into phosphatidylcholine vesicles caused prominent infrared absorption increases at 1641, 1550, and 1517 cm(-)(1).	Phosphatidylcholines	86-105	rhodopsin	Homo sapiens	57-66
10956053-6	2000	When measured in the presence of G(t), replacement of Glu(134) by glutamine abolished the low-frequency part of a broad absorption band at 1735 cm(-)(1) that is normally superimposed on the light-induced absorption changes of Asp(83) and Glu(122) of rhodopsin.	Glutamic Acid	54-57	rhodopsin	Homo sapiens	250-259
10913255-2	2000	To determine whether these effects might be mediated by direct binding interactions with the GPCR or its associated G protein, we studied the binding character of halothane on mammalian rhodopsin, structurally the best understood GPCR, by using direct photoaffinity labeling with [(14)C]halothane.	Halothane	163-172	rhodopsin	Homo sapiens	186-195
10864869-2	2000	Bleaching of diazoketo rhodopsin (DK-Rh) containing 11-cis-3-diazo-4-oxo-retinal yields batho-, lumi-, meta-I-, and meta-II-Rh intermediates corresponding to those of native Rh but at lower temperatures.	11-cis-3-diazo-4-oxo-retinal	52-80	rhodopsin	Homo sapiens	23-32
10891074-2	2000	We have investigated the activation of the GPCR rhodopsin by the construction and analysis of a mutant which contains a total of four disulfide bonds connecting the cytoplasmic ends of helices 1 and 7, and 3 and 5, and the extracellular ends of helices 3 and 4, and 5 and 6.	Disulfides	134-143	rhodopsin	Homo sapiens	48-57
10770924-2	2000	The G-protein-coupled receptor rhodopsin is activated by photoconversion of its covalently bound ligand 11-cis-retinal to the agonist all-trans-retinal.	Retinaldehyde	104-118	rhodopsin	Homo sapiens	31-40
11421342-8	2000	Finding of the occurrence of the Galbeta1-4Fucalpha1- group linked at the C-6 position of the proximal N-acetylglucosamine residue of the hybrid type sugar chains of octopus rhodopsin is one of such examples.	Acetylglucosamine	103-122	rhodopsin	Homo sapiens	174-183
11421342-8	2000	Finding of the occurrence of the Galbeta1-4Fucalpha1- group linked at the C-6 position of the proximal N-acetylglucosamine residue of the hybrid type sugar chains of octopus rhodopsin is one of such examples.	Sugars	150-155	rhodopsin	Homo sapiens	174-183
10789455-1	2000	A stereoselective synthesis of 11Z-retinal 2, which is the chromophore of visual pigment (rhodopsin), was accomplished from the beta-ionylideneacetaldehyde-tricarbonyliron complex 3.	beta-ionylideneacetaldehyde-tricarbonyliron complex	128-179	rhodopsin	Homo sapiens	90-99
10916182-0	2000	Homozygous and heterozygous gly-188-Arg mutation of the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa.	Glycine	28-31	rhodopsin	Homo sapiens	56-65
10916182-0	2000	Homozygous and heterozygous gly-188-Arg mutation of the rhodopsin gene in a family with autosomal dominant retinitis pigmentosa.	Arginine	36-39	rhodopsin	Homo sapiens	56-65
10827943-1	2000	Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses light energy to pump chloride through biological membranes.	Chlorides	90-98	rhodopsin	Homo sapiens	4-13
10769149-1	2000	Site-specific cleavage on the interhelical loop I on the cytoplasmic face of rhodopsin has been observed after activation of a Cu-phenanthroline tethered cleavage reagent attached on the cytoplasmic loop IV.	cu-phenanthroline	127-144	rhodopsin	Homo sapiens	77-86
10737783-4	2000	Solubilization of rhodopsin in cholate allowed binding of the antibody, but the binding caused destabilization as evidenced by the accelerated loss of absorbance at 500 nm.	Cholates	31-38	rhodopsin	Homo sapiens	18-27
10737783-7	2000	Purification of rhodopsin in DM resulted in essentially quantitative removal of endogenous phospholipids.	Phospholipids	91-104	rhodopsin	Homo sapiens	16-25
10737783-8	2000	When rhodopsin thus purified was treated with the above antibody in DM and in cholate, enhanced destabilization (5-fold) was observed in the latter detergent.	dodecyl maltoside	68-70	rhodopsin	Homo sapiens	5-14
10737783-8	2000	When rhodopsin thus purified was treated with the above antibody in DM and in cholate, enhanced destabilization (5-fold) was observed in the latter detergent.	Cholates	78-85	rhodopsin	Homo sapiens	5-14
10652295-2	2000	The transition of rhodopsin from the inactive to the active state is associated with proton uptake at Glu(134) (1), and recent mutagenesis studies suggest that protonation of the homologous amino acid in the alpha(1B) adrenergic receptor (Asp(142)) may be involved in its mechanism of activation (2).	Glutamic Acid	102-105	rhodopsin	Homo sapiens	18-27
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	17-24	rhodopsin	Homo sapiens	212-221
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	17-24	rhodopsin	Homo sapiens	288-297
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	100-107	rhodopsin	Homo sapiens	212-221
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	100-107	rhodopsin	Homo sapiens	288-297
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Water	222-227	rhodopsin	Homo sapiens	212-221
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	100-107	rhodopsin	Homo sapiens	212-221
10681509-9	2000	Amplification of ethanol effects on MII formation and acyl chain packing by osmolytes suggests that ethanol increases the equilibrium concentration of MII both by disordering acyl chain packing and by disrupting rhodopsin-water hydrogen bonds, demonstrating a direct effect of ethanol on rhodopsin.	Ethanol	100-107	rhodopsin	Homo sapiens	288-297
10683246-3	2000	We had modeled the mu-opioid receptor (muR) based on the low-resolution structure of rhodopsin by G. F. X. Schertler, C. Villa, and R. Henderson (1993, Nature 362, 770-772) and proposed that metal ions may be directly involved in the binding of ligands and receptor activation (B. S. Zhorov and V. S. Ananthanarayanan, 1998, J. Biomol.	Metals	191-196	rhodopsin	Homo sapiens	85-94
10652295-2	2000	The transition of rhodopsin from the inactive to the active state is associated with proton uptake at Glu(134) (1), and recent mutagenesis studies suggest that protonation of the homologous amino acid in the alpha(1B) adrenergic receptor (Asp(142)) may be involved in its mechanism of activation (2).	Aspartic Acid	239-242	rhodopsin	Homo sapiens	18-27
10652295-7	2000	In addition, we found that the pH sensitivity of beta(2)AR activation is not abrogated by mutation of Asp(130), which is homologous to the highly conserved acidic amino acids that link protonation to activation of rhodopsin (Glu(134)) and the alpha(1B) adrenergic receptor (Asp(142)).	Glutamic Acid	225-228	rhodopsin	Homo sapiens	214-223
10631288-4	2000	Helix 6 is one of the transmembrane helices of rhodopsin that contains a proline (amino acid residue 267) and the influence of this proline on the structure of this transmembrane domain was unknown.	Proline	73-80	rhodopsin	Homo sapiens	47-56
10631288-4	2000	Helix 6 is one of the transmembrane helices of rhodopsin that contains a proline (amino acid residue 267) and the influence of this proline on the structure of this transmembrane domain was unknown.	Proline	132-139	rhodopsin	Homo sapiens	47-56
11741218-8	2000	Whereas H8 indeed inhibited light-dependent phosphorylation of rhodopsin by GRK2, but with low potency, 3 additional FCD compounds with promising GRK2 scores failed to inhibit GRK2.	N-(2-(methylamino)ethyl)-5-isoquinolinesulfonamide	8-10	rhodopsin	Homo sapiens	63-72
10828169-10	2000	DHA also has significant effects on photoreceptor membranes involved in the signal transduction process, rhodopsin activation, and rod and cone development.	Docosahexaenoic Acids	0-3	rhodopsin	Homo sapiens	105-114
10594365-0	1999	The dolichol pathway in the retina and its involvement in the glycosylation of rhodopsin.	Dolichols	4-12	rhodopsin	Homo sapiens	79-88
10736719-0	2000	Mapping interaction sites between rhodopsin and arrestin by phage display and synthetic peptides.	Peptides	88-96	rhodopsin	Homo sapiens	34-43
10996607-2	2000	By comparison of the results in the presence or absence of 70 microM NADPH and those for bovine or human rhodopsin, a single comprehensive scheme was fit to all the data, including reduction of retinal to retinol by the intrinsic retinol dehydrogenase.	Vitamin A	205-212	rhodopsin	Homo sapiens	105-114
10570143-1	1999	We report high resolution solution (19)F NMR spectra of fluorine-labeled rhodopsin mutants in detergent micelles.	Fluorine	56-64	rhodopsin	Homo sapiens	73-82
10570143-2	1999	Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage.	Cysteine	7-15	rhodopsin	Homo sapiens	64-73
10570143-2	1999	Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage.	trifluoroethylthio	108-126	rhodopsin	Homo sapiens	64-73
10570143-2	1999	Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage.	tet	128-131	rhodopsin	Homo sapiens	64-73
10570143-2	1999	Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage.	Disulfides	165-174	rhodopsin	Homo sapiens	64-73
10570143-3	1999	TET-labeled cysteine mutants at amino acid positions 67, 140, 245, 248, 311, and 316 in rhodopsin were thus prepared.	tet	0-3	rhodopsin	Homo sapiens	88-97
10570143-3	1999	TET-labeled cysteine mutants at amino acid positions 67, 140, 245, 248, 311, and 316 in rhodopsin were thus prepared.	Cysteine	12-20	rhodopsin	Homo sapiens	88-97
10512613-5	1999	Mutations of amino acids in the ring portion of the chromophore binding pocket of rhodopsin serve well as a predictive model for mutations in the blue pigment, but mutations near the Schiff base do not.	Schiff Bases	183-194	rhodopsin	Homo sapiens	82-91
10527670-7	1999	The protein RPE65 is implicated in the metabolism of vitamin A, the precursor of the photoexcitable retinal pigment (rhodopsin).	Vitamin A	53-62	rhodopsin	Homo sapiens	117-126
10504255-0	1999	Psoralen photo-cross-linking by triplex-forming oligonucleotides at multiple sites in the human rhodopsin gene.	triplex-forming oligonucleotides	32-64	rhodopsin	Homo sapiens	96-105
10504255-11	1999	These results indicate that TFO-linker-psoralen conjugates allow simultaneous, efficient targeting of multiple sites in the human rhodopsin gene.	tfo	28-31	rhodopsin	Homo sapiens	130-139
10504260-0	1999	Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.	Disulfides	48-57	rhodopsin	Homo sapiens	26-35
10504260-0	1999	Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.	Disulfides	48-57	rhodopsin	Homo sapiens	97-106
10531390-8	1999	Three-dimensional models built on the basis of the predicted structure of rhodopsin showed that Tyr(308) of the beta(2)AR covered the binding pocket formed by TM2 and TM7 from the upper side, and Thr(117) of the beta(1)AR located in the middle of the binding pocket to provide a hydrogen bonding for the beta(1)-selective agonists.	Tyrosine	96-99	rhodopsin	Homo sapiens	74-83
10531390-8	1999	Three-dimensional models built on the basis of the predicted structure of rhodopsin showed that Tyr(308) of the beta(2)AR covered the binding pocket formed by TM2 and TM7 from the upper side, and Thr(117) of the beta(1)AR located in the middle of the binding pocket to provide a hydrogen bonding for the beta(1)-selective agonists.	Threonine	0-3	rhodopsin	Homo sapiens	74-83
10531390-8	1999	Three-dimensional models built on the basis of the predicted structure of rhodopsin showed that Tyr(308) of the beta(2)AR covered the binding pocket formed by TM2 and TM7 from the upper side, and Thr(117) of the beta(1)AR located in the middle of the binding pocket to provide a hydrogen bonding for the beta(1)-selective agonists.	Hydrogen	279-287	rhodopsin	Homo sapiens	74-83
10531390-8	1999	Three-dimensional models built on the basis of the predicted structure of rhodopsin showed that Tyr(308) of the beta(2)AR covered the binding pocket formed by TM2 and TM7 from the upper side, and Thr(117) of the beta(1)AR located in the middle of the binding pocket to provide a hydrogen bonding for the beta(1)-selective agonists.	beta(1)	212-219	rhodopsin	Homo sapiens	74-83
10508406-0	1999	State-dependent disulfide cross-linking in rhodopsin.	Disulfides	16-25	rhodopsin	Homo sapiens	43-52
10508406-1	1999	In previous studies, we developed a new method for detecting tertiary interactions in rhodopsin using split receptors and disulfide cross-linking.	Disulfides	122-131	rhodopsin	Homo sapiens	86-95
10508406-3	1999	In this study, we utilized this method to examine the cross-linking reactions between native cysteines in the ground state and after photoexcitation of rhodopsin.	Cysteine	93-102	rhodopsin	Homo sapiens	152-161
10508407-1	1999	Previous studies [Yu, H., Kono, M., and Oprian, D. D. (1999) Biochemistry 38, xxxx-xxxx] using split receptors and disulfide cross-linking have shown that native cysteines 140 and 222 on the cytoplasmic side of transmembrane segments (TM) 3 and 5 of rhodopsin, respectively, can cross-link to each other upon treatment with the oxidant Cu(phen)3(2+).	Cysteine	162-171	rhodopsin	Homo sapiens	250-259
10461915-0	1999	The amino terminus with a conserved glutamic acid of G protein-coupled receptor kinases is indispensable for their ability to phosphorylate photoactivated rhodopsin.	Glutamic Acid	36-49	rhodopsin	Homo sapiens	155-164
10462476-5	1999	Uracil nucleotides had a distinct activity profile with respect to disruption of the transitory complex between photoexcited rhodopsin and nucleotide-free transducin.	Uracil Nucleotides	0-18	rhodopsin	Homo sapiens	125-134
10339563-3	1999	We show that in octopus rhodopsin, the glutamic acid has no anionic counterpart.	Glutamic Acid	39-52	rhodopsin	Homo sapiens	24-33
10387035-1	1999	Sixteen single-cysteine substitution mutants of rhodopsin were prepared in the sequence 306-321 which begins in transmembrane helix VII and ends at the palmitoylation sites at 322C and 323C.	Cysteine	15-23	rhodopsin	Homo sapiens	48-57
10387036-0	1999	Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation.	Cysteine	7-15	rhodopsin	Homo sapiens	136-145
10387036-1	1999	Cysteines were introduced, one at a time, at amino acid positions 55-75 in the cytoplasmic region connecting helices I and II in rhodopsin.	Cysteine	0-9	rhodopsin	Homo sapiens	129-138
10358054-3	1999	By substituting histidines for residues at the cytoplasmic ends of helices III and VI in retinal rhodopsin, we engineered a metal-binding site whose occupancy by Zn(II) prevented the receptor from activating a retinal G protein, Gt (Sheikh, S. P., Zvyaga, T. A. , Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Nature 383, 347-350).	Histidine	16-26	rhodopsin	Homo sapiens	97-106
10358054-3	1999	By substituting histidines for residues at the cytoplasmic ends of helices III and VI in retinal rhodopsin, we engineered a metal-binding site whose occupancy by Zn(II) prevented the receptor from activating a retinal G protein, Gt (Sheikh, S. P., Zvyaga, T. A. , Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Nature 383, 347-350).	Metals	124-129	rhodopsin	Homo sapiens	97-106
10358054-3	1999	By substituting histidines for residues at the cytoplasmic ends of helices III and VI in retinal rhodopsin, we engineered a metal-binding site whose occupancy by Zn(II) prevented the receptor from activating a retinal G protein, Gt (Sheikh, S. P., Zvyaga, T. A. , Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Nature 383, 347-350).	Zinc	162-164	rhodopsin	Homo sapiens	97-106
10488366-5	1999	Two RP patients were identified with disease-causing mutations in the rhodopsin gene: one from a black African family in which a codon 347 mutation resulted in a Pro-Leu substitution, and one in a family of Caucasian origin where a codon 58 alteration resulted in a Thr-Arg substitution.	prolylleucine	162-169	rhodopsin	Homo sapiens	70-79
10488366-5	1999	Two RP patients were identified with disease-causing mutations in the rhodopsin gene: one from a black African family in which a codon 347 mutation resulted in a Pro-Leu substitution, and one in a family of Caucasian origin where a codon 58 alteration resulted in a Thr-Arg substitution.	Threonine	266-269	rhodopsin	Homo sapiens	70-79
10488366-5	1999	Two RP patients were identified with disease-causing mutations in the rhodopsin gene: one from a black African family in which a codon 347 mutation resulted in a Pro-Leu substitution, and one in a family of Caucasian origin where a codon 58 alteration resulted in a Thr-Arg substitution.	Arginine	270-273	rhodopsin	Homo sapiens	70-79
10387000-2	1999	The equilibrium concentration of metarhodopsin II (MII), the conformation of photoactivated rhodopsin, which binds and activates transducin, was increased by glycerol, sucrose, and stachyose in a manner which was linear with osmolality.	Glycerol	158-166	rhodopsin	Homo sapiens	37-46
10387000-2	1999	The equilibrium concentration of metarhodopsin II (MII), the conformation of photoactivated rhodopsin, which binds and activates transducin, was increased by glycerol, sucrose, and stachyose in a manner which was linear with osmolality.	Sucrose	168-175	rhodopsin	Homo sapiens	37-46
10369264-1	1999	The metabolic pathways that produce 11-cis retinal are important for vision because this retinoid is the chromophore residing in rhodopsin and the cone opsins.	Retinoids	89-97	rhodopsin	Homo sapiens	129-138
10339563-5	1999	This helps to explain another observation-that the active photoproduct of octopus rhodopsin can be formed without its Schiff base deprotonating.	Schiff Bases	118-129	rhodopsin	Homo sapiens	82-91
9920910-9	1999	Using computer modeling based on the structure of rhodopsin, a revised model of adenosine-A1AR interactions is proposed with the N6-adenine position oriented toward the top of TM3 and the ribose group interacting with the bottom half of TMs 3 and 7.	n6-adenine	129-139	rhodopsin	Homo sapiens	50-59
10075679-1	1999	The visual GTP-binding protein, transducin, couples light-activated rhodopsin (R*) with the effector enzyme, cGMP phosphodiesterase in vertebrate photoreceptor cells.	Guanosine Triphosphate	11-14	rhodopsin	Homo sapiens	68-77
10350478-4	1999	Rhodopsin mutants containing these disulfides demonstrate nativelike absorption spectra and light-dependent activation of transducin, suggesting that large movements on the extracellular side of TM5 with respect to TM6 are not required for receptor activation.	Disulfides	35-45	rhodopsin	Homo sapiens	0-9
10213616-6	1999	A series of alanine mutants within the three cytoplasmic loops of rhodopsin were expressed in HEK-293 cells, reconstituted with 11-cis-retinal, prephosphorylated with rhodopsin kinase, and examined for their ability to bind in vitro-translated, 35S-labeled arrestin.	Alanine	12-19	rhodopsin	Homo sapiens	66-75
10051571-0	1999	Structure and function in rhodopsin: kinetic studies of retinal binding to purified opsin mutants in defined phospholipid-detergent mixtures serve as probes of the retinal binding pocket.	Phospholipids	109-121	rhodopsin	Homo sapiens	26-35
10051572-0	1999	Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.	Cysteine	88-97	rhodopsin	Homo sapiens	26-35
10051572-0	1999	Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.	Cysteine	88-97	rhodopsin	Homo sapiens	127-136
10051572-0	1999	Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.	Cysteine	99-102	rhodopsin	Homo sapiens	26-35
10051572-0	1999	Structure and function in rhodopsin: further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function.	Cysteine	99-102	rhodopsin	Homo sapiens	127-136
10051572-1	1999	The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin.	Disulfides	4-13	rhodopsin	Homo sapiens	139-148
10051572-1	1999	The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin.	Cysteine	27-30	rhodopsin	Homo sapiens	139-148
10051572-1	1999	The disulfide bond between Cys-110 and Cys-187 in the intradiscal domain is required for correct folding in vivo and function of mammalian rhodopsin.	Cysteine	39-42	rhodopsin	Homo sapiens	139-148
10051572-2	1999	Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond.	Disulfides	132-141	rhodopsin	Homo sapiens	14-23
10051572-2	1999	Misfolding in rhodopsin, characterized by the loss of ability to bind 11-cis-retinal, has been shown to be caused by an intradiscal disulfide bond different from the above native disulfide bond.	Disulfides	179-188	rhodopsin	Homo sapiens	14-23
10051572-6	1999	C185A allows the formation of a C110-C187 disulfide bond, with wild-type-like rhodopsin phenotype.	Disulfides	42-51	rhodopsin	Homo sapiens	78-87
9920910-9	1999	Using computer modeling based on the structure of rhodopsin, a revised model of adenosine-A1AR interactions is proposed with the N6-adenine position oriented toward the top of TM3 and the ribose group interacting with the bottom half of TMs 3 and 7.	Ribose	188-194	rhodopsin	Homo sapiens	50-59
9892660-6	1999	The 15N resonance corresponding to the protonated retinylidene Schiff base nitrogen was observed at 156.8 ppm in the MAS spectrum of 6-15N-lysine-labeled rhodopsin.	6-15n-lysine	133-145	rhodopsin	Homo sapiens	154-163
9892660-0	1999	Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line.	retinylidene schiff base	43-67	rhodopsin	Homo sapiens	80-89
9892660-0	1999	Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line.	Nitrogen	68-76	rhodopsin	Homo sapiens	80-89
9892660-0	1999	Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line.	15n-lysine	105-115	rhodopsin	Homo sapiens	80-89
9892660-1	1999	The apoprotein corresponding to the mammalian photoreceptor rhodopsin has been expressed by using suspension cultures of HEK293S cells in defined media that contained 6-15N-lysine and 2-13C-glycine.	6-15n-lysine	167-179	rhodopsin	Homo sapiens	60-69
9892660-1	1999	The apoprotein corresponding to the mammalian photoreceptor rhodopsin has been expressed by using suspension cultures of HEK293S cells in defined media that contained 6-15N-lysine and 2-13C-glycine.	2-13c-glycine	184-197	rhodopsin	Homo sapiens	60-69
9892660-6	1999	The 15N resonance corresponding to the protonated retinylidene Schiff base nitrogen was observed at 156.8 ppm in the MAS spectrum of 6-15N-lysine-labeled rhodopsin.	15n	4-7	rhodopsin	Homo sapiens	154-163
10614048-7	1999	MAS-NMR analysis of [15N]lysine-labelled rhodopsin reveals the presence of a "soft" counterion, requiring intermediate water molecules for stabilization.	15n	21-24	rhodopsin	Homo sapiens	41-50
9892660-6	1999	The 15N resonance corresponding to the protonated retinylidene Schiff base nitrogen was observed at 156.8 ppm in the MAS spectrum of 6-15N-lysine-labeled rhodopsin.	retinylidene schiff base	50-74	rhodopsin	Homo sapiens	154-163
9892660-6	1999	The 15N resonance corresponding to the protonated retinylidene Schiff base nitrogen was observed at 156.8 ppm in the MAS spectrum of 6-15N-lysine-labeled rhodopsin.	Nitrogen	75-83	rhodopsin	Homo sapiens	154-163
9880548-3	1999	We investigated this hypothesis using a series of eight rhodopsin mutants containing single reactive cysteine residues in the region (helix F) where movement was previously detected.	Cysteine	101-109	rhodopsin	Homo sapiens	56-65
9889371-1	1999	Upon activation by light, rhodopsin is subject to phosphorylation by rhodopsin kinase at serine and threonine residues in the carboxyl terminal region of the protein.	Serine	89-95	rhodopsin	Homo sapiens	26-35
9889371-1	1999	Upon activation by light, rhodopsin is subject to phosphorylation by rhodopsin kinase at serine and threonine residues in the carboxyl terminal region of the protein.	Threonine	100-109	rhodopsin	Homo sapiens	26-35
10614048-7	1999	MAS-NMR analysis of [15N]lysine-labelled rhodopsin reveals the presence of a "soft" counterion, requiring intermediate water molecules for stabilization.	Lysine	25-31	rhodopsin	Homo sapiens	41-50
10325541-5	1999	If 6- to 10-nm particles corresponded to the carbohydrate moiety of rhodopsin, concanavalin A binding might tend to preserve this carbohydrate moiety.	Carbohydrates	45-57	rhodopsin	Homo sapiens	68-77
10614048-7	1999	MAS-NMR analysis of [15N]lysine-labelled rhodopsin reveals the presence of a "soft" counterion, requiring intermediate water molecules for stabilization.	Water	119-124	rhodopsin	Homo sapiens	41-50
10325541-5	1999	If 6- to 10-nm particles corresponded to the carbohydrate moiety of rhodopsin, concanavalin A binding might tend to preserve this carbohydrate moiety.	Carbohydrates	130-142	rhodopsin	Homo sapiens	68-77
10614048-8	1999	FT-IR studies on [2H]tyrosine-labelled rhodopsin demonstrate participation of several tyrosin(at)e residues in receptor activation.	Deuterium	18-20	rhodopsin	Homo sapiens	39-48
10614048-8	1999	FT-IR studies on [2H]tyrosine-labelled rhodopsin demonstrate participation of several tyrosin(at)e residues in receptor activation.	Tyrosine	21-29	rhodopsin	Homo sapiens	39-48
10614048-8	1999	FT-IR studies on [2H]tyrosine-labelled rhodopsin demonstrate participation of several tyrosin(at)e residues in receptor activation.	Tyrosine	21-28	rhodopsin	Homo sapiens	39-48
9801137-2	1998	By repeating the measurements with the rhodopsin mutant D83N/E122Q, the spectral variation between the samples in membranes versus detergent could be assigned to a difference band at 1743(+)/1724(-) cm(-1), which does not exhibit a deuteration-induced downshift.	deuteration	232-243	rhodopsin	Homo sapiens	39-48
12579739-6	1998	RESULTS: Three different mutations in the rhodopsin gene were found in 3 of the 83 patients with retinitis pigmentosa(Va1104Phe, Lys311Glu, Pro347Leu).	va1104phe	118-127	rhodopsin	Homo sapiens	42-51
9825706-0	1998	The effects of octanol on the late photointermediates of rhodopsin.	Octanols	15-22	rhodopsin	Homo sapiens	57-66
9698379-3	1998	Using a computer search for sites 15 nucleotides in length and greater than 80% purine, we found 143 distinct sites in the rhodopsin gene and comparable numbers of sites in several other human genes.	purine	80-86	rhodopsin	Homo sapiens	123-132
9765512-9	1998	The RGS 9 gene is within a previously defined locus for retinitis pigmentosa (RP 17), a disease that has been linked to genes in the rhodopsin/transducin/cGMP signaling pathway.	Cyclic GMP	154-158	rhodopsin	Homo sapiens	133-142
9708973-4	1998	The MI-MII equilibrium constant was progressively shifted toward MII as the experimental phosphorylation stoichiometry was increased from 0 to 6.4 phosphates per rhodopsin.	Phosphates	147-157	rhodopsin	Homo sapiens	162-171
9698379-4	1998	By applying more stringent criteria, we selected 17 potential target sites in the rhodopsin gene, screened them with a plasmid binding assay, and found 8 that bound TFOs with submicromolar affinity (Kd = 10(-)9-10(-)7 M).	tfos	165-169	rhodopsin	Homo sapiens	82-91
9516406-0	1998	Regulation of the phosphorylation state of rhodopsin by dopamine.	Dopamine	56-64	rhodopsin	Homo sapiens	43-52
9685370-1	1998	S-modulin controls rhodopsin phosphorylation in a calcium-dependent manner, and it has been suggested that it modulates the light sensitivity of the photoreceptor cell.	Calcium	50-57	rhodopsin	Homo sapiens	19-28
9636052-1	1998	Invertebrate visual signal transduction is initiated by rhodopsin activation of a guanine nucleotide binding protein, Gq, which stimulates phospholipase C (PLC) activity.	Guanine Nucleotides	82-100	rhodopsin	Homo sapiens	56-65
9538004-0	1998	Rhodopsin arginine-135 mutants are phosphorylated by rhodopsin kinase and bind arrestin in the absence of 11-cis-retinal.	Arginine	10-18	rhodopsin	Homo sapiens	0-9
9538004-1	1998	Arginine-135, located at the border between the third transmembrane domain and the second cytoplasmic loop of rhodopsin, is one of the most highly conserved amino acids in the family of G protein-coupled receptors.	Arginine	0-8	rhodopsin	Homo sapiens	110-119
9538004-2	1998	The effect of mutation at Arg-135 on the ability of rhodopsin to undergo desensitization was investigated.	Arginine	26-29	rhodopsin	Homo sapiens	52-61
9797678-0	1998	Ocular signs associated with a rhodopsin mutation (Cys-167-->Arg) in a family with autosomal dominant retinitis pigmentosa.	Cysteine	51-54	rhodopsin	Homo sapiens	31-40
9797678-0	1998	Ocular signs associated with a rhodopsin mutation (Cys-167-->Arg) in a family with autosomal dominant retinitis pigmentosa.	Arginine	64-67	rhodopsin	Homo sapiens	31-40
9539726-4	1998	Light activation of rhodopsin causes a dramatic shift from a disordered conformation of Gtalpha(340-350) to a binding motif with a helical turn followed by an open reverse turn centered at Gly-348, a helix-terminating C capping motif of an alphaL type.	Glycine	189-192	rhodopsin	Homo sapiens	20-29
9539726-5	1998	Docking of the NMR structure to the GDP-bound x-ray structure of Gt reveals that photoexcited rhodopsin promotes the formation of a continuous helix over residues 325-346 terminated by the C-terminal helical cap with a unique cluster of crucial hydrophobic side chains.	Guanosine Diphosphate	36-39	rhodopsin	Homo sapiens	94-103
9516406-3	1998	We show that dopamine increased the rate of dephosphorylation of rhodopsin, the light receptor, in intact frog retinas.	Dopamine	13-21	rhodopsin	Homo sapiens	65-74
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	47-55	rhodopsin	Homo sapiens	92-101
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	47-55	rhodopsin	Homo sapiens	167-176
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	47-55	rhodopsin	Homo sapiens	167-176
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	155-163	rhodopsin	Homo sapiens	92-101
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	155-163	rhodopsin	Homo sapiens	167-176
9516406-4	1998	Further, we found that rod outer segments from dopamine-treated retinas contained increased rhodopsin phosphatase activity, indicating that this effect of dopamine on rhodopsin was mediated by stimulation of rhodopsin phosphatase.	Dopamine	155-163	rhodopsin	Homo sapiens	167-176
9516406-6	1998	Thus, our results identify a pathway for feedback regulation of rhodopsin from the inner retina and illustrate the involvement of dopamine in paracrine regulation of the sensitivity of a GPCR.	Dopamine	130-138	rhodopsin	Homo sapiens	64-73
9425071-5	1998	Rhodopsin was found to incorporate preferentially into the phospholipid bilayer regions, whereas transducin was uniformly distributed over the entire outer surface of the supported patterned membrane.	Phospholipids	59-71	rhodopsin	Homo sapiens	0-9
9635057-8	1998	These data are discussed relative to taurine"s role in the process of rhodopsin regeneration and in the protection of the rod outer segments against osmotic, mechanical and light induced damage.	Taurine	37-44	rhodopsin	Homo sapiens	70-79
9477956-0	1998	Disulfide bond exchange in rhodopsin.	Disulfides	0-9	rhodopsin	Homo sapiens	27-36
9477956-1	1998	Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein.	Cysteine	23-32	rhodopsin	Homo sapiens	0-9
9477956-1	1998	Rhodopsin contains two cysteines (Cys110 and Cys187) that are highly conserved among members of the G protein coupled receptor family and that form a disulfide bond connecting helixes 3 and 4 on the extracellular side of the protein.	Disulfides	150-159	rhodopsin	Homo sapiens	0-9
9477956-2	1998	However, recent work on a rhodopsin mutant split in the cytoplasmic loop connecting helixes 3 and 4 has shown that the amino- and carboxy-terminal fragments of this split protein do not comigrate on nonreducing SDS-PAGE gels, suggesting that the native Cys110-Cys187 disulfide bond is not present in this mutant [Ridge et al.	Disulfides	267-276	rhodopsin	Homo sapiens	26-35
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Disulfides	47-56	rhodopsin	Homo sapiens	155-164
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Sodium Dodecyl Sulfate	65-68	rhodopsin	Homo sapiens	155-164
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Disulfides	93-102	rhodopsin	Homo sapiens	155-164
9477956-9	1998	We show here that the inability to observe the disulfide bond on SDS gels is the result of a disulfide bond exchange reaction which occurs when this split rhodopsin is denatured in preparation for SDS-PAGE.	Sodium Dodecyl Sulfate	197-200	rhodopsin	Homo sapiens	155-164
9477956-11	1998	If the sulfhydryl-specific reagent N-ethylmaleimide is included in the sample during preparation for electrophoresis or if Cys185 is changed to Ser, the two fragments do comigrate with full-length rhodopsin on SDS gels and, therefore, are connected by the native Cys110-Cys187 disulfide bond.	Sulfhydryl Compounds	7-17	rhodopsin	Homo sapiens	197-206
9477956-11	1998	If the sulfhydryl-specific reagent N-ethylmaleimide is included in the sample during preparation for electrophoresis or if Cys185 is changed to Ser, the two fragments do comigrate with full-length rhodopsin on SDS gels and, therefore, are connected by the native Cys110-Cys187 disulfide bond.	Ethylmaleimide	35-51	rhodopsin	Homo sapiens	197-206
9477956-11	1998	If the sulfhydryl-specific reagent N-ethylmaleimide is included in the sample during preparation for electrophoresis or if Cys185 is changed to Ser, the two fragments do comigrate with full-length rhodopsin on SDS gels and, therefore, are connected by the native Cys110-Cys187 disulfide bond.	Sodium Dodecyl Sulfate	210-213	rhodopsin	Homo sapiens	197-206
9477956-11	1998	If the sulfhydryl-specific reagent N-ethylmaleimide is included in the sample during preparation for electrophoresis or if Cys185 is changed to Ser, the two fragments do comigrate with full-length rhodopsin on SDS gels and, therefore, are connected by the native Cys110-Cys187 disulfide bond.	Disulfides	277-286	rhodopsin	Homo sapiens	197-206
9445403-0	1998	Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.	Hydrogen	0-8	rhodopsin	Homo sapiens	56-65
9445403-0	1998	Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.	Water	37-42	rhodopsin	Homo sapiens	56-65
9445403-2	1998	Light absorption by the retinylidene chromophore of rhodopsin triggers an 11-cis-->all-trans isomerization, followed by a series of protein conformational changes, which culminate in the binding and activation of the G-protein transducin by the metarhodopsin II (Meta II) intermediate.	retinylidene	24-36	rhodopsin	Homo sapiens	52-61
9445403-5	1998	Compared with earlier work, several negative bands associated with water molecules in unphotolysed rhodopsin were detected, which shift to lower frequencies upon formation of the Meta I and Meta II intermediates.	Water	67-72	rhodopsin	Homo sapiens	99-108
9478049-6	1998	This phenomenon is due to changing levels of the retinoic acid precursor retinaldehyde, which is released from illuminated rhodopsin, thus providing a mechanism by which light can directly influence gene expression.	Tretinoin	49-62	rhodopsin	Homo sapiens	123-132
9478049-6	1998	This phenomenon is due to changing levels of the retinoic acid precursor retinaldehyde, which is released from illuminated rhodopsin, thus providing a mechanism by which light can directly influence gene expression.	Retinaldehyde	73-86	rhodopsin	Homo sapiens	123-132
9478049-8	1998	The light-induced release of retinaldehyde from rhodopsin, which occurs only in vertebrate but not invertebrate photoreceptors, may have accelerated the rapid evolution of retinoic acid-mediated transcriptional regulation at the transition from invertebrates to vertebrates, and it may explain the prominent role of retinoic acid in the eye.	Retinaldehyde	29-42	rhodopsin	Homo sapiens	48-57
9478049-8	1998	The light-induced release of retinaldehyde from rhodopsin, which occurs only in vertebrate but not invertebrate photoreceptors, may have accelerated the rapid evolution of retinoic acid-mediated transcriptional regulation at the transition from invertebrates to vertebrates, and it may explain the prominent role of retinoic acid in the eye.	Tretinoin	172-185	rhodopsin	Homo sapiens	48-57
9478049-8	1998	The light-induced release of retinaldehyde from rhodopsin, which occurs only in vertebrate but not invertebrate photoreceptors, may have accelerated the rapid evolution of retinoic acid-mediated transcriptional regulation at the transition from invertebrates to vertebrates, and it may explain the prominent role of retinoic acid in the eye.	Tretinoin	316-329	rhodopsin	Homo sapiens	48-57
9425074-0	1998	Role of the C9 methyl group in rhodopsin activation: characterization of mutant opsins with the artificial chromophore 11-cis-9-demethylretinal.	11-cis-9	119-127	rhodopsin	Homo sapiens	31-40
9449322-0	1998	Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.	Hydrogen	49-57	rhodopsin	Homo sapiens	19-28
9449322-0	1998	Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.	Deuterium	58-67	rhodopsin	Homo sapiens	19-28
9449322-2	1998	In order to explore the nature of these conformational changes, time-resolved Fourier transform infrared spectroscopy was used to measure the kinetics of hydrogen/deuterium exchange in rhodopsin upon photoexcitation.	Hydrogen	154-162	rhodopsin	Homo sapiens	185-194
9449322-2	1998	In order to explore the nature of these conformational changes, time-resolved Fourier transform infrared spectroscopy was used to measure the kinetics of hydrogen/deuterium exchange in rhodopsin upon photoexcitation.	Deuterium	163-172	rhodopsin	Homo sapiens	185-194
9449322-4	1998	When rhodopsin films are exposed to D2O in the dark for long periods, the amide II band retains at least 60% of its integrated intensity, reflecting a core of backbone peptide groups that are resistant to H/D exchange.	Deuterium Oxide	36-39	rhodopsin	Homo sapiens	5-14
9449322-4	1998	When rhodopsin films are exposed to D2O in the dark for long periods, the amide II band retains at least 60% of its integrated intensity, reflecting a core of backbone peptide groups that are resistant to H/D exchange.	Amides	74-79	rhodopsin	Homo sapiens	5-14
9449322-5	1998	Upon photoactivation, rhodopsin in the presence of D2O exhibits a new phase of H/D exchange which at 10 degrees C consists of fast (time constant approximately 30 min) and slow (approximately 11 h) components.	Deuterium Oxide	51-54	rhodopsin	Homo sapiens	22-31
9803475-1	1998	The protein-protein interactions that underlie shut-off of the light-activated rhodopsin were studied using synthetic peptides derived from C-terminal region of the rhodopsin.	Peptides	118-126	rhodopsin	Homo sapiens	79-88
10347747-2	1998	A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin].	Phosphates	311-330	rhodopsin	Homo sapiens	94-103
10347747-3	1998	Rhodopsin, isolated in the presence of 1% digitonin following ROS solubilization with 1% digitonin, was capable of stimulating slightly transducin GTPase activity, with an initial rate of 1 pmol of GTP hydrolyzed/min/pmol of rhodopsin.	Digitonin	42-51	rhodopsin	Homo sapiens	0-9
10347747-3	1998	Rhodopsin, isolated in the presence of 1% digitonin following ROS solubilization with 1% digitonin, was capable of stimulating slightly transducin GTPase activity, with an initial rate of 1 pmol of GTP hydrolyzed/min/pmol of rhodopsin.	Digitonin	89-98	rhodopsin	Homo sapiens	0-9
10347747-3	1998	Rhodopsin, isolated in the presence of 1% digitonin following ROS solubilization with 1% digitonin, was capable of stimulating slightly transducin GTPase activity, with an initial rate of 1 pmol of GTP hydrolyzed/min/pmol of rhodopsin.	Guanosine Triphosphate	147-150	rhodopsin	Homo sapiens	0-9
10347747-4	1998	However, rhodopsin purified in the presence of 0.2% n-dodecyl-beta-D-maltoside (DM), following ROS solubilization with either 1% CHAPS or 1% DM, stimulated the enzymatic activity of transducin in a light-dependent manner, with an initial rate of 5 pmol of Pi released/min/pmol of rhodopsin.	dodecyl maltoside	52-78	rhodopsin	Homo sapiens	9-18
10347747-4	1998	However, rhodopsin purified in the presence of 0.2% n-dodecyl-beta-D-maltoside (DM), following ROS solubilization with either 1% CHAPS or 1% DM, stimulated the enzymatic activity of transducin in a light-dependent manner, with an initial rate of 5 pmol of Pi released/min/pmol of rhodopsin.	dodecyl maltoside	52-78	rhodopsin	Homo sapiens	280-289
10347747-4	1998	However, rhodopsin purified in the presence of 0.2% n-dodecyl-beta-D-maltoside (DM), following ROS solubilization with either 1% CHAPS or 1% DM, stimulated the enzymatic activity of transducin in a light-dependent manner, with an initial rate of 5 pmol of Pi released/min/pmol of rhodopsin.	dodecyl maltoside	80-82	rhodopsin	Homo sapiens	280-289
10347747-5	1998	Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively.	egg phosphatidylcholine	19-42	rhodopsin	Homo sapiens	82-91
10347747-5	1998	Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively.	egg phosphatidylcholine	19-42	rhodopsin	Homo sapiens	265-274
10347747-5	1998	Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively.	Phosphatidylcholines	44-46	rhodopsin	Homo sapiens	82-91
10347747-5	1998	Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively.	Phosphatidylcholines	44-46	rhodopsin	Homo sapiens	265-274
10347747-5	1998	Addition of 0.075% egg phosphatidylcholine (PC) to the four different solubilized rhodopsin samples significantly enhanced light-stimulated GTP hydrolysis by transducin, with initial rates increasing from 0 to 1, 1 to 2, and 5 to 30 pmol of Pi released/min/pmol of rhodopsin, respectively.	Guanosine Triphosphate	140-143	rhodopsin	Homo sapiens	82-91
10347747-6	1998	Furthermore, DM-solubilized rhodopsin induced the hydrolysis of the maximum amount of GTP by transducin at 0.0075% PC, while digitonin-solubilized rhodopsin only stimulated the GTPase activity of transducin to a similar value, when the amount of the photoreceptor protein was increased 4-fold and 0.15% PC was added to the assay mixture.	Guanosine Triphosphate	86-89	rhodopsin	Homo sapiens	28-37
10347747-6	1998	Furthermore, DM-solubilized rhodopsin induced the hydrolysis of the maximum amount of GTP by transducin at 0.0075% PC, while digitonin-solubilized rhodopsin only stimulated the GTPase activity of transducin to a similar value, when the amount of the photoreceptor protein was increased 4-fold and 0.15% PC was added to the assay mixture.	Digitonin	125-134	rhodopsin	Homo sapiens	147-156
10347747-7	1998	These results suggest that the effective photoactivation of transducin by rhodopsin requires phospholipids, which seem to be differentially eliminated with the detergent extraction procedure utilized during ROS membranes solubilization and photopigment isolation.	Phospholipids	93-106	rhodopsin	Homo sapiens	74-83
10347747-2	1998	A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin].	Guanosine Triphosphate	52-55	rhodopsin	Homo sapiens	94-103
10347747-2	1998	A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin].	Guanosine Triphosphate	52-55	rhodopsin	Homo sapiens	357-366
10347747-2	1998	A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin].	Digitonin	135-144	rhodopsin	Homo sapiens	94-103
10347747-2	1998	A complete inhibition of transducin light-dependent GTP hydrolytic activity was observed when rhodopsin purified in the presence of 1% digitonin, following rod outer segment (ROS) solubilization with 1% 3-[(3-cholamidopropyl) dimethylammonio]-1-propane-sulfonate (CHAPS), was used for its activation [0 pmol of inorganic phosphate (Pi) released/min/pmol of rhodopsin].	3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate	264-269	rhodopsin	Homo sapiens	94-103
9405601-1	1997	Cysteine mutagenesis and site-directed spin labeling in the C-terminal region of rhodopsin have been used to probe the local structure and proximity of that region to the cytoplasmic loops.	Cysteine	0-8	rhodopsin	Homo sapiens	81-90
9405602-1	1997	The Glu-134-Arg-135 residues in rhodopsin, located near the cytoplasmic end of the C helix, are involved in G protein binding, or activation, or both.	Glutamic Acid	4-7	rhodopsin	Homo sapiens	32-41
9405602-1	1997	The Glu-134-Arg-135 residues in rhodopsin, located near the cytoplasmic end of the C helix, are involved in G protein binding, or activation, or both.	Arginine	12-15	rhodopsin	Homo sapiens	32-41
9527482-4	1997	These studies indicate a succession on rhodopsin-bearing vesicles of rab6, rab11, rab3 and rab8, all members of the small GTP-binding protein family of the known regulators of membrane trafficking.	Guanosine Triphosphate	122-125	rhodopsin	Homo sapiens	39-48
9391044-0	1997	The C9 methyl group of retinal interacts with glycine-121 in rhodopsin.	Glycine	46-53	rhodopsin	Homo sapiens	61-70
9391065-0	1997	Synthesis and characterization of a novel retinylamine analog inhibitor of constitutively active rhodopsin mutants found in patients with autosomal dominant retinitis pigmentosa.	retinylamine	42-54	rhodopsin	Homo sapiens	97-106
9391065-1	1997	Two different mutations of the active-site Lys-296 in rhodopsin, K296E and K296M, have been found to cause autosomal dominant retinitis pigmentosa (ADRP).	Lysine	43-46	rhodopsin	Homo sapiens	54-63
9391065-3	1997	Previous work has highlighted the potential of retinylamine analogs as active-site directed inactivators of constitutively active mutants of rhodopsin with the idea that these or related compounds might be used therapeutically for cases of ADRP involving mutations of the active-site Lys.	retinylamine	47-59	rhodopsin	Homo sapiens	141-150
9391065-3	1997	Previous work has highlighted the potential of retinylamine analogs as active-site directed inactivators of constitutively active mutants of rhodopsin with the idea that these or related compounds might be used therapeutically for cases of ADRP involving mutations of the active-site Lys.	Lysine	284-287	rhodopsin	Homo sapiens	141-150
9391065-4	1997	Unfortunately, however, amine derivatives of 11-cis-retinal, although highly effective against a K296G mutant of rhodopsin, were without affect on the two naturally occurring ADRP mutants, presumably because of the greater steric bulk of Glu and Met side chains in comparison to Gly.	Amines	24-29	rhodopsin	Homo sapiens	113-122
9344665-1	1997	The NRL gene encodes an evolutionarily conserved basic motif-leucine zipper transcription factor that is implicated in regulating the expression of the photoreceptor-specific gene rhodopsin.	Leucine	61-68	rhodopsin	Homo sapiens	180-189
9359876-3	1997	In rod cells, cholesterol strongly inhibits rhodopsin activity.	Cholesterol	14-25	rhodopsin	Homo sapiens	44-53
9359876-4	1997	The relatively higher level of cholesterol in the plasma membrane serves to inhibit, and thereby conserve, the activity of rhodopsin, which becomes fully active in the low-cholesterol environment of the disk membranes of these same cells.	Cholesterol	31-42	rhodopsin	Homo sapiens	123-132
9359876-4	1997	The relatively higher level of cholesterol in the plasma membrane serves to inhibit, and thereby conserve, the activity of rhodopsin, which becomes fully active in the low-cholesterol environment of the disk membranes of these same cells.	Cholesterol	172-183	rhodopsin	Homo sapiens	123-132
9376376-3	1997	The UVRR difference spectra between rhodopsin and mearhodopsin I exhibit small differences assignalbe to tyrosine residues and no differences due to tryptophan.	Tyrosine	105-113	rhodopsin	Homo sapiens	36-45
9376376-3	1997	The UVRR difference spectra between rhodopsin and mearhodopsin I exhibit small differences assignalbe to tyrosine residues and no differences due to tryptophan.	Tryptophan	149-159	rhodopsin	Homo sapiens	36-45
9376376-4	1997	The UVRR difference spectra between rhodopsin and metarhodopsin II exhibit significant differences for vibrations of both tryptophan and tyrosine residues.	Tryptophan	122-132	rhodopsin	Homo sapiens	36-45
9376376-4	1997	The UVRR difference spectra between rhodopsin and metarhodopsin II exhibit significant differences for vibrations of both tryptophan and tyrosine residues.	Tyrosine	137-145	rhodopsin	Homo sapiens	36-45
9376376-6	1997	These difference features are assigned to one or more tryptophan residues that reside in a hydrophobic, weakly hydrogen-bonding environment in rhodopsin and that are transferred to a less hydrophobic, non-hydrogen-bonding environment during rhodopsin activation.	Tryptophan	54-64	rhodopsin	Homo sapiens	143-152
9376376-6	1997	These difference features are assigned to one or more tryptophan residues that reside in a hydrophobic, weakly hydrogen-bonding environment in rhodopsin and that are transferred to a less hydrophobic, non-hydrogen-bonding environment during rhodopsin activation.	Tryptophan	54-64	rhodopsin	Homo sapiens	241-250
9376376-6	1997	These difference features are assigned to one or more tryptophan residues that reside in a hydrophobic, weakly hydrogen-bonding environment in rhodopsin and that are transferred to a less hydrophobic, non-hydrogen-bonding environment during rhodopsin activation.	Hydrogen	111-119	rhodopsin	Homo sapiens	143-152
9376376-6	1997	These difference features are assigned to one or more tryptophan residues that reside in a hydrophobic, weakly hydrogen-bonding environment in rhodopsin and that are transferred to a less hydrophobic, non-hydrogen-bonding environment during rhodopsin activation.	Hydrogen	205-213	rhodopsin	Homo sapiens	241-250
9376376-8	1997	These results are interpreted with a model for rhodopsin activation in which retinal isomerization alters the interaction of Trp265 with the ionone ring of the retinal chromophore.	Norisoprenoids	141-147	rhodopsin	Homo sapiens	47-56
9351965-5	1997	Moreover, TRP forms a supramolecular complex, proposed to be critical for feedback regulation and/or activation, that includes rhodopsin, phospholipase C, protein kinase C, calmodulin, and the PDZ domain-containing protein, INAD.	Tryptophan	10-13	rhodopsin	Homo sapiens	127-136
9287308-2	1997	Rhodopsin consists of the opsin apoprotein and its 11-cis-retinal chromophore, which is covalently bound to a specific lysine residue by a stable protonated Schiff base linkage.	Lysine	119-125	rhodopsin	Homo sapiens	0-9
9287308-2	1997	Rhodopsin consists of the opsin apoprotein and its 11-cis-retinal chromophore, which is covalently bound to a specific lysine residue by a stable protonated Schiff base linkage.	Schiff Bases	157-168	rhodopsin	Homo sapiens	0-9
9299344-0	1997	An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors.	alpha-carbon	3-15	rhodopsin	Homo sapiens	62-71
9296500-2	1997	One such protein is recoverin, a calcium sensor in retinal rod cells, which controls the lifetime of photoexcited rhodopsin by inhibiting rhodopsin kinase.	Calcium	33-40	rhodopsin	Homo sapiens	114-123
9299344-1	1997	A model for the alpha-carbon positions in the seven transmembrane helices in the rhodopsin family of G-protein-coupled receptors is presented.	Carbon	22-28	rhodopsin	Homo sapiens	81-90
9188704-9	1997	In an in vitro assay that monitored rhodopsin-dependent activation of cGMP phosphodiesterase (PDE), wild type arrestin quenched PDE response only when ATP was present to support rhodopsin phosphorylation.	Adenosine Triphosphate	151-154	rhodopsin	Homo sapiens	178-187
9238015-2	1997	Mutant forms of rhodopsin were prepared in which the carboxylic acid counterion was moved relative to the positively charged chromophore Schiff base.	Carboxylic Acids	53-68	rhodopsin	Homo sapiens	16-25
9238015-2	1997	Mutant forms of rhodopsin were prepared in which the carboxylic acid counterion was moved relative to the positively charged chromophore Schiff base.	Schiff Bases	137-148	rhodopsin	Homo sapiens	16-25
9311782-5	1997	By removing ATP to block the deactivation of rhodopsin by phosphorylation, we show that this reaction limits the amplitude of the response and begins within 3.2 s of a flash in a solution containing 1 microM Ca2+, falling to 0.9 s in a zero-Ca2+ solution.	Adenosine Triphosphate	12-15	rhodopsin	Homo sapiens	45-54
9303550-1	1997	Rhodopsin phosphorylation was investigated using synthetic C-terminal peptides from rhodopsin.	Peptides	70-78	rhodopsin	Homo sapiens	0-9
9303550-1	1997	Rhodopsin phosphorylation was investigated using synthetic C-terminal peptides from rhodopsin.	Peptides	70-78	rhodopsin	Homo sapiens	84-93
9188705-2	1997	It has been invoked as a mechanism for high-gain phosphorylation, a phenomenon that is observed at low bleaching levels where up to several hundred moles of phosphate are added to the rhodopsin pool per mole of photolyzed rhodopsin.	Phosphates	157-166	rhodopsin	Homo sapiens	184-193
9188705-2	1997	It has been invoked as a mechanism for high-gain phosphorylation, a phenomenon that is observed at low bleaching levels where up to several hundred moles of phosphate are added to the rhodopsin pool per mole of photolyzed rhodopsin.	Phosphates	157-166	rhodopsin	Homo sapiens	222-231
9129835-2	1997	A negative band around 280 nm in the lumirhodopsin minus rhodopsin spectra suggests that alteration of the environment of some of the tryptophan residues has taken place before the formation of lumirhodopsin.	Tryptophan	134-144	rhodopsin	Homo sapiens	41-50
9169442-2	1997	Phosphorylation of serine and threonine residues located in the COOH terminus of rhodopsin is the first step in this process, followed by the binding of arrestin.	Serine	19-25	rhodopsin	Homo sapiens	81-90
9169442-2	1997	Phosphorylation of serine and threonine residues located in the COOH terminus of rhodopsin is the first step in this process, followed by the binding of arrestin.	Threonine	30-39	rhodopsin	Homo sapiens	81-90
9169442-2	1997	Phosphorylation of serine and threonine residues located in the COOH terminus of rhodopsin is the first step in this process, followed by the binding of arrestin.	Carbonic Acid	64-68	rhodopsin	Homo sapiens	81-90
9169442-11	1997	These results suggest that 2 amino acids, Thr-340 and Ser-343, play important but distinct roles in promoting the binding of arrestin to rhodopsin.	Threonine	42-45	rhodopsin	Homo sapiens	137-146
9169442-11	1997	These results suggest that 2 amino acids, Thr-340 and Ser-343, play important but distinct roles in promoting the binding of arrestin to rhodopsin.	Serine	54-57	rhodopsin	Homo sapiens	137-146
9144172-0	1997	Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base-Asp-73 interhelical salt bridge.	Schiff Bases	105-116	rhodopsin	Homo sapiens	58-67
9144172-0	1997	Constitutive signaling by the phototaxis receptor sensory rhodopsin II from disruption of its protonated Schiff base-Asp-73 interhelical salt bridge.	Aspartic Acid	117-120	rhodopsin	Homo sapiens	58-67
9144172-1	1997	Sensory rhodopsin II (SRII) is a repellent phototaxis receptor in the archaeon Halobacterium salinarum, similar to visual pigments in its seven-helix structure and linkage of retinal to the protein by a protonated Schiff base in helix G. Asp-73 in helix C is shown by spectroscopic analysis to be a counterion to the protonated Schiff base in the unphotolyzed SRII and to be the proton acceptor from the Schiff base during photoconversion to the receptor signaling state.	Schiff Bases	214-225	rhodopsin	Homo sapiens	8-17
9144172-1	1997	Sensory rhodopsin II (SRII) is a repellent phototaxis receptor in the archaeon Halobacterium salinarum, similar to visual pigments in its seven-helix structure and linkage of retinal to the protein by a protonated Schiff base in helix G. Asp-73 in helix C is shown by spectroscopic analysis to be a counterion to the protonated Schiff base in the unphotolyzed SRII and to be the proton acceptor from the Schiff base during photoconversion to the receptor signaling state.	Aspartic Acid	238-241	rhodopsin	Homo sapiens	8-17
9144172-1	1997	Sensory rhodopsin II (SRII) is a repellent phototaxis receptor in the archaeon Halobacterium salinarum, similar to visual pigments in its seven-helix structure and linkage of retinal to the protein by a protonated Schiff base in helix G. Asp-73 in helix C is shown by spectroscopic analysis to be a counterion to the protonated Schiff base in the unphotolyzed SRII and to be the proton acceptor from the Schiff base during photoconversion to the receptor signaling state.	Schiff Bases	328-339	rhodopsin	Homo sapiens	8-17
9144172-1	1997	Sensory rhodopsin II (SRII) is a repellent phototaxis receptor in the archaeon Halobacterium salinarum, similar to visual pigments in its seven-helix structure and linkage of retinal to the protein by a protonated Schiff base in helix G. Asp-73 in helix C is shown by spectroscopic analysis to be a counterion to the protonated Schiff base in the unphotolyzed SRII and to be the proton acceptor from the Schiff base during photoconversion to the receptor signaling state.	Schiff Bases	328-339	rhodopsin	Homo sapiens	8-17
9144172-3	1997	Analogous constitutive signaling has been shown to be produced by the similar neutral residue substitution of the Schiff base counterion and proton acceptor Glu-113 in human rod rhodopsin.	Schiff Bases	114-125	rhodopsin	Homo sapiens	178-187
9144172-3	1997	Analogous constitutive signaling has been shown to be produced by the similar neutral residue substitution of the Schiff base counterion and proton acceptor Glu-113 in human rod rhodopsin.	Glutamic Acid	157-160	rhodopsin	Homo sapiens	178-187
9184137-4	1997	The C=NH stretching frequencies of rhodopsin, the green cone pigment, and the red cone pigment in H2O (D2O) are found at 1656 (1623), 1640 (1618), and 1644 cm(-1), respectively.	Water	98-101	rhodopsin	Homo sapiens	35-44
9184137-4	1997	The C=NH stretching frequencies of rhodopsin, the green cone pigment, and the red cone pigment in H2O (D2O) are found at 1656 (1623), 1640 (1618), and 1644 cm(-1), respectively.	Deuterium Oxide	103-106	rhodopsin	Homo sapiens	35-44
9184137-6	1997	(1994) Biochemistry 33, 2151-2160], these values suggest that red and green pigments have very similar Schiff base environments, while the Schiff base group in rhodopsin is more strongly hydrogen-bonded to its protein environment.	Schiff Bases	139-150	rhodopsin	Homo sapiens	160-169
9184137-6	1997	(1994) Biochemistry 33, 2151-2160], these values suggest that red and green pigments have very similar Schiff base environments, while the Schiff base group in rhodopsin is more strongly hydrogen-bonded to its protein environment.	Hydrogen	187-195	rhodopsin	Homo sapiens	160-169
9184137-10	1997	The increased hydrogen bonding of the protonated Schiff base group in rhodopsin is predicted to account for the 30 nm blue shift of its absorption maximum compared to that of the green pigment.	Hydrogen	14-22	rhodopsin	Homo sapiens	70-79
9184137-10	1997	The increased hydrogen bonding of the protonated Schiff base group in rhodopsin is predicted to account for the 30 nm blue shift of its absorption maximum compared to that of the green pigment.	Schiff Bases	49-60	rhodopsin	Homo sapiens	70-79
9129835-5	1997	In this transformation, drastic changes of amplitude and a shift of a difference absorption band around 280 nm take place, which suggest that some of the tryptophan residues of rhodopsin become exposed to a hydrophilic environment.	Tryptophan	154-164	rhodopsin	Homo sapiens	177-186
9050844-2	1997	RK binds to the cytoplasmic face of rhodopsin, and the binding results in activation of the enzyme which then phosphorylates rhodopsin at several serine and threonine residues near the carboxyl terminus.	Serine	146-152	rhodopsin	Homo sapiens	36-45
9099692-2	1997	We report here that newly synthesized docosahexaenoyl (DHA) phospholipids are sequestered and cotransported by rhodopsin-bearing post-Golgi vesicles to ROS.	docosahexaenoyl (dha) phospholipids	38-73	rhodopsin	Homo sapiens	111-120
9099692-9	1997	At the same time, newly synthesized [35S]rhodopsin shifted from the ER and Golgi toward TGN and post-Golgi fractions.	Sulfur-35	37-40	rhodopsin	Homo sapiens	41-50
9099692-10	1997	Therefore, sequestration and association of [35S]rhodopsin and [3H]DHA-lipids in a TGN membrane domain occurs prior to their exit and subsequent vectorial cotransport on post-Golgi vesicles to ROS.	Sulfur-35	45-48	rhodopsin	Homo sapiens	49-58
9197578-2	1997	We here present the clinical phenotype in 6 patients from a family with autosomal dominant retinitis pigmentosa found to carry a point mutation in the rhodopsin gene (arginine-135-tryptophan).	arginine-135-tryptophan	167-190	rhodopsin	Homo sapiens	151-160
9152227-6	1997	CONCLUSIONS: Like rhodopsin, the folding of the cone opsins appears to be dependent on the formation of a disulfide bond between the third transmembrane helix and the second extracellular loop.	Disulfides	106-115	rhodopsin	Homo sapiens	18-27
9065465-2	1997	Following this period, the rate of rhodopsin dephosphorylation was increased in the phorbol ester-treated retinas, so that by about 30 min the amount of phosphorylation was similar to that in control retinas.	Phorbol Esters	84-97	rhodopsin	Homo sapiens	35-44
9050844-2	1997	RK binds to the cytoplasmic face of rhodopsin, and the binding results in activation of the enzyme which then phosphorylates rhodopsin at several serine and threonine residues near the carboxyl terminus.	Serine	146-152	rhodopsin	Homo sapiens	125-134
9050844-2	1997	RK binds to the cytoplasmic face of rhodopsin, and the binding results in activation of the enzyme which then phosphorylates rhodopsin at several serine and threonine residues near the carboxyl terminus.	Threonine	157-166	rhodopsin	Homo sapiens	36-45
9050844-2	1997	RK binds to the cytoplasmic face of rhodopsin, and the binding results in activation of the enzyme which then phosphorylates rhodopsin at several serine and threonine residues near the carboxyl terminus.	Threonine	157-166	rhodopsin	Homo sapiens	125-134
9054576-5	1997	Here, an extensive survey is done of farnesylcysteine analogs and other lipid molecules, which are tested for their ability to inhibit GTP/GDP exchange in transducin catalyzed by photolyzed rhodopsin.	Guanosine Diphosphate	139-142	rhodopsin	Homo sapiens	190-199
9054576-5	1997	Here, an extensive survey is done of farnesylcysteine analogs and other lipid molecules, which are tested for their ability to inhibit GTP/GDP exchange in transducin catalyzed by photolyzed rhodopsin.	S-farnesylcysteine	37-53	rhodopsin	Homo sapiens	190-199
9047297-0	1997	Time-resolved spectroscopy of the early photolysis intermediates of rhodopsin Schiff base counterion mutants.	Schiff Bases	78-89	rhodopsin	Homo sapiens	68-77
9054576-5	1997	Here, an extensive survey is done of farnesylcysteine analogs and other lipid molecules, which are tested for their ability to inhibit GTP/GDP exchange in transducin catalyzed by photolyzed rhodopsin.	Guanosine Triphosphate	135-138	rhodopsin	Homo sapiens	190-199
9047297-4	1997	The Schiff base counterion mutant E113D showed strong similarities to rhodopsin up to lumi, following the established scheme: batho <==> bsi --> lumi.	Schiff Bases	4-15	rhodopsin	Homo sapiens	70-79
9017214-6	1997	This pumping behavior is similar to that seen in a related bacterial rhodopsin, archaerhodopsin-1, which has a histidine in the position analogous to K129.	Histidine	111-120	rhodopsin	Homo sapiens	69-78
9016765-0	1997	4-Hydroxynonenal interaction with rhodopsin.	4-hydroxy-2-nonenal	0-16	rhodopsin	Homo sapiens	34-43
9016765-1	1997	4-Hydroxynonenal binds easily to rhodopsin and this was accompanied by a decrease in measurable sulfhydryl groups.	4-hydroxy-2-nonenal	0-16	rhodopsin	Homo sapiens	33-42
8841383-0	1996	Effect of cholesterol on rhodopsin stability in disk membranes.	Cholesterol	10-21	rhodopsin	Homo sapiens	25-34
9020785-0	1997	Structural dynamics of water and the peptide backbone around the Schiff base associated with the light-activated process of octopus rhodopsin.	Water	23-28	rhodopsin	Homo sapiens	132-141
9020785-0	1997	Structural dynamics of water and the peptide backbone around the Schiff base associated with the light-activated process of octopus rhodopsin.	Schiff Bases	65-76	rhodopsin	Homo sapiens	132-141
8943295-0	1996	The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin.	Glycine	42-49	rhodopsin	Homo sapiens	82-91
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Serine	102-105	rhodopsin	Homo sapiens	68-77
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Threonine	107-110	rhodopsin	Homo sapiens	68-77
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Valine	112-115	rhodopsin	Homo sapiens	68-77
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Isoleucine	117-120	rhodopsin	Homo sapiens	68-77
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Leucine	122-125	rhodopsin	Homo sapiens	68-77
8943295-4	1996	We prepared a set of seven single amino acid replacement mutants of rhodopsin at position 121 (G121A, Ser, Thr, Val, Ile, Leu, and Trp) and control mutants with replacements of Gly114 or Ala117.	Tryptophan	131-134	rhodopsin	Homo sapiens	68-77
8864113-2	1996	Such changes in rhodopsin were explored by construction of double cysteine mutants, each containing one cysteine at the cytoplasmic end of helix C and one cysteine at various positions in the cytoplasmic end of helix F. Magnetic dipolar interactions between spin labels attached to these residues revealed their proximity, and changes in their interaction upon rhodopsin light activation suggested a rigid body movement of helices relative to one another.	Cysteine	66-74	rhodopsin	Homo sapiens	16-25
8864113-3	1996	Disulfide cross-linking of the helices prevented activation of transducin, which suggests the importance of this movement for activation of rhodopsin.	Disulfides	0-9	rhodopsin	Homo sapiens	140-149
8901623-3	1996	The synthesis is mediated by retinaldehyde dehydrogenases which convert some of the chromophore all-trans retinaldehyde, released from bleached rhodopsin, into RA.	Retinaldehyde	96-119	rhodopsin	Homo sapiens	144-153
8901623-7	1996	Invertebrates differ from vertebrates in the mechanism of chromophore regeneration: while in the invertebrate visual cycle the chromophore remains bound, it is released as free all-trans retinaldehyde from illuminated vertebrate rhodopsin.	trans retinaldehyde	181-200	rhodopsin	Homo sapiens	229-238
8841383-3	1996	The effect of membrane cholesterol on rhodopsin was investigated using three independent techniques: thermal bleaching, differential scanning calorimetry (DSC) and activation of the cGMP cascade.	Cholesterol	23-34	rhodopsin	Homo sapiens	38-47
8841383-4	1996	Rhodopsin exhibited an increased resistance to thermally induced bleaching as the membrane cholesterol level was increased.	Cholesterol	91-102	rhodopsin	Homo sapiens	0-9
8841383-7	1996	These results suggest that cholesterol affects the disk membrane properties such that thermally induced unfolding is inhibited, thus stabilizing the rhodopsin structure.	Cholesterol	27-38	rhodopsin	Homo sapiens	149-158
8810308-0	1996	Modulation of GDP release from transducin by the conserved Glu134-Arg135 sequence in rhodopsin.	Guanosine Diphosphate	14-17	rhodopsin	Homo sapiens	85-94
8810308-3	1996	The cytoplasmic domain of rhodopsin binds and activates Gt, but residues that stimulate GDP release from Gt have not been identified until now.	Guanosine Diphosphate	88-91	rhodopsin	Homo sapiens	26-35
8810308-5	1996	We propose that Glu134 and Arg135 constitute the site that directly provides the signal from rhodopsin to activate GDP release from Gt.	Guanosine Diphosphate	115-118	rhodopsin	Homo sapiens	93-102
8848049-0	1996	Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F. A large superfamily of receptors containing seven transmembrane (TM) helices transmits hormonal and sensory signals across the plasma membrane to heterotrimeric G proteins at the cytoplasmic face of the membrane.	Metals	32-37	rhodopsin	Homo sapiens	0-9
8848049-2	1996	In rhodopsin, the photoreceptor of retinal rod cells, we substituted histidine residues for natural amino acids at the cytoplasmic ends of the TM helices C and F. The resulting mutant proteins were able to activate the visual G protein transducin in the absence but not in the presence of metal ions.	Histidine	69-78	rhodopsin	Homo sapiens	3-12
8702573-0	1996	Primary alcohols modulate the activation of the G protein-coupled receptor rhodopsin by a lipid-mediated mechanism.	Alcohols	8-16	rhodopsin	Homo sapiens	75-84
8905849-1	1996	A large family affected with autosomal dominant retinitis pigmentosa (ADRP) with a sectorial phenotype showed a previously described (G to A) mutation in the rhodopsin gene resulting in the substitution of a glycine residue by an arginine in codon 106 of rhodopsin.	Glycine	208-215	rhodopsin	Homo sapiens	158-167
8905849-1	1996	A large family affected with autosomal dominant retinitis pigmentosa (ADRP) with a sectorial phenotype showed a previously described (G to A) mutation in the rhodopsin gene resulting in the substitution of a glycine residue by an arginine in codon 106 of rhodopsin.	Glycine	208-215	rhodopsin	Homo sapiens	255-264
8905849-1	1996	A large family affected with autosomal dominant retinitis pigmentosa (ADRP) with a sectorial phenotype showed a previously described (G to A) mutation in the rhodopsin gene resulting in the substitution of a glycine residue by an arginine in codon 106 of rhodopsin.	Arginine	230-238	rhodopsin	Homo sapiens	158-167
8905849-1	1996	A large family affected with autosomal dominant retinitis pigmentosa (ADRP) with a sectorial phenotype showed a previously described (G to A) mutation in the rhodopsin gene resulting in the substitution of a glycine residue by an arginine in codon 106 of rhodopsin.	Arginine	230-238	rhodopsin	Homo sapiens	255-264
8702809-1	1996	Rhodopsin is constrained in an inactive conformation by interactions with 11-cis-retinal including formation of a protonated Schiff base with Lys296.	Schiff Bases	125-136	rhodopsin	Homo sapiens	0-9
8702573-2	1996	In this study, we have investigated the effect of a series of n-alcohols on the formation of metarhodopsin II (MII), the photoactivated conformation of rhodopsin, which binds and activates transducin.	n-alcohols	62-72	rhodopsin	Homo sapiens	97-106
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	n-alcohols	57-67	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	Ethanol	119-126	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	Butanols	132-139	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	Hexanols	145-152	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	n-alcohols	175-185	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	n-decyl alcohol	215-222	rhodopsin	Homo sapiens	5-14
8702573-3	1996	When rhodopsin was photolyzed in the presence of several n-alcohols, increased MII formation was observed in the order ethanol > butanol > hexanol, whereas longer chain n-alcohols inhibited MII formation with decanol > octanol.	Octanols	228-235	rhodopsin	Homo sapiens	5-14
8702573-8	1996	Our findings strongly support a lipid-mediated mechanism of action for alcohols on rhodopsin and, by analogy, for other G protein-coupled receptors.	Alcohols	71-79	rhodopsin	Homo sapiens	83-92
8810231-6	1996	Furthermore, autosmal retinitis pigmentosa (RP) with rhodopsin mutation at 296 Lys, which in the binding site of 11-cis-retinal, showed constitutive activation of guanosine 5"-triphosphate (GTP) binding protein and no rhodopsin phosphorylation by rhodopsin kinase.	Guanosine Triphosphate	163-188	rhodopsin	Homo sapiens	53-62
8823930-1	1996	The location of cysteines accessible in octopus rhodopsin were characterized by a spin-labeling technique.	Cysteine	16-25	rhodopsin	Homo sapiens	48-57
8810231-6	1996	Furthermore, autosmal retinitis pigmentosa (RP) with rhodopsin mutation at 296 Lys, which in the binding site of 11-cis-retinal, showed constitutive activation of guanosine 5"-triphosphate (GTP) binding protein and no rhodopsin phosphorylation by rhodopsin kinase.	Guanosine Triphosphate	163-188	rhodopsin	Homo sapiens	218-227
8810231-6	1996	Furthermore, autosmal retinitis pigmentosa (RP) with rhodopsin mutation at 296 Lys, which in the binding site of 11-cis-retinal, showed constitutive activation of guanosine 5"-triphosphate (GTP) binding protein and no rhodopsin phosphorylation by rhodopsin kinase.	Guanosine Triphosphate	190-193	rhodopsin	Homo sapiens	53-62
8813600-0	1996	A rhodopsin-based model for melatonin recognition at its G protein-coupled receptor.	Melatonin	28-37	rhodopsin	Homo sapiens	2-11
8673138-4	1996	Here we report that his affected descendants carry a missense mutation in the gene encoding the alpha subunit of rod transducin the G-protein that couples rhodopsin to cGMP-phosphodiesterase in the phototransduction cascade.	Cyclic GMP	168-172	rhodopsin	Homo sapiens	155-164
8652533-10	1996	Based on existing models of rhodopsin and in vitro biochemical studies of site-directed mutants, it appears likely that Gly90 is in the immediate proximity of the Schiff base chromophore linkage.	Schiff Bases	163-174	rhodopsin	Homo sapiens	28-37
8639566-1	1996	To elucidate the structural changes near the beta-ionone ring region of the chromophore during the photobleaching process of rhodopsin, the photochemical and subsequent thermal reactions of rhodopsin analogs, whose retinylidene chromophores were fixed in a 6s-cis form with a five-membered ring (6,5-rhodopsin) and a seven-membered ring (6,7-rhodopsin), respectively, were investigated by low-temperature spectroscopy.	beta-ionone	45-56	rhodopsin	Homo sapiens	125-134
8639566-1	1996	To elucidate the structural changes near the beta-ionone ring region of the chromophore during the photobleaching process of rhodopsin, the photochemical and subsequent thermal reactions of rhodopsin analogs, whose retinylidene chromophores were fixed in a 6s-cis form with a five-membered ring (6,5-rhodopsin) and a seven-membered ring (6,7-rhodopsin), respectively, were investigated by low-temperature spectroscopy.	retinylidene	215-227	rhodopsin	Homo sapiens	125-134
8639566-1	1996	To elucidate the structural changes near the beta-ionone ring region of the chromophore during the photobleaching process of rhodopsin, the photochemical and subsequent thermal reactions of rhodopsin analogs, whose retinylidene chromophores were fixed in a 6s-cis form with a five-membered ring (6,5-rhodopsin) and a seven-membered ring (6,7-rhodopsin), respectively, were investigated by low-temperature spectroscopy.	retinylidene	215-227	rhodopsin	Homo sapiens	190-199
8639566-1	1996	To elucidate the structural changes near the beta-ionone ring region of the chromophore during the photobleaching process of rhodopsin, the photochemical and subsequent thermal reactions of rhodopsin analogs, whose retinylidene chromophores were fixed in a 6s-cis form with a five-membered ring (6,5-rhodopsin) and a seven-membered ring (6,7-rhodopsin), respectively, were investigated by low-temperature spectroscopy.	retinylidene	215-227	rhodopsin	Homo sapiens	190-199
8639566-1	1996	To elucidate the structural changes near the beta-ionone ring region of the chromophore during the photobleaching process of rhodopsin, the photochemical and subsequent thermal reactions of rhodopsin analogs, whose retinylidene chromophores were fixed in a 6s-cis form with a five-membered ring (6,5-rhodopsin) and a seven-membered ring (6,7-rhodopsin), respectively, were investigated by low-temperature spectroscopy.	retinylidene	215-227	rhodopsin	Homo sapiens	190-199
8813600-7	1996	The rhodopsin-based model can explain the importance of some structural features of melatonin and related active compounds.	Melatonin	84-93	rhodopsin	Homo sapiens	4-13
24203295-2	1996	The synthetic peptides are serine- and threonine-phosphorylated analogs of proteolytic fragments from the C-terminal region of rhodopsin.	Serine	27-33	rhodopsin	Homo sapiens	127-136
8634260-1	1996	ATP, its nonhydrolyzable analogue, AMP-PNP, and albumin were found to promote the dissociation of rhodopsin kinase from rod outer segments (ROS) containing photoactivated-rhodopsin (Rho*).	Adenosine Triphosphate	0-3	rhodopsin	Homo sapiens	156-180
8634260-1	1996	ATP, its nonhydrolyzable analogue, AMP-PNP, and albumin were found to promote the dissociation of rhodopsin kinase from rod outer segments (ROS) containing photoactivated-rhodopsin (Rho*).	Adenylyl Imidodiphosphate	35-42	rhodopsin	Homo sapiens	156-180
8617359-0	1996	Calcium-bound recoverin targets rhodopsin kinase to membranes to inhibit rhodopsin phosphorylation.	Calcium	0-7	rhodopsin	Homo sapiens	32-41
8670743-9	1996	Mannose and N-acetyl-glucosamine are major carbohydrate monomers of the oligosaccaride chains of human rhodopsin, and a relatively high percentage of the oligosaccharide chains are galactosylated.	Mannose	0-7	rhodopsin	Homo sapiens	103-112
8670743-9	1996	Mannose and N-acetyl-glucosamine are major carbohydrate monomers of the oligosaccaride chains of human rhodopsin, and a relatively high percentage of the oligosaccharide chains are galactosylated.	Acetylglucosamine	12-32	rhodopsin	Homo sapiens	103-112
8670743-9	1996	Mannose and N-acetyl-glucosamine are major carbohydrate monomers of the oligosaccaride chains of human rhodopsin, and a relatively high percentage of the oligosaccharide chains are galactosylated.	Carbohydrates	43-55	rhodopsin	Homo sapiens	103-112
8670743-9	1996	Mannose and N-acetyl-glucosamine are major carbohydrate monomers of the oligosaccaride chains of human rhodopsin, and a relatively high percentage of the oligosaccharide chains are galactosylated.	oligosaccaride	72-86	rhodopsin	Homo sapiens	103-112
8608127-1	1996	In rhodopsin, the 11-cis-retinal chromophore forms a complex with Lys296 of opsin via a protonated Schiff base.	Schiff Bases	99-110	rhodopsin	Homo sapiens	3-12
24203295-2	1996	The synthetic peptides are serine- and threonine-phosphorylated analogs of proteolytic fragments from the C-terminal region of rhodopsin.	Threonine	39-48	rhodopsin	Homo sapiens	127-136
8667664-5	1996	Direct DNA sequencing revealed a CGC to CTG change in codon 135, that substitutes arginine for leucine residue in rhodopsin.	Arginine	82-90	rhodopsin	Homo sapiens	114-123
8729118-6	1996	The acyl chain packing free volume of the rhodopsin containing lipid vesicles was characterized by a fractional volume parameter fv derived from measurements of the time-resolved fluorescence anisotropy decay of the hydrophobic membrane probe 1,6-diphenyl-1,3,5-hexatriene.	Diphenylhexatriene	243-272	rhodopsin	Homo sapiens	42-51
8740695-1	1996	One family (ADRP15) was found to have mutation in codon 114 of the rhodopsin gene that led to a substitution of a glycine for an aspartic acid.	Glycine	114-121	rhodopsin	Homo sapiens	67-76
8740695-1	1996	One family (ADRP15) was found to have mutation in codon 114 of the rhodopsin gene that led to a substitution of a glycine for an aspartic acid.	Aspartic Acid	129-142	rhodopsin	Homo sapiens	67-76
8621684-1	1996	Cleavage after lysine 32 in the Ggamma2 subtype and after lysine 36 in the Ggamma3 subtype of purified mixed brain Gbetagamma by endoproteinase Lys-C blocks Gbetagamma-mediated stimulation of phosphorylation of rhodopsin in urea-extracted rod outer segments by recombinant human beta-adrenergic receptor kinase (hbetaARK1) holoenzyme while hbetaARK1 binding to rod outer segments is partially affected.	lys-c	144-149	rhodopsin	Homo sapiens	211-220
8667664-5	1996	Direct DNA sequencing revealed a CGC to CTG change in codon 135, that substitutes arginine for leucine residue in rhodopsin.	Leucine	95-102	rhodopsin	Homo sapiens	114-123
8567690-9	1996	Removal of membrane-bound GTP-binding proteins of the rab family by rab GDP dissociation inhibitor completely abolishes formation of these vesicles and results in the retention of rhodopsin in the Golgi.	Guanosine Triphosphate	26-29	rhodopsin	Homo sapiens	180-189
7556089-9	1995	Alanine substitution at four positions moderately (K341) or severely (L344, G348, L349) impairs the susceptibility of alpha 1 to activation by rhodopsin.	Alanine	0-7	rhodopsin	Homo sapiens	143-152
8800472-2	1996	Rhodopsin is composed of two parts: a polypeptide chain called opsin and an 11-cis-retinal chromophore covalently bound to the protein by means of a protonated Schiff base linkage to Lys296 located in the seventh transmembrane segment of the protein.	Schiff Bases	160-171	rhodopsin	Homo sapiens	0-9
8537363-4	1995	However, proline substitution abolished rhodopsin interaction, suggesting that flexibility is important at this site.	Proline	9-16	rhodopsin	Homo sapiens	40-49
8537363-6	1995	Surprisingly, mutants L344A, L349A, F350stop, and stop351A demonstrated a parallel loss of rhodopsin and guanine nucleotide binding.	Guanine Nucleotides	105-123	rhodopsin	Homo sapiens	91-100
7488079-0	1995	Regulation of rhodopsin phosphorylation by a family of neuronal calcium sensors.	Calcium	64-71	rhodopsin	Homo sapiens	14-23
7488079-1	1995	Recoverin is a calcium sensor that regulates rhodopsin phosphorylation in a calcium-dependent manner.	Calcium	15-22	rhodopsin	Homo sapiens	45-54
7488079-1	1995	Recoverin is a calcium sensor that regulates rhodopsin phosphorylation in a calcium-dependent manner.	Calcium	76-83	rhodopsin	Homo sapiens	45-54
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Phosphates	88-97	rhodopsin	Homo sapiens	11-20
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Phosphates	88-97	rhodopsin	Homo sapiens	42-51
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Serine	128-131	rhodopsin	Homo sapiens	42-51
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Serine	128-131	rhodopsin	Homo sapiens	11-20
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Phosphates	152-162	rhodopsin	Homo sapiens	11-20
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Phosphates	152-162	rhodopsin	Homo sapiens	42-51
7607661-1	1995	Autosomal recessive retinitis pigmentosa (ARRP) is a degenerative disease of photoreceptors in which defects in the genes encoding rhodopsin, the beta subunit of rod phosphodiesterase (PDEB) and, recently, in the gene for rod cGMP-gated channel, have been reported.	Cyclic GMP	226-230	rhodopsin	Homo sapiens	131-140
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Serine	178-181	rhodopsin	Homo sapiens	11-20
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Serine	178-181	rhodopsin	Homo sapiens	42-51
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Threonine	190-193	rhodopsin	Homo sapiens	11-20
7662865-4	1995	Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336.	Threonine	190-193	rhodopsin	Homo sapiens	42-51
7662866-1	1995	The key to understanding the reaction mechanism of rhodopsin lies in determining the structure of the retinal binding site and in defining the charge interactions between Glu113 and the retinal protonated Schiff base chromophore.	Schiff Bases	205-216	rhodopsin	Homo sapiens	51-60
8527802-1	1995	Heterozygous missense mutation in codon 15 of the rhodopsin gene was detected in a patient with autosomal dominant retinitis pigmentosa (ADRP), where a transition of adenine to guanine at the second nucleotide in codon 15 (AAT-->AGT), corresponding to a substitution of serine residue for asparagine residue (Asn-15-Ser) was detected.	Adenine	166-173	rhodopsin	Homo sapiens	50-59
8527802-1	1995	Heterozygous missense mutation in codon 15 of the rhodopsin gene was detected in a patient with autosomal dominant retinitis pigmentosa (ADRP), where a transition of adenine to guanine at the second nucleotide in codon 15 (AAT-->AGT), corresponding to a substitution of serine residue for asparagine residue (Asn-15-Ser) was detected.	Guanine	177-184	rhodopsin	Homo sapiens	50-59
8527802-1	1995	Heterozygous missense mutation in codon 15 of the rhodopsin gene was detected in a patient with autosomal dominant retinitis pigmentosa (ADRP), where a transition of adenine to guanine at the second nucleotide in codon 15 (AAT-->AGT), corresponding to a substitution of serine residue for asparagine residue (Asn-15-Ser) was detected.	Serine	273-279	rhodopsin	Homo sapiens	50-59
8527802-1	1995	Heterozygous missense mutation in codon 15 of the rhodopsin gene was detected in a patient with autosomal dominant retinitis pigmentosa (ADRP), where a transition of adenine to guanine at the second nucleotide in codon 15 (AAT-->AGT), corresponding to a substitution of serine residue for asparagine residue (Asn-15-Ser) was detected.	Asparagine	292-302	rhodopsin	Homo sapiens	50-59
7556467-3	1995	Using intraocular injection of a 3H-phe and 3H-leu mixture, we found that the net synthesis of rhodopsin is light-intensity-dependent and can adjust when an animal encounters a new lighting environment.	3h-phe	33-39	rhodopsin	Homo sapiens	95-104
7556467-3	1995	Using intraocular injection of a 3H-phe and 3H-leu mixture, we found that the net synthesis of rhodopsin is light-intensity-dependent and can adjust when an animal encounters a new lighting environment.	3h-leu	44-50	rhodopsin	Homo sapiens	95-104
7556467-4	1995	Rhodopsin net synthesis dropped dramatically in day 1, 200-lx immigrants; however, preliminary studies show that the opsin mRNA levels in these animal were the same as that found in the 200-lx-native group.	lx	59-61	rhodopsin	Homo sapiens	0-9
7556467-6	1995	Microspectrophotometric measurements on single rod cells revealed that the differences in whole-eye rhodopsin levels between the two cyclic intensity groups, 3 lx and 200 lx, were also present at the single cell level.	lx	160-162	rhodopsin	Homo sapiens	100-109
7556467-6	1995	Microspectrophotometric measurements on single rod cells revealed that the differences in whole-eye rhodopsin levels between the two cyclic intensity groups, 3 lx and 200 lx, were also present at the single cell level.	lx	171-173	rhodopsin	Homo sapiens	100-109
7612621-5	1995	All of the cysteine substitution mutants formed the characteristic rhodopsin chromophore (lambda max, 500 nm) with 11-cis-retinal.	Cysteine	11-19	rhodopsin	Homo sapiens	67-76
7612621-10	1995	These findings highlight intrinsic differences in both the reactivity and accessibility of the different cysteine residues in the CD loop and support the important role for a structure in the second cytoplasmic region of rhodopsin.	Cysteine	105-113	rhodopsin	Homo sapiens	221-230
7775460-14	1995	A molecular model based on the structure of rhodopsin, in which the 5"-NH in NECA is hydrogen bonded to Ser-277 and His-278, was developed in order to visualize the environment of the ligand binding site.	Adenosine-5'-(N-ethylcarboxamide)	77-81	rhodopsin	Homo sapiens	44-53
7601641-3	1995	METHODS: Electroretinograms were recorded from three patients with autosomal dominant retinitis pigmentosa and the pro-23-his rhodopsin mutation, two patients with rod monochromatism, and five normal subjects.	pro-23-his	115-125	rhodopsin	Homo sapiens	126-135
7775460-14	1995	A molecular model based on the structure of rhodopsin, in which the 5"-NH in NECA is hydrogen bonded to Ser-277 and His-278, was developed in order to visualize the environment of the ligand binding site.	Hydrogen	85-93	rhodopsin	Homo sapiens	44-53
7775460-14	1995	A molecular model based on the structure of rhodopsin, in which the 5"-NH in NECA is hydrogen bonded to Ser-277 and His-278, was developed in order to visualize the environment of the ligand binding site.	Serine	104-107	rhodopsin	Homo sapiens	44-53
7775460-14	1995	A molecular model based on the structure of rhodopsin, in which the 5"-NH in NECA is hydrogen bonded to Ser-277 and His-278, was developed in order to visualize the environment of the ligand binding site.	Histidine	116-119	rhodopsin	Homo sapiens	44-53
7588555-1	1995	Somatic mutations in the genes for G-protein-coupled receptors which regulate intracellular levels of cyclic AMP have been found in several regions coding for the receptors of melanocyte-stimulating hormone, adrenaline, luteinizing hormone, rhodopsin and thyrotropin.	Cyclic AMP	102-112	rhodopsin	Homo sapiens	241-250
7632872-3	1995	Recent molecular orbital studies and pH experiments on horseshoe crabs (Limulus) suggest that the thermal isomerization of a relatively unstable form of rhodopsin, one in which the Schiff-base linkage between the chromophore and protein is unprotonated, is responsible for thermal noise.	Schiff Bases	181-192	rhodopsin	Homo sapiens	153-162
7789408-6	1995	Although the levels of EPA and the intermediate, docosapentaenoic acid (22:5 omega 3), were both elevated by EPA supplementation in RBCs of adRP patients with rhodopsin gene mutations and controls, DHA production was elevated only in controls.	Eicosapentaenoic Acid	109-112	rhodopsin	Homo sapiens	159-168
7633434-0	1995	Rhodopsin mutation proline347-to-alanine in a family with autosomal dominant retinitis pigmentosa indicates an important role for proline at position 347.	Proline	19-26	rhodopsin	Homo sapiens	0-9
7724183-0	1995	Disruption of conserved rhodopsin disulfide bond by Cys187Tyr mutation causes early and severe autosomal dominant retinitis pigmentosa.	Disulfides	34-43	rhodopsin	Homo sapiens	24-33
7724183-4	1995	RESULTS: Affected family members are heterozygous for a unique Cys187Tyr rhodopsin mutation which disrupts a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	126-135	rhodopsin	Homo sapiens	73-82
7724183-4	1995	RESULTS: Affected family members are heterozygous for a unique Cys187Tyr rhodopsin mutation which disrupts a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	126-135	rhodopsin	Homo sapiens	161-170
7724183-10	1995	CONCLUSION: An early onset, blinding form of autosomal dominant RP results from a rhodopsin Cys187Tyr mutation that eliminates a residue necessary for the formation of a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	187-196	rhodopsin	Homo sapiens	82-91
7724183-10	1995	CONCLUSION: An early onset, blinding form of autosomal dominant RP results from a rhodopsin Cys187Tyr mutation that eliminates a residue necessary for the formation of a highly conserved disulfide bond essential to normal rhodopsin function.	Disulfides	187-196	rhodopsin	Homo sapiens	222-231
7851528-0	1995	Effect of the C-terminal proline repeats on ordered packing of squid rhodopsin and its mobility in membranes.	Proline	25-32	rhodopsin	Homo sapiens	69-78
7851528-2	1995	The C-terminus of squid rhodopsin contains a negatively charged region followed by 9-10 repeats of a proline-rich sequence, not found in rhodopsins other than those of cephalopod invertebrates, but similar proline repeats are found in other, unrelated membrane proteins.	Proline	101-108	rhodopsin	Homo sapiens	24-33
7836439-4	1995	To identify regions that participate in these processes, a series of alanine mutations were generated in the three cytoplasmic loops of rhodopsin and transiently expressed in HEK-293 cells.	Alanine	69-76	rhodopsin	Homo sapiens	136-145
7846071-0	1995	Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation.	Glycine	62-65	rhodopsin	Homo sapiens	52-61
7776964-2	1995	Indeed, a growing number of G protein-coupled receptors (rhodopsin, beta 2-, and alpha 2-adrenergic receptors) have now been shown to have palmitic acid covalently attached to this position.	Palmitic Acid	139-152	rhodopsin	Homo sapiens	57-66
7827090-8	1995	In both the rhodopsin and bathorhodopsin models, we have included a structural water molecule hydrogen bonded with the Schiff base to account for the high C = N stretching vibrations previously observed.	Water	79-84	rhodopsin	Homo sapiens	12-21
7827090-8	1995	In both the rhodopsin and bathorhodopsin models, we have included a structural water molecule hydrogen bonded with the Schiff base to account for the high C = N stretching vibrations previously observed.	Hydrogen	94-102	rhodopsin	Homo sapiens	12-21
7781920-5	1995	Rhodopsin kinase (GRK1) requires a post-translationally added farnesyl isoprenoid to bind to light-activated rhodopsin.	farnesyl isoprenoid	62-81	rhodopsin	Homo sapiens	109-118
7827090-2	1995	The photoreactive chromophore in rhodopsin is 11-cis-retinal bound to the protein via a protonated Schiff base with Glu113 as the counterion.	Schiff Bases	99-110	rhodopsin	Homo sapiens	33-42
7827090-3	1995	We have used the observed 13C NMR chemical shifts of the conjugated retinal carbons in combination with semiempirical molecular orbital calculations to establish the major charge interactions in the retinal binding site of rhodopsin and its primary photoproduct, bathorhodopsin.	13c	26-29	rhodopsin	Homo sapiens	223-232
7827090-3	1995	We have used the observed 13C NMR chemical shifts of the conjugated retinal carbons in combination with semiempirical molecular orbital calculations to establish the major charge interactions in the retinal binding site of rhodopsin and its primary photoproduct, bathorhodopsin.	Carbon	76-83	rhodopsin	Homo sapiens	223-232
7827090-4	1995	In rhodopsin, the NMR data constrain one of the carboxylate oxygens (O1) of Glu113 to be approximately 3 A from the C12 position of the retinal with the second oxygen oriented away from the conjugated retinal chain.	carboxylate	48-59	rhodopsin	Homo sapiens	3-12
7827090-8	1995	In both the rhodopsin and bathorhodopsin models, we have included a structural water molecule hydrogen bonded with the Schiff base to account for the high C = N stretching vibrations previously observed.	Schiff Bases	119-130	rhodopsin	Homo sapiens	12-21
7827090-8	1995	In both the rhodopsin and bathorhodopsin models, we have included a structural water molecule hydrogen bonded with the Schiff base to account for the high C = N stretching vibrations previously observed.	Carbon	155-156	rhodopsin	Homo sapiens	12-21
7846071-0	1995	Dark-light: model for nightblindness from the human rhodopsin Gly-90-->Asp mutation.	Aspartic Acid	74-77	rhodopsin	Homo sapiens	52-61
7827090-8	1995	In both the rhodopsin and bathorhodopsin models, we have included a structural water molecule hydrogen bonded with the Schiff base to account for the high C = N stretching vibrations previously observed.	Nitrogen	159-160	rhodopsin	Homo sapiens	12-21
7827090-4	1995	In rhodopsin, the NMR data constrain one of the carboxylate oxygens (O1) of Glu113 to be approximately 3 A from the C12 position of the retinal with the second oxygen oriented away from the conjugated retinal chain.	Oxygen	60-67	rhodopsin	Homo sapiens	3-12
7846071-1	1995	A human rhodopsin mutation, Gly-90-->Asp (Gly90Asp), cosegregated with an unusual trait of congenital nightblindness in 22 at-risk members of a large autosomal dominant kindred.	Glycine	28-31	rhodopsin	Homo sapiens	8-17
7846071-1	1995	A human rhodopsin mutation, Gly-90-->Asp (Gly90Asp), cosegregated with an unusual trait of congenital nightblindness in 22 at-risk members of a large autosomal dominant kindred.	Aspartic Acid	40-43	rhodopsin	Homo sapiens	8-17
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Phosphorus-32	130-133	rhodopsin	Homo sapiens	49-58
7827090-4	1995	In rhodopsin, the NMR data constrain one of the carboxylate oxygens (O1) of Glu113 to be approximately 3 A from the C12 position of the retinal with the second oxygen oriented away from the conjugated retinal chain.	o1	69-71	rhodopsin	Homo sapiens	3-12
7827090-4	1995	In rhodopsin, the NMR data constrain one of the carboxylate oxygens (O1) of Glu113 to be approximately 3 A from the C12 position of the retinal with the second oxygen oriented away from the conjugated retinal chain.	Oxygen	60-66	rhodopsin	Homo sapiens	3-12
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Phosphorus-32	130-133	rhodopsin	Homo sapiens	306-315
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Guanosine Triphosphate	134-137	rhodopsin	Homo sapiens	49-58
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Guanosine Triphosphate	134-137	rhodopsin	Homo sapiens	306-315
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Guanosine Triphosphate	179-182	rhodopsin	Homo sapiens	49-58
7738098-2	1995	In our approach to identify proteins involved in rhodopsin transport and sorting in retinal photoreceptors, we have found, using [32P]GTP overlays of 2D gel blots, that six small GTP-binding proteins are tightly bound to the post-Golgi membranes immunoisolated with a mAb to the cytoplasmic domain of frog rhodopsin.	Guanosine Triphosphate	179-182	rhodopsin	Homo sapiens	306-315
7708381-7	1995	Special attention is paid to actin and myosin, as well as a small transient fraction of galactose-containing rhodopsin.	Galactose	88-97	rhodopsin	Homo sapiens	109-118
7947803-0	1994	Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry.	thiol ester	0-11	rhodopsin	Homo sapiens	91-100
7947803-0	1994	Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistry.	p-coumaric acid	19-34	rhodopsin	Homo sapiens	91-100
7926045-0	1994	Calcium-sensitive control of rhodopsin phosphorylation in the reconstituted system consisting of photoreceptor membranes, rhodopsin kinase and recoverin.	Calcium	0-7	rhodopsin	Homo sapiens	29-38
9492758-4	1994	A key enzymatic step required for branching to occur would be the transfer of a residue of N-acetylglucosamine to the terminal unsubstituted mannose residue of the major rhodopsin oligosaccharide.	Acetylglucosamine	91-110	rhodopsin	Homo sapiens	170-179
9492758-4	1994	A key enzymatic step required for branching to occur would be the transfer of a residue of N-acetylglucosamine to the terminal unsubstituted mannose residue of the major rhodopsin oligosaccharide.	Mannose	141-148	rhodopsin	Homo sapiens	170-179
9492758-4	1994	A key enzymatic step required for branching to occur would be the transfer of a residue of N-acetylglucosamine to the terminal unsubstituted mannose residue of the major rhodopsin oligosaccharide.	Oligosaccharides	180-195	rhodopsin	Homo sapiens	170-179
9492758-10	1994	It was also observed that prior galactosylation of rhodopsin blocked the addition of GlcNAc to rhodopsin.	Acetylglucosamine	85-91	rhodopsin	Homo sapiens	51-60
9492758-10	1994	It was also observed that prior galactosylation of rhodopsin blocked the addition of GlcNAc to rhodopsin.	Acetylglucosamine	85-91	rhodopsin	Homo sapiens	95-104
7947779-0	1994	A mutant rhodopsin photoproduct with a protonated Schiff base displays an active-state conformation: a Fourier-transform infrared spectroscopy study.	Schiff Bases	50-61	rhodopsin	Homo sapiens	9-18
7947779-1	1994	In the rhodopsin mutant E113A/A117E the position of the protonated Schiff base counterion, Glu113, is moved by one helix turn from position 113 to 117.	Schiff Bases	67-78	rhodopsin	Homo sapiens	7-16
7947785-7	1994	Addition of all-trans-retinol, NADP, and [32P]ATP to rod outer segments increased rhodopsin phosphorylation.	Vitamin A	12-29	rhodopsin	Homo sapiens	82-91
7947785-7	1994	Addition of all-trans-retinol, NADP, and [32P]ATP to rod outer segments increased rhodopsin phosphorylation.	NADP	31-35	rhodopsin	Homo sapiens	82-91
7947785-7	1994	Addition of all-trans-retinol, NADP, and [32P]ATP to rod outer segments increased rhodopsin phosphorylation.	Phosphorus-32	42-45	rhodopsin	Homo sapiens	82-91
7947785-7	1994	Addition of all-trans-retinol, NADP, and [32P]ATP to rod outer segments increased rhodopsin phosphorylation.	Adenosine Triphosphate	46-49	rhodopsin	Homo sapiens	82-91
7947785-8	1994	Kinetic parameters for the reverse reaction determined with exogenous all-trans-retinol were Km = 10 microM; Vmax = 11 nmol/min/mg rhodopsin.	Vitamin A	70-87	rhodopsin	Homo sapiens	131-140
7972030-2	1994	This cysteine is known to be palmitoylated in rhodopsin, the beta 2-adrenergic receptor (beta 2AR) and the alpha 2A-adrenergic receptor (alpha 2AAR).	Cysteine	5-13	rhodopsin	Homo sapiens	46-55
7972030-13	1994	Thus, the function of this cytoplasmic palmitoylcysteine is distinctly different between the alpha 2AR and other G-protein-coupled receptors such as the beta 2AR and rhodopsin, and this suggests that this molecular attribute may subserve diverse roles among members of this family of receptors.	palmitoylcysteine	39-56	rhodopsin	Homo sapiens	166-175
7957584-2	1994	The receptor for human C5a is a member of the rhodopsin superfamily of G protein-coupled receptors and contains an aspartate residue (Asp82) within the putative second transmembrane domain conserved in all other G protein-linked receptors.	Aspartic Acid	115-124	rhodopsin	Homo sapiens	46-55
7926045-1	1994	Rhodopsin phosphorylation in the reconstituted system consisting of urea-washed photoreceptor membranes, rhodopsin kinase and recoverin is regulated by Ca2+: the process takes place at low [Ca2+] but is suppressed at high [Ca2+].	Urea	68-72	rhodopsin	Homo sapiens	0-9
7929034-0	1994	A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin.	Carboxylic Acids	12-27	rhodopsin	Homo sapiens	90-99
7881178-0	1994	Structural studies of the N-linked sugar chains of human rhodopsin.	Nitrogen	26-27	rhodopsin	Homo sapiens	57-66
7881178-0	1994	Structural studies of the N-linked sugar chains of human rhodopsin.	linked sugar	28-40	rhodopsin	Homo sapiens	57-66
7881178-1	1994	Human rhodopsin is a glycoprotein containing two N-linked sugar chains.	n-linked sugar	49-63	rhodopsin	Homo sapiens	6-15
7881178-6	1994	While the major oligosaccharide species of bovine and human rhodopsin are identical, in contrast to the sugar chains of bovine rhodopsin, human rhodopsin also contains sialylated isomers and a high concentration of a galactosylated isomer.	Oligosaccharides	16-31	rhodopsin	Homo sapiens	60-69
7881178-7	1994	These results suggest that species-specific processing of the sugar chains of rhodopsin occurs.	Sugars	62-67	rhodopsin	Homo sapiens	78-87
7929057-8	1994	Dephosphophosducin blocked binding of the Gt alpha 1 subunit to activated rhodopsin in the presence of stoichiometric amounts of Gt beta gamma, whereas phosphophosducin did not.	dephosphophosducin	0-18	rhodopsin	Homo sapiens	74-83
7929057-8	1994	Dephosphophosducin blocked binding of the Gt alpha 1 subunit to activated rhodopsin in the presence of stoichiometric amounts of Gt beta gamma, whereas phosphophosducin did not.	phosphophosducin	2-18	rhodopsin	Homo sapiens	74-83
7929034-2	1994	In the visual receptor rhodopsin, replacement of the conserved Glu134 by a neutral glutamine results in enhanced transducin activation.	Glutamine	83-92	rhodopsin	Homo sapiens	23-32
7985802-4	1994	The new method is illustrated in two case studies, viz., tris(hydroxyethyl)ammonium cholate in Na+/K(+)-ATPase proteoliposomes and n-dodecyl-beta-D-maltoside in rhodopsin proteoliposomes.	dodecyl maltoside	131-157	rhodopsin	Homo sapiens	161-170
8001180-5	1994	The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains.	Phosphatidylcholines	142-161	rhodopsin	Homo sapiens	70-79
8001180-5	1994	The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains.	Phosphatidylserines	223-225	rhodopsin	Homo sapiens	70-79
8001180-5	1994	The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains.	polyunsaturated docosahexaenoic acid	248-284	rhodopsin	Homo sapiens	70-79
8001180-5	1994	The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains.	Docosahexaenoic Acids	286-289	rhodopsin	Homo sapiens	70-79
7948697-5	1994	We studied the proton binding affinity, pKa, of the Schiff base of both octopus rhodopsin and the gecko cone pigment P521 by spectral titration.	Schiff Bases	52-63	rhodopsin	Homo sapiens	80-89
8068654-0	1994	Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin.	Schiff Bases	104-115	rhodopsin	Homo sapiens	20-29
8068654-0	1994	Characterization of rhodopsin-transducin interaction: a mutant rhodopsin photoproduct with a protonated Schiff base activates transducin.	Schiff Bases	104-115	rhodopsin	Homo sapiens	63-72
8068654-1	1994	Rhodopsin, a G protein-coupled seven-transmembrane helix receptor, contains an 11-cis-retinal chromophore covalently linked to opsin apoprotein by a protonated Schiff base.	Schiff Bases	160-171	rhodopsin	Homo sapiens	0-9
8068654-4	1994	The Schiff base positive charge in rhodopsin is stabilized by a carboxylic acid counterion, Glu113.	Schiff Bases	4-15	rhodopsin	Homo sapiens	35-44
8068654-4	1994	The Schiff base positive charge in rhodopsin is stabilized by a carboxylic acid counterion, Glu113.	Carboxylic Acids	64-79	rhodopsin	Homo sapiens	35-44
8052635-1	1994	We prepared rhodopsin mutants that contained a single reactive cysteine residue per rhodopsin molecule at position 65, 140, 240, or 316 on the cytoplasmic face.	Cysteine	63-71	rhodopsin	Homo sapiens	12-21
8052635-1	1994	We prepared rhodopsin mutants that contained a single reactive cysteine residue per rhodopsin molecule at position 65, 140, 240, or 316 on the cytoplasmic face.	Cysteine	63-71	rhodopsin	Homo sapiens	84-93
8052635-2	1994	A carbene-generating photoactivatable group was linked by a disulfide bond to the cysteine sulfhydryl group of each of the rhodopsin mutants.	carbene	2-9	rhodopsin	Homo sapiens	123-132
8052635-2	1994	A carbene-generating photoactivatable group was linked by a disulfide bond to the cysteine sulfhydryl group of each of the rhodopsin mutants.	Disulfides	60-69	rhodopsin	Homo sapiens	123-132
8052635-2	1994	A carbene-generating photoactivatable group was linked by a disulfide bond to the cysteine sulfhydryl group of each of the rhodopsin mutants.	Cysteine	82-90	rhodopsin	Homo sapiens	123-132
8052635-4	1994	Subsequent photoactivation (355 nm) of the carbene-generating group resulted in crosslinking of the rhodopsin mutant carrying a cysteine residue at position 240 to transducin.	carbene	43-50	rhodopsin	Homo sapiens	100-109
8052635-4	1994	Subsequent photoactivation (355 nm) of the carbene-generating group resulted in crosslinking of the rhodopsin mutant carrying a cysteine residue at position 240 to transducin.	Cysteine	128-136	rhodopsin	Homo sapiens	100-109
8052635-6	1994	An alternative reaction observed during photolysis of the rhodopsin mutants was intramolecular insertion of the carbene into rhodopsin.	carbene	112-119	rhodopsin	Homo sapiens	58-67
8052635-6	1994	An alternative reaction observed during photolysis of the rhodopsin mutants was intramolecular insertion of the carbene into rhodopsin.	carbene	112-119	rhodopsin	Homo sapiens	125-134
7948697-9	1994	The Schiff base pKa is 10.4 for octopus rhodopsin and 9.9 for the gecko cone pigment.	Schiff Bases	4-15	rhodopsin	Homo sapiens	40-49
8180207-1	1994	Fluorescent fatty acid labels have been incorporated into the palmitoylation sites of rhodopsin and used to probe the membrane accessibility and location of these sites.	Fluorescent	0-11	rhodopsin	Homo sapiens	86-95
7850269-1	1994	A mother and daughter with autosomal dominant retinitis pigmentosa (adRP) were found to carry a cytosine-to-adenine transversion mutation at codon 4 of the rhodopsin gene.	Cytosine	96-104	rhodopsin	Homo sapiens	156-165
7850269-1	1994	A mother and daughter with autosomal dominant retinitis pigmentosa (adRP) were found to carry a cytosine-to-adenine transversion mutation at codon 4 of the rhodopsin gene.	Adenine	108-115	rhodopsin	Homo sapiens	156-165
7850269-2	1994	This mutation predicts a substitution of lysine for threonine at one of the glycosylation sites in the rhodopsin molecule (Thr4Lys).	Lysine	41-47	rhodopsin	Homo sapiens	103-112
7850269-2	1994	This mutation predicts a substitution of lysine for threonine at one of the glycosylation sites in the rhodopsin molecule (Thr4Lys).	Threonine	52-61	rhodopsin	Homo sapiens	103-112
7850270-1	1994	A mutation in codon 181 (Glu-->Lys) of the rhodopsin gene in a Japanese family.	Glutamic Acid	25-28	rhodopsin	Homo sapiens	46-55
7850270-1	1994	A mutation in codon 181 (Glu-->Lys) of the rhodopsin gene in a Japanese family.	Lysine	34-37	rhodopsin	Homo sapiens	46-55
7850270-2	1994	The PCR/restriction endonuclease digestion (RE) assay and PCR/SSCP analysis of the rhodopsin gene in 13 Japanese families with autosomal dominant retinitis pigmentosa (ad RP) revealed a G-A substitution of the first nucleotide of codon 181, replacing Glu (GAG) with Lys (AAG), in one family.	Glutamic Acid	251-254	rhodopsin	Homo sapiens	83-92
7850270-2	1994	The PCR/restriction endonuclease digestion (RE) assay and PCR/SSCP analysis of the rhodopsin gene in 13 Japanese families with autosomal dominant retinitis pigmentosa (ad RP) revealed a G-A substitution of the first nucleotide of codon 181, replacing Glu (GAG) with Lys (AAG), in one family.	Glycosaminoglycans	256-259	rhodopsin	Homo sapiens	83-92
7850270-2	1994	The PCR/restriction endonuclease digestion (RE) assay and PCR/SSCP analysis of the rhodopsin gene in 13 Japanese families with autosomal dominant retinitis pigmentosa (ad RP) revealed a G-A substitution of the first nucleotide of codon 181, replacing Glu (GAG) with Lys (AAG), in one family.	Lysine	266-269	rhodopsin	Homo sapiens	83-92
7835405-12	1994	Both the degree and time-course of transfer support the idea that this difference in affinity contributes to the flow of retinol to the RPE during a bleach in vivo and, therefore, may play a role in the physiological regeneration of rhodopsin.	Vitamin A	121-128	rhodopsin	Homo sapiens	233-242
8003504-0	1994	Interactions of the beta-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism.	beta-ionone	20-31	rhodopsin	Homo sapiens	76-85
8003504-2	1994	The photoreactions of rhodopsin regenerated with three 9-cis retinal analogs, modified at or in the vicinity of the beta-ionone ring (namely 5,6-epoxy, 7,8-diH, diethyl-acyclic) have been investigated by UV-vis and FTIR difference spectroscopy.	beta-ionone	116-127	rhodopsin	Homo sapiens	22-31
8003504-2	1994	The photoreactions of rhodopsin regenerated with three 9-cis retinal analogs, modified at or in the vicinity of the beta-ionone ring (namely 5,6-epoxy, 7,8-diH, diethyl-acyclic) have been investigated by UV-vis and FTIR difference spectroscopy.	5,6-epoxy	141-150	rhodopsin	Homo sapiens	22-31
8003504-2	1994	The photoreactions of rhodopsin regenerated with three 9-cis retinal analogs, modified at or in the vicinity of the beta-ionone ring (namely 5,6-epoxy, 7,8-diH, diethyl-acyclic) have been investigated by UV-vis and FTIR difference spectroscopy.	7,8-dih	152-159	rhodopsin	Homo sapiens	22-31
8003504-2	1994	The photoreactions of rhodopsin regenerated with three 9-cis retinal analogs, modified at or in the vicinity of the beta-ionone ring (namely 5,6-epoxy, 7,8-diH, diethyl-acyclic) have been investigated by UV-vis and FTIR difference spectroscopy.	-acyclic	168-176	rhodopsin	Homo sapiens	22-31
8075342-0	1994	Photoactivation of rhodopsin involves alterations in cysteine side chains: detection of an S-H band in the Meta I-->Meta II FTIR difference spectrum.	Cysteine	53-61	rhodopsin	Homo sapiens	19-28
8075342-1	1994	FTIR difference spectroscopy has been used to study the role of cysteine residues in the photoactivation of rhodopsin.	Cysteine	64-72	rhodopsin	Homo sapiens	108-117
8075342-2	1994	A positive band near 2550 cm-1 with a low frequency shoulder is detected during rhodopsin photobleaching, which is assigned on the basis of its frequency and isotope shift to the S-H stretching mode of one or more cysteine residues.	Cysteine	214-222	rhodopsin	Homo sapiens	80-89
8075342-6	1994	On this basis, it is likely that at least one of the four remaining cysteine residues in rhodopsin is structurally active during rhodopsin photoactivation.	Cysteine	68-76	rhodopsin	Homo sapiens	89-98
8075342-6	1994	On this basis, it is likely that at least one of the four remaining cysteine residues in rhodopsin is structurally active during rhodopsin photoactivation.	Cysteine	68-76	rhodopsin	Homo sapiens	129-138
7514180-2	1994	Sixteen rhodopsin derivatives were constructed, each of which carried a 12-amino acid epitope derived from the c-Myc protein flanked by penta-glycine linkers.	penta-glycine	136-149	rhodopsin	Homo sapiens	8-17
8180207-1	1994	Fluorescent fatty acid labels have been incorporated into the palmitoylation sites of rhodopsin and used to probe the membrane accessibility and location of these sites.	Fatty Acids	12-22	rhodopsin	Homo sapiens	86-95
8180207-2	1994	The fluorescence properties of anthroyloxy and pyrenyl fatty acids bound to rhodopsin were investigated in a reconstituted vesicle system.	anthroyloxy and pyrenyl fatty acids	31-66	rhodopsin	Homo sapiens	76-85
8180207-8	1994	These results indicate that the labels at the palmitoylation sites of rhodopsin are situated in the membrane much as a free fatty acid.	Fatty Acids, Nonesterified	119-134	rhodopsin	Homo sapiens	70-79
8110774-2	1994	Approximately 70% of the rhodopsin was depalmitoylated in rod outer segments by a mild hydroxylamine treatment that resulted in minimal bleaching of rhodopsin.	Hydroxylamine	87-100	rhodopsin	Homo sapiens	25-34
8120004-1	1994	Recently, mutations of the active site Lys296 residue in rhodopsin (Lys296-->Glu and Lys296-->Met) have been found as the cause of disease in some patients with autosomal dominant retinitis pigmentosa.	Glutamic Acid	80-83	rhodopsin	Homo sapiens	57-66
8107847-6	1994	We show here that the mutation Gly 90-->Asp (G90D) in the second transmembrane segment of rhodopsin, which causes congenital night blindness, also constitutively activates opsin.	Glycine	31-34	rhodopsin	Homo sapiens	93-102
8107847-6	1994	We show here that the mutation Gly 90-->Asp (G90D) in the second transmembrane segment of rhodopsin, which causes congenital night blindness, also constitutively activates opsin.	Aspartic Acid	43-46	rhodopsin	Homo sapiens	93-102
8107847-8	1994	This demonstrates the proximity of Asp 90 and Lys 296 in the three-dimensional structure of rhodopsin and suggests that the constitutively activating mutations operate by a common molecular mechanism, disrupting a salt bridge between Lys 296 and the Schiff base counterion, Glu 113.	Aspartic Acid	35-38	rhodopsin	Homo sapiens	92-101
8107847-8	1994	This demonstrates the proximity of Asp 90 and Lys 296 in the three-dimensional structure of rhodopsin and suggests that the constitutively activating mutations operate by a common molecular mechanism, disrupting a salt bridge between Lys 296 and the Schiff base counterion, Glu 113.	Lysine	46-49	rhodopsin	Homo sapiens	92-101
8107847-8	1994	This demonstrates the proximity of Asp 90 and Lys 296 in the three-dimensional structure of rhodopsin and suggests that the constitutively activating mutations operate by a common molecular mechanism, disrupting a salt bridge between Lys 296 and the Schiff base counterion, Glu 113.	Lysine	234-237	rhodopsin	Homo sapiens	92-101
8107847-8	1994	This demonstrates the proximity of Asp 90 and Lys 296 in the three-dimensional structure of rhodopsin and suggests that the constitutively activating mutations operate by a common molecular mechanism, disrupting a salt bridge between Lys 296 and the Schiff base counterion, Glu 113.	Schiff Bases	250-261	rhodopsin	Homo sapiens	92-101
8107847-8	1994	This demonstrates the proximity of Asp 90 and Lys 296 in the three-dimensional structure of rhodopsin and suggests that the constitutively activating mutations operate by a common molecular mechanism, disrupting a salt bridge between Lys 296 and the Schiff base counterion, Glu 113.	Glutamic Acid	274-277	rhodopsin	Homo sapiens	92-101
8180184-0	1994	The Schiff base counterion of bacteriorhodopsin is protonated in sensory rhodopsin I: spectroscopic and functional characterization of the mutated proteins D76N and D76A.	Schiff Bases	4-15	rhodopsin	Homo sapiens	38-47
8180184-10	1994	Interestingly, parallels exist between this residue and Asp83 in the visual receptor rhodopsin which has recently been found to exist in a protonated form and to undergo an almost identical change in hydrogen bonding during rhodopsin activation.	Hydrogen	200-208	rhodopsin	Homo sapiens	85-94
8180184-10	1994	Interestingly, parallels exist between this residue and Asp83 in the visual receptor rhodopsin which has recently been found to exist in a protonated form and to undergo an almost identical change in hydrogen bonding during rhodopsin activation.	Hydrogen	200-208	rhodopsin	Homo sapiens	224-233
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Alanine	52-59	rhodopsin	Homo sapiens	26-35
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Alanine	52-59	rhodopsin	Homo sapiens	138-147
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Cysteine	63-71	rhodopsin	Homo sapiens	26-35
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Cysteine	63-71	rhodopsin	Homo sapiens	138-147
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Disulfides	120-129	rhodopsin	Homo sapiens	26-35
8171030-0	1994	Structure and function in rhodopsin: replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state.	Disulfides	120-129	rhodopsin	Homo sapiens	138-147
8171030-1	1994	A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187.	Disulfides	2-11	rhodopsin	Homo sapiens	119-128
8171030-1	1994	A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187.	Cysteine	137-140	rhodopsin	Homo sapiens	119-128
8171030-1	1994	A disulfide bond that is evidently conserved in the guanine nucleotide-binding protein-coupled receptors is present in rhodopsin between Cys-110 and Cys-187.	Cysteine	149-152	rhodopsin	Homo sapiens	119-128
8171030-2	1994	We have replaced these two cysteine residues by alanine residues and now report on the properties of the resulting rhodopsin mutants.	Cysteine	27-35	rhodopsin	Homo sapiens	115-124
8171030-2	1994	We have replaced these two cysteine residues by alanine residues and now report on the properties of the resulting rhodopsin mutants.	Alanine	48-55	rhodopsin	Homo sapiens	115-124
8038384-0	1994	Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange.	Water	21-26	rhodopsin	Homo sapiens	79-88
8038384-0	1994	Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange.	Schiff Bases	56-67	rhodopsin	Homo sapiens	79-88
8038384-0	1994	Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange.	Schiff Bases	135-146	rhodopsin	Homo sapiens	79-88
8038384-1	1994	The retinal chromophores of both rhodopsin and bacteriorhodopsin are bound to their apoproteins via a protonated Schiff base.	Schiff Bases	113-124	rhodopsin	Homo sapiens	33-42
8038384-2	1994	We have employed continuous-flow resonance Raman experiments on both pigments to determine that the exchange of a deuteron on the Schiff base with a proton is very fast, with half-times of 6.9 +/- 0.9 and 1.3 +/- 0.3 ms for rhodopsin and bacteriorhodopsin, respectively.	Deuterium	114-122	rhodopsin	Homo sapiens	224-233
8038384-2	1994	We have employed continuous-flow resonance Raman experiments on both pigments to determine that the exchange of a deuteron on the Schiff base with a proton is very fast, with half-times of 6.9 +/- 0.9 and 1.3 +/- 0.3 ms for rhodopsin and bacteriorhodopsin, respectively.	Schiff Bases	130-141	rhodopsin	Homo sapiens	224-233
8038384-6	1994	The relatively slow calculated exchange rates are essentially due to the high pKa values of the Schiff base in both rhodopsin (pKa > 17) and bacteriorhodopsin (pKa approximately 13.5).	Schiff Bases	96-107	rhodopsin	Homo sapiens	116-125
8038384-9	1994	Remarkably, the water-catalyzed exchange, which has a half-time of 16 +/- 2 ms and which dominates at pH 3.0 and below, is slower than the exchange rate of the Schiff base in rhodopsin and bacteriorhodopsin.	Water	16-21	rhodopsin	Homo sapiens	175-184
8038384-9	1994	Remarkably, the water-catalyzed exchange, which has a half-time of 16 +/- 2 ms and which dominates at pH 3.0 and below, is slower than the exchange rate of the Schiff base in rhodopsin and bacteriorhodopsin.	Schiff Bases	160-171	rhodopsin	Homo sapiens	175-184
8106358-3	1994	In order to characterize the molecular interaction between rhodopsin and arrestin, we have studied the ability of synthetic peptides from the proposed cytoplasmic loops of rhodopsin to inhibit arrestin binding.	Peptides	124-132	rhodopsin	Homo sapiens	172-181
8305429-4	1994	The extent of phosphorylation was found to be limited by two mechanisms: (1) binding of arrestin to phosphorylated rhodopsin (one to three phosphate groups) appeared to prevent further phosphorylation (arrestin has also been observed to promote the initial phosphorylation of rhodopsin at 338Ser in rod outer segment homogenates); and (2) reduction of the photolyzed chromophore all-trans-retinal to all-trans-retinol prevented phosphorylation at more than three sites.	Phosphates	139-148	rhodopsin	Homo sapiens	115-124
8305429-5	1994	We propose that previous observations of higher levels of rhodopsin phosphorylation may be the result of the removal of endogenous arrestin, or of exceeding the capacity of retinol dehydrogenase activity by intense bleaches (e.g., by exhausting endogenous NADPH).	NADP	256-261	rhodopsin	Homo sapiens	58-67
8110774-2	1994	Approximately 70% of the rhodopsin was depalmitoylated in rod outer segments by a mild hydroxylamine treatment that resulted in minimal bleaching of rhodopsin.	Hydroxylamine	87-100	rhodopsin	Homo sapiens	149-158
8110774-3	1994	Subsequent purification by affinity chromatography could be used to remove hydroxylamine-bleached rhodopsin.	Hydroxylamine	75-88	rhodopsin	Homo sapiens	98-107
8169598-4	1994	The steady state cGMP concentration in EP-ROS (0.007 mol cGMP per mol rhodopsin) approached the cGMP concentration in intact ROS.	Cyclic GMP	17-21	rhodopsin	Homo sapiens	70-79
8170923-7	1994	The approach has provided a powerful diagnostic tool for identifying GPCRs, and results are consistent with previous observations that the pheromone, cAMP and secretin-like receptors belong to separate families--these bear their own unique sequence fingerprints by which they may be distinguished from the rhodopsin-like superfamily.	Cyclic AMP	150-154	rhodopsin	Homo sapiens	306-315
8121492-0	1994	Calcium controls light-triggered formation of catalytically active rhodopsin.	Calcium	0-7	rhodopsin	Homo sapiens	67-76
8121492-3	1994	Calcium seems to exert several coordinated effects on the cyclic GMP cascade: a fall in [Ca2+] stimulates cGMP synthesis, increases the affinity of the cGMP-gated channel for cGMP and accelerates rhodopsin deactivation by phosphorylation.	Calcium	0-7	rhodopsin	Homo sapiens	196-205
8286371-4	1994	The bulkiness of the tetramethylene bridge in ret8 led to numerous unexpected obstacles in attempts to reconstitute a ret8-containing rhodopsin (Rh8) embedded in lipid bilayer membranes.	Cyclobutanes	21-35	rhodopsin	Homo sapiens	134-143
8286371-4	1994	The bulkiness of the tetramethylene bridge in ret8 led to numerous unexpected obstacles in attempts to reconstitute a ret8-containing rhodopsin (Rh8) embedded in lipid bilayer membranes.	enfenamic acid	145-148	rhodopsin	Homo sapiens	134-143
8286371-5	1994	These obstacles were solved by using methylated rhodopsin which gave MeRh8 containing 11-cis-ret8 as its chromophore.	merh8	69-74	rhodopsin	Homo sapiens	48-57
8286371-5	1994	These obstacles were solved by using methylated rhodopsin which gave MeRh8 containing 11-cis-ret8 as its chromophore.	11-cis-ret8	86-97	rhodopsin	Homo sapiens	48-57
8218279-1	1993	Five mutations of rhodopsin have been produced, each of which contains a unique cysteine residue at positions 62, 65, 140, 240, or 316 in the cytoplasmic domain.	Cysteine	80-88	rhodopsin	Homo sapiens	18-27
8260489-4	1993	Centrifugation of the membranes after illumination and subsequent polyacrylamide gel electrophoresis demonstrates light-dependent binding of rhodopsin kinase to the membranes.	polyacrylamide	66-80	rhodopsin	Homo sapiens	141-150
8260489-7	1993	(ii) The dissociation constant of the complex is 0.3 < KD < 0.5 microM in the absence of ATP, but with ATP, it decreases by at least a factor of 10; however, phosphorylation of rhodopsin or (auto)phosphorylation of rhodopsin kinase leads to destabilization of the complex.	Adenosine Triphosphate	95-98	rhodopsin	Homo sapiens	183-192
8260489-7	1993	(ii) The dissociation constant of the complex is 0.3 < KD < 0.5 microM in the absence of ATP, but with ATP, it decreases by at least a factor of 10; however, phosphorylation of rhodopsin or (auto)phosphorylation of rhodopsin kinase leads to destabilization of the complex.	Adenosine Triphosphate	95-98	rhodopsin	Homo sapiens	221-230
8260489-7	1993	(ii) The dissociation constant of the complex is 0.3 < KD < 0.5 microM in the absence of ATP, but with ATP, it decreases by at least a factor of 10; however, phosphorylation of rhodopsin or (auto)phosphorylation of rhodopsin kinase leads to destabilization of the complex.	Adenosine Triphosphate	109-112	rhodopsin	Homo sapiens	183-192
8260489-7	1993	(ii) The dissociation constant of the complex is 0.3 < KD < 0.5 microM in the absence of ATP, but with ATP, it decreases by at least a factor of 10; however, phosphorylation of rhodopsin or (auto)phosphorylation of rhodopsin kinase leads to destabilization of the complex.	Adenosine Triphosphate	109-112	rhodopsin	Homo sapiens	221-230
8399169-0	1993	Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation.	Hydrogen	110-118	rhodopsin	Homo sapiens	54-63
8232538-3	1993	The random spontaneous events are strongly temperature-dependent and have been attributed to thermal isomerizations of the vitamin A chromophore of rhodopsin, the light-sensitive molecule in photoreceptors.	Vitamin A	123-132	rhodopsin	Homo sapiens	148-157
8232538-5	1993	We propose that photoreceptor noise results from the thermal isomerization of a relatively unstable form of rhodopsin, one in which the Schiff-base linkage between the chromophore and protein is unprotonated.	Schiff Bases	136-147	rhodopsin	Homo sapiens	108-117
8399169-0	1993	Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation.	Hydrogen	110-118	rhodopsin	Homo sapiens	93-102
8399169-0	1993	Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation.	Aspartic Acid	145-158	rhodopsin	Homo sapiens	54-63
8399169-0	1993	Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding change in residue aspartic acid-83 during meta II formation.	Aspartic Acid	145-158	rhodopsin	Homo sapiens	93-102
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Aspartic Acid	73-76	rhodopsin	Homo sapiens	4-13
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Aspartic Acid	73-76	rhodopsin	Homo sapiens	24-33
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Asparagine	85-88	rhodopsin	Homo sapiens	4-13
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Asparagine	85-88	rhodopsin	Homo sapiens	24-33
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Glutamic Acid	100-103	rhodopsin	Homo sapiens	4-13
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Glutamic Acid	100-103	rhodopsin	Homo sapiens	24-33
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Aspartic Acid	113-116	rhodopsin	Homo sapiens	4-13
8399169-2	1993	The rhodopsin-->bathorhodopsin FTIR difference spectra of the mutants Asp-83-->Asn (D83N) and Glu-134-->Asp (E134D) incorporated into membranes are similar to that of native rhodopsin in the photoreceptor membrane, demonstrating that the retinal chromophores of these mutants undergo a normal 11-cis to all-trans photoisomerization.	Aspartic Acid	113-116	rhodopsin	Homo sapiens	24-33
8399169-3	1993	Two bands assigned to the C = O stretching mode of Asp and/or Glu carboxylic acid groups are absent in the D83N rhodopsin-->metarhodopsin II FTIR difference spectrum.	Aspartic Acid	51-54	rhodopsin	Homo sapiens	112-121
8399169-3	1993	Two bands assigned to the C = O stretching mode of Asp and/or Glu carboxylic acid groups are absent in the D83N rhodopsin-->metarhodopsin II FTIR difference spectrum.	Glutamic Acid	62-65	rhodopsin	Homo sapiens	112-121
8399169-3	1993	Two bands assigned to the C = O stretching mode of Asp and/or Glu carboxylic acid groups are absent in the D83N rhodopsin-->metarhodopsin II FTIR difference spectrum.	Carboxylic Acids	66-81	rhodopsin	Homo sapiens	112-121
8399169-5	1993	The most straightforward explanation is that the carboxylic acid group of Asp-83 remains protonated in rhodopsin and its bleaching intermediates but undergoes an increase in its hydrogen bonding during the metarhodopsin I-->metarhodopsin II transition.	Aspartic Acid	74-77	rhodopsin	Homo sapiens	103-112
8352776-0	1993	The nucleotide exchange rates of rho and rac small GTP-binding proteins are enhanced to different extents by their regulatory protein Smg GDS.	Guanosine Triphosphate	51-54	rhodopsin	Homo sapiens	33-44
8365491-0	1993	Interaction of GTP-binding protein Gq with photoactivated rhodopsin in the photoreceptor membranes of crayfish.	Guanosine Triphosphate	15-18	rhodopsin	Homo sapiens	58-67
8349693-1	1993	Phorbol ester treatment of 32P-labeled retinas results in a light-dependent alteration in the phosphorylation state of rhodopsin.	Phorbol Esters	0-13	rhodopsin	Homo sapiens	119-128
8349693-1	1993	Phorbol ester treatment of 32P-labeled retinas results in a light-dependent alteration in the phosphorylation state of rhodopsin.	Phosphorus-32	27-30	rhodopsin	Homo sapiens	119-128
8349693-2	1993	Previously we reported that phorbol myristate acetate causes an increase in the phosphorylation state of rhodopsin in retinas exposed to a brief flash of light, with the greatest increase in phosphorylation observed at lower (< or = 10%) bleach levels (Newton, A. C., and Williams, D. S. (1991) J. Biol.	Tetradecanoylphorbol Acetate	28-53	rhodopsin	Homo sapiens	105-114
8349693-5	1993	Here we show that phorbol myristate acetate causes a decrease in the phosphorylation of rhodopsin after exposure to levels of illumination that result in maximal bleaching of the visual receptor.	Tetradecanoylphorbol Acetate	18-43	rhodopsin	Homo sapiens	88-97
8349693-7	1993	Partial proteolysis revealed that phorbol esters alter the phosphorylation of the carboxyl-terminal domain of rhodopsin.	Phorbol Esters	34-48	rhodopsin	Homo sapiens	110-119
8349693-8	1993	Rhodopsin is the major protein whose phosphorylation state is affected significantly by phorbol esters in situ, although a number of rod outer segment cytosolic and membrane proteins are phosphorylated by protein kinase C in vitro.	Phorbol Esters	88-102	rhodopsin	Homo sapiens	0-9
8399151-1	1993	Through low-temperature photochemistry, UV/vis spectroscopy, and chromophore extraction experiments, we have established that 7,9-dicis-rhodopsin undergoes one-photon-two-bond photoisomerization to a batho intermediate (its absorption maximum is slightly blue shifted from that of bathorhodopsin) containing the all-trans geometry, while 9,11-dicis-12-fluororhodopsin undergoes one-photon-one-bond isomerization to the corresponding 9-cis isomer and then the all-trans batho intermediate.	,9-dicis	127-135	rhodopsin	Homo sapiens	136-145
8395213-1	1993	The single-turn GTP hydrolysis by isolated and soluble transducin has been time-resolved using a rapid flow filtration technique which takes advantage of the GTP-requiring detachment of transducin alpha-subunits (T alpha) from photoactivated rhodopsin (R*).	Guanosine Triphosphate	16-19	rhodopsin	Homo sapiens	242-251
8395213-1	1993	The single-turn GTP hydrolysis by isolated and soluble transducin has been time-resolved using a rapid flow filtration technique which takes advantage of the GTP-requiring detachment of transducin alpha-subunits (T alpha) from photoactivated rhodopsin (R*).	Guanosine Triphosphate	158-161	rhodopsin	Homo sapiens	242-251
8105993-0	1993	Localization of the retinal protonated Schiff base counterion in rhodopsin.	Schiff Bases	39-50	rhodopsin	Homo sapiens	65-74
8346919-1	1993	Rhodopsin kinase catalyzes the incorporation of up to seven phosphates into the carboxyl terminal region of freshly bleached rhodopsin.	Phosphates	60-70	rhodopsin	Homo sapiens	125-134
8346919-9	1993	Our data suggest that the rate of incorporation of the first phosphates into rhodopsin is slower than the rate of formation of more highly phosphorylated species.	Phosphates	61-71	rhodopsin	Homo sapiens	77-86
8400551-0	1993	Identification and oligosaccharide structure analysis of rhodopsin glycoforms containing galactose and sialic acid.	Oligosaccharides	19-34	rhodopsin	Homo sapiens	57-66
8400551-0	1993	Identification and oligosaccharide structure analysis of rhodopsin glycoforms containing galactose and sialic acid.	Galactose	89-98	rhodopsin	Homo sapiens	57-66
8400551-0	1993	Identification and oligosaccharide structure analysis of rhodopsin glycoforms containing galactose and sialic acid.	N-Acetylneuraminic Acid	103-114	rhodopsin	Homo sapiens	57-66
8400551-3	1993	The amino acid sequence data demonstrated that the glycopeptides were derived from rhodopsin and confirmed the presence of two N-glycosylation sites, at residues Asn2 and Asn15.	Glycopeptides	51-64	rhodopsin	Homo sapiens	83-92
8105993-1	1993	Semiempirical molecular orbital calculations are combined with 13C NMR chemical shifts to localize the counterion in the retinal binding site of vertebrate rhodopsin.	13c	63-66	rhodopsin	Homo sapiens	156-165
8105993-4	1993	In contrast, the observed 13C NMR data of rhodopsin exhibit downfield chemical shifts from C8 to C13 relative to the 11-cis-RPSB.Cl corresponding to a net increase of partial positive or decrease of partial negative charge at these positions (Smith, S. O., I. Palings, M. E. Miley, J. Courtin, H. de Groot, J. Lugtenburg, R. A. Mathies, and R. G. Griffin.	13c	26-29	rhodopsin	Homo sapiens	42-51
8105993-11	1993	These data constrain the location and the orientation of the Glu113 side chain, which is known to be the counterion in rhodopsin, and argue for a strong interaction centered at C12 of the retinylidene chain.	retinylidene	188-200	rhodopsin	Homo sapiens	119-128
8343512-0	1993	Regulation of the rhodopsin-transducin interaction by a highly conserved carboxylic acid group.	Carboxylic Acids	73-88	rhodopsin	Homo sapiens	18-27
8343512-4	1993	The role of the conserved Glu-134 was studied by site-specific mutagenesis of rhodopsin in combination with a real-time fluorescence assay of G protein (transducin) activation.	Glutamic Acid	26-29	rhodopsin	Homo sapiens	78-87
8343512-11	1993	The data suggest that the protonated state of Glu-134 favors binding of rhodopsin to transducin and that Glu-134 is not titratable in the rhodopsin-transducin complex.	Glutamic Acid	46-49	rhodopsin	Homo sapiens	72-81
8396448-0	1993	The kinetics and thermodynamics of bleaching of rhodopsin in dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	61-91	rhodopsin	Homo sapiens	48-57
8504090-1	1993	Photolyzed rhodopsin is phosphorylated at multiple serine and threonine residues during the quenching of phototransduction.	Serine	51-57	rhodopsin	Homo sapiens	11-20
8504090-1	1993	Photolyzed rhodopsin is phosphorylated at multiple serine and threonine residues during the quenching of phototransduction.	Threonine	62-71	rhodopsin	Homo sapiens	11-20
8396448-11	1993	The results indicate that rhodopsin has extensive photochemical activity when reconstituted in dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	95-125	rhodopsin	Homo sapiens	26-35
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	Lysine	84-90	rhodopsin	Homo sapiens	46-55
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	Glutamic Acid	109-122	rhodopsin	Homo sapiens	46-55
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	disulphide	193-203	rhodopsin	Homo sapiens	46-55
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	schiff"s base	176-189	rhodopsin	Homo sapiens	46-55
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	Cystine	212-219	rhodopsin	Homo sapiens	46-55
8469290-3	1993	A wealth of biochemical data is available for rhodopsin: 11-cis retinal is bound to lysine 296 in helix VII; glutamic acid 113 on helix III is the counterion to the protonated Schiff"s base; a disulphide bridge, cystine 110-187, connects helix III to the second extracellular loop e2 (refs 13, 14); the carboxy terminus has two palmitoylated cysteines forming a cytoplasmic loop i4 (ref.	Cysteine	342-351	rhodopsin	Homo sapiens	46-55
8463305-1	1993	We have shown previously that GTP-binding regulatory protein (G protein) beta gamma subunits stimulate the agonist- or light-dependent phosphorylation of muscarinic acetylcholine receptors (mAChRs) and rhodopsin by a protein kinase partially purified from porcine brain (mAChR kinase) but not the phosphorylation of rhodopsin by rhodopsin kinase (Haga, K., and Haga, T. (1992) J. Biol.	Guanosine Triphosphate	30-33	rhodopsin	Homo sapiens	202-211
8386638-6	1993	Prior to analysis of the phosphorylation mixture, the phosphorylated form of photoexcited rhodopsin was converted into phospho-opsin by treatment with NH2OH.	Hydroxylamine	151-156	rhodopsin	Homo sapiens	90-99
8463305-1	1993	We have shown previously that GTP-binding regulatory protein (G protein) beta gamma subunits stimulate the agonist- or light-dependent phosphorylation of muscarinic acetylcholine receptors (mAChRs) and rhodopsin by a protein kinase partially purified from porcine brain (mAChR kinase) but not the phosphorylation of rhodopsin by rhodopsin kinase (Haga, K., and Haga, T. (1992) J. Biol.	Guanosine Triphosphate	30-33	rhodopsin	Homo sapiens	316-325
8386638-8	1993	The phosphorylation reaction under different bleaching conditions was also studied in a completely soluble system (using 2% dodecyl maltoside) and the pattern of phosphate incorporation into rhodopsin versus opsin was identical to that in the membrane system.	Phosphates	162-171	rhodopsin	Homo sapiens	191-200
8386638-14	1993	The algebraic equation used to obtain these values highlights the fact that the ratio of the concentrations of the two substrates, photoexcited rhodopsin and rhodopsin, in a sample, determines the final distribution of phosphate between bleached and unbleached rhodopsin.	Phosphates	219-228	rhodopsin	Homo sapiens	144-153
8463305-5	1993	We also report that recombinant beta-adrenergic receptor kinase 1 (beta-ARK1) expressed in COS-7 cells phosphorylates mAChRs (human m2 subtype) and rhodopsin in an agonist- or light-dependent manner, respectively, and that this phosphorylation is stimulated by G protein beta gamma subunits.	carbonyl sulfide	91-94	rhodopsin	Homo sapiens	148-157
8386638-14	1993	The algebraic equation used to obtain these values highlights the fact that the ratio of the concentrations of the two substrates, photoexcited rhodopsin and rhodopsin, in a sample, determines the final distribution of phosphate between bleached and unbleached rhodopsin.	Phosphates	219-228	rhodopsin	Homo sapiens	158-167
8386638-14	1993	The algebraic equation used to obtain these values highlights the fact that the ratio of the concentrations of the two substrates, photoexcited rhodopsin and rhodopsin, in a sample, determines the final distribution of phosphate between bleached and unbleached rhodopsin.	Phosphates	219-228	rhodopsin	Homo sapiens	158-167
8425608-1	1993	Existence of a long-lived intermediate and the states of the carboxylic group of Asp-81 in rhodopsin and its photoproducts.	Aspartic Acid	81-84	rhodopsin	Homo sapiens	91-100
7679248-1	1993	A 49-year-old Japanese man had autosomal dominant retinitis pigmentosa with a point mutation in codon 17 of the rhodopsin gene, resulting in a threonine-to-methionine change, and retinal neovascularization in both eyes.	Threonine	143-152	rhodopsin	Homo sapiens	112-121
7679248-1	1993	A 49-year-old Japanese man had autosomal dominant retinitis pigmentosa with a point mutation in codon 17 of the rhodopsin gene, resulting in a threonine-to-methionine change, and retinal neovascularization in both eyes.	Methionine	156-166	rhodopsin	Homo sapiens	112-121
7678445-1	1993	Photobleaching of rhodopsin in rod photoreceptors activates the visual cascade system leading to a decrease in cyclic GMP and the closure of cGMP-gated channels in the rod outer segment plasma membrane.	Cyclic GMP	141-145	rhodopsin	Homo sapiens	18-27
1492129-1	1992	The photochemical bleaching of vertebrate rhodopsin results in the cis to trans isomerization of the 11-cis-retinal protonated Schiff base.	Schiff Bases	127-138	rhodopsin	Homo sapiens	42-51
8466475-4	1993	Formation of MII requires deprotonation of rhodopsin"s protonated Schiff base which appears to facilitate some opening of the rhodopsin structure.	Schiff Bases	66-77	rhodopsin	Homo sapiens	43-52
8466475-4	1993	Formation of MII requires deprotonation of rhodopsin"s protonated Schiff base which appears to facilitate some opening of the rhodopsin structure.	Schiff Bases	66-77	rhodopsin	Homo sapiens	126-135
1492131-1	1992	Light induced phosphorylation of octopus rhodopsin was greatly enhanced by guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S), suggesting that the kinases are involved in regulating interaction between rhodopsin and G-protein.	Guanosine 5'-O-(3-Thiotriphosphate)	75-110	rhodopsin	Homo sapiens	41-50
1492131-1	1992	Light induced phosphorylation of octopus rhodopsin was greatly enhanced by guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S), suggesting that the kinases are involved in regulating interaction between rhodopsin and G-protein.	Guanosine 5'-O-(3-Thiotriphosphate)	75-110	rhodopsin	Homo sapiens	201-210
1492131-1	1992	Light induced phosphorylation of octopus rhodopsin was greatly enhanced by guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S), suggesting that the kinases are involved in regulating interaction between rhodopsin and G-protein.	Guanosine Triphosphate	112-115	rhodopsin	Homo sapiens	41-50
1492131-1	1992	Light induced phosphorylation of octopus rhodopsin was greatly enhanced by guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S), suggesting that the kinases are involved in regulating interaction between rhodopsin and G-protein.	Guanosine Triphosphate	112-115	rhodopsin	Homo sapiens	201-210
1492131-2	1992	We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.	Guanosine Triphosphate	89-92	rhodopsin	Homo sapiens	145-154
1492131-2	1992	We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.	Guanosine Triphosphate	89-92	rhodopsin	Homo sapiens	145-154
1492131-2	1992	We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.	Guanosine Triphosphate	167-170	rhodopsin	Homo sapiens	49-58
1492131-2	1992	We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.	Guanosine Triphosphate	167-170	rhodopsin	Homo sapiens	145-154
1450111-0	1992	ATP-independent deactivation of squid rhodopsin.	Adenosine Triphosphate	0-3	rhodopsin	Homo sapiens	38-47
1450111-1	1992	Deactivation of light-activated squid rhodopsin was studied in vitro using GTP gamma S binding by G-protein as a direct measure of rhodopsin activity.	Guanosine Triphosphate	75-78	rhodopsin	Homo sapiens	38-47
1492131-2	1992	We determined phosphorylated peptides of octopus rhodopsin in the presence or absence of GTP gamma S. Possible phosphorylation sites for octopus rhodopsin enhanced by GTP gamma S were Thr329, Thr330 and/or Thr336, which suggest that the G-protein associates with cytoplasmic loops including C-terminal peptide in the seventh helix of octopus rhodopsin.	Guanosine Triphosphate	167-170	rhodopsin	Homo sapiens	145-154
1356370-1	1992	Two critical amino acids in the visual pigment rhodopsin are Lys-296, the site of attachment of retinal to the protein through a protonated Schiff base linkage, and Glu-113, the Schiff base counterion.	Lysine	61-64	rhodopsin	Homo sapiens	47-56
1444916-1	1992	Two members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine mutation in the second nucleotide of codon 267 in the rhodopsin gene that resulted in a proline-to-leucine change.	Cytosine	90-98	rhodopsin	Homo sapiens	164-173
1444916-1	1992	Two members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine mutation in the second nucleotide of codon 267 in the rhodopsin gene that resulted in a proline-to-leucine change.	Thymine	102-109	rhodopsin	Homo sapiens	164-173
1444916-1	1992	Two members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine mutation in the second nucleotide of codon 267 in the rhodopsin gene that resulted in a proline-to-leucine change.	Proline	198-205	rhodopsin	Homo sapiens	164-173
1444916-1	1992	Two members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine mutation in the second nucleotide of codon 267 in the rhodopsin gene that resulted in a proline-to-leucine change.	Leucine	209-216	rhodopsin	Homo sapiens	164-173
1444916-2	1992	Two members of another family with autosomal dominant retinitis pigmentosa showed a guanine-to-thymine mutation in the first nucleotide of codon 190 in the rhodopsin gene that resulted in an aspartate-to-tyrosine change.	Guanine	84-91	rhodopsin	Homo sapiens	156-165
1444916-2	1992	Two members of another family with autosomal dominant retinitis pigmentosa showed a guanine-to-thymine mutation in the first nucleotide of codon 190 in the rhodopsin gene that resulted in an aspartate-to-tyrosine change.	Thymine	95-102	rhodopsin	Homo sapiens	156-165
1444916-2	1992	Two members of another family with autosomal dominant retinitis pigmentosa showed a guanine-to-thymine mutation in the first nucleotide of codon 190 in the rhodopsin gene that resulted in an aspartate-to-tyrosine change.	Aspartic Acid	191-200	rhodopsin	Homo sapiens	156-165
1444916-2	1992	Two members of another family with autosomal dominant retinitis pigmentosa showed a guanine-to-thymine mutation in the first nucleotide of codon 190 in the rhodopsin gene that resulted in an aspartate-to-tyrosine change.	Tyrosine	204-212	rhodopsin	Homo sapiens	156-165
1445212-0	1992	Activation of the GTP-binding protein Gq by rhodopsin in squid photoreceptors.	Guanosine Triphosphate	18-21	rhodopsin	Homo sapiens	44-53
1445212-4	1992	Guanine-nucleotide-binding displacement analysis gave a stoichiometry of 1 G-protein per 12.5 rhodopsin molecules, the same as in vertebrate rod photoreceptors.	Guanine Nucleotides	0-18	rhodopsin	Homo sapiens	94-103
1356370-1	1992	Two critical amino acids in the visual pigment rhodopsin are Lys-296, the site of attachment of retinal to the protein through a protonated Schiff base linkage, and Glu-113, the Schiff base counterion.	Schiff Bases	140-151	rhodopsin	Homo sapiens	47-56
1356370-1	1992	Two critical amino acids in the visual pigment rhodopsin are Lys-296, the site of attachment of retinal to the protein through a protonated Schiff base linkage, and Glu-113, the Schiff base counterion.	Glutamic Acid	165-168	rhodopsin	Homo sapiens	47-56
1356370-1	1992	Two critical amino acids in the visual pigment rhodopsin are Lys-296, the site of attachment of retinal to the protein through a protonated Schiff base linkage, and Glu-113, the Schiff base counterion.	Schiff Bases	178-189	rhodopsin	Homo sapiens	47-56
1431805-3	1992	Rhodopsin was inactivated by exposure to hydroxylamine and bright light.	Hydroxylamine	41-54	rhodopsin	Homo sapiens	0-9
1522899-4	1992	Covalent modification in vivo of rhodopsin kinase by a 15-C (farnesyl) isoprenoid enables the kinase to anchor to photon-activated rhodopsin.	15-c (farnesyl) isoprenoid	55-81	rhodopsin	Homo sapiens	33-42
1522899-5	1992	Mutations that alter or eliminate the isoprenoid, fully disable light-specific Rhodopsin kinase translocation.	Terpenes	38-48	rhodopsin	Homo sapiens	79-88
1484692-2	1992	Swedish family with autosomal dominant retinitis pigmentosa with a previously unknown rhodopsin, exon 2, mutation, Arg-135-Leu (CGG to CTG).	ctg	135-138	rhodopsin	Homo sapiens	86-95
1386362-0	1992	The role of arrestin and retinoids in the regeneration pathway of rhodopsin.	Retinoids	25-34	rhodopsin	Homo sapiens	66-75
1496129-0	1992	Effect of lithium on rod photoreceptor rhodopsin-coupled G-protein (transducin).	Lithium	10-17	rhodopsin	Homo sapiens	39-48
1512242-5	1992	By using the MIANS moiety as a fluorescent reporter group, we were able to monitor directly the binding of the MIANS-beta gamma T complex to light-activated rhodopsin, which was reconstituted into phosphatidylcholine vesicles, through an enhancement (30-50%) in the MIANS fluorescence.	Phosphatidylcholines	197-216	rhodopsin	Homo sapiens	157-166
1512242-7	1992	The interactions between the MIANS-beta gamma T complex and rhodopsin also resulted in a quenching of the rhodopsin tryptophan fluorescence (approximately 30%), which most likely reflected resonance energy transfer between the tryptophan residues and the MIANS moieties.	Tryptophan	116-126	rhodopsin	Homo sapiens	60-69
1512242-7	1992	The interactions between the MIANS-beta gamma T complex and rhodopsin also resulted in a quenching of the rhodopsin tryptophan fluorescence (approximately 30%), which most likely reflected resonance energy transfer between the tryptophan residues and the MIANS moieties.	Tryptophan	116-126	rhodopsin	Homo sapiens	106-115
1512242-7	1992	The interactions between the MIANS-beta gamma T complex and rhodopsin also resulted in a quenching of the rhodopsin tryptophan fluorescence (approximately 30%), which most likely reflected resonance energy transfer between the tryptophan residues and the MIANS moieties.	Tryptophan	227-237	rhodopsin	Homo sapiens	60-69
1512242-7	1992	The interactions between the MIANS-beta gamma T complex and rhodopsin also resulted in a quenching of the rhodopsin tryptophan fluorescence (approximately 30%), which most likely reflected resonance energy transfer between the tryptophan residues and the MIANS moieties.	Tryptophan	227-237	rhodopsin	Homo sapiens	106-115
1512242-14	1992	Studies with synthetic peptides representing different regions of the cytoplasmic domain of rhodopsin demonstrated that a portion of the putative carboxyl-terminal tail (amino acid residues 310-324) was capable of eliciting changes in the MIANS-beta gamma T fluorescence as well as inhibiting the MIANS-beta gamma T-induced quenching of the rhodopsin tryptophan fluorescence.	Tryptophan	351-361	rhodopsin	Homo sapiens	92-101
1512243-3	1992	In these studies we have investigated the role of the beta gamma T subunit complex in promoting the rhodopsin-stimulated guanine nucleotide exchange reaction (i.e. the activation event) of the alpha T subunit.	Guanine Nucleotides	121-139	rhodopsin	Homo sapiens	100-109
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Diphosphate	23-26	rhodopsin	Homo sapiens	4-13
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Diphosphate	23-26	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Diphosphate	23-26	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine 5'-O-(3-Thiotriphosphate)	27-62	rhodopsin	Homo sapiens	4-13
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine 5'-O-(3-Thiotriphosphate)	27-62	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine 5'-O-(3-Thiotriphosphate)	27-62	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Triphosphate	64-67	rhodopsin	Homo sapiens	4-13
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Triphosphate	64-67	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Guanosine Triphosphate	64-67	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	tgtp	180-184	rhodopsin	Homo sapiens	4-13
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	tgtp	180-184	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	tgtp	180-184	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Phospholipids	231-243	rhodopsin	Homo sapiens	4-13
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Phospholipids	231-243	rhodopsin	Homo sapiens	107-116
1512243-5	1992	The rhodopsin-promoted GDP/guanosine 5"-O-(3-thiotriphosphate) (GTP gamma S) exchange reaction, within the rhodopsin-alpha T complex, then results in the dissociation of the alpha TGTP gamma S species from the rhodopsin-containing phospholipid vesicles.	Phospholipids	231-243	rhodopsin	Homo sapiens	107-116
1386362-7	1992	In this study, we show that the reduction of the photolyzed chromophore all-trans-retinal to all-trans-retinol is essential for recycling photoactivated rhodopsin.	Vitamin A	102-110	rhodopsin	Homo sapiens	153-162
1330032-0	1992	Oxygen diffusion-concentration product in rhodopsin as observed by a pulse ESR spin labeling method.	Oxygen	0-6	rhodopsin	Homo sapiens	42-51
1330032-1	1992	Permeation of molecular oxygen in rhodopsin, an integral membrane protein, has been investigated by monitoring the bimolecular collision rate between molecular oxygen and the nitroxide spin label using a pulse electron spin resonance (ESR) T1 method.	Oxygen	24-30	rhodopsin	Homo sapiens	34-43
1330032-1	1992	Permeation of molecular oxygen in rhodopsin, an integral membrane protein, has been investigated by monitoring the bimolecular collision rate between molecular oxygen and the nitroxide spin label using a pulse electron spin resonance (ESR) T1 method.	Oxygen	160-166	rhodopsin	Homo sapiens	34-43
1330032-1	1992	Permeation of molecular oxygen in rhodopsin, an integral membrane protein, has been investigated by monitoring the bimolecular collision rate between molecular oxygen and the nitroxide spin label using a pulse electron spin resonance (ESR) T1 method.	Hydroxylamine	175-184	rhodopsin	Homo sapiens	34-43
1330032-2	1992	Rhodopsin was labeled by regeneration with the spin-labeled 9-cis retinal analogue in which the beta-ionone ring of retinal is replaced by the nitroxide tetramethyl-oxypyrrolidine ring.	beta-ionone	96-107	rhodopsin	Homo sapiens	0-9
1330032-2	1992	Rhodopsin was labeled by regeneration with the spin-labeled 9-cis retinal analogue in which the beta-ionone ring of retinal is replaced by the nitroxide tetramethyl-oxypyrrolidine ring.	nitroxide tetramethyl-oxypyrrolidine	143-179	rhodopsin	Homo sapiens	0-9
1330032-4	1992	W-values at the beta-ionone binding site in spin-labeled rhodopsin are in the range of 0.02-0.13 microseconds-1, which are 10-60 times smaller than W"s in water and 1.1-20 times smaller than in model membranes in the gel phase, indicating that membrane proteins create significant permeation resistance to transport of molecular oxygen inside and across the membrane.	beta-ionone	16-27	rhodopsin	Homo sapiens	57-66
1330032-4	1992	W-values at the beta-ionone binding site in spin-labeled rhodopsin are in the range of 0.02-0.13 microseconds-1, which are 10-60 times smaller than W"s in water and 1.1-20 times smaller than in model membranes in the gel phase, indicating that membrane proteins create significant permeation resistance to transport of molecular oxygen inside and across the membrane.	Oxygen	329-335	rhodopsin	Homo sapiens	57-66
1330032-5	1992	W(thereby the oxygen diffusion-concentration product) is larger in the meta II-enriched sample than in rhodopsin, indicating light-induced conformational changes of opsin around the beta-ionone binding site.	Oxygen	14-20	rhodopsin	Homo sapiens	103-112
1330032-5	1992	W(thereby the oxygen diffusion-concentration product) is larger in the meta II-enriched sample than in rhodopsin, indicating light-induced conformational changes of opsin around the beta-ionone binding site.	beta-ionone	182-193	rhodopsin	Homo sapiens	103-112
1627593-5	1992	On the basis of absorption microspectroscopic measurements and of inhibition experiments on pigment biosynthetic pathways, we have recently suggested that a rhodopsin could be the functional receptor of the visual process in Euglena gracilis, a flagellate which can use light directly to promote photosynthetic reactions, or as an incident flux of information to adjust its swimming orientation.	flagellate	245-255	rhodopsin	Homo sapiens	157-166
1733928-9	1992	83, 2797-2801) and were inhibited by low concentrations of heparin, an inhibitor of beta-adrenergic receptor kinase, (IC50 = 15 nM), suggesting that both mAChR and rhodopsin are phosphorylated by the same or very similar kinase(s) belonging to the beta-adrenergic receptor kinase family.	Heparin	59-66	rhodopsin	Homo sapiens	164-173
1577792-5	1992	Nonpolar residues normally present in rhodopsin and in the green pigment were substituted by hydroxyl-bearing residues normally present in the red pigment.	Hydroxyl Radical	93-101	rhodopsin	Homo sapiens	38-47
1580841-2	1992	Three members of one family and one person from another family were found to have a guanine-to-adenine transition mutation in the first nucleotide of codon 106 in the rhodopsin gene that results in a glycine-to-arginine change.	Guanine	84-91	rhodopsin	Homo sapiens	167-176
1580841-2	1992	Three members of one family and one person from another family were found to have a guanine-to-adenine transition mutation in the first nucleotide of codon 106 in the rhodopsin gene that results in a glycine-to-arginine change.	Adenine	95-102	rhodopsin	Homo sapiens	167-176
1580841-2	1992	Three members of one family and one person from another family were found to have a guanine-to-adenine transition mutation in the first nucleotide of codon 106 in the rhodopsin gene that results in a glycine-to-arginine change.	Glycine	200-207	rhodopsin	Homo sapiens	167-176
1580841-2	1992	Three members of one family and one person from another family were found to have a guanine-to-adenine transition mutation in the first nucleotide of codon 106 in the rhodopsin gene that results in a glycine-to-arginine change.	Arginine	211-219	rhodopsin	Homo sapiens	167-176
1532320-0	1992	Histidine residues regulate the transition of photoexcited rhodopsin to its active conformation, metarhodopsin II.	Histidine	0-9	rhodopsin	Homo sapiens	59-68
1497755-1	1992	Light-induced H+ release and reuptake as well as surface potential changes inherent in the bacterio-rhodopsin reaction cycle were measured between 10 degrees C and 50 degrees C. Signals of optical pH indicators covalently bound to Lys-129 at the extracellular surface of bacteriorhodopsin were compared with absorbance changes of probes residing in the aqueous bulk phase.	Lysine	231-234	rhodopsin	Homo sapiens	100-109
1317509-2	1992	Light-activated rhodopsin catalyses the exchange of GDP for GTP on multiple transducin molecules.	Guanosine Diphosphate	52-55	rhodopsin	Homo sapiens	16-25
1317509-2	1992	Light-activated rhodopsin catalyses the exchange of GDP for GTP on multiple transducin molecules.	Guanosine Triphosphate	60-63	rhodopsin	Homo sapiens	16-25
1540127-1	1992	Using the radionuclide 65Zn, we have demonstrated the direct binding of zinc to purified rhodopsin.	radionuclide 65zn	10-27	rhodopsin	Homo sapiens	89-98
1540127-2	1992	65Zn is eluted with detergent-solubilized rhodopsin from concanavalin A columns and remains bound to the visual pigment through a subsequent gel-filtration step.	Zinc-65	0-4	rhodopsin	Homo sapiens	42-51
1477634-0	1992	Diffuse loss of rod function in autosomal dominant retinitis pigmentosa with pro-347-leu mutation of rhodopsin.	Proline	77-80	rhodopsin	Homo sapiens	101-110
1731921-6	1992	The metarhodopsin I in equilibrium with meta II equilibrium constant, Keq has a linear relationship with fv for rhodopsin in PAPC vesicles with and without cholesterol as well as for rhodopsin in DMPC vesicles, and these two correlation lines have different slopes.	Cholesterol	156-167	rhodopsin	Homo sapiens	8-17
1731921-6	1992	The metarhodopsin I in equilibrium with meta II equilibrium constant, Keq has a linear relationship with fv for rhodopsin in PAPC vesicles with and without cholesterol as well as for rhodopsin in DMPC vesicles, and these two correlation lines have different slopes.	Dimyristoylphosphatidylcholine	196-200	rhodopsin	Homo sapiens	8-17
1731723-1	1992	Six members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine transition mutation in the second nucleotide of codon 17 in the rhodopsin gene that resulted in a threonine to methionine change.	Cytosine	90-98	rhodopsin	Homo sapiens	174-183
1731723-1	1992	Six members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine transition mutation in the second nucleotide of codon 17 in the rhodopsin gene that resulted in a threonine to methionine change.	Thymine	102-109	rhodopsin	Homo sapiens	174-183
1731723-1	1992	Six members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine transition mutation in the second nucleotide of codon 17 in the rhodopsin gene that resulted in a threonine to methionine change.	Threonine	208-217	rhodopsin	Homo sapiens	174-183
1731723-1	1992	Six members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-thymine transition mutation in the second nucleotide of codon 17 in the rhodopsin gene that resulted in a threonine to methionine change.	Methionine	221-231	rhodopsin	Homo sapiens	174-183
1731723-2	1992	Three members from another family with autosomal dominant retinitis pigmentosa showed a guanine-to-adenine transition mutation in the first nucleotide of codon 182 in the rhodopsin gene that resulted in a glycine to serine change.	Guanine	88-95	rhodopsin	Homo sapiens	171-180
1731723-2	1992	Three members from another family with autosomal dominant retinitis pigmentosa showed a guanine-to-adenine transition mutation in the first nucleotide of codon 182 in the rhodopsin gene that resulted in a glycine to serine change.	Adenine	99-106	rhodopsin	Homo sapiens	171-180
1731723-2	1992	Three members from another family with autosomal dominant retinitis pigmentosa showed a guanine-to-adenine transition mutation in the first nucleotide of codon 182 in the rhodopsin gene that resulted in a glycine to serine change.	Glycine	205-212	rhodopsin	Homo sapiens	171-180
1731723-2	1992	Three members from another family with autosomal dominant retinitis pigmentosa showed a guanine-to-adenine transition mutation in the first nucleotide of codon 182 in the rhodopsin gene that resulted in a glycine to serine change.	Serine	216-222	rhodopsin	Homo sapiens	171-180
1422899-5	1992	Rhodopsin becomes enzymatically active and catalyses the activation by GTP of a great number of transducins, which in turn activate cGMP phosphodiesterase.	Guanosine Triphosphate	71-74	rhodopsin	Homo sapiens	0-9
1616497-2	1992	T beta gamma-2 enhances GTP binding to the alpha-subunit of transducin (T alpha) in the presence of a photobleaching intermediate of rhodopsin, while T beta gamma-1 is an inactive component with little enhancement ability (Fukada, Y., Ohguro, H., Saito, T., Yoshizawa, T., and Akino, T. (1989) J. Biol.	Guanosine Triphosphate	24-27	rhodopsin	Homo sapiens	133-142
1477634-0	1992	Diffuse loss of rod function in autosomal dominant retinitis pigmentosa with pro-347-leu mutation of rhodopsin.	Leucine	85-88	rhodopsin	Homo sapiens	101-110
1477634-5	1992	All displayed the same rhodopsin gene mutation at codon 347, which exchanges the amino acid proline for leucine (pro-347-leu).	Proline	92-99	rhodopsin	Homo sapiens	23-32
1477634-5	1992	All displayed the same rhodopsin gene mutation at codon 347, which exchanges the amino acid proline for leucine (pro-347-leu).	Leucine	104-111	rhodopsin	Homo sapiens	23-32
1477634-5	1992	All displayed the same rhodopsin gene mutation at codon 347, which exchanges the amino acid proline for leucine (pro-347-leu).	Proline	92-95	rhodopsin	Homo sapiens	23-32
1477634-5	1992	All displayed the same rhodopsin gene mutation at codon 347, which exchanges the amino acid proline for leucine (pro-347-leu).	Leucine	104-107	rhodopsin	Homo sapiens	23-32
1936273-3	1991	We show that GTP analogs permanently activate an ADP-ribosylating factor (ARF) which mediates CT action on retinal cell membranes: when transducin-depleted membranes were pre-activated by GTP analogs, re-added transducin became sensitive to CT in the absence of nucleotide, and presence of photoexcited rhodopsin (R*).	Guanosine Triphosphate	13-16	rhodopsin	Homo sapiens	303-312
1765153-2	1991	In this study, we show that highly phosphorylated forms of inositol compete against the arrestin-rhodopsin interaction.	Inositol	59-67	rhodopsin	Homo sapiens	97-106
1765153-4	1991	Only a small control amount of inositol phosphates is bound, when arrestin interacts with phosphorylated rhodopsin.	Inositol Phosphates	31-50	rhodopsin	Homo sapiens	105-114
1765153-5	1991	This argues for a release of bound inositol phosphates by interaction with rhodopsin.	Inositol Phosphates	35-54	rhodopsin	Homo sapiens	75-84
1782650-10	1991	Studies using synthetic peptides from amino acid sequences corresponding to Gt and rhodopsin have provided information on the sites of rhodopsin-Gt interaction.	Peptides	24-32	rhodopsin	Homo sapiens	83-92
1782650-10	1991	Studies using synthetic peptides from amino acid sequences corresponding to Gt and rhodopsin have provided information on the sites of rhodopsin-Gt interaction.	Peptides	24-32	rhodopsin	Homo sapiens	135-144
1775314-5	1991	The authors present a family with Pro-23-His rhodopsin-associated RP in which all six affected individuals had a regional distribution of the retinal degeneration in which the inferior hemisphere of the retina was most severely affected.	pro-23-his	34-44	rhodopsin	Homo sapiens	45-54
1794572-2	1991	New results are presented on the structure of squid rhodopsin, which possesses an extensive proline-rich repeat at its C-terminus, using negative-stain electron microscopy.	Proline	92-99	rhodopsin	Homo sapiens	52-61
1946353-7	1991	A similar steric trigger is essential for activation of mammalian rhodopsin, indicating a common mechanism for receptor activation in archaebacterial and vertebrate retinylidene photosensors.	retinylidene	165-177	rhodopsin	Homo sapiens	66-75
1925597-4	1991	These measurements demonstrate that the first step in vision, the 11-cis----11-trans torsional isomerization of the rhodopsin chromophore, is essentially complete in only 200 femtoseconds.	11-cis----11	66-78	rhodopsin	Homo sapiens	116-125
1655754-2	1991	In rod photoreceptor cells, the light response is triggered by an enzymatic cascade that causes cGMP levels to fall: excited rhodopsin (Rho*)----rod G-protein (transducin, Gt)----cGMP-phosphodiesterase (PDE).	Cyclic GMP	96-100	rhodopsin	Homo sapiens	125-134
1764418-1	1991	The phosphorylation of photoexcited rhodopsin (Rho*) is thought to inactivate this receptor by inhibiting its interaction with the GTP-binding protein transducin (Gt).	Guanosine Triphosphate	131-134	rhodopsin	Homo sapiens	36-45
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	79-82	rhodopsin	Homo sapiens	59-68
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	79-82	rhodopsin	Homo sapiens	237-246
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	183-186	rhodopsin	Homo sapiens	59-68
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	183-186	rhodopsin	Homo sapiens	237-246
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	183-186	rhodopsin	Homo sapiens	59-68
1764418-3	1991	The dephosphorylation of greater than 10(7) phosphorylated rhodopsin molecules/ROS following a bright flash can be blocked by prior dim continuous illumination (generating 10(3) Rho*/ROS/s) that cumulatively bleaches approximately 10(5) rhodopsin molecules/ROS.	ros	183-186	rhodopsin	Homo sapiens	237-246
1764418-4	1991	The phenomenon has not been previously noted because these low levels of light are emitted as a result of Cerenkov radiation from the 32P isotope that is usually employed to monitor rhodopsin phosphorylation.	Phosphorus-32	134-137	rhodopsin	Homo sapiens	182-191
1764418-5	1991	The inhibition of rhodopsin dephosphorylation by dim conditioning illumination is observed in intact ROS-RIS but is lost when ROS-RIS are electropermeabilized or fragmented.	ros-ris	101-108	rhodopsin	Homo sapiens	18-27
1764418-5	1991	The inhibition of rhodopsin dephosphorylation by dim conditioning illumination is observed in intact ROS-RIS but is lost when ROS-RIS are electropermeabilized or fragmented.	ros-ris	126-133	rhodopsin	Homo sapiens	18-27
1929926-1	1991	Eight members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-guanine (C-to-G) transversion mutation in the second nucleotide of codon 58 of the rhodopsin gene, causing a substitution of the amino acid arginine for threonine.	cytosine-to-guanine	92-111	rhodopsin	Homo sapiens	187-196
1929926-1	1991	Eight members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-guanine (C-to-G) transversion mutation in the second nucleotide of codon 58 of the rhodopsin gene, causing a substitution of the amino acid arginine for threonine.	amino acid arginine	233-252	rhodopsin	Homo sapiens	187-196
1929926-1	1991	Eight members of a family with autosomal dominant retinitis pigmentosa were found to have a cytosine-to-guanine (C-to-G) transversion mutation in the second nucleotide of codon 58 of the rhodopsin gene, causing a substitution of the amino acid arginine for threonine.	Threonine	257-266	rhodopsin	Homo sapiens	187-196
1658789-2	1991	This phototransduction is mediated by a guanine nucleotide-binding (G) protein cascade in which rhodopsin is the receptor, transducin is the G-protein, and the cGMP-specific phosphodiesterase (PDE) is the effector.	Guanine Nucleotides	40-58	rhodopsin	Homo sapiens	96-105
1897520-6	1991	We have used this assay to detect three previously unreported rhodopsin base substitutions associated with ADRP.	adrp	107-111	rhodopsin	Homo sapiens	62-71
1649627-0	1991	13C magic-angle spinning NMR studies of bathorhodopsin, the primary photoproduct of rhodopsin.	13c	0-3	rhodopsin	Homo sapiens	45-54
1840561-0	1991	Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa.	Proline	0-3	rhodopsin	Homo sapiens	28-37
1840561-0	1991	Pro-347-Arg mutation of the rhodopsin gene in autosomal dominant retinitis pigmentosa.	Arginine	8-11	rhodopsin	Homo sapiens	28-37
1882937-2	1991	In a family with a stop codon mutation at the carboxyl end of the molecule (glutamine-344), young members with the mutation were asymptomatic and clinically unaffected but showed about 1 log unit of rod sensitivity loss across the visual field and decreased rhodopsin levels; at this stage, cone function was essentially normal.	Glutamine	76-85	rhodopsin	Homo sapiens	258-267
2040617-7	1991	Conditions which resulted in the activation of the alpha T.GDP subunit (i.e. the addition of AlF4- or the addition of rhodopsin-containing vesicles and GTP gamma S) resulted in a reversal of the alpha T.GDP-induced enhancement of the MIANS beta gamma T fluorescence.	Guanosine Diphosphate	59-62	rhodopsin	Homo sapiens	118-127
1905716-2	1991	We have developed a reconstitution assay using rhodopsin-catalyzed guanosine 5"-3-O-(thio)triphosphate (GTP gamma S) binding to resolved alpha subunit of the retinal G-protein transducin (Gt alpha) to quantitate the activity of beta gamma proteins.	Guanosine 5'-O-(3-Thiotriphosphate)	67-102	rhodopsin	Homo sapiens	47-56
1905716-3	1991	Rhodopsin facilitates the exchange of GTP gamma S for GDP bound to Gt alpha beta gamma with a 60-fold higher apparent affinity than for Gt alpha alone.	Guanosine Triphosphate	38-41	rhodopsin	Homo sapiens	0-9
1905716-3	1991	Rhodopsin facilitates the exchange of GTP gamma S for GDP bound to Gt alpha beta gamma with a 60-fold higher apparent affinity than for Gt alpha alone.	Guanosine Diphosphate	54-57	rhodopsin	Homo sapiens	0-9
1905716-4	1991	At limiting rhodopsin, G-protein-derived beta gamma subunits catalytically enhance the rate of GTP gamma S binding to resolved Gt alpha.	Guanosine Triphosphate	95-98	rhodopsin	Homo sapiens	12-21
1905716-5	1991	The isolated beta gamma subunit of retinal G-protein (beta 1, gamma 1 genes) facilitates rhodopsin-catalyzed GTP gamma S exchange on Gt alpha in a concentration-dependent manner (K0.5 = 254 +/- 21 nM).	Guanosine Triphosphate	109-112	rhodopsin	Homo sapiens	89-98
1905716-9	1991	However, human placental beta 35 gamma facilitates rhodopsin-catalyzed GTP gamma S exchange on Gt alpha with a higher apparent affinity than Gt beta gamma (K0.5 = 76 +/- 54 nM).	Guanosine Triphosphate	71-74	rhodopsin	Homo sapiens	51-60
2040617-7	1991	Conditions which resulted in the activation of the alpha T.GDP subunit (i.e. the addition of AlF4- or the addition of rhodopsin-containing vesicles and GTP gamma S) resulted in a reversal of the alpha T.GDP-induced enhancement of the MIANS beta gamma T fluorescence.	Guanosine Triphosphate	152-155	rhodopsin	Homo sapiens	118-127
2040617-7	1991	Conditions which resulted in the activation of the alpha T.GDP subunit (i.e. the addition of AlF4- or the addition of rhodopsin-containing vesicles and GTP gamma S) resulted in a reversal of the alpha T.GDP-induced enhancement of the MIANS beta gamma T fluorescence.	Guanosine Diphosphate	203-206	rhodopsin	Homo sapiens	118-127
1710937-4	1991	The amide I and II frequencies are at 1,656 and 1,546 cm-1, close to the frequency of the amide I and II bands of rhodopsin, bacteriorhodopsin and other alpha-helical proteins.	Amides	4-9	rhodopsin	Homo sapiens	114-123
2021172-1	1991	We studied the ocular findings in eight unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-thymine transition in the second nucleotide of codon 347 of the rhodopsin gene.	Cytosine	127-135	rhodopsin	Homo sapiens	203-212
2021172-1	1991	We studied the ocular findings in eight unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-thymine transition in the second nucleotide of codon 347 of the rhodopsin gene.	Thymine	139-146	rhodopsin	Homo sapiens	203-212
1710937-4	1991	The amide I and II frequencies are at 1,656 and 1,546 cm-1, close to the frequency of the amide I and II bands of rhodopsin, bacteriorhodopsin and other alpha-helical proteins.	Amides	90-95	rhodopsin	Homo sapiens	114-123
1990431-2	1991	The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296.	Schiff Bases	71-82	rhodopsin	Homo sapiens	27-36
1990431-2	1991	The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296.	Lysine	121-124	rhodopsin	Homo sapiens	27-36
1985460-5	1991	We have sequenced the rhodopsin gene in a C17-linked ADRP family and have identified in the 4th exon and in-frame 3-bp deletion which deletes one of the two isoleucine monomers at codons 255 and 256.	Isoleucine	157-167	rhodopsin	Homo sapiens	22-31
1988047-4	1991	One such process involves the biosynthesis of 11-cis-retinal, the chromophore of rhodopsin, from all-trans-retinol (vitamin A).	Vitamin A	97-114	rhodopsin	Homo sapiens	81-90
1988047-4	1991	One such process involves the biosynthesis of 11-cis-retinal, the chromophore of rhodopsin, from all-trans-retinol (vitamin A).	Vitamin A	116-125	rhodopsin	Homo sapiens	81-90
1987955-2	1991	A cytosine-to-adenine transversion in codon 23 of rhodopsin, the rod visual pigment gene, was reported recently by Dryja et al in 17 of 148 unrelated patients with autosomal dominant retinitis pigmentosa, but the clinical findings associated with this deletion have not been reported in detail.	cytosine-to-adenine	2-21	rhodopsin	Homo sapiens	50-59
1987956-1	1991	Ocular findings are presented from 17 unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-adenine transversion in codon 23 of the rhodopsin gene corresponding to a substitution of histidine for proline in the 23rd amino acid of rhodopsin (designated rhodopsin, Pro-23-His).	Cytosine	125-133	rhodopsin	Homo sapiens	177-186
1987956-1	1991	Ocular findings are presented from 17 unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-adenine transversion in codon 23 of the rhodopsin gene corresponding to a substitution of histidine for proline in the 23rd amino acid of rhodopsin (designated rhodopsin, Pro-23-His).	Adenine	137-144	rhodopsin	Homo sapiens	177-186
1987956-1	1991	Ocular findings are presented from 17 unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-adenine transversion in codon 23 of the rhodopsin gene corresponding to a substitution of histidine for proline in the 23rd amino acid of rhodopsin (designated rhodopsin, Pro-23-His).	Histidine	227-236	rhodopsin	Homo sapiens	177-186
1987956-1	1991	Ocular findings are presented from 17 unrelated patients with a form of autosomal dominant retinitis pigmentosa and the same cytosine-to-adenine transversion in codon 23 of the rhodopsin gene corresponding to a substitution of histidine for proline in the 23rd amino acid of rhodopsin (designated rhodopsin, Pro-23-His).	Proline	241-248	rhodopsin	Homo sapiens	177-186
1808803-6	1991	Patients so far studied with rhodopsin, Val345Met, have smaller 0.5-Hz full-field ERG amplitudes, on average, than those with Pro23His or Thr58Arg and larger ERG amplitudes than those with Pro347Leu or Pro347Ser.	pro347ser	202-211	rhodopsin	Homo sapiens	29-38
2207250-2	1990	The chromophore of octopus rhodopsin is 11-cis retinal, linked via a protonated Schiff base to the protein backbone.	Schiff Bases	80-91	rhodopsin	Homo sapiens	27-36
2239971-1	1990	In exon 1 at codon 23 of the rhodopsin gene, a mutation resulting in a proline-to-histidine substitution has previously been observed in approximately 12% of American autosomal dominant retinitis pigmentosa (ADRP) patients.	Proline	71-78	rhodopsin	Homo sapiens	29-38
2239971-1	1990	In exon 1 at codon 23 of the rhodopsin gene, a mutation resulting in a proline-to-histidine substitution has previously been observed in approximately 12% of American autosomal dominant retinitis pigmentosa (ADRP) patients.	Histidine	82-91	rhodopsin	Homo sapiens	29-38
2229054-0	1990	Displacement of rhodopsin by GDP from three-loop interaction with transducin depends critically on the diphosphate beta-position.	Diphosphates	103-114	rhodopsin	Homo sapiens	16-25
2229054-1	1990	We have studied the effect of GDP and its analog guanyl-5"-yl thiophosphate (GDP beta S) on the interaction between rhodopsin and transducin (Gt).	Guanosine Diphosphate	30-33	rhodopsin	Homo sapiens	116-125
2229054-1	1990	We have studied the effect of GDP and its analog guanyl-5"-yl thiophosphate (GDP beta S) on the interaction between rhodopsin and transducin (Gt).	guanosine 5'-O-(2-thiodiphosphate)	49-75	rhodopsin	Homo sapiens	116-125
2229054-1	1990	We have studied the effect of GDP and its analog guanyl-5"-yl thiophosphate (GDP beta S) on the interaction between rhodopsin and transducin (Gt).	guanosine 5'-O-(2-thiodiphosphate)	77-87	rhodopsin	Homo sapiens	116-125
2229054-3	1990	Extra-MII can be completely abolished by GDP, with a half-suppression at 10 microM under the conditions (4 degrees C, pH 8, 7.5 nM photoactivated rhodopsin).	Guanosine Diphosphate	41-44	rhodopsin	Homo sapiens	146-155
2229054-6	1990	However, GDP beta S enhanced considerably the efficiency of synthetic rhodopsin peptide competition against the formation of extra-MII.	guanosine 5'-O-(2-thiodiphosphate)	9-19	rhodopsin	Homo sapiens	70-79
2229054-9	1990	We discuss a generalized induced fit mechanism, where MII induces opening of the Gt nucleotide site and release of GDP which in turn is obligatory to establish the MII-stabilizing rhodopsin-Gt three-loop interaction (Konig, B., Arendt, A., McDowell, J.H., Kahlert, M., Hargrave, P.A., and Hofmann, K.P.	Guanosine Diphosphate	115-118	rhodopsin	Homo sapiens	180-189
2229054-15	1990	The GDP beta S/GDP difference is discussed in terms of bound GDP disturbing the interaction with two and GDP beta S with only one of the rhodopsin binding sites.	guanosine 5'-O-(2-thiodiphosphate)	4-14	rhodopsin	Homo sapiens	137-146
2229054-15	1990	The GDP beta S/GDP difference is discussed in terms of bound GDP disturbing the interaction with two and GDP beta S with only one of the rhodopsin binding sites.	Guanosine Diphosphate	4-7	rhodopsin	Homo sapiens	137-146
2229054-15	1990	The GDP beta S/GDP difference is discussed in terms of bound GDP disturbing the interaction with two and GDP beta S with only one of the rhodopsin binding sites.	Guanosine Diphosphate	15-18	rhodopsin	Homo sapiens	137-146
2394724-3	1990	Flashes of light exciting 1000 or fewer of the 3 x 10(9) rhodopsins present/ROS results in the incorporation of 1400 phosphates from ATP into the rhodopsin pool for each excited rhodopsin (Rho*).	Phosphates	117-127	rhodopsin	Homo sapiens	57-66
2394724-3	1990	Flashes of light exciting 1000 or fewer of the 3 x 10(9) rhodopsins present/ROS results in the incorporation of 1400 phosphates from ATP into the rhodopsin pool for each excited rhodopsin (Rho*).	Phosphates	117-127	rhodopsin	Homo sapiens	146-155
2394724-3	1990	Flashes of light exciting 1000 or fewer of the 3 x 10(9) rhodopsins present/ROS results in the incorporation of 1400 phosphates from ATP into the rhodopsin pool for each excited rhodopsin (Rho*).	Adenosine Triphosphate	133-136	rhodopsin	Homo sapiens	57-66
2394724-3	1990	Flashes of light exciting 1000 or fewer of the 3 x 10(9) rhodopsins present/ROS results in the incorporation of 1400 phosphates from ATP into the rhodopsin pool for each excited rhodopsin (Rho*).	Adenosine Triphosphate	133-136	rhodopsin	Homo sapiens	146-155
2081598-4	1990	Recent studies have indicated the presence of a point mutation at codon 23 in exon 1 of rhodopsin which results in the substitution of histidine for the highly conserved amino acid proline, suggesting that this mutation is a cause of rhodopsin-linked ADRP.	Histidine	135-144	rhodopsin	Homo sapiens	88-97
2081598-4	1990	Recent studies have indicated the presence of a point mutation at codon 23 in exon 1 of rhodopsin which results in the substitution of histidine for the highly conserved amino acid proline, suggesting that this mutation is a cause of rhodopsin-linked ADRP.	Histidine	135-144	rhodopsin	Homo sapiens	234-243
2081598-4	1990	Recent studies have indicated the presence of a point mutation at codon 23 in exon 1 of rhodopsin which results in the substitution of histidine for the highly conserved amino acid proline, suggesting that this mutation is a cause of rhodopsin-linked ADRP.	Proline	181-188	rhodopsin	Homo sapiens	88-97
2081598-4	1990	Recent studies have indicated the presence of a point mutation at codon 23 in exon 1 of rhodopsin which results in the substitution of histidine for the highly conserved amino acid proline, suggesting that this mutation is a cause of rhodopsin-linked ADRP.	Proline	181-188	rhodopsin	Homo sapiens	234-243
2265683-1	1990	Upon absorption of a photon, the 11-cis retinaldehyde chromophore of rhodopsin is isomerized and reduced to all-trans retinol (vitamin A) in the photoreceptor outer segments, whereupon it leaves the photoreceptors, and moves to the retinal pigment epithelium (RPE).	Vitamin A	118-125	rhodopsin	Homo sapiens	69-78
2265683-1	1990	Upon absorption of a photon, the 11-cis retinaldehyde chromophore of rhodopsin is isomerized and reduced to all-trans retinol (vitamin A) in the photoreceptor outer segments, whereupon it leaves the photoreceptors, and moves to the retinal pigment epithelium (RPE).	Vitamin A	127-136	rhodopsin	Homo sapiens	69-78
2150755-2	1990	Two hypotheses for its role in quenching the light activation of cyclic GMP cascade suggest that the protein binds to either phosphodiesterase or phosphorylated rhodopsin.	Cyclic GMP	65-75	rhodopsin	Homo sapiens	161-170
2168406-4	1990	Illumination results in more amplified activation of the GTP-binding protein transducin (Gt) than previously observed: bleaching as little as approximately 1 rhodopsin molecule (Rho*) in every 10 disks within a single ROS activates 37,000 molecules of Gt per Rho*, equivalent to 70% of the light-activatable Gt present on a single disk face.	Guanosine Triphosphate	57-60	rhodopsin	Homo sapiens	158-167
1697545-3	1990	Light-induced conformational changes in rhodopsin facilitate the binding of a guanosine nucleotide-binding protein, transducin, which then undergoes a GTP-GDP exchange reaction and dissociation of the transducin complex.	guanosine nucleotide	78-98	rhodopsin	Homo sapiens	40-49
1697545-3	1990	Light-induced conformational changes in rhodopsin facilitate the binding of a guanosine nucleotide-binding protein, transducin, which then undergoes a GTP-GDP exchange reaction and dissociation of the transducin complex.	Guanosine Triphosphate	151-154	rhodopsin	Homo sapiens	40-49
1697545-3	1990	Light-induced conformational changes in rhodopsin facilitate the binding of a guanosine nucleotide-binding protein, transducin, which then undergoes a GTP-GDP exchange reaction and dissociation of the transducin complex.	Guanosine Diphosphate	155-158	rhodopsin	Homo sapiens	40-49
1697545-9	1990	Phototransduction in invertebrate photoreceptors uses rhodopsin to activate a cascade that uses phosphoinositides and calcium ion to regulate membrane polarization.	Phosphatidylinositols	96-113	rhodopsin	Homo sapiens	54-63
1697545-9	1990	Phototransduction in invertebrate photoreceptors uses rhodopsin to activate a cascade that uses phosphoinositides and calcium ion to regulate membrane polarization.	Calcium	118-125	rhodopsin	Homo sapiens	54-63
2207250-8	1990	Comparison of the measured surface charge density with values from octopus rhodopsin model structures suggests that the measured value is for the extracellular surface and so the Schiff base in metarhodopsin is freely accessible to protons from the extracellular side of the membrane.	Schiff Bases	179-190	rhodopsin	Homo sapiens	75-84
2207250-9	1990	The intrinsic Schiff base pK of metarhodopsin is 8.44 +/- 0.12, whereas that of rhodopsin is found to be 10.65 +/- 0.10 in 4.0 M KCl.	Schiff Bases	14-25	rhodopsin	Homo sapiens	36-45
2207250-12	1990	The difference in the pK for the octopus rhodopsin compared with metarhodopsin is attributed to the relative freedom of the latter"s chromophore-binding site to rearrange itself after deprotonation of the Schiff base.	Schiff Bases	205-216	rhodopsin	Homo sapiens	41-50
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	44-47	rhodopsin	Homo sapiens	34-43
2223753-6	1990	Both the rate and the extent of the GTP-induced fluorescence enhancement are dependent on [rhodopsin], while only the rate (and not the extent) of the GTP gamma S-induced enhancement is dependent on the levels of rhodopsin.	Guanosine Triphosphate	36-39	rhodopsin	Homo sapiens	91-100
2223753-8	1990	At high [rhodopsin], the rates for GTP binding and GTPase are sufficiently different such that the GTP-induced enhancement essentially reflects GTP binding.	Guanosine Triphosphate	35-38	rhodopsin	Homo sapiens	9-18
2223753-8	1990	At high [rhodopsin], the rates for GTP binding and GTPase are sufficiently different such that the GTP-induced enhancement essentially reflects GTP binding.	Guanosine Triphosphate	51-54	rhodopsin	Homo sapiens	9-18
2223753-8	1990	At high [rhodopsin], the rates for GTP binding and GTPase are sufficiently different such that the GTP-induced enhancement essentially reflects GTP binding.	Guanosine Triphosphate	51-54	rhodopsin	Homo sapiens	9-18
2207073-5	1990	(4) ATP gamma S is a good substrate for rhodopsin kinase (thus rhodopsin phosphorothioate, a phosphatase-resistant product, can be formed in order to study the role of phosphorylation in rod outer segments).	Adenosine Triphosphate	4-7	rhodopsin	Homo sapiens	40-49
2207073-5	1990	(4) ATP gamma S is a good substrate for rhodopsin kinase (thus rhodopsin phosphorothioate, a phosphatase-resistant product, can be formed in order to study the role of phosphorylation in rod outer segments).	Sulfur	14-15	rhodopsin	Homo sapiens	40-49
2207073-5	1990	(4) ATP gamma S is a good substrate for rhodopsin kinase (thus rhodopsin phosphorothioate, a phosphatase-resistant product, can be formed in order to study the role of phosphorylation in rod outer segments).	Parathion	73-89	rhodopsin	Homo sapiens	40-49
2161251-1	1990	In the presence of G protein and phosphodiesterase, GTP induces aggregation of phospholipid-free rhodopsin-detergent micelles or rhodopsin reconstituted in phospholipid vesicles.	Phospholipids	79-91	rhodopsin	Homo sapiens	97-106
2161251-1	1990	In the presence of G protein and phosphodiesterase, GTP induces aggregation of phospholipid-free rhodopsin-detergent micelles or rhodopsin reconstituted in phospholipid vesicles.	Phospholipids	156-168	rhodopsin	Homo sapiens	97-106
2119661-0	1990	Surfaces of interaction between Gt and rhodopsin in the GDP-bound and empty-pocket configurations.	Guanosine Diphosphate	56-59	rhodopsin	Homo sapiens	39-48
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Serine	196-199	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glutamine	90-93	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glutamine	90-93	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glycine	82-85	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2372541-0	1990	Estimation of disk membrane lateral pressure and molecular area of rhodopsin by the measurement of its orientation at the nitrogen-water interface from an ellipsometric study.	Nitrogen	122-130	rhodopsin	Homo sapiens	67-76
2372541-0	1990	Estimation of disk membrane lateral pressure and molecular area of rhodopsin by the measurement of its orientation at the nitrogen-water interface from an ellipsometric study.	Water	131-136	rhodopsin	Homo sapiens	67-76
2372541-4	1990	The orientation of rhodopsin at the nitrogen-water interface was determined by using ellipsometry, which can measure the thickness of the film.	Nitrogen	36-44	rhodopsin	Homo sapiens	19-28
2372541-4	1990	The orientation of rhodopsin at the nitrogen-water interface was determined by using ellipsometry, which can measure the thickness of the film.	Water	45-50	rhodopsin	Homo sapiens	19-28
2159396-6	1990	Of the 7 retinas studied so far, rhodopsin has been regenerated to 0.1-0.35 nmol/mg protein, cGMP to 23.5-49.2 pmol/mg protein, and PIII to 20-50 microV: in some cases a b-wave was also seen.	Cyclic GMP	93-97	rhodopsin	Homo sapiens	33-42
2256961-2	1990	Synthetic peptides based on the amino acid sequence of portions of the molecule that interact with rhodopsin can themselves bind the rhodopsin and thus behave as competitive inhibitors of rhodopsin-G-protein interaction.	Peptides	10-18	rhodopsin	Homo sapiens	99-108
2256961-2	1990	Synthetic peptides based on the amino acid sequence of portions of the molecule that interact with rhodopsin can themselves bind the rhodopsin and thus behave as competitive inhibitors of rhodopsin-G-protein interaction.	Peptides	10-18	rhodopsin	Homo sapiens	133-142
2256961-2	1990	Synthetic peptides based on the amino acid sequence of portions of the molecule that interact with rhodopsin can themselves bind the rhodopsin and thus behave as competitive inhibitors of rhodopsin-G-protein interaction.	Peptides	10-18	rhodopsin	Homo sapiens	133-142
2169289-3	1990	When light bleaches rhodopsin there is an induced exchange of GTP for GDP bound to the alpha subunit of the retinal G-protein, transducin (T).	Guanosine Triphosphate	62-65	rhodopsin	Homo sapiens	20-29
2169289-3	1990	When light bleaches rhodopsin there is an induced exchange of GTP for GDP bound to the alpha subunit of the retinal G-protein, transducin (T).	Guanosine Diphosphate	70-73	rhodopsin	Homo sapiens	20-29
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Phenylalanine	406-409	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Proline	48-51	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glycine	82-85	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glutamine	90-93	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Serine	196-199	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glutamine	56-59	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glycine	60-63	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Glycine	82-85	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Serine	184-187	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Threonine	192-195	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Serine	196-199	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Serine	196-199	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Phenylalanine	216-219	rhodopsin	Homo sapiens	34-43
2139224-3	1990	The consensus peptide for each is rhodopsin Tyr Pro Pro Gln Gly synaptophysin Tyr Gly Pro Gln Gly synexin Tyr Pro Pro Pro Pro Gly gliadin Tyr Pro Pro Pro Gln Pro RNA polymerase II Tyr Ser Pro Thr Ser Pro Ser hordein Phe Pro Gln Gln Pro Gln Gln Pro gluten Tyr Pro Thr Ser Pro Gln Gln Gly Tyr Although there is obvious variation of sequence and of length, the penta- to nonapeptides share an initial Tyr (or Phe) and have high Pro contents and abundant Gly, Gln, and Ser.	Tyrosine	78-81	rhodopsin	Homo sapiens	34-43
33236904-1	2020	Using a quantum mechanical/molecular mechanical approach, the absorption wavelength of the retinal Schiff base was calculated based on 13 microbial rhodopsin crystal structures.	Schiff Bases	99-110	rhodopsin	Homo sapiens	148-157
34798368-2	2022	Among the several rhodopsin mutations related to retinitis pigmentosa (RP), those affecting the C-terminal VAPA-COOH motif that is implicated in rhodopsin trafficking from the Golgi to the rod outer segment are notably associated with more aggressive RP forms.	Carbonic Acid	112-116	rhodopsin	Homo sapiens	18-27
33777460-2	2020	p.Thr58Arg rhodopsin mutation leads to misfolding of rhodopsin, subsequent accumulation in the endoplasmic reticulum, and leads to consecutive atrophy of photoreceptor cells through apoptosis.	thr58arg	2-10	rhodopsin	Homo sapiens	11-20
33777460-2	2020	p.Thr58Arg rhodopsin mutation leads to misfolding of rhodopsin, subsequent accumulation in the endoplasmic reticulum, and leads to consecutive atrophy of photoreceptor cells through apoptosis.	thr58arg	2-10	rhodopsin	Homo sapiens	53-62
33777460-6	2020	Genotyping confirmed p.Thr58Arg rhodopsin mutation.	thr58arg	23-31	rhodopsin	Homo sapiens	32-41
32795534-0	2020	Disruption of Hydrogen-Bond Network in Rhodopsin Mutations Cause Night Blindness.	Hydrogen	14-22	rhodopsin	Homo sapiens	39-48
32795534-1	2020	Rhodopsin is the photosensitive protein, which binds to 11-cis-retinal as its chromophore.	Retinaldehyde	56-70	rhodopsin	Homo sapiens	0-9
32795534-8	2020	Our results further show an altered water-mediated H-bond network around the central transmembrane region of mutant rhodopsin, which is reminiscent of the active Meta-II state.	Water	36-41	rhodopsin	Homo sapiens	116-125
32795534-9	2020	This altered water-mediated H-bond network may cause thermal isomerization of the chromophore and facilitate rhodopsin dark activation.	Water	13-18	rhodopsin	Homo sapiens	109-118
34798368-2	2022	Among the several rhodopsin mutations related to retinitis pigmentosa (RP), those affecting the C-terminal VAPA-COOH motif that is implicated in rhodopsin trafficking from the Golgi to the rod outer segment are notably associated with more aggressive RP forms.	Carbonic Acid	112-116	rhodopsin	Homo sapiens	145-154
34798368-4	2022	In this work, clinically relevant rhodopsin mutations at the P347 site within the VAPA-COOH motif were investigated by molecular dynamics (MD) simulations and compared to the wild-type (WT) system.	Carbonic Acid	87-91	rhodopsin	Homo sapiens	34-43
34946802-0	2021	Beyond Sector Retinitis Pigmentosa: Expanding the Phenotype and Natural History of the Rhodopsin Gene Codon 106 Mutation (Gly-to-Arg) in Autosomal Dominant Retinitis Pigmentosa.	Glycine	122-125	rhodopsin	Homo sapiens	87-96
34853839-1	2021	The protonated Schiff-base retinal acts as the chromophore in bacteriorhodopsin as well as in rhodopsin.	Schiff Bases	15-26	rhodopsin	Homo sapiens	94-103
34946802-0	2021	Beyond Sector Retinitis Pigmentosa: Expanding the Phenotype and Natural History of the Rhodopsin Gene Codon 106 Mutation (Gly-to-Arg) in Autosomal Dominant Retinitis Pigmentosa.	Arginine	129-132	rhodopsin	Homo sapiens	87-96
34213033-0	2021	Cation ordering and exsolution in copper-containing forms of the flexible zeolite Rho (Cu,M-Rho; M = H, Na) and their consequences for CO2 adsorption.	Copper	34-40	rhodopsin	Homo sapiens	87-95
34509506-0	2021	Styrene-Maleic Acid Copolymer Effects on the Function of the GPCR Rhodopsin in Lipid Nanoparticles.	Styrene	0-7	rhodopsin	Homo sapiens	66-75
34509506-0	2021	Styrene-Maleic Acid Copolymer Effects on the Function of the GPCR Rhodopsin in Lipid Nanoparticles.	maleic acid copolymer	8-29	rhodopsin	Homo sapiens	66-75
34598550-1	2021	Nonadiabatic trajectory surface hopping simulations are reported for trans-C5H6NH2 +, a model of the rhodopsin chromophore, using the augmented fewest-switches algorithm.	trans-c5h6nh2 +	69-84	rhodopsin	Homo sapiens	101-110
34351751-5	2021	Here, we study the triplet energy transfer process between porphyrin, a prototypical energy transfer donor, and different biologically relevant acceptors, including molecular oxygen, carotenoids, and rhodopsin.	Porphyrins	59-68	rhodopsin	Homo sapiens	200-209
34379429-4	2021	The method is benchmarked by computing the ground-state room-temperature relative stabilities between (i) the cis and trans isomers of prototypal animal and microbial rhodopsins and (ii) the analogue isomers of a rhodopsin-like light-driven molecular switch in methanol.	Methanol	261-269	rhodopsin	Homo sapiens	213-222
34670076-5	2021	Molecular dynamics simulations of a visual rhodopsin indicate that the conserved hydrogen-bond network from static structure can recruit dynamic hydrogen bonds and extend throughout most of the receptor.	Hydrogen	81-89	rhodopsin	Homo sapiens	43-52
34670076-5	2021	Molecular dynamics simulations of a visual rhodopsin indicate that the conserved hydrogen-bond network from static structure can recruit dynamic hydrogen bonds and extend throughout most of the receptor.	Hydrogen	145-153	rhodopsin	Homo sapiens	43-52
34710119-5	2021	The analysis showed that a subset of the parameters influencing the circulating dark current, such as the turnover rate of cGMP in the dark, may be most influential for variance with experimental flash response, while the shut-off rates of photoexcited rhodopsin and phosphodiesterase also exerted sizable effect.	Cyclic GMP	123-127	rhodopsin	Homo sapiens	253-284
34710119-6	2021	The activation rate of transducin by rhodopsin and the light-induced hydrolysis rate of cGMP exerted measurable effects as well but were estimated as relatively less significant.	Cyclic GMP	88-92	rhodopsin	Homo sapiens	37-46
34601881-2	2021	Metagenomics studies have recently identified a new category of rhodopsin intermediates between type-1 rhodopsins and heliorhodopsins, named schizorhodopsins (SzRs).	heliorhodopsins	118-133	rhodopsin	Homo sapiens	64-73
34601881-2	2021	Metagenomics studies have recently identified a new category of rhodopsin intermediates between type-1 rhodopsins and heliorhodopsins, named schizorhodopsins (SzRs).	schizorhodopsins	141-157	rhodopsin	Homo sapiens	64-73
34601881-2	2021	Metagenomics studies have recently identified a new category of rhodopsin intermediates between type-1 rhodopsins and heliorhodopsins, named schizorhodopsins (SzRs).	szrs	159-163	rhodopsin	Homo sapiens	64-73
34680158-1	2021	Most opioid analgesics used clinically, including morphine and fentanyl, as well as the recreational drug heroin, act primarily through the mu opioid receptor, a class A Rhodopsin-like G protein-coupled receptor (GPCR).	Morphine	50-58	rhodopsin	Homo sapiens	170-179
34680158-1	2021	Most opioid analgesics used clinically, including morphine and fentanyl, as well as the recreational drug heroin, act primarily through the mu opioid receptor, a class A Rhodopsin-like G protein-coupled receptor (GPCR).	Fentanyl	63-71	rhodopsin	Homo sapiens	170-179
34680158-1	2021	Most opioid analgesics used clinically, including morphine and fentanyl, as well as the recreational drug heroin, act primarily through the mu opioid receptor, a class A Rhodopsin-like G protein-coupled receptor (GPCR).	Heroin	106-112	rhodopsin	Homo sapiens	170-179
34213033-0	2021	Cation ordering and exsolution in copper-containing forms of the flexible zeolite Rho (Cu,M-Rho; M = H, Na) and their consequences for CO2 adsorption.	Carbon Dioxide	135-138	rhodopsin	Homo sapiens	87-95
34436392-7	2021	On the other hand, a significant enhancement of 45% in ideal CO2/CH4 selectivity was attained by MMMs incorporated with 2 wt% of zeolite NH2-RHO compared to a pristine PSf membrane.	Carbon Dioxide	61-64	rhodopsin	Homo sapiens	137-144
34436392-3	2021	This current work investigated the incorporation of zeolite RHO and silane-modified zeolite RHO (NH2-RHO) into polysulfone (PSf) based MMMs with the primary aim of enhancing the membrane"s gas permeation and separation performance.	polysulfone P 1700	111-122	rhodopsin	Homo sapiens	97-104
34477756-0	2021	Differences in SMA-like polymer architecture dictate the conformational changes exhibited by the membrane protein rhodopsin encapsulated in lipid nano-particles.	Polymers	24-31	rhodopsin	Homo sapiens	114-123
34477756-4	2021	The photoactivation pathway of rhodopsin (Rho), a G-protein-coupled receptor (GPCR), comprises structurally-defined intermediates with characteristic absorbance spectra that revealed conformational restrictions with styrene-containing SMA and SMI, so that photoactivation proceeded only as far as metarhodopsin-I, absorbing at 478 nm, in a SMALP or SMILP.	Styrene	216-223	rhodopsin	Homo sapiens	31-40
34436392-7	2021	On the other hand, a significant enhancement of 45% in ideal CO2/CH4 selectivity was attained by MMMs incorporated with 2 wt% of zeolite NH2-RHO compared to a pristine PSf membrane.	Methane	65-68	rhodopsin	Homo sapiens	137-144
34436392-7	2021	On the other hand, a significant enhancement of 45% in ideal CO2/CH4 selectivity was attained by MMMs incorporated with 2 wt% of zeolite NH2-RHO compared to a pristine PSf membrane.	Zeolites	129-136	rhodopsin	Homo sapiens	137-144
34436392-8	2021	Besides, all MMMs incorporated with zeolite NH2-RHO displayed higher ideal CO2/CH4 selectivity than that of the MMMs incorporated with zeolite RHO.	mmms	13-17	rhodopsin	Homo sapiens	44-51
34436392-8	2021	Besides, all MMMs incorporated with zeolite NH2-RHO displayed higher ideal CO2/CH4 selectivity than that of the MMMs incorporated with zeolite RHO.	Zeolites	36-43	rhodopsin	Homo sapiens	44-51
34436392-8	2021	Besides, all MMMs incorporated with zeolite NH2-RHO displayed higher ideal CO2/CH4 selectivity than that of the MMMs incorporated with zeolite RHO.	Carbon Dioxide	75-78	rhodopsin	Homo sapiens	44-51
34436392-8	2021	Besides, all MMMs incorporated with zeolite NH2-RHO displayed higher ideal CO2/CH4 selectivity than that of the MMMs incorporated with zeolite RHO.	Methane	79-82	rhodopsin	Homo sapiens	44-51
35355518-2	2022	The ligand-binding pocket of inactive rhodopsin is completely enclosed, whereas active rhodopsin displays pores accessible from the lipid bilayer.	Lipid Bilayers	132-145	rhodopsin	Homo sapiens	87-96
34199888-8	2021	Recent evidence suggests that certain flavonoids could help stabilize the correctly folded conformation of the visual photoreceptor protein rhodopsin and offset the deleterious effect of retinitis pigmentosa mutations.	Flavonoids	38-48	rhodopsin	Homo sapiens	140-149
34199888-9	2021	In this regard, certain polyphenols, like the flavonoids mentioned before, have been shown to improve the stability, expression, regeneration and folding of rhodopsin mutants in experimental in vitro studies.	Polyphenols	24-35	rhodopsin	Homo sapiens	157-166
34199888-9	2021	In this regard, certain polyphenols, like the flavonoids mentioned before, have been shown to improve the stability, expression, regeneration and folding of rhodopsin mutants in experimental in vitro studies.	Flavonoids	46-56	rhodopsin	Homo sapiens	157-166
34199888-11	2021	We anticipate that polyphenol compounds can be used to target visual photoreceptor proteins, such as rhodopsin, in a way that has only been recently proposed and that these can be used in novel approaches for the treatment of retinal degenerative diseases like retinitis pigmentosa; however, studies in this field are limited and further research is needed in order to properly characterize the effects of these compounds on retinal degenerative diseases through the proposed mechanisms.	Polyphenols	19-29	rhodopsin	Homo sapiens	101-110
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Octoxynol	242-254	rhodopsin	Homo sapiens	7-16
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Octoxynol	242-254	rhodopsin	Homo sapiens	92-101
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Octoxynol	242-254	rhodopsin	Homo sapiens	145-154
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Sodium Dodecyl Sulfate	259-262	rhodopsin	Homo sapiens	7-16
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Sodium Dodecyl Sulfate	259-262	rhodopsin	Homo sapiens	92-101
34151231-3	2021	Tara76 rhodopsin has a thermal stability approximately 20 times higher than that of thermal rhodopsin at 80 C and is even stable at 85 C. Tara76 rhodopsin is also stable at pH 0.02 to 13 and exhibits strong resistance in detergent, including Triton X-100 and SDS.	Sodium Dodecyl Sulfate	259-262	rhodopsin	Homo sapiens	145-154
35597714-2	2022	recently reported the molecular mechanism of chloride transport through a light-activated pumping rhodopsin, a key process involved in a range of cellular functions.	Chlorides	45-53	rhodopsin	Homo sapiens	98-107
35524714-6	2022	Subsequent diversification of rhodopsin functions and peak absorption frequencies was enabled by the expansion of surface ecological niches induced by the accumulation of atmospheric oxygen.	Oxygen	183-189	rhodopsin	Homo sapiens	30-39
35302684-3	2022	Rhodopsin (RH1) is the only opsin responsible for dim-light vision in vertebrates and has been shown to evolve in response to the respective light conditions, including along a water depth gradient in fishes.	Water	177-182	rhodopsin	Homo sapiens	0-9
35388214-6	2022	Considering the lipids ejected with rhodopsin, we demonstrate that opsin can be regenerated in membranes through photoisomerized retinal-lipid conjugates, and we provide evidence for increased association of rhodopsin with unsaturated long-chain phosphatidylcholine during signalling.	unsaturated long-chain phosphatidylcholine	223-265	rhodopsin	Homo sapiens	208-217
35262367-0	2022	Calcium Binding to TAT Rhodopsin.	Calcium	0-7	rhodopsin	Homo sapiens	23-32
35262367-5	2022	Here, we report Ca2+ binding to a wild-type microbial rhodopsin, which is achieved for the neutral retinal chromophore with a deprotonated Schiff base.	Schiff Bases	139-150	rhodopsin	Homo sapiens	54-63
35262367-6	2022	TAT rhodopsin from marine bacteria contains protonated and deprotonated retinal Schiff bases at physiological pH (pH ~ 8), which absorb visible and UV light, respectively.	Schiff Bases	80-92	rhodopsin	Homo sapiens	4-13
34240976-0	2021	Structural and dynamical heterogeneity of water trapped inside Na+-pumping KR2 rhodopsin in the dark state.	Water	42-47	rhodopsin	Homo sapiens	79-88
34240976-4	2021	In this paper, we systematically investigate the localization, structure, dynamics, and energetics of the water molecules along the channel for the resting/dark state of KR2 rhodopsin.	Water	106-111	rhodopsin	Homo sapiens	174-183
35584119-2	2022	Our osmotic stress studies of the visual receptor rhodopsin have redefined the standard model of GPCR signaling by revealing the essential role of bulk water.	Water	152-157	rhodopsin	Homo sapiens	50-59
35584119-3	2022	We show results consistent with a large number of water molecules flooding the rhodopsin interior during activation to stabilize the effector binding conformation.	Water	50-55	rhodopsin	Homo sapiens	79-88
35563803-2	2022	Here, we demonstrated the effect of 4-phenylbutyric acid (PBA), a chemical chaperon that can suppress endoplasmic reticulum (ER) stress, in P23H mutant rhodopsin knock-in RP models.	4-phenylbutyric acid	36-56	rhodopsin	Homo sapiens	152-161
35563803-2	2022	Here, we demonstrated the effect of 4-phenylbutyric acid (PBA), a chemical chaperon that can suppress endoplasmic reticulum (ER) stress, in P23H mutant rhodopsin knock-in RP models.	4-phenylbutyric acid	58-61	rhodopsin	Homo sapiens	152-161
35355518-3	2022	Stabilization of active rhodopsin impedes 11CR binding and photoreceptor dark adaptation.	11cr	42-46	rhodopsin	Homo sapiens	24-33
35364923-8	2022	The optimized function was cL(rho)=0.35(rho-rhow)+ cL,w m/s, where w denotes water, giving the tested laminae a mean bulk density of 1600 +- 30 kg/m3 and a mean bulk cL of 1670 +- 60 m/s.	Water	77-82	rhodopsin	Homo sapiens	27-34
35195241-4	2022	Here, we present a case report of a patient with RP caused by a p.D190N mutation in Rhodopsin (RHO) associated with abnormally high quantitative autofluorescence values after long-term vitamin A supplementation.	Vitamin A	185-194	rhodopsin	Homo sapiens	84-93
34984789-1	2022	The recently discovered rhodopsin family of heliorhodopsins (HeRs) is abundant in diverse microbial environments.	heliorhodopsins	44-59	rhodopsin	Homo sapiens	24-33