PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8400551-5	1993	Unlike bovine rhodopsin, however, a sizable fraction of the total glycans of frog rhodopsin also contained sialic acid (NeuAc), with the sialylated oligosaccharides being present exclusively at the Asn2 site.	N-Acetylneuraminic Acid	107-118	rhodopsin	Bos taurus	82-91
8400551-5	1993	Unlike bovine rhodopsin, however, a sizable fraction of the total glycans of frog rhodopsin also contained sialic acid (NeuAc), with the sialylated oligosaccharides being present exclusively at the Asn2 site.	N-Acetylneuraminic Acid	120-125	rhodopsin	Bos taurus	82-91
8400551-1	1993	The N-linked oligosaccharides of frog (Rana pipiens) rhodopsin were analysed by sequential exoglycosidase digestion and gel filtration chromatography, following reductive tritiation.	n-linked oligosaccharides	4-29	rhodopsin	Bos taurus	53-62
8384876-1	1993	Treatment of outer segment membranes from Loligo forbesi with endoprotease-V8 from Staphylococcus aureus results in cleavage of the C-terminal extension of the squid rhodopsin, with accompanying reduction of the apparent molecular weight from 47,000 to 36,000 on sodium dodecyl sulfate/polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	263-285	rhodopsin	Bos taurus	166-175
8400551-4	1993	The predominant glycan (approximately 60% of total) had the structure GlcNAc beta 1-2Man alpha 1-3(Man alpha 1-6) Man beta 1-4GlcNAc beta 1-4GlcNAc-(Asn), with the remaining structures containing 1-3 additional hexose residues, as reported previously for bovine rhodopsin.	Polysaccharides	16-22	rhodopsin	Bos taurus	262-271
8400551-5	1993	Unlike bovine rhodopsin, however, a sizable fraction of the total glycans of frog rhodopsin also contained sialic acid (NeuAc), with the sialylated oligosaccharides being present exclusively at the Asn2 site.	Polysaccharides	66-73	rhodopsin	Bos taurus	82-91
8507634-6	1993	These results identify serines 338 and 343 as the major sites of phosphorylation within the C-terminal region of bleached bovine rhodopsin and constitute the first example of mass spectrometric characterization of phosphorylation sites in a G-protein coupled receptor.	Serine	23-30	rhodopsin	Bos taurus	129-138
8490033-1	1993	Bovine rhodopsin has been phosphorylated in rod outer segments by ATP and endogenous rhodopsin kinase.	Adenosine Triphosphate	66-69	rhodopsin	Bos taurus	7-16
8490033-3	1993	Nearly all of the phosphate is found in peptide 330-348, formed by digestion of phosphorhodopsins with endoproteinase Asp-N. Sequence analysis of the phosphopeptides shows that monophosphorylated rhodopsin consists of a mixture containing rhodopsins phosphorylated at 338Ser and 343Ser.	Phosphates	18-27	rhodopsin	Bos taurus	87-96
8490033-4	1993	Diphosphorylated rhodopsin is phosphorylated at both 338Ser and 343Ser.	338ser	53-59	rhodopsin	Bos taurus	17-26
8490033-5	1993	When rhodopsin becomes triphosphorylated it does not become phosphorylated on 334Ser but appears to become phosphorylated on one or more of the four threonine residues: 335Thr, 336Thr, 340Thr, and 342Thr.	334ser	78-84	rhodopsin	Bos taurus	5-14
8490033-5	1993	When rhodopsin becomes triphosphorylated it does not become phosphorylated on 334Ser but appears to become phosphorylated on one or more of the four threonine residues: 335Thr, 336Thr, 340Thr, and 342Thr.	Threonine	149-158	rhodopsin	Bos taurus	5-14
8391868-0	1993	pKa of the protonated Schiff base of bovine rhodopsin.	Schiff Bases	22-33	rhodopsin	Bos taurus	44-53
8391868-2	1993	Artificial bovine rhodopsin pigments derived from synthetic retinal analogues carrying electron-withdrawing substituents (fluorine and chlorine) were prepared.	Fluorine	122-130	rhodopsin	Bos taurus	18-27
8391868-2	1993	Artificial bovine rhodopsin pigments derived from synthetic retinal analogues carrying electron-withdrawing substituents (fluorine and chlorine) were prepared.	Chlorine	135-143	rhodopsin	Bos taurus	18-27
8391868-5	1993	However, the alternative possibility that the retinal Schiff base linkage in bovine rhodopsin is not accessible for titration from the aqueous bulk medium cannot be definitely ruled out.	Schiff Bases	54-65	rhodopsin	Bos taurus	84-93
8483923-1	1993	The primary photochemical event in rhodopsin is an 11-cis to 11-trans photoisomerization of its retinylidene chromophore to form the primary intermediate photorhodopsin.	retinylidene	96-108	rhodopsin	Bos taurus	35-44
8483923-3	1993	Results from a rhodopsin analog formed from a retinal with locked 11-ene structure through the more flexible eight-membered ring (Ret8) are described.	11-ene	66-72	rhodopsin	Bos taurus	15-24
8471607-2	1993	The phosphorylation of rhodopsin"s C-terminus was evaluated using synthetic peptides derived from the last 12 amino acids (337-348) as substrates and their phosphorylated counterparts as inhibitors.	Peptides	76-84	rhodopsin	Bos taurus	23-32
8471607-3	1993	It was found that synthetic peptides were phosphorylated at the serine residue corresponding to Ser-343 in the primary sequence of bovine rhodopsin.	Peptides	28-36	rhodopsin	Bos taurus	138-147
8471607-3	1993	It was found that synthetic peptides were phosphorylated at the serine residue corresponding to Ser-343 in the primary sequence of bovine rhodopsin.	Serine	64-70	rhodopsin	Bos taurus	138-147
8471607-3	1993	It was found that synthetic peptides were phosphorylated at the serine residue corresponding to Ser-343 in the primary sequence of bovine rhodopsin.	Serine	96-99	rhodopsin	Bos taurus	138-147
8471607-6	1993	The phosphopeptides were found to have a greater affinity for the kinase compared with their nonphosphorylated counterparts; for the peptides corresponding to residues 337-348 of rhodopsin the affinity increased in the order VSKTETSQVAPA < VSKTETS[PO3H2]QVAPA < VS[PO3H2]KTETS[PO3H2]QVAPA.	po3h2	251-256	rhodopsin	Bos taurus	179-188
8471607-6	1993	The phosphopeptides were found to have a greater affinity for the kinase compared with their nonphosphorylated counterparts; for the peptides corresponding to residues 337-348 of rhodopsin the affinity increased in the order VSKTETSQVAPA < VSKTETS[PO3H2]QVAPA < VS[PO3H2]KTETS[PO3H2]QVAPA.	qvapa	232-237	rhodopsin	Bos taurus	179-188
8471607-6	1993	The phosphopeptides were found to have a greater affinity for the kinase compared with their nonphosphorylated counterparts; for the peptides corresponding to residues 337-348 of rhodopsin the affinity increased in the order VSKTETSQVAPA < VSKTETS[PO3H2]QVAPA < VS[PO3H2]KTETS[PO3H2]QVAPA.	po3h2	271-276	rhodopsin	Bos taurus	179-188
8471607-6	1993	The phosphopeptides were found to have a greater affinity for the kinase compared with their nonphosphorylated counterparts; for the peptides corresponding to residues 337-348 of rhodopsin the affinity increased in the order VSKTETSQVAPA < VSKTETS[PO3H2]QVAPA < VS[PO3H2]KTETS[PO3H2]QVAPA.	po3h2	271-276	rhodopsin	Bos taurus	179-188
8471607-6	1993	The phosphopeptides were found to have a greater affinity for the kinase compared with their nonphosphorylated counterparts; for the peptides corresponding to residues 337-348 of rhodopsin the affinity increased in the order VSKTETSQVAPA < VSKTETS[PO3H2]QVAPA < VS[PO3H2]KTETS[PO3H2]QVAPA.	qvapa	257-262	rhodopsin	Bos taurus	179-188
8504860-3	1993	The Km-values of the enzyme were 3.8 microM for rhodopsin and 22 microM for ATP; the Vmax-value was 9.9 mol phosphate/mol beta ARK/min.	Adenosine Triphosphate	76-79	rhodopsin	Bos taurus	48-57
8504860-3	1993	The Km-values of the enzyme were 3.8 microM for rhodopsin and 22 microM for ATP; the Vmax-value was 9.9 mol phosphate/mol beta ARK/min.	Phosphates	108-117	rhodopsin	Bos taurus	48-57
8385131-7	1993	264, 7564-7569) whereas chemical removal of palmitate from bovine rhodopsin enhances coupling to Gt (Morrison, D. F., O"Brien, P. J., and Pepperberg, D. R. (1991) J. Biol.	Palmitates	44-53	rhodopsin	Bos taurus	66-75
8384876-1	1993	Treatment of outer segment membranes from Loligo forbesi with endoprotease-V8 from Staphylococcus aureus results in cleavage of the C-terminal extension of the squid rhodopsin, with accompanying reduction of the apparent molecular weight from 47,000 to 36,000 on sodium dodecyl sulfate/polyacrylamide gel electrophoresis.	polyacrylamide	286-300	rhodopsin	Bos taurus	166-175
8384876-3	1993	Fourier transform infrared spectra of the amide I band of the protein indicate that removal of the C-terminal extension increases the relative alpha-helical content of squid rhodopsin to a level comparable to that for bovine rhodopsin in disk membranes, and to an extent which suggests that the alpha-helical structure lies mainly in the M(r) 36,000 (transmembrane) section of the protein.	Amides	42-47	rhodopsin	Bos taurus	174-183
8384876-4	1993	Saturation-transfer electron spin resonance (ESR) spectroscopy of the spin-labeled protein reveals that the rotational diffusion of squid rhodopsin in outer segment membranes that have been extensively washed with urea to remove peripheral proteins is much slower than that of bovine rhodopsin in rod outer segment disk membranes.	Urea	214-218	rhodopsin	Bos taurus	138-147
8384876-5	1993	This reduction in rotational mobility is also found with purified squid rhodopsin reconstituted in egg phosphatidylcholine and in urea-washed outer segment membranes which have been treated with endoprotease-V8 to remove the C-terminal extension of squid rhodopsin.	Phosphatidylcholines	103-122	rhodopsin	Bos taurus	72-81
8384876-5	1993	This reduction in rotational mobility is also found with purified squid rhodopsin reconstituted in egg phosphatidylcholine and in urea-washed outer segment membranes which have been treated with endoprotease-V8 to remove the C-terminal extension of squid rhodopsin.	Urea	130-134	rhodopsin	Bos taurus	255-264
8422414-4	1993	Mass spectrometric, PicoTag, and hexose analyses of the tryptic 1-16 N-terminal peptides further indicated that the post-translational glycosylation of plasma membrane rhodopsin is identical to that of disk membrane rhodopsin.	Peptides	80-88	rhodopsin	Bos taurus	168-177
8443184-7	1993	The recombinants of rhodopsin with egg PC, either alone or in combination with egg PC-derived phosphatidylethanolamine (PE) or phosphatidylserine (PS), exhibited substantially reduced photochemical activity at pH 7.0.	phosphatidylethanolamine	94-118	rhodopsin	Bos taurus	20-29
8443184-7	1993	The recombinants of rhodopsin with egg PC, either alone or in combination with egg PC-derived phosphatidylethanolamine (PE) or phosphatidylserine (PS), exhibited substantially reduced photochemical activity at pH 7.0.	phosphatidylethanolamine	120-122	rhodopsin	Bos taurus	20-29
8443184-7	1993	The recombinants of rhodopsin with egg PC, either alone or in combination with egg PC-derived phosphatidylethanolamine (PE) or phosphatidylserine (PS), exhibited substantially reduced photochemical activity at pH 7.0.	Phosphatidylserines	127-145	rhodopsin	Bos taurus	20-29
8443184-7	1993	The recombinants of rhodopsin with egg PC, either alone or in combination with egg PC-derived phosphatidylethanolamine (PE) or phosphatidylserine (PS), exhibited substantially reduced photochemical activity at pH 7.0.	Phosphatidylserines	147-149	rhodopsin	Bos taurus	20-29
8444840-0	1993	Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition.	retinylidene	16-28	rhodopsin	Bos taurus	55-64
8444840-0	1993	Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition.	Schiff Bases	29-40	rhodopsin	Bos taurus	55-64
8444840-1	1993	The environment of the retinylidene Schiff base in bovine rhodopsin has been studied by movement of its carboxylic acid counterion from position 113 to position 117 by site-specific mutagenesis.	retinylidene schiff base	23-47	rhodopsin	Bos taurus	58-67
8444840-1	1993	The environment of the retinylidene Schiff base in bovine rhodopsin has been studied by movement of its carboxylic acid counterion from position 113 to position 117 by site-specific mutagenesis.	Carboxylic Acids	104-119	rhodopsin	Bos taurus	58-67
8444840-10	1993	We conclude that the Schiff base counterion in rhodopsin can be repositioned to form a pigment with an apparently unperturbed Schiff base pKa.	Schiff Bases	21-32	rhodopsin	Bos taurus	47-56
8444840-10	1993	We conclude that the Schiff base counterion in rhodopsin can be repositioned to form a pigment with an apparently unperturbed Schiff base pKa.	Schiff Bases	126-137	rhodopsin	Bos taurus	47-56
8299414-1	1993	In retinal rods photoexcited rhodopsin (R*) catalyses the activation of transducin (T) by GTP, which in turn activates the cGMP phosphodiesterase (PDE).	Guanosine Triphosphate	90-93	rhodopsin	Bos taurus	29-38
1472495-3	1992	In this report, pH-rate profiles for the rhodopsin-catalyzed exchange of GTPgS for GDP on transducin are established for the constitutively active opsin mutants.	Guanosine Diphosphate	83-86	rhodopsin	Bos taurus	41-50
8392355-1	1993	The visual pigment rhodopsin was used as an intrinsic probe to measure the effect of incorporation of enflurane into bovine rod outer segment disk membranes.	Enflurane	102-111	rhodopsin	Bos taurus	19-28
8392355-2	1993	At moderately low enflurane concentration, we find that, while extrinsic probes show little membrane perturbation, rhodopsin may experience large changes with respect to the native lipid-protein interactions which modulate some of its properties.	Enflurane	18-27	rhodopsin	Bos taurus	115-124
8392355-4	1993	As a function of enflurane concentration, there appears to be an increasing population of rhodopsin molecules for which the metarhodopsin I-->II transition is blocked, while it is accelerated in the remaining population.	Enflurane	17-26	rhodopsin	Bos taurus	90-99
8392355-6	1993	These results are all consistent with a reduction of the membrane order accompanied by lateral aggregation of rhodopsin in the presence of enflurane.	Enflurane	139-148	rhodopsin	Bos taurus	110-119
8392355-7	1993	By comparison with the perturbation probed by a spin label, the large molecular environment change experienced by the rhodopsin molecule suggests that enflurane may concentrate at the lipid-protein interface.	Enflurane	151-160	rhodopsin	Bos taurus	118-127
8419942-1	1993	Previously, bovine rhodopsin has been shown to be palmitoylated at cysteine residues 322 and 323.	Cysteine	67-75	rhodopsin	Bos taurus	19-28
1337211-1	1992	Magic angle spinning (MAS)13C-NMR spectra of the metarhodopsin II intermediate have been obtained using bovine rhodopsin regenerated with retinal 13C-labeled at the C-13 and C-15 positions to investigate the protonation state of the retinal Schiff base linkage.	13c	26-29	rhodopsin	Bos taurus	53-62
1334080-2	1992	Photoexcitation of retinal rod photoreceptor cells involves the activation of cGMP enzyme cascade in which sequential activation of rhodopsin, transducin, and the cGMP phosphodiesterase in the rod outer segment constitutes the signal amplification mechanism.	Cyclic GMP	78-82	rhodopsin	Bos taurus	132-141
1337211-1	1992	Magic angle spinning (MAS)13C-NMR spectra of the metarhodopsin II intermediate have been obtained using bovine rhodopsin regenerated with retinal 13C-labeled at the C-13 and C-15 positions to investigate the protonation state of the retinal Schiff base linkage.	13c	146-149	rhodopsin	Bos taurus	53-62
1492127-0	1992	Spin labeled cysteines as sensors for protein-lipid interaction and conformation in rhodopsin.	Cysteine	13-22	rhodopsin	Bos taurus	84-93
1337211-2	1992	The 13C-labeled rhodopsin was reconstituted into 1,2-dipalmitoleoylphosphatidylcholine bilayers to increase the amount of meta II trapped at low temperature.	13c	4-7	rhodopsin	Bos taurus	16-25
1337211-2	1992	The 13C-labeled rhodopsin was reconstituted into 1,2-dipalmitoleoylphosphatidylcholine bilayers to increase the amount of meta II trapped at low temperature.	1,2-dipalmitoleoylphosphatidylcholine	49-86	rhodopsin	Bos taurus	16-25
1492127-1	1992	In stoichiometric amounts, the spin label N-tempoyl-(p-chloromercuribenzamide) reacts rapidly with one cysteine residue in membrane-bound bovine rhodopsin.	n-tempoyl-	42-52	rhodopsin	Bos taurus	145-154
1492127-1	1992	In stoichiometric amounts, the spin label N-tempoyl-(p-chloromercuribenzamide) reacts rapidly with one cysteine residue in membrane-bound bovine rhodopsin.	p-chloromercuribenzamide	53-77	rhodopsin	Bos taurus	145-154
1492127-1	1992	In stoichiometric amounts, the spin label N-tempoyl-(p-chloromercuribenzamide) reacts rapidly with one cysteine residue in membrane-bound bovine rhodopsin.	Cysteine	103-111	rhodopsin	Bos taurus	145-154
1337214-0	1992	Photolysis of rhodopsin results in deprotonation of its retinal Schiff"s base prior to formation of metarhodopsin II.	schiff"s base	64-77	rhodopsin	Bos taurus	14-23
1512231-2	1992	Bovine rhodopsin has been reported to be S-palmitylated at cysteines 322 and 323 (Ovchinnikov, Y.	Cysteine	59-68	rhodopsin	Bos taurus	7-16
1329948-0	1992	Changing the location of the Schiff base counterion in rhodopsin.	Schiff Bases	29-40	rhodopsin	Bos taurus	55-64
1329948-1	1992	Rhodopsin and all of the vertebrate visual pigments have a carboxylic acid residue, Glu113, in the third transmembrane segment that serves as a counterion to the protonated Schiff base nitrogen of the chromophore.	Carboxylic Acids	59-74	rhodopsin	Bos taurus	0-9
1329948-1	1992	Rhodopsin and all of the vertebrate visual pigments have a carboxylic acid residue, Glu113, in the third transmembrane segment that serves as a counterion to the protonated Schiff base nitrogen of the chromophore.	Schiff Bases	173-184	rhodopsin	Bos taurus	0-9
1329948-1	1992	Rhodopsin and all of the vertebrate visual pigments have a carboxylic acid residue, Glu113, in the third transmembrane segment that serves as a counterion to the protonated Schiff base nitrogen of the chromophore.	Nitrogen	185-193	rhodopsin	Bos taurus	0-9
1329948-9	1992	These results suggest that the Schiff base nitrogen in rhodopsin is located between residues 113 and 117 but there is enough flexibility in the protein to allow partial interaction with an Asp at position 120.	Schiff Bases	31-42	rhodopsin	Bos taurus	55-64
1329948-9	1992	These results suggest that the Schiff base nitrogen in rhodopsin is located between residues 113 and 117 but there is enough flexibility in the protein to allow partial interaction with an Asp at position 120.	Nitrogen	43-51	rhodopsin	Bos taurus	55-64
1329948-9	1992	These results suggest that the Schiff base nitrogen in rhodopsin is located between residues 113 and 117 but there is enough flexibility in the protein to allow partial interaction with an Asp at position 120.	Aspartic Acid	189-192	rhodopsin	Bos taurus	55-64
1483505-1	1992	At best, only trace amounts of galactose have been detected as constituents of rhodopsin as analysed by several laboratories.	Galactose	31-40	rhodopsin	Bos taurus	79-88
1483505-13	1992	After bleaching by visible light, opsin was preferred over rhodopsin as an acceptor of galactose by the galactosyltransferases of bovine and embryonic chick retinas and by rat liver.	Galactose	87-96	rhodopsin	Bos taurus	59-68
1483505-17	1992	The linkage of galactose in enzymatically galactosylated rhodopsin and opsin was beta(1-4).	Galactose	15-24	rhodopsin	Bos taurus	57-66
1324716-0	1992	Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance.	saturated	101-110	rhodopsin	Bos taurus	86-95
1324716-0	1992	Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance.	diacylphosphatidylcholines	111-137	rhodopsin	Bos taurus	86-95
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	Cyanogen Bromide	148-164	rhodopsin	Bos taurus	7-16
1324716-1	1992	Bovine rhodopsin has been reconstituted in seven different saturated diacylphosphatidylcholine species of odd and even chain lengths from C-12 to C-18 at a lipid/protein ratio (60:1 mol/mol) comparable to that in the native rod outer segment disk membrane.	saturated diacylphosphatidylcholine	59-94	rhodopsin	Bos taurus	7-16
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	val-thr-thr-leu-cys	189-208	rhodopsin	Bos taurus	7-16
1324716-1	1992	Bovine rhodopsin has been reconstituted in seven different saturated diacylphosphatidylcholine species of odd and even chain lengths from C-12 to C-18 at a lipid/protein ratio (60:1 mol/mol) comparable to that in the native rod outer segment disk membrane.	Carbon	138-139	rhodopsin	Bos taurus	7-16
1324716-1	1992	Bovine rhodopsin has been reconstituted in seven different saturated diacylphosphatidylcholine species of odd and even chain lengths from C-12 to C-18 at a lipid/protein ratio (60:1 mol/mol) comparable to that in the native rod outer segment disk membrane.	Carbon	146-147	rhodopsin	Bos taurus	7-16
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	Cysteine	205-208	rhodopsin	Bos taurus	7-16
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	Glycine	213-216	rhodopsin	Bos taurus	7-16
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	Lysine	217-220	rhodopsin	Bos taurus	7-16
1512231-6	1992	Bovine rhodopsin in disc membranes was digested with thermolysin to generate the C-terminal fragment (241-327), which was subsequently cleaved with cyanogen bromide to generate the peptide Val-Thr-Thr-Leu-Cys-Cys-Gly-Lys-Asn-Pro (318-327).	asparaginyl-proline	221-228	rhodopsin	Bos taurus	7-16
1512231-10	1992	These results prove the modification of cysteines 322 and 323 with palmitic acid in bovine rhodopsin, and illustrate the utility of mass spectrometry to characterize the post-translational modifications in G-protein coupled receptors.	Cysteine	40-49	rhodopsin	Bos taurus	91-100
1512231-10	1992	These results prove the modification of cysteines 322 and 323 with palmitic acid in bovine rhodopsin, and illustrate the utility of mass spectrometry to characterize the post-translational modifications in G-protein coupled receptors.	Palmitic Acid	67-80	rhodopsin	Bos taurus	91-100
1590758-6	1992	In contrast to bovine brain G proteins, both purified transducin beta gamma subunits and beta gamma released from rhodopsin-activated transducin bound to calmodulin-Sepharose in a Ca(2+)-dependent manner.	Sepharose	165-174	rhodopsin	Bos taurus	114-123
1508983-5	1992	Comparing the difference spectra with that of unmodified rhodopsin, clear deviations in the amide-I and amide-II spectral range are observed.	Amides	92-97	rhodopsin	Bos taurus	57-66
1508983-5	1992	Comparing the difference spectra with that of unmodified rhodopsin, clear deviations in the amide-I and amide-II spectral range are observed.	Amides	104-109	rhodopsin	Bos taurus	57-66
1508983-8	1992	The difference spectra of rhodopsin modified with 10 mM dithiothreitol support the existence of the 4th loop which also undergoes conformational changes.	Dithiothreitol	56-70	rhodopsin	Bos taurus	26-35
1521582-1	1992	The influence of the carbohydrate groups of rhodopsin on its ability to regenerate upon incubation with 11-cis retinaldehyde after photobleaching was examined.	Carbohydrates	21-33	rhodopsin	Bos taurus	44-53
1521582-1	1992	The influence of the carbohydrate groups of rhodopsin on its ability to regenerate upon incubation with 11-cis retinaldehyde after photobleaching was examined.	11-cis retinaldehyde	104-124	rhodopsin	Bos taurus	44-53
1521582-5	1992	After photobleaching, deglycosylated rhodopsin reacted with 11-cis retinaldehyde in a manner similar to the native material, restoring the spectral properties lost after light-exposure.	11-cis retinaldehyde	60-80	rhodopsin	Bos taurus	37-46
1587149-1	1992	Bovine rhodopsin was subjected to reductive methylation in the dark using formaldehyde and high specific activity sodium borotritide.	Formaldehyde	74-86	rhodopsin	Bos taurus	7-16
1587149-1	1992	Bovine rhodopsin was subjected to reductive methylation in the dark using formaldehyde and high specific activity sodium borotritide.	sodium borohydride	114-132	rhodopsin	Bos taurus	7-16
1587149-3	1992	[3H]-Reductively methylated rhodopsin (specific activity, 32 Ci/mmole) was suitable for use in radioimmunoassays for rhodopsin, having many advantages over radioiodinated rhodopsin for this purpose.	Tritium	1-3	rhodopsin	Bos taurus	28-37
1587149-3	1992	[3H]-Reductively methylated rhodopsin (specific activity, 32 Ci/mmole) was suitable for use in radioimmunoassays for rhodopsin, having many advantages over radioiodinated rhodopsin for this purpose.	Tritium	1-3	rhodopsin	Bos taurus	117-126
1387847-0	1992	Hydroxylamine-dependent inhibition of rhodopsin phosphorylation in the isolated retina.	Hydroxylamine	0-13	rhodopsin	Bos taurus	38-47
1387847-1	1992	Hydroxylamine (NH2OH), a substance known to accelerate the decay of the metarhodopsin II bleaching intermediate of rhodopsin, was examined for its effect on the light-dependent phosphorylation of rhodopsin in the intact, isolated retina.	Hydroxylamine	0-13	rhodopsin	Bos taurus	76-85
1587149-3	1992	[3H]-Reductively methylated rhodopsin (specific activity, 32 Ci/mmole) was suitable for use in radioimmunoassays for rhodopsin, having many advantages over radioiodinated rhodopsin for this purpose.	Tritium	1-3	rhodopsin	Bos taurus	117-126
1387847-1	1992	Hydroxylamine (NH2OH), a substance known to accelerate the decay of the metarhodopsin II bleaching intermediate of rhodopsin, was examined for its effect on the light-dependent phosphorylation of rhodopsin in the intact, isolated retina.	Hydroxylamine	0-13	rhodopsin	Bos taurus	115-124
1837929-5	1991	In parallel experiments under absolutely identical conditions we find related to the value of CHAPSO solubilized rhodopsin (identical to 1) a quantum efficiency of bleaching for the 3-hydroxy pigment of 1.2.	chapso	94-100	rhodopsin	Bos taurus	113-122
1387847-1	1992	Hydroxylamine (NH2OH), a substance known to accelerate the decay of the metarhodopsin II bleaching intermediate of rhodopsin, was examined for its effect on the light-dependent phosphorylation of rhodopsin in the intact, isolated retina.	Hydroxylamine	15-20	rhodopsin	Bos taurus	76-85
1387847-1	1992	Hydroxylamine (NH2OH), a substance known to accelerate the decay of the metarhodopsin II bleaching intermediate of rhodopsin, was examined for its effect on the light-dependent phosphorylation of rhodopsin in the intact, isolated retina.	Hydroxylamine	15-20	rhodopsin	Bos taurus	115-124
1387847-7	1992	The results indicate that the light-dependent phosphorylation of rhodopsin in situ is substantially inhibited by NH2OH at millimolar levels.	Hydroxylamine	113-118	rhodopsin	Bos taurus	65-74
1730692-2	1992	The primary structure of bovine rhodopsin kinase (RK), which phosphorylates light-activated rhodopsin (Rho*), terminates with the amino acid sequence Cys558-Val-Leu-Ser561, a motif that has been shown to direct the isoprenylation and alpha-carboxyl methylation of many proteins (e.g. p21Ha-ras).	Leucine	161-164	rhodopsin	Bos taurus	32-41
1540695-9	1992	The high-pH form results from the low-pH form by the deprotonation of a single group with a pK of approximately 10.2 for rhodopsin in rod disk membranes in 4.0 M KCl.	Potassium Chloride	162-165	rhodopsin	Bos taurus	121-130
1917988-4	1991	When bound to arrestin, heparin also mimics phosphorylated rhodopsin by similarly exposing arrestin to limited proteolysis.	Heparin	24-31	rhodopsin	Bos taurus	59-68
1946406-7	1991	Exchange of rhodopsin"s exchangeable protons for deuterons does not affect the observed dynamics.	Deuterium	49-58	rhodopsin	Bos taurus	12-21
1917916-2	1991	Pretreatment of intact retinas with phorbol myristate acetate markedly increased the light-dependent phosphorylation of rhodopsin, with the greatest effects observed at lower light levels.	Tetradecanoylphorbol Acetate	36-61	rhodopsin	Bos taurus	120-129
1936188-3	1991	Treatment of bovine rod outer segments (ROS) with galactose oxidase followed by reduction with tritium-labeled sodium borohydride revealed the presence of existing molecules of galactose on rhodopsin.	Tritium	95-102	rhodopsin	Bos taurus	190-199
1936188-3	1991	Treatment of bovine rod outer segments (ROS) with galactose oxidase followed by reduction with tritium-labeled sodium borohydride revealed the presence of existing molecules of galactose on rhodopsin.	sodium borohydride	111-129	rhodopsin	Bos taurus	190-199
1936188-3	1991	Treatment of bovine rod outer segments (ROS) with galactose oxidase followed by reduction with tritium-labeled sodium borohydride revealed the presence of existing molecules of galactose on rhodopsin.	Galactose	50-59	rhodopsin	Bos taurus	190-199
1917916-3	1991	Phorbol myristate acetate treatment did not affect rhodopsin phosphorylation in retinas not exposed to light, suggesting that protein kinase C modulates the phosphorylation state of rhodopsin in a light-dependent manner.	Tetradecanoylphorbol Acetate	0-25	rhodopsin	Bos taurus	182-191
1905955-6	1991	The diminishing ability of bleached rhodopsin to activate Gt was measured by monitoring the level of catalyzed exchange of Gt-bound GDP for a nonhydrolyzable GTP analogue.	Guanosine Diphosphate	132-135	rhodopsin	Bos taurus	36-45
1936170-3	1991	This finding led to the hypothesis that IRBP may act as a shuttle for vitamin A during the visual cycle that regenerates rhodopsin.	Vitamin A	70-79	rhodopsin	Bos taurus	121-130
1651717-0	1991	Cyclic phosphorylation-dephosphorylation of rhodopsin in retina by protein kinase FA (the activator of ATP.Mg-dependent protein phosphatase).	cyclic	0-6	rhodopsin	Bos taurus	44-53
1651717-0	1991	Cyclic phosphorylation-dephosphorylation of rhodopsin in retina by protein kinase FA (the activator of ATP.Mg-dependent protein phosphatase).	Adenosine Triphosphate	103-106	rhodopsin	Bos taurus	44-53
1651717-2	1991	Furthermore, rhodopsin, the visual light pigment associated with rod outer segments in retina, could be well phosphorylated by kinase FA to about 0.9 mol of phosphates per mol of protein.	Phosphates	157-167	rhodopsin	Bos taurus	13-22
1651717-3	1991	Moreover, more than 90% of the phosphates in [32P]-rhodopsin could be completely removed by ATP.Mg-dependent protein phosphatase and the rhodopsin phosphatase activity was strictly kinase FA-dependent.	Phosphates	31-41	rhodopsin	Bos taurus	51-60
1651717-3	1991	Moreover, more than 90% of the phosphates in [32P]-rhodopsin could be completely removed by ATP.Mg-dependent protein phosphatase and the rhodopsin phosphatase activity was strictly kinase FA-dependent.	Phosphates	31-41	rhodopsin	Bos taurus	137-146
1651717-3	1991	Moreover, more than 90% of the phosphates in [32P]-rhodopsin could be completely removed by ATP.Mg-dependent protein phosphatase and the rhodopsin phosphatase activity was strictly kinase FA-dependent.	Adenosine Triphosphate	92-95	rhodopsin	Bos taurus	51-60
1651717-3	1991	Moreover, more than 90% of the phosphates in [32P]-rhodopsin could be completely removed by ATP.Mg-dependent protein phosphatase and the rhodopsin phosphatase activity was strictly kinase FA-dependent.	Adenosine Triphosphate	92-95	rhodopsin	Bos taurus	137-146
1833217-2	1991	The oligosaccharide chains of native and denatured opsin and rhodopsin, both solubilized and membrane-bound, were shown to be cleaved by endohexosaminidase H, endohexosaminidase F, and peptide-N-glycosidase F (PNGase F) as revealed by SDS-PAGE.	Oligosaccharides	4-19	rhodopsin	Bos taurus	61-70
1833217-2	1991	The oligosaccharide chains of native and denatured opsin and rhodopsin, both solubilized and membrane-bound, were shown to be cleaved by endohexosaminidase H, endohexosaminidase F, and peptide-N-glycosidase F (PNGase F) as revealed by SDS-PAGE.	Sodium Dodecyl Sulfate	235-238	rhodopsin	Bos taurus	61-70
1905955-6	1991	The diminishing ability of bleached rhodopsin to activate Gt was measured by monitoring the level of catalyzed exchange of Gt-bound GDP for a nonhydrolyzable GTP analogue.	Guanosine Triphosphate	158-161	rhodopsin	Bos taurus	36-45
2014228-0	1991	The role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa.	retinylidene schiff base	16-40	rhodopsin	Bos taurus	55-64
1795712-3	1991	Analysis of calcium binding process curves by photoreceptor membranes allow to conclude, that crystalline areas of rhodopsin (receptor domains) can be formed in the structure of photoreceptor membranes.	Calcium	12-19	rhodopsin	Bos taurus	115-124
2014228-0	1991	The role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa.	Schiff Bases	29-40	rhodopsin	Bos taurus	55-64
2014228-1	1991	Glu-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.	Glutamic Acid	0-3	rhodopsin	Bos taurus	68-77
2014228-1	1991	Glu-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.	retinylidene schiff base	22-46	rhodopsin	Bos taurus	68-77
2014228-2	1991	Purified mutant rhodopsin pigments were prepared in which Glu-113 was replaced individually by Gln (E113Q), Asp (E113D), Asn (E113N), or Ala (E113A).	Glutamic Acid	58-61	rhodopsin	Bos taurus	16-25
2014228-2	1991	Purified mutant rhodopsin pigments were prepared in which Glu-113 was replaced individually by Gln (E113Q), Asp (E113D), Asn (E113N), or Ala (E113A).	Glutamine	95-98	rhodopsin	Bos taurus	16-25
2014228-14	1991	The lambda max values and solute anion dependencies of the Glu-113 mutants indicate that interactions between Schiff base and its counterion play a significant role in determining the lambda max of rhodopsin.	Glutamic Acid	59-62	rhodopsin	Bos taurus	198-207
2014228-14	1991	The lambda max values and solute anion dependencies of the Glu-113 mutants indicate that interactions between Schiff base and its counterion play a significant role in determining the lambda max of rhodopsin.	Schiff Bases	110-121	rhodopsin	Bos taurus	198-207
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Phenylalanine	113-116	rhodopsin	Bos taurus	56-65
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Alanine	122-125	rhodopsin	Bos taurus	56-65
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Serine	149-152	rhodopsin	Bos taurus	56-65
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Glutamic Acid	131-134	rhodopsin	Bos taurus	56-65
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Tryptophan	162-165	rhodopsin	Bos taurus	56-65
1999419-1	1991	By using a photoactivatable analog of 11-cis-retinal in rhodopsin, we have previously identified the amino acids Phe-115, Ala-117, Glu-122, Trp-126, Ser-127, and Trp-265 as major sites of cross-linking to the chromophore.	Tryptophan	140-143	rhodopsin	Bos taurus	56-65
1986361-8	1991	Additionally, the syntenic association of TF with SST in the cow permits the prediction that the rhodopsin gene (RHO) is proximal to TF on HSA 3q.	Altretamine	139-142	rhodopsin	Bos taurus	97-106
1999419-3	1991	The mutant rhodopsin genes were expressed in monkey kidney cells (COS-1) and purified.	carbonyl sulfide	66-69	rhodopsin	Bos taurus	11-20
1990970-13	1991	These data suggest that the relative intensities of tyrosine and tryptophan fluorescence are sensitive to the structural integrity of the native (i.e., rhodopsin binding) state of arrestin, and can thus serve as useful markers of conformational transitions of this protein.	Tyrosine	52-60	rhodopsin	Bos taurus	152-161
1990970-13	1991	These data suggest that the relative intensities of tyrosine and tryptophan fluorescence are sensitive to the structural integrity of the native (i.e., rhodopsin binding) state of arrestin, and can thus serve as useful markers of conformational transitions of this protein.	Tryptophan	65-75	rhodopsin	Bos taurus	152-161
1873341-1	1991	A protein p26 with molecular weight 26 kDa capable of binding to delipidated rhodopsin immobilized on Concanavalin A-Sepharose was found in photoreceptor cells of bovine retina.	Sepharose	117-126	rhodopsin	Bos taurus	77-86
1899020-0	1991	Rhodopsin in dimyristoylphosphatidylcholine-reconstituted bilayers forms metarhodopsin II and activates Gt.	Dimyristoylphosphatidylcholine	13-43	rhodopsin	Bos taurus	0-9
1899020-4	1991	Purified bovine rhodopsin was incorporated into vesicles consisting of dimyristoylphosphatidylcholine (DMPC), and the rapid formation of a photochemical intermediate absorbing maximally at 380 nm was quantified via both flash photolysis and equilibrium spectral measurements.	Dimyristoylphosphatidylcholine	71-101	rhodopsin	Bos taurus	16-25
1899020-4	1991	Purified bovine rhodopsin was incorporated into vesicles consisting of dimyristoylphosphatidylcholine (DMPC), and the rapid formation of a photochemical intermediate absorbing maximally at 380 nm was quantified via both flash photolysis and equilibrium spectral measurements.	Dimyristoylphosphatidylcholine	103-107	rhodopsin	Bos taurus	16-25
2123802-0	1990	Interaction of recombinant rho A GTP-binding proteins with photoexcited rhodopsin.	Guanosine Triphosphate	33-36	rhodopsin	Bos taurus	72-81
2006550-2	1991	In order to select these antibodies, hybridoma supernatants that contained anti-rhodopsin antibodies have been screened by enzyme-linked immunosorbent assay (ELISA) in the presence of synthetic peptides from rhodopsin"s cytoplasmic regions.	Peptides	194-202	rhodopsin	Bos taurus	208-217
2006550-14	1991	Antibody A11-82P, specific for phosphorylated rhodopsin, recognized rhodopsin containing two or more phosphates and inhibited its further phosphorylation.	Phosphates	101-111	rhodopsin	Bos taurus	46-55
2006550-14	1991	Antibody A11-82P, specific for phosphorylated rhodopsin, recognized rhodopsin containing two or more phosphates and inhibited its further phosphorylation.	Phosphates	101-111	rhodopsin	Bos taurus	68-77
1891805-3	1991	The progressive increase of bleached rhodopsin results in a parallel increase of all-trans-retinol in retina and of both all-trans- and 11-cis-retinyl esters in pigment epithelium.	Vitamin A	84-98	rhodopsin	Bos taurus	37-46
1891805-3	1991	The progressive increase of bleached rhodopsin results in a parallel increase of all-trans-retinol in retina and of both all-trans- and 11-cis-retinyl esters in pigment epithelium.	3-azido-2,7-naphthalene disulfonate	130-135	rhodopsin	Bos taurus	37-46
1891805-3	1991	The progressive increase of bleached rhodopsin results in a parallel increase of all-trans-retinol in retina and of both all-trans- and 11-cis-retinyl esters in pigment epithelium.	-cis-retinyl esters	138-157	rhodopsin	Bos taurus	37-46
1891805-6	1991	When a considerable portion of rhodopsin is bleached (about 70%), substantial amounts of all-trans-retinol, along with minor amounts of 11-cis-retinol, accumulate in RPE subcellular organelles.	Vitamin A	89-106	rhodopsin	Bos taurus	31-40
1891805-6	1991	When a considerable portion of rhodopsin is bleached (about 70%), substantial amounts of all-trans-retinol, along with minor amounts of 11-cis-retinol, accumulate in RPE subcellular organelles.	Vitamin A	136-150	rhodopsin	Bos taurus	31-40
2123802-2	1990	The possible interaction of recombinant rho A proteins expressed in E. coli with photoexcited rhodopsin was studied by reconstitution with bovine rod outer segment (ROS) membranes depleted of endogenous GTP-binding proteins by treatment with urea.	Urea	242-246	rhodopsin	Bos taurus	94-103
1698790-4	1990	In control studies anti-rhodopsin monoclonal antibody (Rho 1D4)-Sepharose beads removed residual rhodopsin, but not the 63/240-kDa complex or channel activity.	Sepharose	64-73	rhodopsin	Bos taurus	24-33
1698790-4	1990	In control studies anti-rhodopsin monoclonal antibody (Rho 1D4)-Sepharose beads removed residual rhodopsin, but not the 63/240-kDa complex or channel activity.	Sepharose	64-73	rhodopsin	Bos taurus	97-106
2145276-0	1990	Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.	Disulfides	44-53	rhodopsin	Bos taurus	23-32
1980212-0	1990	Determinants of visual pigment absorbance: identification of the retinylidene Schiff"s base counterion in bovine rhodopsin.	retinylidene schiff"s base	65-91	rhodopsin	Bos taurus	113-122
1980212-1	1990	The role of negatively charged residues in tuning the absorbance spectrum of bovine rhodopsin has been tested by mutating each aspartate and glutamate to asparagine and glutamine, respectively.	Aspartic Acid	127-136	rhodopsin	Bos taurus	84-93
1980212-9	1990	I infer, therefore, that glutamate113 is the retinylidene Schiff"s base counterion in wild-type rhodopsin.	glutamate113	25-37	rhodopsin	Bos taurus	96-105
1980212-9	1990	I infer, therefore, that glutamate113 is the retinylidene Schiff"s base counterion in wild-type rhodopsin.	retinylidene schiff"s base	45-71	rhodopsin	Bos taurus	96-105
2145276-0	1990	Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187.	Cysteine	67-75	rhodopsin	Bos taurus	23-32
2145276-1	1990	Cysteine residues 110 and 187 are essential for the formation of the correct bovine rhodopsin structure (Karnik, S. S., Sakmar, T. P., Chen, H.-B., and Khorana, H. G. (1988) Proc.	Cysteine	0-8	rhodopsin	Bos taurus	84-93
2145276-8	1990	Rhodopsin mutants containing cysteine----serine substitutions were prepared as follows.	Cysteine	29-37	rhodopsin	Bos taurus	0-9
1980212-16	1990	These data support a model in which spectral tuning in bovine rhodopsin results from interactions between the polyene chain of 11-cis-retinal and uncharged amino acids in the binding pocket.	Polyenes	110-117	rhodopsin	Bos taurus	62-71
2145276-8	1990	Rhodopsin mutants containing cysteine----serine substitutions were prepared as follows.	Serine	41-47	rhodopsin	Bos taurus	0-9
2145276-9	1990	In one mutant, CysVII, all the 10 cysteine residues of rhodopsin were replaced by serines.	Cysteine	34-42	rhodopsin	Bos taurus	55-64
1980212-16	1990	These data support a model in which spectral tuning in bovine rhodopsin results from interactions between the polyene chain of 11-cis-retinal and uncharged amino acids in the binding pocket.	Retinaldehyde	127-141	rhodopsin	Bos taurus	62-71
2145276-9	1990	In one mutant, CysVII, all the 10 cysteine residues of rhodopsin were replaced by serines.	Serine	82-89	rhodopsin	Bos taurus	55-64
2145276-11	1990	Only mutant CysX formed functional rhodopsin.	cysx	12-16	rhodopsin	Bos taurus	35-44
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Disulfides	14-23	rhodopsin	Bos taurus	42-51
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Disulfides	75-84	rhodopsin	Bos taurus	42-51
2145276-14	1990	The C110-C187 disulfide bond is buried in rhodopsin because reactions with disulfide reducing agents and cyanide ion require prior treatment with denaturants.	Cyanides	105-112	rhodopsin	Bos taurus	42-51
2144289-3	1990	The linkage site of the analog to the opsin was confirmed to be Lys-296 as in 11-cis-retinal rhodopsin.	Lysine	64-67	rhodopsin	Bos taurus	93-102
2271572-1	1990	Bovine rhodopsin was bleached and regenerated with 7,9-dicis-retinal to form 7,9-dicis-rhodopsin, which was purified on a concanavalin A affinity column.	7,9-dicis-retinal	51-68	rhodopsin	Bos taurus	7-16
2271572-1	1990	Bovine rhodopsin was bleached and regenerated with 7,9-dicis-retinal to form 7,9-dicis-rhodopsin, which was purified on a concanavalin A affinity column.	7,9-dicis-retinal	51-68	rhodopsin	Bos taurus	87-96
2271572-3	1990	Rapid-flow resonance Raman spectra have been obtained of 7,9-dicis-rhodopsin in H2O and D2O at room temperature.	Water	80-83	rhodopsin	Bos taurus	67-76
2271572-7	1990	However, the Schiff base C = NH+ stretching frequency and its D2O shift in 7,9-dicis-rhodopsin are very similar to those in 11-cis- and 9-cis-rhodopsin, indicating that the Schiff base electrostatic/hydrogen-bonding environments are effectively the same.	Schiff Bases	13-24	rhodopsin	Bos taurus	85-94
2271572-7	1990	However, the Schiff base C = NH+ stretching frequency and its D2O shift in 7,9-dicis-rhodopsin are very similar to those in 11-cis- and 9-cis-rhodopsin, indicating that the Schiff base electrostatic/hydrogen-bonding environments are effectively the same.	Deuterium Oxide	62-65	rhodopsin	Bos taurus	85-94
2271572-7	1990	However, the Schiff base C = NH+ stretching frequency and its D2O shift in 7,9-dicis-rhodopsin are very similar to those in 11-cis- and 9-cis-rhodopsin, indicating that the Schiff base electrostatic/hydrogen-bonding environments are effectively the same.	Schiff Bases	173-184	rhodopsin	Bos taurus	85-94
2271572-7	1990	However, the Schiff base C = NH+ stretching frequency and its D2O shift in 7,9-dicis-rhodopsin are very similar to those in 11-cis- and 9-cis-rhodopsin, indicating that the Schiff base electrostatic/hydrogen-bonding environments are effectively the same.	Schiff Bases	173-184	rhodopsin	Bos taurus	142-151
2271572-7	1990	However, the Schiff base C = NH+ stretching frequency and its D2O shift in 7,9-dicis-rhodopsin are very similar to those in 11-cis- and 9-cis-rhodopsin, indicating that the Schiff base electrostatic/hydrogen-bonding environments are effectively the same.	Hydrogen	199-207	rhodopsin	Bos taurus	85-94
2271572-8	1990	The C = N trans (anti) Schiff base geometry of 7,9-dicis-rhodopsin and the insensitivity of its Schiff base vibrational properties to orientation are rationalized by examining the binding site specificity with molecular modeling.	n trans (anti) schiff base	8-34	rhodopsin	Bos taurus	57-66
2194988-2	1990	In retinal pigment epithelium, cathepsin D degrades rod outer segments and rhodopsin into glycopeptides.	Glycopeptides	90-103	rhodopsin	Bos taurus	75-84
2271572-8	1990	The C = N trans (anti) Schiff base geometry of 7,9-dicis-rhodopsin and the insensitivity of its Schiff base vibrational properties to orientation are rationalized by examining the binding site specificity with molecular modeling.	7,9-dicis	47-56	rhodopsin	Bos taurus	57-66
2271572-8	1990	The C = N trans (anti) Schiff base geometry of 7,9-dicis-rhodopsin and the insensitivity of its Schiff base vibrational properties to orientation are rationalized by examining the binding site specificity with molecular modeling.	Schiff Bases	23-34	rhodopsin	Bos taurus	57-66
2261469-1	1990	Solid-state 13C NMR spectra have been obtained of bovine rhodopsin and isorhodopsin regenerated with retinal selectively 13C labeled along the polyene chain.	13c	12-15	rhodopsin	Bos taurus	57-66
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	13c	38-41	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	13c	45-48	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	13c	45-48	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	13c	45-48	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	13c	45-48	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	Schiff Bases	154-165	rhodopsin	Bos taurus	3-12
2261469-2	1990	In rhodopsin, the chemical shifts for 13C-5, 13C-6, 13C-7, 13C-14, and 13C-15 correspond closely to the chemical shifts observed in the 11-cis protonated Schiff base (PSB) model compound.	psb	167-170	rhodopsin	Bos taurus	3-12
2261469-4	1990	The localized deshielding at C-13 supports previous models of the opsin shift in rhodopsin that place a protein perturbation in the vicinity of position 13.	Carbon	29-30	rhodopsin	Bos taurus	81-90
2143135-8	1990	In analogy to the 11-cis-locked rhodopsin analogs Rh5 and Rh7, the 510-nm-absorbing pigment, (7E,9E,13E)-10,20-methanorhodopsin, was dubbed Rh6 and the 494-nm-absorbing pigment.	methyl (5aS,8aS,10S)-8,8a,9,10-tetrahydro-5H-5a,10-epoxypyrrolo[3',4':4,5]cyclohepta[1,2-b]pyrazine-7(6H)-carboxylate	58-61	rhodopsin	Bos taurus	32-41
2143135-8	1990	In analogy to the 11-cis-locked rhodopsin analogs Rh5 and Rh7, the 510-nm-absorbing pigment, (7E,9E,13E)-10,20-methanorhodopsin, was dubbed Rh6 and the 494-nm-absorbing pigment.	rh6	140-143	rhodopsin	Bos taurus	32-41
2143135-11	1990	Rh6 and Iso6 are nearly as stable as rhodopsin towards hydroxylamine and solubilization in detergent solution and could be easily purified and reconstituted into proteoliposomes by established procedures.	Hydroxylamine	55-68	rhodopsin	Bos taurus	37-46
2164156-8	1990	We have now used time-resolved microcalorimetry in bovine rod outer segments (ROS) to monitor the heat release due to the hydrolysis of GTP by a transducin population that had been quickly activated by flash illumination of rhodopsin.	Guanosine Triphosphate	136-139	rhodopsin	Bos taurus	224-233
19431766-3	1990	Bovine rhodopsin (R) in 2% ammonyx LO was used as a photon counter.	dodecyldimethylamine oxide	27-37	rhodopsin	Bos taurus	7-16
1695508-7	1990	Furthermore, as in rhodopsin and other members of the G protein-coupled receptor family, this Cys residue is located within a hydrophilic, basic, and possibly cytoplasmic, domain.	Cysteine	94-97	rhodopsin	Bos taurus	19-28
2164156-2	1990	The T alpha subunit of transducin (composed of subunits T alpha, T beta and T gamma) is triggered by photoexcited rhodopsin (R*) to release GDP and bind GTP.	Guanosine Diphosphate	140-143	rhodopsin	Bos taurus	114-123
2164156-2	1990	The T alpha subunit of transducin (composed of subunits T alpha, T beta and T gamma) is triggered by photoexcited rhodopsin (R*) to release GDP and bind GTP.	Guanosine Triphosphate	153-156	rhodopsin	Bos taurus	114-123
2367520-11	1990	We conclude that the first step in the assembly of the rhodopsin molecule is the formation of a three-dimensional structure in the intradiscal domain involving the bulk of the out-of-the-membrane polypeptide segments followed by the linkage of Cys-110 and Cys-187 through a disulfide bond.	Cysteine	244-247	rhodopsin	Bos taurus	55-64
2367520-11	1990	We conclude that the first step in the assembly of the rhodopsin molecule is the formation of a three-dimensional structure in the intradiscal domain involving the bulk of the out-of-the-membrane polypeptide segments followed by the linkage of Cys-110 and Cys-187 through a disulfide bond.	Cysteine	256-259	rhodopsin	Bos taurus	55-64
2367520-11	1990	We conclude that the first step in the assembly of the rhodopsin molecule is the formation of a three-dimensional structure in the intradiscal domain involving the bulk of the out-of-the-membrane polypeptide segments followed by the linkage of Cys-110 and Cys-187 through a disulfide bond.	Disulfides	274-283	rhodopsin	Bos taurus	55-64
2357235-3	1990	Functional expression of bovine visual rhodopsin in the cell-free translation system with cotranslational insertion of the protein into phosphatidylcholine liposomes is described.	Phosphatidylcholines	136-155	rhodopsin	Bos taurus	39-48
2116165-1	1990	Go, a guanine nucleotide binding protein found predominantly in neural tissues, interacts in vitro with rhodopsin, muscarinic, and other receptors and has been implicated in the regulation of ion channels.	Guanine Nucleotides	6-24	rhodopsin	Bos taurus	104-113
2187531-0	1990	Guanine nucleotide binding characteristics of transducin: essential role of rhodopsin for rapid exchange of guanine nucleotides.	Guanine Nucleotides	0-18	rhodopsin	Bos taurus	76-85
2187531-0	1990	Guanine nucleotide binding characteristics of transducin: essential role of rhodopsin for rapid exchange of guanine nucleotides.	Guanine Nucleotides	108-127	rhodopsin	Bos taurus	76-85
2187531-2	1990	Light-activated rhodopsin is known to catalyze GN exchange on Gt, resulting in the formation of the active state of the Gt alpha-GTP complex.	Guanine Nucleotides	47-49	rhodopsin	Bos taurus	16-25
2187531-2	1990	Light-activated rhodopsin is known to catalyze GN exchange on Gt, resulting in the formation of the active state of the Gt alpha-GTP complex.	alpha-gtp	123-132	rhodopsin	Bos taurus	16-25
2187531-7	1990	GN-binding activity of Gt-I preparations was dependent on reaction temperature, and no binding was observed at 4 degrees C. In the presence of 10 microM bleached rhodopsin, Gt-I preparations bound GTP gamma S at 4 degrees C. However, hexylagarose chromatography of Gt-I preparations led to a preparation of Gt that showed less than 0.1 mol/mol binding activity following 60-min incubation at 30 degrees C in the absence of rhodopsin (Gt-II preparations).	Guanine Nucleotides	0-2	rhodopsin	Bos taurus	162-171
2187531-7	1990	GN-binding activity of Gt-I preparations was dependent on reaction temperature, and no binding was observed at 4 degrees C. In the presence of 10 microM bleached rhodopsin, Gt-I preparations bound GTP gamma S at 4 degrees C. However, hexylagarose chromatography of Gt-I preparations led to a preparation of Gt that showed less than 0.1 mol/mol binding activity following 60-min incubation at 30 degrees C in the absence of rhodopsin (Gt-II preparations).	aminohexyl-sepharose	234-246	rhodopsin	Bos taurus	162-171
2140896-1	1990	Expression of functionally active bovine visual rhodopsin was achieved by sequential transcription and translation in vitro of rhodopsin gene cDNA with co-translational insertion of the protein into phosphatidylcholine liposomes.	Phosphatidylcholines	199-218	rhodopsin	Bos taurus	48-57
1972155-4	1990	Km and Vmax for (Sp)-GTP alpha S (at low [Ca2+], 20 nM) are 3.7 mM and 1.1 nmol/min/mg of rhodopsin, respectively, compared with 1.1 mM and 23.1 nmol/min/mg of rhodopsin for GTP.	(sp)-gtp	16-24	rhodopsin	Bos taurus	90-99
1972155-4	1990	Km and Vmax for (Sp)-GTP alpha S (at low [Ca2+], 20 nM) are 3.7 mM and 1.1 nmol/min/mg of rhodopsin, respectively, compared with 1.1 mM and 23.1 nmol/min/mg of rhodopsin for GTP.	(sp)-gtp	16-24	rhodopsin	Bos taurus	160-169
1972155-4	1990	Km and Vmax for (Sp)-GTP alpha S (at low [Ca2+], 20 nM) are 3.7 mM and 1.1 nmol/min/mg of rhodopsin, respectively, compared with 1.1 mM and 23.1 nmol/min/mg of rhodopsin for GTP.	Guanosine Triphosphate	21-24	rhodopsin	Bos taurus	90-99
1694260-6	1990	In the absence of photolyzed rhodopsin, both intact 2H3 and Fab fragments of 2H3 were able to inhibit completely, in a concentration-dependent manner, ADP-ribosylation of transducin by pertussis toxin 2H3 had no effect on ADP-ribosylation in the presence of photolyzed rhodopsin.	Inositol	52-55	rhodopsin	Bos taurus	269-278
1694260-6	1990	In the absence of photolyzed rhodopsin, both intact 2H3 and Fab fragments of 2H3 were able to inhibit completely, in a concentration-dependent manner, ADP-ribosylation of transducin by pertussis toxin 2H3 had no effect on ADP-ribosylation in the presence of photolyzed rhodopsin.	FAB protocol	60-63	rhodopsin	Bos taurus	269-278
1694260-6	1990	In the absence of photolyzed rhodopsin, both intact 2H3 and Fab fragments of 2H3 were able to inhibit completely, in a concentration-dependent manner, ADP-ribosylation of transducin by pertussis toxin 2H3 had no effect on ADP-ribosylation in the presence of photolyzed rhodopsin.	Inositol	77-80	rhodopsin	Bos taurus	269-278
1694260-7	1990	The GTPase activity of transducin, which is dependent on rhodopsin, was inhibited only 50% by 2H3.	Inositol	94-97	rhodopsin	Bos taurus	57-66
1694260-9	1990	Further, reactions of gamma with 2H3 appear to be prevented by interaction with rhodopsin, suggesting that its interaction either shields or alters the epitope recognized by 2H3.	Inositol	33-36	rhodopsin	Bos taurus	80-89
1694260-9	1990	Further, reactions of gamma with 2H3 appear to be prevented by interaction with rhodopsin, suggesting that its interaction either shields or alters the epitope recognized by 2H3.	Inositol	174-177	rhodopsin	Bos taurus	80-89
2605220-1	1989	Rhodopsin kinase phosphorylates serine- and threonine-containing peptides from bovine rhodopsin"s carboxyl-terminal sequence.	Serine	32-38	rhodopsin	Bos taurus	86-95
2105232-1	1990	Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment.	Glutamic Acid	109-112	rhodopsin	Bos taurus	153-162
2105232-1	1990	Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment.	Aspartic Acid	114-117	rhodopsin	Bos taurus	153-162
2105232-1	1990	Site-specific mutagenesis was employed to investigate the proposed contribution of proton-donating residues (Glu, Asp) in the membrane domains of bovine rhodopsin to protonation of the Schiff base-linking protein and chromophore or to wavelength modulation of this visual pigment.	Schiff Bases	185-196	rhodopsin	Bos taurus	153-162
2132942-4	1990	This corroborates the results of experiments on the phase behavior of the detergent solution and on the distribution of rhodopsin between the salt-rich and detergent-rich phases formed at high salt concentrations.	Salts	142-146	rhodopsin	Bos taurus	120-129
2132942-4	1990	This corroborates the results of experiments on the phase behavior of the detergent solution and on the distribution of rhodopsin between the salt-rich and detergent-rich phases formed at high salt concentrations.	Salts	193-197	rhodopsin	Bos taurus	120-129
2573063-0	1989	Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.	Glutamic Acid	0-13	rhodopsin	Bos taurus	78-87
2573063-0	1989	Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin.	retinylidene schiff base	32-56	rhodopsin	Bos taurus	78-87
2573063-7	1989	We conclude that glutamic acid-113 serves as the retinylidene Schiff base counterion in rhodopsin.	glutamic acid-113	17-34	rhodopsin	Bos taurus	88-97
2573063-7	1989	We conclude that glutamic acid-113 serves as the retinylidene Schiff base counterion in rhodopsin.	retinylidene schiff base	49-73	rhodopsin	Bos taurus	88-97
2140051-6	1990	On the basis of the spectral properties of fluorinated analogues, a polar group in the chromophore binding site of iodopsin as well as rhodopsin was estimated to be located near the hydrogen atom at the C10 position of the retinylidene chromophore.	Hydrogen	182-190	rhodopsin	Bos taurus	135-144
2140051-6	1990	On the basis of the spectral properties of fluorinated analogues, a polar group in the chromophore binding site of iodopsin as well as rhodopsin was estimated to be located near the hydrogen atom at the C10 position of the retinylidene chromophore.	retinylidene	223-235	rhodopsin	Bos taurus	135-144
2611326-0	1989	Transition dipole orientations in the early photolysis intermediates of rhodopsin.	dipole	11-17	rhodopsin	Bos taurus	72-81
2605220-1	1989	Rhodopsin kinase phosphorylates serine- and threonine-containing peptides from bovine rhodopsin"s carboxyl-terminal sequence.	Threonine	44-53	rhodopsin	Bos taurus	86-95
2605220-1	1989	Rhodopsin kinase phosphorylates serine- and threonine-containing peptides from bovine rhodopsin"s carboxyl-terminal sequence.	Peptides	65-73	rhodopsin	Bos taurus	86-95
2605220-2	1989	Km"s for the peptides decrease as the length of the peptide is increased over the range 12-31 amino acids, reaching 1.7 mM for peptide 318-348 from the rhodopsin sequence.	Peptides	13-20	rhodopsin	Bos taurus	152-161
2605220-3	1989	The Km for phosphorylation of rhodopsin is about 10(3) lower than that for the peptides, which suggests that binding of rhodopsin kinase to its substrate, photolyzed rhodopsin, involves more than just binding to the carboxyl-terminal peptide region that is to be phosphorylated.	Peptides	79-87	rhodopsin	Bos taurus	30-39
2605220-3	1989	The Km for phosphorylation of rhodopsin is about 10(3) lower than that for the peptides, which suggests that binding of rhodopsin kinase to its substrate, photolyzed rhodopsin, involves more than just binding to the carboxyl-terminal peptide region that is to be phosphorylated.	Peptides	79-87	rhodopsin	Bos taurus	120-129
2605220-3	1989	The Km for phosphorylation of rhodopsin is about 10(3) lower than that for the peptides, which suggests that binding of rhodopsin kinase to its substrate, photolyzed rhodopsin, involves more than just binding to the carboxyl-terminal peptide region that is to be phosphorylated.	Peptides	79-87	rhodopsin	Bos taurus	120-129
2605220-4	1989	A synthetic peptide from the rhodopsin sequence that contains both serines and threonines is improved as a substrate by substitution of serines for the threonines, suggesting that serine residues are preferred as substrates.	Serine	67-74	rhodopsin	Bos taurus	29-38
2605220-4	1989	A synthetic peptide from the rhodopsin sequence that contains both serines and threonines is improved as a substrate by substitution of serines for the threonines, suggesting that serine residues are preferred as substrates.	Threonine	79-89	rhodopsin	Bos taurus	29-38
2605220-4	1989	A synthetic peptide from the rhodopsin sequence that contains both serines and threonines is improved as a substrate by substitution of serines for the threonines, suggesting that serine residues are preferred as substrates.	Serine	136-143	rhodopsin	Bos taurus	29-38
2605220-4	1989	A synthetic peptide from the rhodopsin sequence that contains both serines and threonines is improved as a substrate by substitution of serines for the threonines, suggesting that serine residues are preferred as substrates.	Threonine	152-162	rhodopsin	Bos taurus	29-38
2605220-4	1989	A synthetic peptide from the rhodopsin sequence that contains both serines and threonines is improved as a substrate by substitution of serines for the threonines, suggesting that serine residues are preferred as substrates.	Serine	67-73	rhodopsin	Bos taurus	29-38
2605220-8	1989	Polycations such as spermine or spermidine are nonessential activators of phosphorylation of rhodopsin or its synthetic peptide 324-348.	Spermine	20-28	rhodopsin	Bos taurus	93-102
2605220-8	1989	Polycations such as spermine or spermidine are nonessential activators of phosphorylation of rhodopsin or its synthetic peptide 324-348.	Spermidine	32-42	rhodopsin	Bos taurus	93-102
2605220-10	1989	Poly(L-aspartic acid) is a competitive inhibitor with respect to rhodopsin (KI = 300 microM) and shows mixed type inhibition with respect to ATP.	poly(l-aspartic acid	0-20	rhodopsin	Bos taurus	65-74
2511928-1	1989	It was shown that delipidated rhodopsin immobilized on concanavalin A-Sepharose (Rimm) binds with high selectivity transducin from total extracts of rod outer segment protein as well as the regulatory GTP-binding Gi- and Go-like proteins from solubilized membranes of bovine brain.	Sepharose	70-79	rhodopsin	Bos taurus	30-39
2511928-1	1989	It was shown that delipidated rhodopsin immobilized on concanavalin A-Sepharose (Rimm) binds with high selectivity transducin from total extracts of rod outer segment protein as well as the regulatory GTP-binding Gi- and Go-like proteins from solubilized membranes of bovine brain.	Guanosine Triphosphate	201-204	rhodopsin	Bos taurus	30-39
2539198-1	1989	FT-IR spectroscopy has been used to investigate the conformation of rhodopsin in bovine rod outer segment membranes, dispersed in aqueous suspension in both 2H2O and H2O.	2h2o	157-161	rhodopsin	Bos taurus	68-77
2790133-1	1989	Picosecond laser photolysis of rhodopsin in polyacrylamide.	polyacrylamide	44-58	rhodopsin	Bos taurus	31-40
2790133-2	1989	Picosecond laser photolysis of rhodopsin in 15% polyacrylamide gel was performed for estimating absolute absorption spectra of the primary intermediates of cattle rhodopsin (bathorhodopsin and photorhodopsin).	polyacrylamide	48-62	rhodopsin	Bos taurus	31-40
2790133-2	1989	Picosecond laser photolysis of rhodopsin in 15% polyacrylamide gel was performed for estimating absolute absorption spectra of the primary intermediates of cattle rhodopsin (bathorhodopsin and photorhodopsin).	polyacrylamide	48-62	rhodopsin	Bos taurus	163-172
2790133-3	1989	Using a rhodopsin digitonin extract embedded in 15% polyacrylamide gel, a precise percentage of bleaching of rhodopsin after excitation of a picosecond laser pulse was measured.	Digitonin	18-27	rhodopsin	Bos taurus	8-17
2790133-3	1989	Using a rhodopsin digitonin extract embedded in 15% polyacrylamide gel, a precise percentage of bleaching of rhodopsin after excitation of a picosecond laser pulse was measured.	Digitonin	18-27	rhodopsin	Bos taurus	109-118
2790133-3	1989	Using a rhodopsin digitonin extract embedded in 15% polyacrylamide gel, a precise percentage of bleaching of rhodopsin after excitation of a picosecond laser pulse was measured.	polyacrylamide	52-66	rhodopsin	Bos taurus	109-118
2790007-1	1989	Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps).	4-[(3~{R})-1-oxidanyl-3,4-dihydro-2,1-benzoxaborinin-3-yl]-2-(pyridin-3-ylmethoxy)benzenecarboximidamide	63-66	rhodopsin	Bos taurus	42-51
2790007-1	1989	Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps).	methyl (5aS,8aS,10S)-8,8a,9,10-tetrahydro-5H-5a,10-epoxypyrrolo[3',4':4,5]cyclohepta[1,2-b]pyrazine-7(6H)-carboxylate	71-74	rhodopsin	Bos taurus	42-51
2790007-1	1989	Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps).	cyclopenta	83-93	rhodopsin	Bos taurus	42-51
2790007-1	1989	Primary photochemical behaviors of cattle rhodopsin analogues (Rh5 and Rh7) having cyclopenta- and cycloheptatrienylidene 11-cis-locked retinals (Ret5 and Ret7, respectively) were studied by excitation with a picosecond laser pulse (wavelength 532 nm; duration 21 ps).	cycloheptatrienylidene	99-121	rhodopsin	Bos taurus	42-51
2502113-1	1989	We have shown that delipidated rhodopsin immobilized on Concanavalin A-Sepharose is capable of binding transducin from crude bovine rod outer segment proteins and GIP-binding proteins (G proteins) of Go/Gi-type from solubilized bovine brain membrane as well.	Sepharose	71-80	rhodopsin	Bos taurus	31-40
2539198-11	1989	Bacteriorhodopsin under similar conditions, in 2H2O, has 20% more unexchanged amide protons than does rhodopsin.	2h2o	47-51	rhodopsin	Bos taurus	8-17
2539198-11	1989	Bacteriorhodopsin under similar conditions, in 2H2O, has 20% more unexchanged amide protons than does rhodopsin.	Amides	78-83	rhodopsin	Bos taurus	8-17
2524196-4	1989	Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane.	11-cis-Retinal	68-88	rhodopsin	Bos taurus	7-16
2524196-4	1989	Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane.	11-cis-Retinal	68-88	rhodopsin	Bos taurus	20-29
2524196-4	1989	Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane.	trans-retinoyl chloromethane	137-165	rhodopsin	Bos taurus	7-16
2524196-4	1989	Native rhodopsin or rhodopsin regenerated from opsin by addition of 11-cis-retinaldehyde is completely protected against inactivation by trans-retinoyl chloromethane.	trans-retinoyl chloromethane	137-165	rhodopsin	Bos taurus	20-29
2925642-1	1989	During the process of transduction of a photon signal in vertebrate rod outer segments, transducin, a guanine nucleotide binding protein, mediates between a photobleaching intermediate of rhodopsin and a cGMP-phosphodiesterase.	Guanine Nucleotides	102-120	rhodopsin	Bos taurus	188-197
2925642-8	1989	In the presence of a photobleaching intermediate of either unphosphorylated or phosphorylated rhodopsin, the binding of guanosine 5"-(beta, gamma-imido)triphosphate (GppNHp) to the alpha-subunit of transducin (T alpha) was remarkably enhanced with increasing concentrations of purified T beta gamma-2.	Guanylyl Imidodiphosphate	120-164	rhodopsin	Bos taurus	94-103
2925642-8	1989	In the presence of a photobleaching intermediate of either unphosphorylated or phosphorylated rhodopsin, the binding of guanosine 5"-(beta, gamma-imido)triphosphate (GppNHp) to the alpha-subunit of transducin (T alpha) was remarkably enhanced with increasing concentrations of purified T beta gamma-2.	Guanylyl Imidodiphosphate	166-172	rhodopsin	Bos taurus	94-103
2539198-1	1989	FT-IR spectroscopy has been used to investigate the conformation of rhodopsin in bovine rod outer segment membranes, dispersed in aqueous suspension in both 2H2O and H2O.	Water	158-161	rhodopsin	Bos taurus	68-77
2539198-3	1989	The frequency of the major amide I component is consistent with the presence of predominantly alpha-helices within the rhodopsin structure.	Amides	27-32	rhodopsin	Bos taurus	119-128
2539198-6	1989	This value of w gives an estimate of the unexchanged amide protons, in rhodopsin, of 51%.	Amides	53-58	rhodopsin	Bos taurus	71-80
2539198-9	1989	A comparison, after second-derivative and deconvolution analysis, of the spectra of rhodopsin with that of bacteriorhodopsin shows that both proteins exhibit a similar number of amide I components.	Amides	178-183	rhodopsin	Bos taurus	84-93
2525050-6	1989	The absorption maxima of bovine artificial pigments formed by regenerating opsin with the 11-cis dihydro series of chromophores support a color regulation model for bovine rhodopsin in which the chromophore-binding site of the protein has two negative charges: one directly hydrogen bonded to the Schiff base nitrogen and another near carbon-13.	Schiff Bases	297-308	rhodopsin	Bos taurus	172-181
2525050-6	1989	The absorption maxima of bovine artificial pigments formed by regenerating opsin with the 11-cis dihydro series of chromophores support a color regulation model for bovine rhodopsin in which the chromophore-binding site of the protein has two negative charges: one directly hydrogen bonded to the Schiff base nitrogen and another near carbon-13.	Nitrogen	309-317	rhodopsin	Bos taurus	172-181
2525050-6	1989	The absorption maxima of bovine artificial pigments formed by regenerating opsin with the 11-cis dihydro series of chromophores support a color regulation model for bovine rhodopsin in which the chromophore-binding site of the protein has two negative charges: one directly hydrogen bonded to the Schiff base nitrogen and another near carbon-13.	Hydrogen	274-282	rhodopsin	Bos taurus	172-181
2525050-6	1989	The absorption maxima of bovine artificial pigments formed by regenerating opsin with the 11-cis dihydro series of chromophores support a color regulation model for bovine rhodopsin in which the chromophore-binding site of the protein has two negative charges: one directly hydrogen bonded to the Schiff base nitrogen and another near carbon-13.	Carbon	335-341	rhodopsin	Bos taurus	172-181
2713437-1	1989	The photolysis intermediates of an artificial bovine rhodopsin pigment, cis-5,6-dihydro-isorhodopsin (cis-5,6,-diH-ISORHO, lambda max 461 nm), which contains a cis-5,6-dihydro-9-cis-retinal chromophore, are investigated by room temperature, nanosecond laser photolysis, and low temperature irradiation studies.	cis-5,6-dihydro-isorhodopsin	72-100	rhodopsin	Bos taurus	53-62
2713437-1	1989	The photolysis intermediates of an artificial bovine rhodopsin pigment, cis-5,6-dihydro-isorhodopsin (cis-5,6,-diH-ISORHO, lambda max 461 nm), which contains a cis-5,6-dihydro-9-cis-retinal chromophore, are investigated by room temperature, nanosecond laser photolysis, and low temperature irradiation studies.	cis-5,6,-dih	102-114	rhodopsin	Bos taurus	53-62
2713437-1	1989	The photolysis intermediates of an artificial bovine rhodopsin pigment, cis-5,6-dihydro-isorhodopsin (cis-5,6,-diH-ISORHO, lambda max 461 nm), which contains a cis-5,6-dihydro-9-cis-retinal chromophore, are investigated by room temperature, nanosecond laser photolysis, and low temperature irradiation studies.	isorho	115-121	rhodopsin	Bos taurus	53-62
2713437-1	1989	The photolysis intermediates of an artificial bovine rhodopsin pigment, cis-5,6-dihydro-isorhodopsin (cis-5,6,-diH-ISORHO, lambda max 461 nm), which contains a cis-5,6-dihydro-9-cis-retinal chromophore, are investigated by room temperature, nanosecond laser photolysis, and low temperature irradiation studies.	cis-5,6-dihydro-9-cis	160-181	rhodopsin	Bos taurus	53-62
2540498-1	1989	The primary photochemical reactions of cattle rhodopsin suspended in H2O or D2O were compared between excitation with both a weak and an intense picosecond laser pulse (wavelength, 532 nm; duration, 25 ps) at room temperature.	Water	69-72	rhodopsin	Bos taurus	46-55
2540499-1	1989	Decay of metarhodopsin II was accelerated by hydroxylamine treatment or dark incubation of metarhodopsin II at 30 degrees C. The products thus obtained after decay of metarhodopsin II induced GTPase activity on transducin as well as metarhodopsin II suggesting that rhodopsin could activate transducin after the decay of metarhodopsin II intermediate.	Hydroxylamine	45-58	rhodopsin	Bos taurus	13-22
2540499-2	1989	After urea-treated bovine rod outer segment membrane was completely bleached, rhodopsin in the membrane was regenerated by the addition of 11-cis retinal at various temperatures between 0 and 37 degrees C. The capacity to induce GTPase activity on transducin and phosphate incorporating capacity catalyzed by rhodopsin kinase were measured on such rhodopsins.	Urea	6-10	rhodopsin	Bos taurus	78-87
2540499-2	1989	After urea-treated bovine rod outer segment membrane was completely bleached, rhodopsin in the membrane was regenerated by the addition of 11-cis retinal at various temperatures between 0 and 37 degrees C. The capacity to induce GTPase activity on transducin and phosphate incorporating capacity catalyzed by rhodopsin kinase were measured on such rhodopsins.	Phosphates	263-272	rhodopsin	Bos taurus	78-87
3186735-0	1988	Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin.	Cysteine	0-8	rhodopsin	Bos taurus	93-102
2462253-5	1988	These results raise the possibility that opsin or rhodopsin, an opsin/rhodopsin isoform, or an opsin/isoform multimer serves as a cGMP-modulated pore in the rod outer segment.	Cyclic GMP	130-134	rhodopsin	Bos taurus	50-59
2462253-5	1988	These results raise the possibility that opsin or rhodopsin, an opsin/rhodopsin isoform, or an opsin/isoform multimer serves as a cGMP-modulated pore in the rod outer segment.	Cyclic GMP	130-134	rhodopsin	Bos taurus	70-79
3186735-6	1988	Thus, of the 10 cysteines in bovine rhodopsin, only intradiscal Cys-110 and Cys-187 are essential for the correct tertiary structure of the protein.	Cysteine	16-25	rhodopsin	Bos taurus	36-45
3186735-6	1988	Thus, of the 10 cysteines in bovine rhodopsin, only intradiscal Cys-110 and Cys-187 are essential for the correct tertiary structure of the protein.	Cysteine	64-67	rhodopsin	Bos taurus	36-45
3186735-6	1988	Thus, of the 10 cysteines in bovine rhodopsin, only intradiscal Cys-110 and Cys-187 are essential for the correct tertiary structure of the protein.	Cysteine	76-79	rhodopsin	Bos taurus	36-45
3050446-1	1988	Rhodopsin kinase was purified from bovine retina rod outer segments as a 62-64-kDa protein that phosphorylated purified rhodopsin reconstituted into egg phosphatidylcholine/phosphatidylethanolamine liposomes.	Phosphatidylcholines	153-172	rhodopsin	Bos taurus	120-129
3207703-0	1988	Equilibrium and dynamic bilayer structural properties of unsaturated acyl chain phosphatidylcholine-cholesterol-rhodopsin recombinant vesicles and rod outer segment disk membranes as determined from higher order analysis of fluorescence anisotropy decay.	Phosphatidylcholines	80-99	rhodopsin	Bos taurus	112-121
3207703-0	1988	Equilibrium and dynamic bilayer structural properties of unsaturated acyl chain phosphatidylcholine-cholesterol-rhodopsin recombinant vesicles and rod outer segment disk membranes as determined from higher order analysis of fluorescence anisotropy decay.	Cholesterol	100-111	rhodopsin	Bos taurus	112-121
3050446-1	1988	Rhodopsin kinase was purified from bovine retina rod outer segments as a 62-64-kDa protein that phosphorylated purified rhodopsin reconstituted into egg phosphatidylcholine/phosphatidylethanolamine liposomes.	phosphatidylethanolamine	173-197	rhodopsin	Bos taurus	120-129
3416032-3	1988	This has enabled us to determine the change in geometry upon electronic excitation of rhodopsin"s 11-cis-retinal protonated Schiff base chromophore along 25 normal coordinates.	Schiff Bases	124-135	rhodopsin	Bos taurus	86-95
3207686-8	1988	From these results, it is concluded that, whereas the environment of the Schiff base in rhodopsin, bathorhodopsin, and isorhodopsin is approximately the same, large changes occur with the formation of lumirhodopsin.	Schiff Bases	73-84	rhodopsin	Bos taurus	88-97
2975508-5	1988	The addition of 9,13-dicis-retinal to the ROS suspension containing opsin produced 9-cis-rhodopsin in 97% yield.	9,13-dicis	16-26	rhodopsin	Bos taurus	89-98
2975508-5	1988	The addition of 9,13-dicis-retinal to the ROS suspension containing opsin produced 9-cis-rhodopsin in 97% yield.	ros	42-45	rhodopsin	Bos taurus	89-98
2839365-4	1988	When rhodopsin deactivation is accelerated (in the presence of NH2OH), PA-signal recovery is also accelerated.	Hydroxylamine	63-68	rhodopsin	Bos taurus	5-14
2839365-4	1988	When rhodopsin deactivation is accelerated (in the presence of NH2OH), PA-signal recovery is also accelerated.	Protactinium	71-73	rhodopsin	Bos taurus	5-14
2845967-0	1988	Electron spin resonance study of light-induced conformational changes in nitroxide labelled bovine rhodopsin.	Hydroxylamine	73-82	rhodopsin	Bos taurus	99-108
2845967-1	1988	Bovine rhodopsin was isolated in the unbleached form as a retinal disc membrane suspension and spin-labelled with 4-maleimido-2,2,6,6-tetramethylpiperidine-N-oxyl.	4-maleimido-2,2,6,6-tetramethylpiperidine-n-oxyl	114-162	rhodopsin	Bos taurus	7-16
3136032-4	1988	In this paper, using a convenient, non-invasive light scattering assay, we demonstrate that in an intact stack of disks, where active transducin stays membrane associated and is rapidly deactivated, the activity of rhodopsin can also be quenched in the time range of seconds when soluble ROS proteins are supplemented.	ros	288-291	rhodopsin	Bos taurus	215-224
3365383-0	1988	Phospholipid species containing long and very long polyenoic fatty acids remain with rhodopsin after hexane extraction of photoreceptor membranes.	Phospholipids	0-12	rhodopsin	Bos taurus	85-94
3350146-0	1988	Two adjacent cysteine residues in the C-terminal cytoplasmic fragment of bovine rhodopsin are palmitylated.	Cysteine	13-21	rhodopsin	Bos taurus	80-89
3350146-1	1988	Covalent coupling of bovine rhodopsin to CPG-thiol glass was used for separation of CNBr peptides.	Sulfhydryl Compounds	45-50	rhodopsin	Bos taurus	28-37
3350146-2	1988	It is shown that cysteine residues 322 and 323 in the C-terminal cytoplasmic fragment of rhodopsin are modified with palmitic acid.	Cysteine	17-25	rhodopsin	Bos taurus	89-98
3350146-2	1988	It is shown that cysteine residues 322 and 323 in the C-terminal cytoplasmic fragment of rhodopsin are modified with palmitic acid.	Palmitic Acid	117-130	rhodopsin	Bos taurus	89-98
3343097-4	1988	In another series of experiments, rhodopsin on the surface of fixed ROS was densely labeled with gold-dextran particles conjugated to an N-terminal-specific (rho 4D2) rhodopsin monoclonal antibody or its F(ab")2 fragment in an effort to block binding and phagocytosis by RPE cells.	Dextrans	102-109	rhodopsin	Bos taurus	34-43
3382623-4	1988	Rhodopsin kinase can phosphorylate synthetic peptides containing the appropriate sequences from bovine rhodopsin; however, the Km values for these peptides are about 3 orders of magnitude higher than that for rhodopsin or ATP.	Peptides	45-53	rhodopsin	Bos taurus	103-112
3382015-4	1988	The purified rhodopsin kinase had an apparent molecular weight of 68,000 and phosphorylated rhodopsin at the rate of 10 nmol phosphate/min/mg of the enzyme.	Phosphates	125-134	rhodopsin	Bos taurus	13-22
3365383-0	1988	Phospholipid species containing long and very long polyenoic fatty acids remain with rhodopsin after hexane extraction of photoreceptor membranes.	polyenoic fatty acids	51-72	rhodopsin	Bos taurus	85-94
3365383-0	1988	Phospholipid species containing long and very long polyenoic fatty acids remain with rhodopsin after hexane extraction of photoreceptor membranes.	Hexanes	101-107	rhodopsin	Bos taurus	85-94
3365383-4	1988	After hexane extraction of lyophilized disks, PC is the major component of the fraction of lipids that remains associated with rhodopsin, followed by phosphatidylserine, while a large proportion of the phosphatidylethanolamine is removed.	Phosphatidylcholines	46-48	rhodopsin	Bos taurus	127-136
3365383-7	1988	VLCPUFA-containing PCs are the most highly concentrated species in the rhodopsin-associated lipid fraction.	Phosphatidylcholines	19-22	rhodopsin	Bos taurus	71-80
3365383-9	1988	It is hypothesized that their unusually long polyenoic fatty acids could be well suited to partially surround alpha-helical segments of rhodopsin.	polyenoic fatty acids	45-66	rhodopsin	Bos taurus	136-145
3135154-1	1988	Information available at present documents the existence of three well-defined classes of guanine nucleotide binding proteins functioning as signal transducers: Gs and Gi which stimulate and inhibit adenylate cyclase, respectively, and transducin which transmits and amplifies the signal from light-activated rhodopsin to cGMP-dependent phosphodiesterase in ROS membranes.	Guanine Nucleotides	90-108	rhodopsin	Bos taurus	309-318
3118952-0	1987	Deoxylysolecithin and a new biphenyl detergent as solubilizing agents for bovine rhodopsin.	deoxylysolecithin	0-17	rhodopsin	Bos taurus	81-90
3316207-2	1987	The GTP-induced dissociation of T alpha from T beta gamma initiates the release of transducin from photolyzed rhodopsin and the subsequent activation of the cGMP phosphodiesterase.	Guanosine Triphosphate	4-7	rhodopsin	Bos taurus	110-119
2823926-0	1987	[Structural stabilization of lipids and visual pigment rhodopsin in the photoreceptor membrane by vitamin E].	Vitamin E	98-107	rhodopsin	Bos taurus	55-64
2823926-1	1987	Interaction of alpha-tocopherol with free fatty acids in bovine retinal photoreceptor membranes was studied using ESR spin-probe technique and measurements of rhodopsin thermal denaturation rates.	alpha-Tocopherol	15-31	rhodopsin	Bos taurus	159-168
2823926-2	1987	Exogenous alpha-tocopherol incorporated into photoreceptor membranes prevented thermal destabilization of rhodopsin caused by free fatty acids.	alpha-Tocopherol	10-26	rhodopsin	Bos taurus	106-115
2823926-2	1987	Exogenous alpha-tocopherol incorporated into photoreceptor membranes prevented thermal destabilization of rhodopsin caused by free fatty acids.	Fatty Acids, Nonesterified	126-142	rhodopsin	Bos taurus	106-115
3427083-0	1987	A study of the Schiff base mode in bovine rhodopsin and bathorhodopsin.	Schiff Bases	15-26	rhodopsin	Bos taurus	42-51
3427083-3	1987	Apart from the doubly labeled retinal, we find that the protonated Schiff base frequency is the same, within experimental error, for both rhodopsin and bathorhodopsin for all the substitutions measured here and elsewhere.	Schiff Bases	67-78	rhodopsin	Bos taurus	138-147
3427083-4	1987	We develop a force field that accurately fits the observed ethylenic (C = C) and protonated Schiff base stretching frequencies of rhodopsin and labeled derivatives.	Schiff Bases	92-103	rhodopsin	Bos taurus	130-139
3427084-8	1987	These data are particularly interesting since the absorption maximum of 345 nm for rhodopsin might be expected to originate from an unprotonated Schiff base linkage.	Schiff Bases	145-156	rhodopsin	Bos taurus	83-92
3427084-9	1987	That the Schiff base linkage in the owlfly rhodopsin, like in bovine and in octopus, is protonated suggests that a charged chromophore is essential to visual transduction.	Schiff Bases	9-20	rhodopsin	Bos taurus	43-52
3118952-4	1987	One of them is [3-(lauroyloxy)propyl]phosphorylcholine, which has a high conformational flexibility in its hydrophobic moiety like most of the known detergents for rhodopsin.	[3-(lauroyloxy)propyl]phosphorylcholine	15-54	rhodopsin	Bos taurus	164-173
3118952-14	1987	For rhodopsin reconstituted in lipid bilayers, normal MII formation requires a well-adjusted fluidity of the hydrocarbon environment of the protein [Baldwin, P. A., & Hubbell, W. L. (1984) Biochemistry 24, 2633-2639], which was explained by an appropriate interfacial pressure at the protein-lipid interface.	Hydrocarbons	109-120	rhodopsin	Bos taurus	4-13
3118952-14	1987	For rhodopsin reconstituted in lipid bilayers, normal MII formation requires a well-adjusted fluidity of the hydrocarbon environment of the protein [Baldwin, P. A., & Hubbell, W. L. (1984) Biochemistry 24, 2633-2639], which was explained by an appropriate interfacial pressure at the protein-lipid interface.	Adenosine Monophosphate	166-169	rhodopsin	Bos taurus	4-13
3557868-4	1987	These observation indicate that lectin-like recognition involving the sugar groups of rhodopsin is not involved in the binding of rhodopsin-containing membranes by the RPE cells.	Sugars	70-75	rhodopsin	Bos taurus	86-95
3117105-8	1987	Go alpha in the presence of G beta gamma is a substrate for pertussis toxin catalyzed ADP-ribosylation; the modification was inhibited by photolyzed rhodopsin and enhanced by guanosine 5"-O-(2-thiodiphosphate).	Adenosine Diphosphate	86-89	rhodopsin	Bos taurus	149-158
2959317-0	1987	Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogues.	retinylidene	34-46	rhodopsin	Bos taurus	72-81
2959317-0	1987	Electrostatic interaction between retinylidene chromophore and opsin in rhodopsin studied by fluorinated rhodopsin analogues.	retinylidene	34-46	rhodopsin	Bos taurus	105-114
2959317-5	1987	Upon irradiation with red light at -191 degrees C, batho-12-F-rhodopsin was converted to a mixture of 12-F-rhodopsin and 9-cis-12-F-rhodopsin like that of the natural bathorhodopsin, whereas batho-10-F-rhodopsin was not converted to 9-cis-10-F-rhodopsin but only to 10-F-rhodopsin.	-10-f	196-201	rhodopsin	Bos taurus	62-71
2959317-5	1987	Upon irradiation with red light at -191 degrees C, batho-12-F-rhodopsin was converted to a mixture of 12-F-rhodopsin and 9-cis-12-F-rhodopsin like that of the natural bathorhodopsin, whereas batho-10-F-rhodopsin was not converted to 9-cis-10-F-rhodopsin but only to 10-F-rhodopsin.	9-cis-10-f	233-243	rhodopsin	Bos taurus	62-71
2959317-7	1987	On irradiation with blue light at -191 degrees C, 9-cis-10-F-rhodopsin was converted to another bathochromic intermediate that was different in absorption spectrum from batho-10-F-rhodopsin.	Fluorine	59-60	rhodopsin	Bos taurus	61-70
2959317-7	1987	On irradiation with blue light at -191 degrees C, 9-cis-10-F-rhodopsin was converted to another bathochromic intermediate that was different in absorption spectrum from batho-10-F-rhodopsin.	Fluorine	59-60	rhodopsin	Bos taurus	180-189
2959317-8	1987	9-cis-10-F-rhodopsin was practically "photoinsensitive" at liquid helium temperature (-265 degrees C), whereas 10-F-rhodopsin was converted to a photo-steady-state mixture of 10-F-rhodopsin and batho-10-F-rhodopsin.	Helium	66-72	rhodopsin	Bos taurus	11-20
3558391-4	1987	A further increase is found when ConA-Sepharose-purified rhodopsin is used as the source of both "enzyme" and acceptor.	Sepharose	38-47	rhodopsin	Bos taurus	57-66
3558391-7	1987	However, the acylation of rhodopsin is not an artifact since analysis of purified native rhodopsin reveals the presence of covalently bound palmitate and we showed that whole bovine retinas incubated with [3H] palmitate incorporated the fatty acid into rhodopsin (O"Brien, P.J., and Zatz, M. (1984) J. Biol.	Palmitates	140-149	rhodopsin	Bos taurus	89-98
3558391-7	1987	However, the acylation of rhodopsin is not an artifact since analysis of purified native rhodopsin reveals the presence of covalently bound palmitate and we showed that whole bovine retinas incubated with [3H] palmitate incorporated the fatty acid into rhodopsin (O"Brien, P.J., and Zatz, M. (1984) J. Biol.	Palmitates	140-149	rhodopsin	Bos taurus	89-98
3558391-14	1987	Incubation of labeled rhodopsin with mercaptoethanol resulted in release of the labeled palmitate indicating the presence of a thioester bond.	Mercaptoethanol	37-52	rhodopsin	Bos taurus	22-31
3558391-14	1987	Incubation of labeled rhodopsin with mercaptoethanol resulted in release of the labeled palmitate indicating the presence of a thioester bond.	Palmitates	88-97	rhodopsin	Bos taurus	22-31
3557868-0	1987	Are sugars involved in the binding of rhodopsin-membranes by the retinal pigment epithelium?	Sugars	4-10	rhodopsin	Bos taurus	38-47
3675552-1	1987	Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges.	Carbon-14	25-28	rhodopsin	Bos taurus	119-128
3675552-1	1987	Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges.	Tritium	33-35	rhodopsin	Bos taurus	119-128
3675552-1	1987	Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges.	Iodoacetic Acid	45-60	rhodopsin	Bos taurus	119-128
3675552-1	1987	Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges.	Cysteine	91-99	rhodopsin	Bos taurus	119-128
3675552-1	1987	Carboxymethylation using 14C- or 3H-labelled iodoacetic acid has been used to identify the cysteine residues in bovine rhodopsin involved in the formation of the two intramolecular disulphide bridges.	disulphide	181-191	rhodopsin	Bos taurus	119-128
3031071-3	1987	Antibodies directed against the cytoplasmic loop between transmembrane domains 1 and 2, as well as those directed against the serine/threonine-rich region of the COOH terminus of bovine rhodopsin, also recognized purified beta-adrenergic receptor isolated from mouse S49 lymphoma cells.	Serine	126-132	rhodopsin	Bos taurus	186-195
3031071-3	1987	Antibodies directed against the cytoplasmic loop between transmembrane domains 1 and 2, as well as those directed against the serine/threonine-rich region of the COOH terminus of bovine rhodopsin, also recognized purified beta-adrenergic receptor isolated from mouse S49 lymphoma cells.	Threonine	133-142	rhodopsin	Bos taurus	186-195
3816805-0	1987	High-resolution solid-state 13C-NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin.	13c	28-31	rhodopsin	Bos taurus	95-104
3109470-6	1987	The dissociation of the FITC-transducin-Gpp(NH)p complex from rhodopsin membrane remained unchanged.	fitc-transducin-gpp(nh)p	24-48	rhodopsin	Bos taurus	62-71
3593680-0	1987	Low-temperature solid-state 13C NMR studies of the retinal chromophore in rhodopsin.	13c	28-31	rhodopsin	Bos taurus	74-83
3593680-1	1987	Magic angle sample spinning (MASS) 13C NMR spectra have been obtained of bovine rhodopsin regenerated with retinal prosthetic groups isotopically enriched with 13C at C-5 and C-14.	13c	35-38	rhodopsin	Bos taurus	80-89
3593680-3	1987	The isotropic chemical shift and principal values of the chemical shift tensor of the 13C-5 label indicate that the retinal chromophore is in the twisted 6-s-cis conformation in rhodopsin, in contrast to the planar 6-s-trans conformation found in bacteriorhodopsin.	13c	86-89	rhodopsin	Bos taurus	178-187
3816805-0	1987	High-resolution solid-state 13C-NMR study of carbons C-5 and C-12 of the chromophore of bovine rhodopsin.	Carbon	45-52	rhodopsin	Bos taurus	95-104
3816805-2	1987	Solid-state 13C magic-angle spinning NMR spectroscopy has been employed to study the conformation of the 11-cis-retinylidene Schiff base chromophore in bovine rhodopsin.	13c	12-15	rhodopsin	Bos taurus	159-168
3816805-2	1987	Solid-state 13C magic-angle spinning NMR spectroscopy has been employed to study the conformation of the 11-cis-retinylidene Schiff base chromophore in bovine rhodopsin.	11-cis-retinylidene schiff base	105-136	rhodopsin	Bos taurus	159-168
3816805-3	1987	Spectra were obtained from lyophilized samples of bovine rhodopsin selectively 13C-labeled at position C-5 or C-12 of the retinyl moiety, and reconstituted in the fully saturated branched-chain phospholipid diphytanoyl glycerophosphocholine.	13c	79-82	rhodopsin	Bos taurus	57-66
3816805-3	1987	Spectra were obtained from lyophilized samples of bovine rhodopsin selectively 13C-labeled at position C-5 or C-12 of the retinyl moiety, and reconstituted in the fully saturated branched-chain phospholipid diphytanoyl glycerophosphocholine.	Carbon	81-82	rhodopsin	Bos taurus	57-66
3816805-5	1987	(1985) Biochemistry 24, 6955-6962], indicate that in bovine rhodopsin the C-6-C-7 single bond has the unperturbed cis conformation.	Carbon	74-75	rhodopsin	Bos taurus	60-69
3816805-5	1987	(1985) Biochemistry 24, 6955-6962], indicate that in bovine rhodopsin the C-6-C-7 single bond has the unperturbed cis conformation.	Carbon	78-79	rhodopsin	Bos taurus	60-69
3816805-7	1987	The NMR parameters for bovine [12-13C]rhodopsin present evidence for the presence of a negative charge interacting with the retinyl moiety near C-12, in agreement with the model for the opsin shift presented by Honig and Nakanishi and coworkers [Kakitani et al.	13c	34-37	rhodopsin	Bos taurus	38-47
3816805-7	1987	The NMR parameters for bovine [12-13C]rhodopsin present evidence for the presence of a negative charge interacting with the retinyl moiety near C-12, in agreement with the model for the opsin shift presented by Honig and Nakanishi and coworkers [Kakitani et al.	Carbon	36-37	rhodopsin	Bos taurus	38-47
2420630-5	1986	Cone outer segments (COS) were labeled with only one antibody, rho 3D6, having a specificity for the 1"-4" C-terminus of bovine rhodopsin.	carbonyl sulfide	21-24	rhodopsin	Bos taurus	128-137
3790525-1	1986	The studies reported are concerned with the functional consequences of the chemical modifications of the lysines and carboxyl-containing amino acids of bovine rhodopsin.	Lysine	105-112	rhodopsin	Bos taurus	159-168
3790525-1	1986	The studies reported are concerned with the functional consequences of the chemical modifications of the lysines and carboxyl-containing amino acids of bovine rhodopsin.	carboxyl-containing amino acids	117-148	rhodopsin	Bos taurus	159-168
3790525-2	1986	The 10 non-active-site lysine residues of rhodopsin can be completely dimethylated and partially acetimidated (8-9 residues) with no loss in the ability of the proteins to activate the G protein when photolyzed or to regenerate with 11-cis-retinal.	Lysine	23-29	rhodopsin	Bos taurus	42-51
3790525-4	1986	Surprisingly, heavy acetylation of these lysines (eight to nine residues) with acetic anhydride, which neutralizes the positive charges of the lysine residues, yields a modified rhodopsin fully capable of activating the G protein and being regenerated.	Lysine	41-48	rhodopsin	Bos taurus	178-187
3790525-4	1986	Surprisingly, heavy acetylation of these lysines (eight to nine residues) with acetic anhydride, which neutralizes the positive charges of the lysine residues, yields a modified rhodopsin fully capable of activating the G protein and being regenerated.	acetic anhydride	79-95	rhodopsin	Bos taurus	178-187
3790525-4	1986	Surprisingly, heavy acetylation of these lysines (eight to nine residues) with acetic anhydride, which neutralizes the positive charges of the lysine residues, yields a modified rhodopsin fully capable of activating the G protein and being regenerated.	Lysine	41-47	rhodopsin	Bos taurus	178-187
3790525-5	1986	It is concluded that the non-active-site lysine residues of rhodopsin are not importantly and directly involved in interactions with the G protein during photolysis.	Lysine	41-47	rhodopsin	Bos taurus	60-69
3790525-7	1986	The active-site lysine of rhodopsin was readily modified and prevented from regenerating with 11-cis-retinal and with o-salicylaldehyde and o-phthalaldehyde/mercaptoethanol, two sterically similar aromatic aldehyde containing reagents which react by entirely different mechanisms.	Lysine	16-22	rhodopsin	Bos taurus	26-35
3790525-7	1986	The active-site lysine of rhodopsin was readily modified and prevented from regenerating with 11-cis-retinal and with o-salicylaldehyde and o-phthalaldehyde/mercaptoethanol, two sterically similar aromatic aldehyde containing reagents which react by entirely different mechanisms.	o-salicylaldehyde	118-135	rhodopsin	Bos taurus	26-35
3790525-7	1986	The active-site lysine of rhodopsin was readily modified and prevented from regenerating with 11-cis-retinal and with o-salicylaldehyde and o-phthalaldehyde/mercaptoethanol, two sterically similar aromatic aldehyde containing reagents which react by entirely different mechanisms.	o-Phthalaldehyde	140-156	rhodopsin	Bos taurus	26-35
3790525-7	1986	The active-site lysine of rhodopsin was readily modified and prevented from regenerating with 11-cis-retinal and with o-salicylaldehyde and o-phthalaldehyde/mercaptoethanol, two sterically similar aromatic aldehyde containing reagents which react by entirely different mechanisms.	Mercaptoethanol	157-172	rhodopsin	Bos taurus	26-35
3790525-7	1986	The active-site lysine of rhodopsin was readily modified and prevented from regenerating with 11-cis-retinal and with o-salicylaldehyde and o-phthalaldehyde/mercaptoethanol, two sterically similar aromatic aldehyde containing reagents which react by entirely different mechanisms.	Aldehydes	127-135	rhodopsin	Bos taurus	26-35
3089334-3	1986	The GTP-site in modified transducin binds Gpp(NH)p at the same rate and reveals the same sensitivity to rhodopsin as does native transducin.	Guanosine Triphosphate	4-7	rhodopsin	Bos taurus	104-113
3015261-4	1986	The mode of transducin interaction with bleached rhodopsin also depends on the nature of the bound guanyl nucleotide: in the presence of GDP rhodopsin-containing membranes bind 70-100% of transducin, whereas in the presence of Gpp(NH)p the membranes bind only 13% of the protein.	guanyl nucleotide	99-116	rhodopsin	Bos taurus	49-58
3015261-4	1986	The mode of transducin interaction with bleached rhodopsin also depends on the nature of the bound guanyl nucleotide: in the presence of GDP rhodopsin-containing membranes bind 70-100% of transducin, whereas in the presence of Gpp(NH)p the membranes bind only 13% of the protein.	guanyl nucleotide	99-116	rhodopsin	Bos taurus	141-150
3015261-4	1986	The mode of transducin interaction with bleached rhodopsin also depends on the nature of the bound guanyl nucleotide: in the presence of GDP rhodopsin-containing membranes bind 70-100% of transducin, whereas in the presence of Gpp(NH)p the membranes bind only 13% of the protein.	Guanosine Diphosphate	137-140	rhodopsin	Bos taurus	49-58
3015261-4	1986	The mode of transducin interaction with bleached rhodopsin also depends on the nature of the bound guanyl nucleotide: in the presence of GDP rhodopsin-containing membranes bind 70-100% of transducin, whereas in the presence of Gpp(NH)p the membranes bind only 13% of the protein.	Guanosine Diphosphate	137-140	rhodopsin	Bos taurus	141-150
3015261-5	1986	The experimental results suggest that GDP and GTP convert transducin into two different functional states, i.e., the transducin X GTP complex binds to phosphodiesterase causing its stimulation, while the transducin X GDP complex is predominantly bound to rhodopsin.	Guanosine Diphosphate	38-41	rhodopsin	Bos taurus	255-264
3015261-5	1986	The experimental results suggest that GDP and GTP convert transducin into two different functional states, i.e., the transducin X GTP complex binds to phosphodiesterase causing its stimulation, while the transducin X GDP complex is predominantly bound to rhodopsin.	Guanosine Triphosphate	46-49	rhodopsin	Bos taurus	255-264
3015261-5	1986	The experimental results suggest that GDP and GTP convert transducin into two different functional states, i.e., the transducin X GTP complex binds to phosphodiesterase causing its stimulation, while the transducin X GDP complex is predominantly bound to rhodopsin.	Guanosine Triphosphate	130-133	rhodopsin	Bos taurus	255-264
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	Sulfur-35	156-159	rhodopsin	Bos taurus	66-75
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	Sulfur-35	156-159	rhodopsin	Bos taurus	131-140
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	guanosine 5"-o-	160-175	rhodopsin	Bos taurus	66-75
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	guanosine 5"-o-	160-175	rhodopsin	Bos taurus	131-140
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	thiotriphosphate	176-192	rhodopsin	Bos taurus	66-75
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	thiotriphosphate	176-192	rhodopsin	Bos taurus	131-140
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	Guanosine Triphosphate	221-224	rhodopsin	Bos taurus	66-75
3007475-6	1986	The functional consequence of protein kinase C phosphorylation of rhodopsin was a reduced ability to stimulate the light-dependent rhodopsin activation of [35S]guanosine 5"-O-(thiotriphosphate) binding to transducin, the GTP-binding regulatory protein present in ROS.	Guanosine Triphosphate	221-224	rhodopsin	Bos taurus	131-140
3949781-2	1986	Infrared spectroscopy in the interval from 1800 to 1300 cm-1 has been used to investigate the secondary structure and the hydrogen/deuterium exchange behavior of bacteriorhodopsin and bovine rhodopsin in their respective native membranes.	Hydrogen	122-130	rhodopsin	Bos taurus	170-179
3949781-2	1986	Infrared spectroscopy in the interval from 1800 to 1300 cm-1 has been used to investigate the secondary structure and the hydrogen/deuterium exchange behavior of bacteriorhodopsin and bovine rhodopsin in their respective native membranes.	Deuterium	131-140	rhodopsin	Bos taurus	170-179
3949781-6	1986	The shape of the amide I" band was pH-sensitive for photoreceptor membranes, but not for purple membrane, indicating that membrane-bound rhodopsin undergoes a conformation change at acidic pH.	Amides	17-22	rhodopsin	Bos taurus	137-146
3949781-7	1986	Peptide hydrogen exchange of bacteriorhodopsin and rhodopsin was monitored by observing the change in the ratio of integrated absorbance (Aamide II"/Aamide I") during the interval from 1.5 to 25 h after membranes were introduced into buffered D2O.	Hydrogen	8-16	rhodopsin	Bos taurus	37-46
3949781-7	1986	Peptide hydrogen exchange of bacteriorhodopsin and rhodopsin was monitored by observing the change in the ratio of integrated absorbance (Aamide II"/Aamide I") during the interval from 1.5 to 25 h after membranes were introduced into buffered D2O.	aamide ii"	138-148	rhodopsin	Bos taurus	37-46
3949781-7	1986	Peptide hydrogen exchange of bacteriorhodopsin and rhodopsin was monitored by observing the change in the ratio of integrated absorbance (Aamide II"/Aamide I") during the interval from 1.5 to 25 h after membranes were introduced into buffered D2O.	aamide i	138-146	rhodopsin	Bos taurus	37-46
3949781-7	1986	Peptide hydrogen exchange of bacteriorhodopsin and rhodopsin was monitored by observing the change in the ratio of integrated absorbance (Aamide II"/Aamide I") during the interval from 1.5 to 25 h after membranes were introduced into buffered D2O.	Deuterium Oxide	243-246	rhodopsin	Bos taurus	37-46
3023137-5	1986	It has been found that ATP enhances the AT signal, the relative effect being the largest for low photoexcitation (approximately 1 rhodopsin per disc membrane).	Adenosine Triphosphate	23-26	rhodopsin	Bos taurus	130-139
3023137-6	1986	At a high rhodopsin turnover, which saturates the AT amplitude, the effect of ATP is to accelerate the rise of the signal.	Adenosine Triphosphate	78-81	rhodopsin	Bos taurus	10-19
3529395-1	1986	Transducin is a guanyl nucleotide-binding protein that couples rhodopsin photolysis to hydrolysis of guanosine 3",5"-monophosphate in rod photoreceptor cells of vertebrate retinas.	Cyclic GMP	101-130	rhodopsin	Bos taurus	63-72
3768315-0	1986	Protein-lipid interactions at membrane surfaces: a deuterium and phosphorus nuclear magnetic resonance study of the interaction between bovine rhodopsin and the bilayer head groups of dimyristoylphosphatidylcholine.	Dimyristoylphosphatidylcholine	184-214	rhodopsin	Bos taurus	143-152
3768315-1	1986	Rhodopsin, isolated from bovine retinal rod outer segment disk membranes, has been reconstituted into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine which was deuterated in the terminal methyl groups of the choline polar head group.	Dimyristoylphosphatidylcholine	114-157	rhodopsin	Bos taurus	0-9
3768315-1	1986	Rhodopsin, isolated from bovine retinal rod outer segment disk membranes, has been reconstituted into bilayers of 1,2-dimyristoyl-sn-glycero-3-phosphocholine which was deuterated in the terminal methyl groups of the choline polar head group.	Choline	150-157	rhodopsin	Bos taurus	0-9
3768315-2	1986	By use of a mixed detergent system of cholate and octyl glucoside to solubilize the phospholipid and rhodopsin, 15 membrane complexes of predetermined phospholipid to rhodopsin mole ratios of between 350:1 and 65:1 have been produced by exhaustive dialysis and studied by a variety of techniques.	Cholates	38-45	rhodopsin	Bos taurus	101-110
3768315-2	1986	By use of a mixed detergent system of cholate and octyl glucoside to solubilize the phospholipid and rhodopsin, 15 membrane complexes of predetermined phospholipid to rhodopsin mole ratios of between 350:1 and 65:1 have been produced by exhaustive dialysis and studied by a variety of techniques.	Cholates	38-45	rhodopsin	Bos taurus	167-176
3768315-2	1986	By use of a mixed detergent system of cholate and octyl glucoside to solubilize the phospholipid and rhodopsin, 15 membrane complexes of predetermined phospholipid to rhodopsin mole ratios of between 350:1 and 65:1 have been produced by exhaustive dialysis and studied by a variety of techniques.	octyl-beta-D-glucoside	50-65	rhodopsin	Bos taurus	101-110
3768315-2	1986	By use of a mixed detergent system of cholate and octyl glucoside to solubilize the phospholipid and rhodopsin, 15 membrane complexes of predetermined phospholipid to rhodopsin mole ratios of between 350:1 and 65:1 have been produced by exhaustive dialysis and studied by a variety of techniques.	octyl-beta-D-glucoside	50-65	rhodopsin	Bos taurus	167-176
3768315-2	1986	By use of a mixed detergent system of cholate and octyl glucoside to solubilize the phospholipid and rhodopsin, 15 membrane complexes of predetermined phospholipid to rhodopsin mole ratios of between 350:1 and 65:1 have been produced by exhaustive dialysis and studied by a variety of techniques.	Phospholipids	84-96	rhodopsin	Bos taurus	167-176
3768315-5	1986	Deuterium nuclear magnetic resonance (NMR) spectra from the lipid head groups of bilayers above the gel to liquid-crystalline phase transition temperature were shown to be sensitive in a systematic way to the presence of rhodopsin which could be bleached to 380 nm.	Deuterium	0-9	rhodopsin	Bos taurus	221-230
3768315-6	1986	The measured quadrupole splittings, taken as the separation of the turning points of the recorded NMR spectra, decreased from a value of 1.28 kHz for protein-free bilayers to approximately 0.40 kHz for bilayers containing 65 molecules of phospholipid for each rhodopsin at 32 degrees C.(ABSTRACT TRUNCATED AT 250 WORDS)	Phospholipids	238-250	rhodopsin	Bos taurus	260-269
3089334-3	1986	The GTP-site in modified transducin binds Gpp(NH)p at the same rate and reveals the same sensitivity to rhodopsin as does native transducin.	Guanylyl Imidodiphosphate	42-50	rhodopsin	Bos taurus	104-113
3007475-5	1986	Phosphorylation sites map to serine and threonine residues on the cytoplasmic carboxylterminal domain of rhodopsin for both kinases.	Serine	29-35	rhodopsin	Bos taurus	105-114
3007475-5	1986	Phosphorylation sites map to serine and threonine residues on the cytoplasmic carboxylterminal domain of rhodopsin for both kinases.	Threonine	40-49	rhodopsin	Bos taurus	105-114
3461782-7	1986	These results suggest that the serine and threonine residues in the rhodopsin C-terminal peptides Rhod-1 and Rhod-3 are critical for reconstitution of transducin GTPase activity.	Serine	31-37	rhodopsin	Bos taurus	68-77
3461782-7	1986	These results suggest that the serine and threonine residues in the rhodopsin C-terminal peptides Rhod-1 and Rhod-3 are critical for reconstitution of transducin GTPase activity.	Threonine	42-51	rhodopsin	Bos taurus	68-77
2427696-23	1986	Na-Ca exchange could release 1.5 mol Ca2+ mol-1 rhodopsin from disks as compared with a cyclic-GMP-induced release of 0.15 mol Ca2+ mol-1 rhodopsin.	Cyclic GMP	88-98	rhodopsin	Bos taurus	138-147
3955023-5	1986	The species with four and five phosphates per rhodopsin were approximately 50% rhodopsin-50% isorhodopsin.	Phosphates	31-41	rhodopsin	Bos taurus	46-55
3955023-5	1986	The species with four and five phosphates per rhodopsin were approximately 50% rhodopsin-50% isorhodopsin.	Phosphates	31-41	rhodopsin	Bos taurus	79-88
3955023-8	1986	At a 4% bleach level, approximately 0.5 rhodopsin was phosphorylated with four to five phosphates for each rhodopsin that was bleached and phosphorylated.	Phosphates	87-97	rhodopsin	Bos taurus	40-49
2420630-7	1986	Immunogold-dextran labeling was also used to study the cross-reactivity of these antibodies to rhodopsin in red and green frog ROS and COS.	carbonyl sulfide	135-138	rhodopsin	Bos taurus	95-104
2420630-12	1986	The labeling of frog red ROS in relation to multiple forms of rhodopsin observed by SDS-gel electrophoresis is discussed.	Sodium Dodecyl Sulfate	84-87	rhodopsin	Bos taurus	62-71
3937555-0	1985	Methylation of the active-site lysine of rhodopsin.	Lysine	31-37	rhodopsin	Bos taurus	41-50
3083106-7	1986	Two-dimensional tetrameric arrays of molecules, possibly rhodopsin, were seen in samples of bovine retinal rod outer segments in the presence of ammonium sulphate.	Ammonium Sulfate	145-162	rhodopsin	Bos taurus	57-66
3937555-1	1985	Purified bovine rhodopsin was reductively methylated with formaldehyde and pyridine/borane with the incorporation of approximately 20 methyl groups in the protein.	Formaldehyde	58-70	rhodopsin	Bos taurus	16-25
3937555-1	1985	Purified bovine rhodopsin was reductively methylated with formaldehyde and pyridine/borane with the incorporation of approximately 20 methyl groups in the protein.	pyridine	75-83	rhodopsin	Bos taurus	16-25
3937555-1	1985	Purified bovine rhodopsin was reductively methylated with formaldehyde and pyridine/borane with the incorporation of approximately 20 methyl groups in the protein.	Boranes	84-90	rhodopsin	Bos taurus	16-25
3937555-2	1985	Rhodopsin contains 10 non-active-site lysines, which account for the uptake of the 20 methyl groups.	Lysine	38-45	rhodopsin	Bos taurus	0-9
3937555-4	1985	The critical active-site lysine of permethylated rhodopsin can be liberated by photolysis.	Lysine	25-31	rhodopsin	Bos taurus	49-58
3002442-0	1985	all-trans-retinoids and dihydroretinoids as probes of the role of chromophore structure in rhodopsin activation.	all-trans-retinoids	0-19	rhodopsin	Bos taurus	91-100
3002442-7	1985	Therefore, the possibility that rhodopsin is energized by mechanisms involving photochemically induced charge transfer from the protonated Schiff base to the beta-ionone ring can be discarded.	beta-ionone	158-169	rhodopsin	Bos taurus	32-41
3002442-1	1985	The absorption of a photon of light by rhodopsin results in the cis to trans isomerization of the 11-cis-retinal Schiff base chromophore.	11-cis-retinal schiff base	98-124	rhodopsin	Bos taurus	39-48
3002442-7	1985	Therefore, the possibility that rhodopsin is energized by mechanisms involving photochemically induced charge transfer from the protonated Schiff base to the beta-ionone ring can be discarded.	Schiff Bases	139-150	rhodopsin	Bos taurus	32-41
4089029-0	1985	Functional properties of cattle rhodopsin in soluble complex with phospholipids and deoxycholate.	Phospholipids	66-79	rhodopsin	Bos taurus	32-41
4089029-0	1985	Functional properties of cattle rhodopsin in soluble complex with phospholipids and deoxycholate.	Deoxycholic Acid	84-96	rhodopsin	Bos taurus	32-41
4016199-4	1985	Replacing all of rhodopsin"s exchangeable protons with deuterons by suspending rhodopsin in D2O had no effect on either the kinetics of the emission or the value of the quantum yield.	Deuterium Oxide	92-95	rhodopsin	Bos taurus	79-88
3929835-1	1985	In an in vitro incubation, 8-azidoguanosine 5"-[gamma-32P]triphosphate ( [gamma-32P]-8-azido-GTP) labeled bleached rhodopsin independent of ultraviolet light.	8-azidoguanosine 5"-[gamma-32p]triphosphate	27-70	rhodopsin	Bos taurus	115-124
3929835-1	1985	In an in vitro incubation, 8-azidoguanosine 5"-[gamma-32P]triphosphate ( [gamma-32P]-8-azido-GTP) labeled bleached rhodopsin independent of ultraviolet light.	[gamma-32p]-8-azido-gtp	73-96	rhodopsin	Bos taurus	115-124
4015644-0	1985	Effect of calmodulin on the structural state of photoreceptor membranes and rhodopsin-containing phospholipid vesicles.	Phospholipids	97-109	rhodopsin	Bos taurus	76-85
4027217-8	1985	Thus, the rhodopsin-dimyristoylphosphatidylcholine recombinants offer a unique system for the study of the effect of the phospholipid bilayer environment on the conformation of an intrinsic membrane protein.	Phospholipids	121-133	rhodopsin	Bos taurus	10-19
3978208-6	1985	This was accomplished by using the sulfur content of rhodopsin as an internal reference.	Sulfur	35-41	rhodopsin	Bos taurus	53-62
4027217-6	1985	Electron spin resonance studies using a novel disulfide spin-label that is covalently linked to rhodopsin indicate that the apparent arrest of the protein at the metarhodopsin I stage is not due to simple aggregation of the protein in this short-chain, saturated lipid bilayer but must be understood in terms of the effect of the lipid host on the conformational energies of individual protein molecules.	Disulfides	46-55	rhodopsin	Bos taurus	96-105
3160387-11	1985	This is consistent with the notion that a protonated Schiff base is critical for the function of rhodopsin.	Schiff Bases	53-64	rhodopsin	Bos taurus	97-106
3978208-8	1985	Upper limits were placed on the amount of manganese, molybdenum, and nickel per rhodopsin as 0.019, 0.019, and 0.006, respectively.	Manganese	42-51	rhodopsin	Bos taurus	80-89
3978208-8	1985	Upper limits were placed on the amount of manganese, molybdenum, and nickel per rhodopsin as 0.019, 0.019, and 0.006, respectively.	Nickel	69-75	rhodopsin	Bos taurus	80-89
3838249-0	1985	Reactivity with lectins of the saccharide components of rhodopsin in reconstituted membranes.	Carbohydrates	31-41	rhodopsin	Bos taurus	56-65
2982661-1	1985	ATP quenches light-dependent phosphodiesterase (PDE) activation in rod outer segments presumably due to rhodopsin phosphorylation.	Adenosine Triphosphate	0-3	rhodopsin	Bos taurus	104-113
3156050-1	1985	Conformational changes in the extradiscal regions of rhodopsin induced by illumination were investigated by modifying the visual pigment by mild treatment with cyanogen bromide prior to and after light exposure.	Cyanogen Bromide	160-176	rhodopsin	Bos taurus	53-62
3838249-3	1985	As part of the characterization of this preparation, the surface orientation of the carbohydrates of rhodopsin, assembled from purified bovine rhodopsin and egg phosphatidylcholine was examined, and is the topic of this report.	Carbohydrates	84-97	rhodopsin	Bos taurus	101-110
3838249-3	1985	As part of the characterization of this preparation, the surface orientation of the carbohydrates of rhodopsin, assembled from purified bovine rhodopsin and egg phosphatidylcholine was examined, and is the topic of this report.	Carbohydrates	84-97	rhodopsin	Bos taurus	143-152
3838249-3	1985	As part of the characterization of this preparation, the surface orientation of the carbohydrates of rhodopsin, assembled from purified bovine rhodopsin and egg phosphatidylcholine was examined, and is the topic of this report.	Phosphatidylcholines	161-180	rhodopsin	Bos taurus	101-110
3838249-15	1985	Scatchard analysis of the binding of 125I-labeled succinylated concanavalin A by rhodopsin liposomes indicated the presence of a single class of binding site as the preferred fit, with an apparent Kd of 2.8 X 10(-7) M. The binding was destroyed or extensively interfered with by trypsinization and by periodate treatment.	Iodine-125	37-41	rhodopsin	Bos taurus	81-90
3838249-15	1985	Scatchard analysis of the binding of 125I-labeled succinylated concanavalin A by rhodopsin liposomes indicated the presence of a single class of binding site as the preferred fit, with an apparent Kd of 2.8 X 10(-7) M. The binding was destroyed or extensively interfered with by trypsinization and by periodate treatment.	succinylated	50-62	rhodopsin	Bos taurus	81-90
3881128-0	1985	Rhodopsin-egg phosphatidylcholine reconstitution by an octyl glucoside dilution procedure.	Phosphatidylcholines	14-33	rhodopsin	Bos taurus	0-9
2581604-3	1985	When an average of one phosphate is incorporated per rhodopsin, the binding reactivity of rhodopsin for these antibodies decreases to 30% that of nonphosphorylated rhodopsin as measured in radioimmune competition assays.	Phosphates	23-32	rhodopsin	Bos taurus	53-62
2581604-3	1985	When an average of one phosphate is incorporated per rhodopsin, the binding reactivity of rhodopsin for these antibodies decreases to 30% that of nonphosphorylated rhodopsin as measured in radioimmune competition assays.	Phosphates	23-32	rhodopsin	Bos taurus	90-99
2581604-3	1985	When an average of one phosphate is incorporated per rhodopsin, the binding reactivity of rhodopsin for these antibodies decreases to 30% that of nonphosphorylated rhodopsin as measured in radioimmune competition assays.	Phosphates	23-32	rhodopsin	Bos taurus	90-99
2581604-8	1985	When an average of one phosphate per rhodopsin is incorporated, cleavage decreases to 40% that of nonphosphorylated rhodopsin as measured by high-performance liquid chromatography.	Phosphates	23-32	rhodopsin	Bos taurus	37-46
2581604-8	1985	When an average of one phosphate per rhodopsin is incorporated, cleavage decreases to 40% that of nonphosphorylated rhodopsin as measured by high-performance liquid chromatography.	Phosphates	23-32	rhodopsin	Bos taurus	116-125
3881128-0	1985	Rhodopsin-egg phosphatidylcholine reconstitution by an octyl glucoside dilution procedure.	octyl-beta-D-glucoside	55-70	rhodopsin	Bos taurus	0-9
3881128-1	1985	The transmembrane protein bovine rhodopsin was reconstituted with egg phosphatidylcholine (PC) by using a modified detergent dilution technique employing the nonionic detergent octyl-beta-D-glucoside (octyl glucoside).	Phosphatidylcholines	70-89	rhodopsin	Bos taurus	33-42
3881128-1	1985	The transmembrane protein bovine rhodopsin was reconstituted with egg phosphatidylcholine (PC) by using a modified detergent dilution technique employing the nonionic detergent octyl-beta-D-glucoside (octyl glucoside).	octyl-beta-D-glucoside	177-199	rhodopsin	Bos taurus	33-42
3881128-1	1985	The transmembrane protein bovine rhodopsin was reconstituted with egg phosphatidylcholine (PC) by using a modified detergent dilution technique employing the nonionic detergent octyl-beta-D-glucoside (octyl glucoside).	octyl-beta-D-glucoside	201-216	rhodopsin	Bos taurus	33-42
3881128-6	1985	In the latter case, the highest molar phospholipid/protein ratio that could be obtained when reconstituting rhodopsin with egg PC was approximately 50:1.	Phospholipids	38-50	rhodopsin	Bos taurus	108-117
3003171-2	1985	Protein kinase C behaves as an extrinsic membrane protein and phosphorylates rhodopsin in a calcium-dependent manner.	Calcium	92-99	rhodopsin	Bos taurus	77-86
2983663-2	1985	Light-activated hydrolysis of cyclic GMP is achieved through the photoexcitation of rhodopsin, a process which then triggers the replacement of GDP for GTP by a retinal guanosine 5"-triphosphatase referred to as "transducin".	Cyclic GMP	30-40	rhodopsin	Bos taurus	84-93
2983663-2	1985	Light-activated hydrolysis of cyclic GMP is achieved through the photoexcitation of rhodopsin, a process which then triggers the replacement of GDP for GTP by a retinal guanosine 5"-triphosphatase referred to as "transducin".	Guanosine Diphosphate	144-147	rhodopsin	Bos taurus	84-93
2983663-2	1985	Light-activated hydrolysis of cyclic GMP is achieved through the photoexcitation of rhodopsin, a process which then triggers the replacement of GDP for GTP by a retinal guanosine 5"-triphosphatase referred to as "transducin".	Guanosine Triphosphate	152-155	rhodopsin	Bos taurus	84-93
3879038-2	1985	The rhodopsin from single specimens of R. pipiens displayed two closely-spaced bands with Mr at 34.7 and 37.0 k on SDS polyacrylamide gels.	Sodium Dodecyl Sulfate	115-118	rhodopsin	Bos taurus	4-13
4078886-1	1985	Purified, delipidated rhodopsin is recombined with phospholipid using octyl-glucoside (OG) and preformed vesicles.	Phospholipids	51-63	rhodopsin	Bos taurus	22-31
4078886-1	1985	Purified, delipidated rhodopsin is recombined with phospholipid using octyl-glucoside (OG) and preformed vesicles.	octyl-beta-D-glucoside	70-85	rhodopsin	Bos taurus	22-31
4078886-1	1985	Purified, delipidated rhodopsin is recombined with phospholipid using octyl-glucoside (OG) and preformed vesicles.	octyl-beta-D-glucoside	87-89	rhodopsin	Bos taurus	22-31
4078886-9	1985	A model containing at least three different phospholipid environments in the presence of the membrane protein rhodopsin is described.	Phospholipids	44-56	rhodopsin	Bos taurus	110-119
3879038-2	1985	The rhodopsin from single specimens of R. pipiens displayed two closely-spaced bands with Mr at 34.7 and 37.0 k on SDS polyacrylamide gels.	polyacrylamide	119-133	rhodopsin	Bos taurus	4-13
6237688-6	1984	A partial fractionation of the antibody into two groups showing differential reactivities toward opsin and rhodopsin was achieved by affinity chromatography on opsin-Sepharose.	Sepharose	166-175	rhodopsin	Bos taurus	107-116
6529569-0	1984	Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides.	Peptides	114-122	rhodopsin	Bos taurus	66-75
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	asp18"	160-166	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	Glutamic Acid	167-170	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	ala16"	171-177	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	Serine	178-181	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	Threonine	182-185	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	Threonine	186-189	rhodopsin	Bos taurus	149-158
6529569-1	1984	The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin: Asp18"-Glu-Ala16"-Ser-Thr-Thr-Val12"-Ser-Lys-Thr-Gl u8"-Thr-Ser-Gln-Val4"-Ala-Pr o -Ala1".	Serine	197-200	rhodopsin	Bos taurus	149-158
6529569-4	1984	Antibody rho 1D4 binding was not inhibited by peptides 2"-13" or 3"-18", indicating that the C-terminal alanine residue of rhodopsin was required.	Alanine	104-111	rhodopsin	Bos taurus	123-132
6098298-0	1984	Studies on structure and function of rhodopsin by use of cyclopentatrienylidene 11-cis-locked-rhodopsin.	cyclopentatrienylidene	57-79	rhodopsin	Bos taurus	37-46
6098298-0	1984	Studies on structure and function of rhodopsin by use of cyclopentatrienylidene 11-cis-locked-rhodopsin.	cyclopentatrienylidene	57-79	rhodopsin	Bos taurus	94-103
6098298-1	1984	The photochemical reaction of cyclopentatrienylidene 11-cis-locked-rhodopsin derived from cyclopentatrienylidene 11-cis-locked-retinal and cattle opsin was spectrophotometrically studied.	cyclopentatrienylidene	30-52	rhodopsin	Bos taurus	67-76
6098298-1	1984	The photochemical reaction of cyclopentatrienylidene 11-cis-locked-rhodopsin derived from cyclopentatrienylidene 11-cis-locked-retinal and cattle opsin was spectrophotometrically studied.	cyclopentatrienylidene	90-112	rhodopsin	Bos taurus	67-76
6098298-2	1984	The difference absorption spectrum between the cyclopentatrienylidene 11-cis-locked-rhodopsin and its retinal oxime had its maximum at 495 nm (P-495).	cyclopentatrienylidene	47-69	rhodopsin	Bos taurus	84-93
6098298-2	1984	The difference absorption spectrum between the cyclopentatrienylidene 11-cis-locked-rhodopsin and its retinal oxime had its maximum at 495 nm (P-495).	Oximes	110-115	rhodopsin	Bos taurus	84-93
6098298-11	1984	This result suggests that the isomerization of the retinylidene chromophore of rhodopsin is indispensable in the phototransduction process.	retinylidene	51-63	rhodopsin	Bos taurus	79-88
6477897-2	1984	This rhodopsin analog was prepared by incubating 9-cis-7,8-dihydroretinal with bovine opsin in the dark.	9-cis-7,8-dihydroretinal	49-73	rhodopsin	Bos taurus	5-14
6477897-5	1984	Thus, the mechanism of formation of bathorhodopsin (in bovine rhodopsin system) may be considered as some change of the interaction between the conjugated double-bond system from C-9 to the Schiff base nitrogen and its surrounding charges in opsin, caused by rotation of 11-12 double-bond.	Schiff Bases	190-201	rhodopsin	Bos taurus	41-50
6477897-5	1984	Thus, the mechanism of formation of bathorhodopsin (in bovine rhodopsin system) may be considered as some change of the interaction between the conjugated double-bond system from C-9 to the Schiff base nitrogen and its surrounding charges in opsin, caused by rotation of 11-12 double-bond.	Nitrogen	202-210	rhodopsin	Bos taurus	41-50
6715336-0	1984	Acylation of bovine rhodopsin by [3H]palmitic acid.	[3h]palmitic acid	33-50	rhodopsin	Bos taurus	20-29
6477578-1	1984	When isolated bovine rod outer segment fragments were incubated with [gamma-32P]ATP, 32P, as revealed by autoradiography, was rapidly incorporated into rhodopsin bands on sodium dodecyl sulfate polyacrylamide gels, and into a low Mr lipid band.	[gamma-32p]atp	69-83	rhodopsin	Bos taurus	152-161
6477578-1	1984	When isolated bovine rod outer segment fragments were incubated with [gamma-32P]ATP, 32P, as revealed by autoradiography, was rapidly incorporated into rhodopsin bands on sodium dodecyl sulfate polyacrylamide gels, and into a low Mr lipid band.	Phosphorus-32	76-79	rhodopsin	Bos taurus	152-161
6477578-6	1984	Up to 1 mol phosphatidic acid was formed per 18 to 40 mol rhodopsin present.	Phosphatidic Acids	12-29	rhodopsin	Bos taurus	58-67
6480737-5	1984	A comparison of the elution profiles of rhodopsin purified by this method with that purified by Concanavalin A-Sepharose 4B affinity chromatography suggested that rhodopsin from high-performance chromatography was slightly purer than the conventionally purified rhodopsin.	Sepharose	111-123	rhodopsin	Bos taurus	163-172
6480737-5	1984	A comparison of the elution profiles of rhodopsin purified by this method with that purified by Concanavalin A-Sepharose 4B affinity chromatography suggested that rhodopsin from high-performance chromatography was slightly purer than the conventionally purified rhodopsin.	Sepharose	111-123	rhodopsin	Bos taurus	163-172
6743754-2	1984	After photoexcitation with a 500-nm flash delivered by a dye laser, a negative photovoltage was observed on the bilayer under normal ionic strengths (100 mM KCl), which had a rise phase of 1-3 ms at 20 degrees C. The photoresponse was obviously due to bleaching of rhodopsin as it decreased for successive flashes of light.	Potassium Chloride	157-160	rhodopsin	Bos taurus	265-274
6743754-3	1984	It originated most probably during the metarhodopsin-I metarhodopsin-II (meta-I-II) transition of rhodopsin because it was pH dependent at 2 degrees C but not at 20 degrees C. At 10 mM KCl, i.e., under hypotonic conditions, a positive photovoltage with slower kinetics than at high salt was observed.	Potassium Chloride	185-188	rhodopsin	Bos taurus	43-52
6586721-6	1984	Maximal incorporation of ADP-ribose was achieved when guanosine 5"-(beta, gamma-imido)triphosphate (Gpp(NH)p) and T beta gamma were present at concentrations equal to that of T alpha and when rhodopsin was continuously irradiated with visible light in the 400-500 nm region.	Adenosine Diphosphate Ribose	25-35	rhodopsin	Bos taurus	192-201
6586721-6	1984	Maximal incorporation of ADP-ribose was achieved when guanosine 5"-(beta, gamma-imido)triphosphate (Gpp(NH)p) and T beta gamma were present at concentrations equal to that of T alpha and when rhodopsin was continuously irradiated with visible light in the 400-500 nm region.	Guanylyl Imidodiphosphate	100-108	rhodopsin	Bos taurus	192-201
6468381-14	1984	This effect was shown to be due to conversion of partially digested rhodopsin to a photolytic product that at room temperature lived for minutes even in the presence of NH2OH.	Hydroxylamine	169-174	rhodopsin	Bos taurus	68-77
6480737-1	1984	Bovine rhodopsin was purified from n-octylglucoside-solubilized retinas by high-performance size-exclusion chromatography.	Octyl glucoside	35-51	rhodopsin	Bos taurus	7-16
6373446-2	1984	The antibody was raised against bovine rhodopsin purified on SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	61-64	rhodopsin	Bos taurus	39-48
6373446-2	1984	The antibody was raised against bovine rhodopsin purified on SDS-polyacrylamide gel electrophoresis.	polyacrylamide	65-79	rhodopsin	Bos taurus	39-48
6715336-1	1984	Bovine retinas or preparations of rod outer segments incorporate [3H]palmitic acid into rhodopsin.	[3h]palmitic acid	65-82	rhodopsin	Bos taurus	88-97
6715336-7	1984	These results demonstrate the formation of an ester bond between [3H]palmitic acid and rhodopsin.	Esters	46-51	rhodopsin	Bos taurus	87-96
6715336-7	1984	These results demonstrate the formation of an ester bond between [3H]palmitic acid and rhodopsin.	[3h]palmitic acid	65-82	rhodopsin	Bos taurus	87-96
6242325-2	1984	A rhodopsin, a rod visual pigment, is composed of an 11-cis-retinal bound with an apo-protein, opsin, through a protonated Schiff-base.	Schiff Bases	123-134	rhodopsin	Bos taurus	2-11
6466718-3	1984	The model of animal rhodopsin was suggested to have 13 phenylalanine residues forming a chain which "connects" 6 transmembrane segments and runs from one surface of the membrane to the opposite one.	Phenylalanine	55-68	rhodopsin	Bos taurus	20-29
6202429-3	1984	The antibody used in our study was raised against bovine rhodopsin purified by SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	79-82	rhodopsin	Bos taurus	57-66
6202429-3	1984	The antibody used in our study was raised against bovine rhodopsin purified by SDS-polyacrylamide gel electrophoresis.	polyacrylamide gels	83-101	rhodopsin	Bos taurus	57-66
6229282-1	1984	Opsin readily undergoes Schiff base formation between an active site lysine and 9-cis- or 11-cis-retinaldehyde to form the visual pigments isorhodopsin (lambda max = 487 nm) and rhodopsin (lambda max = 500 nm), respectively (Dratz, 1977).	Schiff Bases	24-35	rhodopsin	Bos taurus	142-151
6229282-1	1984	Opsin readily undergoes Schiff base formation between an active site lysine and 9-cis- or 11-cis-retinaldehyde to form the visual pigments isorhodopsin (lambda max = 487 nm) and rhodopsin (lambda max = 500 nm), respectively (Dratz, 1977).	Lysine	69-75	rhodopsin	Bos taurus	142-151
6229282-1	1984	Opsin readily undergoes Schiff base formation between an active site lysine and 9-cis- or 11-cis-retinaldehyde to form the visual pigments isorhodopsin (lambda max = 487 nm) and rhodopsin (lambda max = 500 nm), respectively (Dratz, 1977).	9-cis- or 11-cis-retinaldehyde	80-110	rhodopsin	Bos taurus	142-151
6242325-11	1984	7-Membered-rhodopsin, in which the rotation of 11-12 double bond of the retinylidene chromophore is locked, did not form bathorhodopsin by excitation of picosecond laser photolysis.	retinylidene	72-84	rhodopsin	Bos taurus	11-20
6242325-3	1984	Competitive inhibition of beta-ionone on regeneration of rhodopsin from an 11-cis-retinal and cattle opsin demonstrated the existence of a hydrophobic linkage between the beta-ionone ring of the retinal and the hydrophobic region of opsin.	beta-ionone	26-37	rhodopsin	Bos taurus	57-66
6242325-14	1984	The reversal of the sign of CD indicates that not only large conformational change of the retinylidene chromophore occurs during the conversion of rhodopsin to bathorhodopsin, but also the direction of twist of the chromophore reverses.	retinylidene	90-102	rhodopsin	Bos taurus	147-156
6242325-3	1984	Competitive inhibition of beta-ionone on regeneration of rhodopsin from an 11-cis-retinal and cattle opsin demonstrated the existence of a hydrophobic linkage between the beta-ionone ring of the retinal and the hydrophobic region of opsin.	beta-ionone	171-182	rhodopsin	Bos taurus	57-66
6242325-10	1984	Irradiation of 7-cis- and 9-cis-rhodopsins at liquid nitrogen temperature produced the same bathorhodopsin as that from 11-cis-rhodopsin, indicating that the chromophore of bathorhodopsin should be in all-trans or transoid form.	Nitrogen	53-61	rhodopsin	Bos taurus	32-41
6099932-2	1984	For example, 4 +/- 1 phosphates are incorporated per bleached rhodopsin (Rho*) in 30 sec and 6 +/- 2 phosphates are incorporated in 75 sec in response to bleaching 1% of the rhodopsin in the presence of 1 mM [gamma-32P]ATP and 0.1 mM nonradioactive GTP.	[gamma-32p]atp	208-222	rhodopsin	Bos taurus	174-183
6099932-0	1984	Phosphorylation at sites near rhodopsin"s carboxyl-terminus regulates light initiated cGMP hydrolysis.	Cyclic GMP	86-90	rhodopsin	Bos taurus	30-39
6099932-2	1984	For example, 4 +/- 1 phosphates are incorporated per bleached rhodopsin (Rho*) in 30 sec and 6 +/- 2 phosphates are incorporated in 75 sec in response to bleaching 1% of the rhodopsin in the presence of 1 mM [gamma-32P]ATP and 0.1 mM nonradioactive GTP.	Phosphates	21-31	rhodopsin	Bos taurus	62-71
6099932-2	1984	For example, 4 +/- 1 phosphates are incorporated per bleached rhodopsin (Rho*) in 30 sec and 6 +/- 2 phosphates are incorporated in 75 sec in response to bleaching 1% of the rhodopsin in the presence of 1 mM [gamma-32P]ATP and 0.1 mM nonradioactive GTP.	Guanosine Triphosphate	249-252	rhodopsin	Bos taurus	174-183
6099932-3	1984	Omission of GTP leads to ca 70% inhibition of rhodopsin phosphorylation, presumably due to the GTP-binding protein blocking access of rhodopsin kinase to rhodopsin.	Guanosine Triphosphate	12-15	rhodopsin	Bos taurus	46-55
6099932-3	1984	Omission of GTP leads to ca 70% inhibition of rhodopsin phosphorylation, presumably due to the GTP-binding protein blocking access of rhodopsin kinase to rhodopsin.	Guanosine Triphosphate	12-15	rhodopsin	Bos taurus	134-143
6099932-3	1984	Omission of GTP leads to ca 70% inhibition of rhodopsin phosphorylation, presumably due to the GTP-binding protein blocking access of rhodopsin kinase to rhodopsin.	Guanosine Triphosphate	95-98	rhodopsin	Bos taurus	46-55
6099932-3	1984	Omission of GTP leads to ca 70% inhibition of rhodopsin phosphorylation, presumably due to the GTP-binding protein blocking access of rhodopsin kinase to rhodopsin.	Guanosine Triphosphate	95-98	rhodopsin	Bos taurus	134-143
6099932-5	1984	The kinetics of rhodopsin phosphorylation vary with conditions and from preparation to preparation, however, they are always at least as fast as the ATP dependent quenching of PDE activation.	Adenosine Triphosphate	149-152	rhodopsin	Bos taurus	16-25
6099932-10	1984	However, in the presence of ATP the extent of the removal of C-terminal rhodopsin residues has large effects on the light activation and the shut-off of PDE.	Adenosine Triphosphate	28-31	rhodopsin	Bos taurus	72-81
6679755-2	1983	Carboxymethylated bovine rhodopsin was subjected to cyanogen bromide cleavage at methionine residues.	Cyanogen Bromide	52-68	rhodopsin	Bos taurus	25-34
6580636-8	1983	Therefore, the environment in the retinal rod outer segment disk membranes characterized by the broad resonance may arise from the influence of the integral membrane protein rhodopsin on the membrane phospholipid bilayer.	Phospholipids	200-212	rhodopsin	Bos taurus	174-183
6315431-3	1983	In particular the GTP-binding protein (G) has the same subunit composition, the same abundance relative to rhodopsin (1/10) and it undergoes the same light and nucleotide-dependent interactions with rhodopsin in both preparations.	Guanosine Triphosphate	18-21	rhodopsin	Bos taurus	199-208
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Diphosphate	201-204	rhodopsin	Bos taurus	71-80
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Triphosphate	205-208	rhodopsin	Bos taurus	71-80
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Triphosphate	265-268	rhodopsin	Bos taurus	71-80
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Triphosphate	265-268	rhodopsin	Bos taurus	71-80
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Diphosphate	317-320	rhodopsin	Bos taurus	71-80
6315431-4	1983	Previous work on cattle rod outer segments has shown that photoexcited rhodopsin (R*), in a state identified with metarhodopsin II, associates with the G protein as a first step to the light-activated GDP/GTP exchange on G. The complex R*-G is stable in absence of GTP, but is rapidly dissociated by GTP owing to the GDP/GTP exchange reaction.	Guanosine Triphosphate	265-268	rhodopsin	Bos taurus	71-80
6679755-2	1983	Carboxymethylated bovine rhodopsin was subjected to cyanogen bromide cleavage at methionine residues.	Methionine	81-91	rhodopsin	Bos taurus	25-34
6679755-4	1983	Gel-filtration on Bio-Gel P-30 in 80% formic acid of each group followed by rechromatography and high performance liquid chromatography resulted in 15 peptides embracing the whole polypeptide chain of rhodopsin.	formic acid	38-49	rhodopsin	Bos taurus	201-210
6870827-4	1983	The sequence analysis of the latter showed that the retinal-binding lysine residue was located at position 296 from the N-terminal of rhodopsin (or residue 53 from the C-terminal).	Lysine	68-74	rhodopsin	Bos taurus	134-143
6136509-4	1983	Previous studies have demonstrated that photolyzed rhodopsin catalyzed the exchange of GTP for GDP bound to transducin.	Guanosine Triphosphate	87-90	rhodopsin	Bos taurus	51-60
6136509-4	1983	Previous studies have demonstrated that photolyzed rhodopsin catalyzed the exchange of GTP for GDP bound to transducin.	Guanosine Diphosphate	95-98	rhodopsin	Bos taurus	51-60
6136510-11	1983	These results indicate that the guanine nucleotide binding and rhodopsin binding sites are located in topologically distinct regions of the T alpha subunit and proved evidence that a large conformational transition of the molecule occurs upon the conversion of the bound GDP to GTP.	Guanosine Diphosphate	271-274	rhodopsin	Bos taurus	63-72
6136510-11	1983	These results indicate that the guanine nucleotide binding and rhodopsin binding sites are located in topologically distinct regions of the T alpha subunit and proved evidence that a large conformational transition of the molecule occurs upon the conversion of the bound GDP to GTP.	Guanosine Triphosphate	278-281	rhodopsin	Bos taurus	63-72
6626668-0	1983	Picosecond kinetic absorption and fluorescence studies of bovine rhodopsin with a fixed 11-ene.	11-ene	88-94	rhodopsin	Bos taurus	65-74
6882742-4	1983	In each sample, a fraction of one of the three phospholipids was labeled with 14N spin-label while a 15N spin-labeled fatty acid was covalently linked to rhodopsin.	15n	101-104	rhodopsin	Bos taurus	154-163
6882742-4	1983	In each sample, a fraction of one of the three phospholipids was labeled with 14N spin-label while a 15N spin-labeled fatty acid was covalently linked to rhodopsin.	Fatty Acids	118-128	rhodopsin	Bos taurus	154-163
6882742-6	1983	It was found that all three spin-labeled phospholipids utilized for these experiments can interact magnetically with the spin-labeled rhodopsin.	Phospholipids	41-54	rhodopsin	Bos taurus	134-143
6882742-8	1983	Calculation of the diffusion constant of the phospholipids at the boundary of rhodopsin proves that the lifetime of the phospholipids at the protein boundary is short and that no long-lived annular lipids are segregated.	Phospholipids	45-58	rhodopsin	Bos taurus	78-87
6882742-8	1983	Calculation of the diffusion constant of the phospholipids at the boundary of rhodopsin proves that the lifetime of the phospholipids at the protein boundary is short and that no long-lived annular lipids are segregated.	Phospholipids	120-133	rhodopsin	Bos taurus	78-87
6222914-4	1983	The substrate for these studies was bovine rhodopsin labeled by in vitro techniques with [3H]-glucosamine or [3H]-mannose, the former being the derivative most extensively examined.	Tritium	90-92	rhodopsin	Bos taurus	43-52
6222914-4	1983	The substrate for these studies was bovine rhodopsin labeled by in vitro techniques with [3H]-glucosamine or [3H]-mannose, the former being the derivative most extensively examined.	Glucosamine	94-105	rhodopsin	Bos taurus	43-52
6222914-4	1983	The substrate for these studies was bovine rhodopsin labeled by in vitro techniques with [3H]-glucosamine or [3H]-mannose, the former being the derivative most extensively examined.	Tritium	110-112	rhodopsin	Bos taurus	43-52
6222914-4	1983	The substrate for these studies was bovine rhodopsin labeled by in vitro techniques with [3H]-glucosamine or [3H]-mannose, the former being the derivative most extensively examined.	Mannose	114-121	rhodopsin	Bos taurus	43-52
6222914-12	1983	Although stable as a crude extract, the activity of the rhodopsin-cleaving enzyme, as well as the bovine serum albumin (BSA)-cleaving enzyme (cathepsin-D) were rapidly lost upon purification by DEAE-Sephacel and pepstatin-Sepharose.	deae-sephacel	194-207	rhodopsin	Bos taurus	56-65
6222914-12	1983	Although stable as a crude extract, the activity of the rhodopsin-cleaving enzyme, as well as the bovine serum albumin (BSA)-cleaving enzyme (cathepsin-D) were rapidly lost upon purification by DEAE-Sephacel and pepstatin-Sepharose.	pepstatin	212-221	rhodopsin	Bos taurus	56-65
6222914-12	1983	Although stable as a crude extract, the activity of the rhodopsin-cleaving enzyme, as well as the bovine serum albumin (BSA)-cleaving enzyme (cathepsin-D) were rapidly lost upon purification by DEAE-Sephacel and pepstatin-Sepharose.	Sepharose	222-231	rhodopsin	Bos taurus	56-65
6222914-14	1983	Using N-retinylopsin as a substrate for the rhodopsin-cleaving enzyme, it was shown that the regions of the cleavage products containing vitamin A were not associated with the glycopeptide.	Vitamin A	137-146	rhodopsin	Bos taurus	44-53
6849933-13	1983	Exposure of rod outer segments or rhodopsin to antioxidants or removal of phospholipids led to an alteration in the relative abundance of the multiple isoelectric forms, but not to a change in their isoelectric point.	Phospholipids	74-87	rhodopsin	Bos taurus	34-43
6850048-3	1983	In contrast, proteolytic digestion of rhodopsin phosphorylated at -10 degrees C released negligible amounts of phosphate-containing peptides.	Phosphates	111-120	rhodopsin	Bos taurus	38-47
6296072-2	1983	ATP reduced both initial velocity (V0) and turn off time (toff) of phosphodiesterase activated by a flash that bleached 1.5 X 10(-5) of the rhodopsin present.	Adenosine Triphosphate	0-3	rhodopsin	Bos taurus	140-149
6296072-6	1983	Thermolysin cleavage of rhodopsin"s COOH-terminal dodecapeptide eliminated ATP"s effect on toff, but did not diminish its effect on V0.	Adenosine Triphosphate	75-78	rhodopsin	Bos taurus	24-33
6296072-7	1983	Thus, the effects of ATP and kinase on V0 may be mediated by sites proximal to and effects on toff by sites distal to the thermolysin cleavage point at rhodopsin"s COOH-terminal end.	Adenosine Triphosphate	21-24	rhodopsin	Bos taurus	152-161
6342691-1	1983	We have isolated 16 peptides from a cyanogen bromide digest of rhodopsin.	Cyanogen Bromide	36-52	rhodopsin	Bos taurus	63-72
6291939-17	1982	The shift is reversed by GTP, which dissociates the rhodopsin--GTP-binding protein complex.	Guanosine Triphosphate	25-28	rhodopsin	Bos taurus	52-61
6342691-3	1983	Methionine-containing peptides from other chemical and enzymatic digests of rhodopsin have allowed us to place the cyanogen bromide peptides in order, yielding the sequence of the protein.	Methionine	0-10	rhodopsin	Bos taurus	76-85
6342691-3	1983	Methionine-containing peptides from other chemical and enzymatic digests of rhodopsin have allowed us to place the cyanogen bromide peptides in order, yielding the sequence of the protein.	Cyanogen Bromide	115-131	rhodopsin	Bos taurus	76-85
6603057-7	1983	One and a half times more bleached rhodopsin is required to compete to the same extent as unbleached rhodopsin when the RIA is performed in digitonin.	Digitonin	140-149	rhodopsin	Bos taurus	35-44
6603057-7	1983	One and a half times more bleached rhodopsin is required to compete to the same extent as unbleached rhodopsin when the RIA is performed in digitonin.	Digitonin	140-149	rhodopsin	Bos taurus	101-110
6279394-0	1982	Light-induced interactions between rhodopsin and the GTP-binding protein.	Guanosine Triphosphate	53-56	rhodopsin	Bos taurus	35-44
6279394-7	1982	The signal observed in the presence of GTP has been interpreted as being related to the rhodopsin-catalyzed exchange of GTP for GDP bound to the GTP-binding protein, i.e. to the formation of the activator of the cGMP phosphodiesterase [B.K.K.	Guanosine Triphosphate	39-42	rhodopsin	Bos taurus	88-97
6279394-7	1982	The signal observed in the presence of GTP has been interpreted as being related to the rhodopsin-catalyzed exchange of GTP for GDP bound to the GTP-binding protein, i.e. to the formation of the activator of the cGMP phosphodiesterase [B.K.K.	Guanosine Triphosphate	120-123	rhodopsin	Bos taurus	88-97
6279394-7	1982	The signal observed in the presence of GTP has been interpreted as being related to the rhodopsin-catalyzed exchange of GTP for GDP bound to the GTP-binding protein, i.e. to the formation of the activator of the cGMP phosphodiesterase [B.K.K.	Guanosine Diphosphate	128-131	rhodopsin	Bos taurus	88-97
6279394-7	1982	The signal observed in the presence of GTP has been interpreted as being related to the rhodopsin-catalyzed exchange of GTP for GDP bound to the GTP-binding protein, i.e. to the formation of the activator of the cGMP phosphodiesterase [B.K.K.	Guanosine Triphosphate	120-123	rhodopsin	Bos taurus	88-97
7098866-0	1982	Structural analysis of carbohydrate moiety of bovine rhodopsin.	Carbohydrates	23-35	rhodopsin	Bos taurus	53-62
6275924-5	1982	For the phosphatidylcholine spin label there are effectively 55 +/- 5 lipids/200,000-dalton cytochrome oxidase, 58 +/- 4 mol lipid/265,000 dalton (Na+, K+)-ATPase, and 24 +/- 3 and 22 +/- 2 mol lipid/37,000 dalton rhodopsin for the bovine and frog preparations, respectively.	Phosphatidylcholines	8-27	rhodopsin	Bos taurus	214-223
6892133-10	1982	The total binding capacity was estimated to represent 4-5% of the retinol released from a total rhodopsin bleach.	Vitamin A	66-73	rhodopsin	Bos taurus	96-105
6979137-0	1982	[Fatty acid composition of the bilayer phospholipids in the photoreceptor membranes and aminophospholipids from the rhodopsin microenvironment of warm-blooded and cold-blooded vertebrates].	aminophospholipids	88-106	rhodopsin	Bos taurus	116-125
6979137-1	1982	Studies have been made on the distribution of phospholipids between rhodopsin and free lipids of photoreceptor membranes of the outer segments of retinal rods from cattle, frog Rana temporaria and fish Teragra chalcogramma.	Phospholipids	46-59	rhodopsin	Bos taurus	68-77
6979137-2	1982	comparative investigation of fatty acid composition of phospholipids from rhodopsin microboundary and lipid bilayer in photoreceptor membranes was made as well.	Fatty Acids	29-39	rhodopsin	Bos taurus	74-83
6979137-2	1982	comparative investigation of fatty acid composition of phospholipids from rhodopsin microboundary and lipid bilayer in photoreceptor membranes was made as well.	Phospholipids	55-68	rhodopsin	Bos taurus	74-83
6979137-3	1982	Amino phospholipids from rhodopsin microboundry were revealed using glutaraldehyde.	amino phospholipids	0-19	rhodopsin	Bos taurus	25-34
6979137-3	1982	Amino phospholipids from rhodopsin microboundry were revealed using glutaraldehyde.	Glutaral	68-82	rhodopsin	Bos taurus	25-34
6979137-6	1982	It was demonstrated that fatty acid composition of phospholipids of lipid bilayer differs from that of amino phospholipids from rhodopsin microboundary.	amino phospholipids	103-122	rhodopsin	Bos taurus	128-137
6979137-7	1982	In the animals investigated, fatty acids of phospholipids from lipid bilayer were found to be more unsaturated than fatty acids of amino phospholipids from rhodopsin microboundary.	Fatty Acids	116-127	rhodopsin	Bos taurus	156-165
19431487-0	1982	P NMR investigation of rhodopsin-phospholipid interactions in bovine rod outer segment disk membranes.	Phospholipids	33-45	rhodopsin	Bos taurus	23-32
6222537-1	1982	Twenty two compounds, bearing some structural similarity either to the ring-end or aldehyde-end of 11-cis-retinal, have been screened for their effectiveness in decreasing the rate of regeneration of rhodopsin in vitro from 11-cis retinal and bovine opsin.	Aldehydes	83-91	rhodopsin	Bos taurus	200-209
6305022-2	1982	Intact bovine ROS showed a total nucleotide concentration of 1.0 mM, ATP and GTP being the major components (0.1-0.2 mol per mol of rhodopsin).	ros	14-17	rhodopsin	Bos taurus	132-141
6979137-7	1982	In the animals investigated, fatty acids of phospholipids from lipid bilayer were found to be more unsaturated than fatty acids of amino phospholipids from rhodopsin microboundary.	amino phospholipids	131-150	rhodopsin	Bos taurus	156-165
6794609-15	1981	The maximum stoichiometry is approximately 1 mol of calcium release per mol of rhodopsin bleached.	Calcium	52-59	rhodopsin	Bos taurus	79-88
7275981-1	1981	Two sulfhydryl groups of bovine rhodopsin, available for chemical modification only after bleaching, were specifically labeled with radioactive iodoacetamide.	Iodoacetamide	144-157	rhodopsin	Bos taurus	32-41
6264958-4	1981	For the 14-doxyl stearic acid spin label this more immobilized component has an outer splitting of 59 G at 0 degrees C, with a considerable temperature dependence, the effective outer splitting decreasing to 54 G at 24 degrees C. Spin label lipid chains covalently attached to rhodopsin can also display a two-component spectrum in rod outer segment membranes.	14-doxylstearic acid	8-29	rhodopsin	Bos taurus	277-286
7272450-0	1981	Flash photolysis and low temperature photochemistry of bovine rhodopsin with a fixed 11-ene.	11-ene	85-91	rhodopsin	Bos taurus	62-71
7322116-4	1981	Photoregenerated rhodopsin is identical to unbleached rhodopsin in spectra and in stability to NH2OH.	Hydroxylamine	95-100	rhodopsin	Bos taurus	17-26
7236851-1	1981	The relative quantum yields of the photoreactions Rhodopsin in equilibrium Bathorhodopsin in equilibrium Isorhodopsin over an extended wavelength region have been determined in cattle and squid rhodopsins at 77 degrees K. The quantum yields were found to be wavelength independent and unchanged for samples suspended in D2O.	Deuterium Oxide	320-323	rhodopsin	Bos taurus	50-59
6452903-2	1981	When 9-cis- 13-dm-rhodopsin was irradiated at-190 degrees C, batho-13-dm-rhodopsin was produced.	9-cis- 13-dm	5-17	rhodopsin	Bos taurus	18-27
6786333-1	1981	The metabolism of the chromophore of rhodopsin in the cytosol compartment of isolated intact cattle rod outer segments was used as an indicator for changes of the cytosolic Mg2+ and Ca2+ concentration upon changes of the external Mg2+ and Ca2+ concentration.	magnesium ion	173-177	rhodopsin	Bos taurus	37-46
6786333-1	1981	The metabolism of the chromophore of rhodopsin in the cytosol compartment of isolated intact cattle rod outer segments was used as an indicator for changes of the cytosolic Mg2+ and Ca2+ concentration upon changes of the external Mg2+ and Ca2+ concentration.	magnesium ion	230-234	rhodopsin	Bos taurus	37-46
6786333-2	1981	The reduction of retinal to retinol upon photolysis of rhodopsin in situ in intact rod outer segments was critically dependent on the availability of cytosolic Mg2+.	Vitamin A	28-35	rhodopsin	Bos taurus	55-64
6786333-2	1981	The reduction of retinal to retinol upon photolysis of rhodopsin in situ in intact rod outer segments was critically dependent on the availability of cytosolic Mg2+.	magnesium ion	160-164	rhodopsin	Bos taurus	55-64
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	57-65	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	57-65	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	lumi-13-dm	102-112	rhodopsin	Bos taurus	66-75
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	lumi-13-dm	102-112	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	lumi-13-dm	102-112	rhodopsin	Bos taurus	113-122
6452903-2	1981	When 9-cis- 13-dm-rhodopsin was irradiated at-190 degrees C, batho-13-dm-rhodopsin was produced.	9-cis- 13-dm	5-17	rhodopsin	Bos taurus	73-82
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	57-65	rhodopsin	Bos taurus	66-75
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	57-65	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	57-65	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	lumi-13-dm	102-112	rhodopsin	Bos taurus	113-122
7248356-2	1980	It was found that similar to bovine rhodopsin, the protein from wall-eyed pollock contains in its carbohydrate moiety only two types of monosaccharides, i. e. mannose and glucosamine (1,78 +/- 0,13 moles of mannose per one mole of glucosamine).	Carbohydrates	98-110	rhodopsin	Bos taurus	36-45
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	lumi-13-dm	102-112	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	146-154	rhodopsin	Bos taurus	66-75
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	146-154	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	146-154	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	146-154	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	bl-13-dm	146-154	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	batho-13-dm	232-243	rhodopsin	Bos taurus	66-75
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	batho-13-dm	232-243	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	batho-13-dm	232-243	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	batho-13-dm	232-243	rhodopsin	Bos taurus	113-122
6452903-5	1981	Above-180 degrees C, it converted to a new intermediate, BL-13-dm-rhodopsin, which in turn changed to lumi-13-dm-rhodopsin- above -140 degrees C. BL-13-dm-rhodopsin was "photosensitive" at temperatures around -188 degrees C, though batho-13-dm-rhodopsin and lumi-13-dm-rhodopsin was "photosensitive" at the same temperature.	batho-13-dm	232-243	rhodopsin	Bos taurus	113-122
6450610-1	1980	A dipeptide containing the binding site for retinal in bovine rhodopsin has been isolated and its sequence determined.	Dipeptides	2-11	rhodopsin	Bos taurus	62-71
6450610-2	1980	Rhodopsin containing [11-3H]retinal was prepared in chromatographically pure form, and the [3H]retinal was reductively linked to its binding site on opsin by using borane--dimethylamine.	Tritium	25-27	rhodopsin	Bos taurus	0-9
6450610-2	1980	Rhodopsin containing [11-3H]retinal was prepared in chromatographically pure form, and the [3H]retinal was reductively linked to its binding site on opsin by using borane--dimethylamine.	Tritium	92-94	rhodopsin	Bos taurus	0-9
6450610-2	1980	Rhodopsin containing [11-3H]retinal was prepared in chromatographically pure form, and the [3H]retinal was reductively linked to its binding site on opsin by using borane--dimethylamine.	borane--dimethylamine	164-185	rhodopsin	Bos taurus	0-9
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	Tritium	123-125	rhodopsin	Bos taurus	71-80
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	Tritium	123-125	rhodopsin	Bos taurus	134-143
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	Tritium	123-125	rhodopsin	Bos taurus	134-143
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	sodium borohydride	197-215	rhodopsin	Bos taurus	71-80
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	sodium borohydride	197-215	rhodopsin	Bos taurus	134-143
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	sodium borohydride	197-215	rhodopsin	Bos taurus	134-143
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	borane--dimethylamine	219-240	rhodopsin	Bos taurus	71-80
6450610-5	1980	The retinyl binding site is located in the carboxyl-terminal region of rhodopsin: when rod cell disk membranes containing [3H]retinal rhodopsin were digested with thermolysin and then reacted with sodium borohydride or borane--dimethylamine, [3H]retinal was reduced onto the F2 (Mr congruent to 6000) fragment, which derives from rhodopsin"s carboxyl-terminal region.	Tritium	243-245	rhodopsin	Bos taurus	71-80
7248356-0	1980	[Carbohydrate composition of wall-eyed pollock rhodopsin].	Carbohydrates	1-13	rhodopsin	Bos taurus	47-56
7248356-1	1980	Using gas-liquid and column chromatography, the carbohydrate composition of the visual protein rhodopsin from wall-eyed pollock purified by SDS-electrophoresis was studied.	Carbohydrates	48-60	rhodopsin	Bos taurus	95-104
7225464-0	1981	Chemical cleavage of bovine rhodopsin at tryptophanyl bonds; characterization of the polypeptide fragments and the phosphorylated site.	tryptophanyl	41-53	rhodopsin	Bos taurus	28-37
7225464-1	1981	Bovine rhodopsin from retinal rod photoreceptors, a protein of 39,000 molecular weight, was cleaved by BNPS-Skatole at the level of tryptophanyl bonds.	Skatole	108-115	rhodopsin	Bos taurus	7-16
7225464-4	1981	S2, S3 and S4 contain the glycanes of native rhodopsin and their N-termini are blocked.	glycanes	26-34	rhodopsin	Bos taurus	45-54
7248356-1	1980	Using gas-liquid and column chromatography, the carbohydrate composition of the visual protein rhodopsin from wall-eyed pollock purified by SDS-electrophoresis was studied.	Sodium Dodecyl Sulfate	140-143	rhodopsin	Bos taurus	95-104
7248356-2	1980	It was found that similar to bovine rhodopsin, the protein from wall-eyed pollock contains in its carbohydrate moiety only two types of monosaccharides, i. e. mannose and glucosamine (1,78 +/- 0,13 moles of mannose per one mole of glucosamine).	Monosaccharides	136-151	rhodopsin	Bos taurus	36-45
7248356-2	1980	It was found that similar to bovine rhodopsin, the protein from wall-eyed pollock contains in its carbohydrate moiety only two types of monosaccharides, i. e. mannose and glucosamine (1,78 +/- 0,13 moles of mannose per one mole of glucosamine).	Mannose	159-166	rhodopsin	Bos taurus	36-45
7248356-2	1980	It was found that similar to bovine rhodopsin, the protein from wall-eyed pollock contains in its carbohydrate moiety only two types of monosaccharides, i. e. mannose and glucosamine (1,78 +/- 0,13 moles of mannose per one mole of glucosamine).	Glucosamine	171-182	rhodopsin	Bos taurus	36-45
7248356-3	1980	One mole of rhodopsin contains 9,43 +/- 1,5 moles of mannose and 5,3 moles of glucosamine.	Mannose	53-60	rhodopsin	Bos taurus	12-21
7248356-3	1980	One mole of rhodopsin contains 9,43 +/- 1,5 moles of mannose and 5,3 moles of glucosamine.	Glucosamine	78-89	rhodopsin	Bos taurus	12-21
7248356-4	1980	The data obtained suggest a similarity of the carbohydrate component of wall-eyed pollock rhodopsin to that of the traditional object--bovine rhodopsin.	Carbohydrates	46-58	rhodopsin	Bos taurus	90-99
7248356-4	1980	The data obtained suggest a similarity of the carbohydrate component of wall-eyed pollock rhodopsin to that of the traditional object--bovine rhodopsin.	Carbohydrates	46-58	rhodopsin	Bos taurus	142-151
7407117-8	1980	The rhodopsin preparation in which cholate was exchanged for digitonin gave almost the same CD, thermal stability and regenerability as those of native rhodopsin in the membrane but metarhodopsin I still retained its long lifetime.	Cadmium	92-94	rhodopsin	Bos taurus	4-13
7407117-0	1980	Further characterization of the lipid-depleted bovine rhodopsin obtained by cholate-ammonium sulfate fractionation.	Cholates	76-83	rhodopsin	Bos taurus	54-63
7439323-3	1980	Assay of the final preparation for rhodopsin content gives a ratio of 2.4 for DO280nm/DO498nm.	do280nm	78-85	rhodopsin	Bos taurus	35-44
7439323-3	1980	Assay of the final preparation for rhodopsin content gives a ratio of 2.4 for DO280nm/DO498nm.	do498	86-91	rhodopsin	Bos taurus	35-44
7407117-0	1980	Further characterization of the lipid-depleted bovine rhodopsin obtained by cholate-ammonium sulfate fractionation.	Ammonium Sulfate	84-100	rhodopsin	Bos taurus	54-63
7407117-1	1980	The rhodopsin preparation obtained by the method of ammonium sulfate fractionation contained 3-6 mol phospholipid and about 18 mol cholate per mol rhodopsin.	Ammonium Sulfate	52-68	rhodopsin	Bos taurus	4-13
7407117-1	1980	The rhodopsin preparation obtained by the method of ammonium sulfate fractionation contained 3-6 mol phospholipid and about 18 mol cholate per mol rhodopsin.	Phospholipids	101-113	rhodopsin	Bos taurus	4-13
7407117-1	1980	The rhodopsin preparation obtained by the method of ammonium sulfate fractionation contained 3-6 mol phospholipid and about 18 mol cholate per mol rhodopsin.	Cholates	131-138	rhodopsin	Bos taurus	4-13
7407117-2	1980	The purified rhodopsin had 74% helical structure and showed a visible CD spectrum different from that of rhodopsin in the membrane.	Cadmium	70-72	rhodopsin	Bos taurus	13-22
7407117-5	1980	50 mol of phosphatidylcholine were maximally bound to 1 mol rhodopsin when the purified rhodopsin was mixed with phosphatidylcholine in 0.5% cholate.	Phosphatidylcholines	10-29	rhodopsin	Bos taurus	60-69
7397132-0	1980	Circular dichroism of cattle rhodopsin and bathorhodopsin at liquid nitrogen temperatures.	Nitrogen	68-76	rhodopsin	Bos taurus	29-38
7407117-5	1980	50 mol of phosphatidylcholine were maximally bound to 1 mol rhodopsin when the purified rhodopsin was mixed with phosphatidylcholine in 0.5% cholate.	Phosphatidylcholines	10-29	rhodopsin	Bos taurus	88-97
7407117-5	1980	50 mol of phosphatidylcholine were maximally bound to 1 mol rhodopsin when the purified rhodopsin was mixed with phosphatidylcholine in 0.5% cholate.	Phosphatidylcholines	113-132	rhodopsin	Bos taurus	60-69
7407117-5	1980	50 mol of phosphatidylcholine were maximally bound to 1 mol rhodopsin when the purified rhodopsin was mixed with phosphatidylcholine in 0.5% cholate.	Cholates	141-148	rhodopsin	Bos taurus	60-69
7407117-5	1980	50 mol of phosphatidylcholine were maximally bound to 1 mol rhodopsin when the purified rhodopsin was mixed with phosphatidylcholine in 0.5% cholate.	Cholates	141-148	rhodopsin	Bos taurus	88-97
7407117-8	1980	The rhodopsin preparation in which cholate was exchanged for digitonin gave almost the same CD, thermal stability and regenerability as those of native rhodopsin in the membrane but metarhodopsin I still retained its long lifetime.	Cholates	35-42	rhodopsin	Bos taurus	4-13
7407117-8	1980	The rhodopsin preparation in which cholate was exchanged for digitonin gave almost the same CD, thermal stability and regenerability as those of native rhodopsin in the membrane but metarhodopsin I still retained its long lifetime.	Digitonin	61-70	rhodopsin	Bos taurus	4-13
7407235-0	1980	The N-terminal residue of bovine rhodopsin is acetylmethionine.	N-acetylmethionine	46-62	rhodopsin	Bos taurus	33-42
7397132-4	1980	The measurement of circular dichroism of rhodopsin extract (containing 66% or 75% of glycerol) at liquid nitrogen temperatures (-195 degrees C) by a conventional spectropolarimeter induced an extraordinary large signal, owing to linear dichroism originated from conversion of rhodopsin to bathorhodopsin by the measuring light.	Glycerol	85-93	rhodopsin	Bos taurus	41-50
7397132-4	1980	The measurement of circular dichroism of rhodopsin extract (containing 66% or 75% of glycerol) at liquid nitrogen temperatures (-195 degrees C) by a conventional spectropolarimeter induced an extraordinary large signal, owing to linear dichroism originated from conversion of rhodopsin to bathorhodopsin by the measuring light.	Glycerol	85-93	rhodopsin	Bos taurus	276-285
7397132-4	1980	The measurement of circular dichroism of rhodopsin extract (containing 66% or 75% of glycerol) at liquid nitrogen temperatures (-195 degrees C) by a conventional spectropolarimeter induced an extraordinary large signal, owing to linear dichroism originated from conversion of rhodopsin to bathorhodopsin by the measuring light.	Nitrogen	105-113	rhodopsin	Bos taurus	41-50
7397132-8	1980	The change of the positive sign to negative one at alpha-band of circular dichroism spectrum supports the hypothesis that the conversion of rhodopsin is due to rotation of the chromophoric retinal about C-11--12 double bond ("photoisomerization model").	Carbon	203-204	rhodopsin	Bos taurus	140-149
6252443-2	1980	The constant levels of phosphorylation, reached within 10--15 min, are 100 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP and 2--4 pmol 32P/nmol of rhodopsin for [gamma-32P]GTP.	Phosphorus-32	87-90	rhodopsin	Bos taurus	99-108
6252443-2	1980	The constant levels of phosphorylation, reached within 10--15 min, are 100 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP and 2--4 pmol 32P/nmol of rhodopsin for [gamma-32P]GTP.	[gamma-32p]atp	113-127	rhodopsin	Bos taurus	99-108
6252443-2	1980	The constant levels of phosphorylation, reached within 10--15 min, are 100 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP and 2--4 pmol 32P/nmol of rhodopsin for [gamma-32P]GTP.	Phosphorus-32	120-123	rhodopsin	Bos taurus	99-108
6252443-2	1980	The constant levels of phosphorylation, reached within 10--15 min, are 100 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP and 2--4 pmol 32P/nmol of rhodopsin for [gamma-32P]GTP.	GTP-Gamma-32P	168-182	rhodopsin	Bos taurus	99-108
6252443-4	1980	In the presence of histone the constant level of phosphorylation is increased up to 200 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP, but is not changed when [gamma-32P]GTP is used.	Phosphorus-32	100-103	rhodopsin	Bos taurus	112-121
6252443-4	1980	In the presence of histone the constant level of phosphorylation is increased up to 200 +/- 30 pmol 32P/nmol of rhodopsin for [gamma-32P]ATP, but is not changed when [gamma-32P]GTP is used.	[gamma-32p]atp	126-140	rhodopsin	Bos taurus	112-121
7378353-0	1980	Tryptophan in bovine rhodopsin: its content, spectral properties and environment.	Tryptophan	0-10	rhodopsin	Bos taurus	21-30
7378353-1	1980	The tryptophan content of purified bovine rhodopsin was obtained by two independent methods: direct analysis of hydrolysates prepared by digestion of opsin with methanesulfonic acid containing 0.2% 3-(2-aminoethyl)indole and a computer-assisted analysis of the near-UV spectrum of rhodopsin.	Tryptophan	4-14	rhodopsin	Bos taurus	42-51
7378353-2	1980	Both methods gave a value of eight tryptophan residues per rhodopsin.	Tryptophan	35-45	rhodopsin	Bos taurus	59-68
7378362-3	1980	Upon irradiation of 7-cis-rhodopsin at liquid nitrogen temperature (-190 degrees C) with blue light, its spectrum shifted to the longer wavelengths, indicating the formation of a bathoproduct.	Nitrogen	46-54	rhodopsin	Bos taurus	26-35
41733-0	1979	Ethanolamine attack of the bovine rhodopsin chromophore.	Ethanolamine	0-12	rhodopsin	Bos taurus	34-43
7362819-5	1980	Spectra of delipidated rhodopsin and rhodopsin membranes reconstituted from dioleyl-phosphatidylcholine were compared with native photoreceptor membrane from rod outer segments in order to facilitate peak assgnments.	1,2-oleoylphosphatidylcholine	76-103	rhodopsin	Bos taurus	37-46
6767558-0	1980	[Purification and partial sequence of a hydrophobic polypeptide from BNPS-skatole cleaved bovine rhodopsin].	Skatole	74-81	rhodopsin	Bos taurus	97-106
6767558-1	1980	Rhodopsin isolated from outer segments of cattle retinas was cleaved at tryptophan residues by the BNPS-skatole.	Tryptophan	72-82	rhodopsin	Bos taurus	0-9
6767558-1	1980	Rhodopsin isolated from outer segments of cattle retinas was cleaved at tryptophan residues by the BNPS-skatole.	Skatole	104-111	rhodopsin	Bos taurus	0-9
7260248-3	1980	Our results show that the Schiff base of bathorhodopsin is fully protonated and that the extent of protonation is unaffected by its photochemical formation from either rhodopsin or isorhodopsin.	Schiff Bases	26-37	rhodopsin	Bos taurus	46-55
6243483-2	1980	Purified rhodopsin from bovine retina has been incorporated into phospholipid bilayers.	Phospholipids	65-77	rhodopsin	Bos taurus	9-18
6243483-4	1980	In order to probe the lipid-protein interface specifically, a spin-labeled fatty acid was covalently bound to rhodopsin via an isocyanate reacting group.	Fatty Acids	75-85	rhodopsin	Bos taurus	110-119
6243483-4	1980	In order to probe the lipid-protein interface specifically, a spin-labeled fatty acid was covalently bound to rhodopsin via an isocyanate reacting group.	Isocyanates	127-137	rhodopsin	Bos taurus	110-119
6243483-6	1980	The following results were obtained: (1) The kinetics of reduction by ascorbate of the spin-labeled fatty acid covalently bound to rhodopsin demonstrate that the alkyl chain attached to the protein is positioned in the membrane in the same way as the alkyl chains of a phospholipid.	Ascorbic Acid	70-79	rhodopsin	Bos taurus	131-140
6243483-6	1980	The following results were obtained: (1) The kinetics of reduction by ascorbate of the spin-labeled fatty acid covalently bound to rhodopsin demonstrate that the alkyl chain attached to the protein is positioned in the membrane in the same way as the alkyl chains of a phospholipid.	Fatty Acids	100-110	rhodopsin	Bos taurus	131-140
6243483-6	1980	The following results were obtained: (1) The kinetics of reduction by ascorbate of the spin-labeled fatty acid covalently bound to rhodopsin demonstrate that the alkyl chain attached to the protein is positioned in the membrane in the same way as the alkyl chains of a phospholipid.	Phospholipids	269-281	rhodopsin	Bos taurus	131-140
6243483-16	1980	The differences in the results obtained with the various phosphatidylcholines above their transition temperature suggest that the solubility of rhodopsin in bilayers depends not only on the fluidity of the lipids, but also, to some extent, on the phospholipid chain length.	Phosphatidylcholines	57-77	rhodopsin	Bos taurus	144-153
6243483-16	1980	The differences in the results obtained with the various phosphatidylcholines above their transition temperature suggest that the solubility of rhodopsin in bilayers depends not only on the fluidity of the lipids, but also, to some extent, on the phospholipid chain length.	Phospholipids	247-259	rhodopsin	Bos taurus	144-153
20487738-1	1980	The amino-terminal 39 amino acids of bovine rhodopsin have the sequence where both carbohydrate attachment sites (CHO) contain GlcNAc(3)Man(3).	Carbohydrates	83-95	rhodopsin	Bos taurus	44-53
20487738-1	1980	The amino-terminal 39 amino acids of bovine rhodopsin have the sequence where both carbohydrate attachment sites (CHO) contain GlcNAc(3)Man(3).	CAV protocol	114-117	rhodopsin	Bos taurus	44-53
20487738-1	1980	The amino-terminal 39 amino acids of bovine rhodopsin have the sequence where both carbohydrate attachment sites (CHO) contain GlcNAc(3)Man(3).	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	127-133	rhodopsin	Bos taurus	44-53
20487738-14	1980	1-azldopyrene, a hydrophobic nitrene precursor, is being used to map those regions of the rhodopsin sequence which are located in a hydrophobic environment.	1-azldopyrene	0-13	rhodopsin	Bos taurus	90-99
20487738-14	1980	1-azldopyrene, a hydrophobic nitrene precursor, is being used to map those regions of the rhodopsin sequence which are located in a hydrophobic environment.	phenylnitrene	29-36	rhodopsin	Bos taurus	90-99
20487739-0	1980	The oligosaccharide moiety of rhodopsin-its structure and cellular location.	Oligosaccharides	4-19	rhodopsin	Bos taurus	30-39
20487739-1	1980	The sugar chains of bovine rhodopsin released from opsin by hydrazinolysis were reduced with NaB((3)H)(4) and fractionated by paper chromatography.	Sugars	4-9	rhodopsin	Bos taurus	27-36
20487739-1	1980	The sugar chains of bovine rhodopsin released from opsin by hydrazinolysis were reduced with NaB((3)H)(4) and fractionated by paper chromatography.	nab	93-96	rhodopsin	Bos taurus	27-36
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Sugars	21-26	rhodopsin	Bos taurus	37-46
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Sugars	21-26	rhodopsin	Bos taurus	163-172
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Acetylglucosamine	90-96	rhodopsin	Bos taurus	37-46
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Galactose	107-116	rhodopsin	Bos taurus	37-46
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Sugars	147-152	rhodopsin	Bos taurus	37-46
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	Sugars	147-152	rhodopsin	Bos taurus	163-172
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	((3)h)-galactose	226-242	rhodopsin	Bos taurus	37-46
20487739-5	1980	The structure of the sugar moiety of rhodopsin was thus identified as: Since the terminal GlcNac serves as galactose acceptor, the location of the sugar moiety of rhodopsin in the disc membrane was studied by incorporation of ((3)H)-galactose (from UDP-((3)H)-galactose) into the disk membrane.	udp-((3)h)-galactose	249-269	rhodopsin	Bos taurus	37-46
20487739-6	1980	After inversion of disks by freeze-thawing, rhodopsin in the membrane incorporated one mole of ((3)H)-galactose per mole purified pigment.	((3)h)-galactose	95-111	rhodopsin	Bos taurus	44-53
20487739-8	1980	It was therefore concluded that the sugar moiety of rhodopsin is located on the internal surface of disk membrane.	Sugars	36-41	rhodopsin	Bos taurus	52-61
20487739-11	1980	Since intact sealed rod outer segments bind concanavalin A, the sugar moiety of rhodopsin in the plasma membrane is probably exposed on the external surface of the rod.	Sugars	64-69	rhodopsin	Bos taurus	80-89
486439-9	1979	Based on these results, it was infered that the formation of batho-rhodopsin is due to photoisomerization of the chromophoric retinal of rhodopsin and is not due to translocation of a proton on the ring or on the side chain from C-6 to C-8 of the chromophoric retinal to the Schiff-base nitrogen.	Carbon	229-230	rhodopsin	Bos taurus	67-76
486439-9	1979	Based on these results, it was infered that the formation of batho-rhodopsin is due to photoisomerization of the chromophoric retinal of rhodopsin and is not due to translocation of a proton on the ring or on the side chain from C-6 to C-8 of the chromophoric retinal to the Schiff-base nitrogen.	Schiff Bases	275-286	rhodopsin	Bos taurus	67-76
486439-9	1979	Based on these results, it was infered that the formation of batho-rhodopsin is due to photoisomerization of the chromophoric retinal of rhodopsin and is not due to translocation of a proton on the ring or on the side chain from C-6 to C-8 of the chromophoric retinal to the Schiff-base nitrogen.	Nitrogen	287-295	rhodopsin	Bos taurus	67-76
114221-7	1979	The Scatchard plot of calcium binding of rods indicates the presence of a single set of intradiskal binding sites with a maximal capacity of 8-9 mol calcium/mol rhodopsin and an affinity constant of 55 microM to calcium.	Calcium	22-29	rhodopsin	Bos taurus	161-170
447724-0	1979	Structure of the carbohydrate moieties of bovine rhodopsin.	Carbohydrates	17-29	rhodopsin	Bos taurus	49-58
447724-1	1979	The sugar chains of bovine rhodopsin were released from the polypeptide moiety by hydrazinolysis and reduced with NaB[3H]4 after N-acetylation.	Sugars	4-9	rhodopsin	Bos taurus	27-36
447724-1	1979	The sugar chains of bovine rhodopsin were released from the polypeptide moiety by hydrazinolysis and reduced with NaB[3H]4 after N-acetylation.	nab	114-117	rhodopsin	Bos taurus	27-36
447724-1	1979	The sugar chains of bovine rhodopsin were released from the polypeptide moiety by hydrazinolysis and reduced with NaB[3H]4 after N-acetylation.	Tritium	118-120	rhodopsin	Bos taurus	27-36
114221-7	1979	The Scatchard plot of calcium binding of rods indicates the presence of a single set of intradiskal binding sites with a maximal capacity of 8-9 mol calcium/mol rhodopsin and an affinity constant of 55 microM to calcium.	Calcium	149-156	rhodopsin	Bos taurus	161-170
114221-7	1979	The Scatchard plot of calcium binding of rods indicates the presence of a single set of intradiskal binding sites with a maximal capacity of 8-9 mol calcium/mol rhodopsin and an affinity constant of 55 microM to calcium.	Calcium	149-156	rhodopsin	Bos taurus	161-170
375978-0	1979	Light-induced calcium release in isolated intact cattle rod outer segments upon photoexcitation of rhodopsin.	Calcium	14-21	rhodopsin	Bos taurus	99-108
36143-4	1979	(2) Endogenous cofactors (NADPH, NADPH-regenerating system) are still available in the rod cytosol and consequently retinol is the final photoproduct of photolysis of rhodopsin.	NADP	33-38	rhodopsin	Bos taurus	167-176
36143-4	1979	(2) Endogenous cofactors (NADPH, NADPH-regenerating system) are still available in the rod cytosol and consequently retinol is the final photoproduct of photolysis of rhodopsin.	Vitamin A	116-123	rhodopsin	Bos taurus	167-176
447620-0	1979	Orientation of the rhodopsin sugar moiety in bovine disk membrane.	Sugars	29-34	rhodopsin	Bos taurus	19-28
447620-1	1979	Rhodopsin from the bovine rod outer segment contains a covalently linked carbohydrate moiety (Heller, J.	Carbohydrates	73-85	rhodopsin	Bos taurus	0-9
447620-8	1979	From these experiments we conclude that the carbohydrate moiety of bovine rhodopsin is located on the inner surface of the disk membrane, in agreement with the report by Rohlich on the frog rod outer segment disk membrane (Rohlich, P. (1976) Nature 263, 789--791).	Carbohydrates	44-56	rhodopsin	Bos taurus	74-83
375978-2	1979	It is shown that light-induced calcium signals can be unambiguously discriminated from underlying absorption changes due to photolysis of rhodopsin and apparent absorption changes resulting from lightscattering transients.	Calcium	31-38	rhodopsin	Bos taurus	138-147
375978-6	1979	Photoexcitation of rhodopsin results in calcium release from intradiscal binding sites.	Calcium	40-47	rhodopsin	Bos taurus	19-28
375978-12	1979	The stoichiometric ratio of calcium released/rhodopsin bleached is 0.5 at a free calcium concentration of 2 microM.	Calcium	81-88	rhodopsin	Bos taurus	45-54
375978-13	1979	The amount of calcium released is proportional to the precentage of rhodopsin bleaching (from 1--10%).	Calcium	14-21	rhodopsin	Bos taurus	68-77
427251-0	1979	Interaction of bovine rhodopsin with calcium ions.	Calcium	37-44	rhodopsin	Bos taurus	22-31
427251-4	1979	The regeneration of rhodopsin from opsin by adding 11-cis retinal to ROS-suspensions and rhodopsin digitonin solutions was measured spectrophotometrically.	Digitonin	99-108	rhodopsin	Bos taurus	89-98
427252-0	1979	Interaction of bovine rhodopsin with calcium ions.	Calcium	37-44	rhodopsin	Bos taurus	22-31
427252-2	1979	The calcium content of bovine rod outer segment (ROS) suspensions was determined by flame spectrophotometry to be about 0.2 Ca2+ per molecule rhodopsin.	Calcium	4-11	rhodopsin	Bos taurus	142-151
427252-6	1979	This indicates that a light induced Ca2+-release of 12 calcium ions per photoactivated rhodopsin is coupled in time with the formation of metarhodopsin II.	Calcium	55-62	rhodopsin	Bos taurus	87-96
318532-0	1979	Linear dichroism of rhodopsin in air-water interface films.	Water	37-42	rhodopsin	Bos taurus	20-29
728380-5	1978	This structure can be generated from either rhodopsin or isorhodopsin by a similar motion (simultaneously rotating chromophore carbon atoms 10 and 11 out-of-plane).	Carbon	127-133	rhodopsin	Bos taurus	44-53
217412-6	1979	The reassociated protein kinase is insensitive to exogenous cyclic nucleotides, and it catalyzes the phosphorylation of the membrane protein, bleached rhodopsin.	Nucleotides, Cyclic	60-78	rhodopsin	Bos taurus	151-160
217412-7	1979	While the soluble and membrane-associated protein kinases may be interchangeable, they appear to be modulated by different biological signals; soluble protein kinase activity is increased by cyclic nucleotides whereas membrane-bound activity is enhanced when rhodopsin is bleached by light.	Nucleotides, Cyclic	191-209	rhodopsin	Bos taurus	259-268
718881-2	1978	Squid rhodopsin has positive CD bands at wavelengths corresponding the alpha- and beta-absorption bands at liquid nitrogen temperature (CD maxima: 485 nm at alpha-band and 348 nm at beta-band) as well as at room temperature (CD maxima: 474 nm at alpha-band and 347 nm at beta-band).	Nitrogen	114-122	rhodopsin	Bos taurus	6-15
719048-6	1978	This effect was observed also after the splitting of the rhodopsin fragment by papaine.	papaine	79-86	rhodopsin	Bos taurus	57-66
318532-1	1979	Air-water interface films of purified cattle rhodopsin and defined phospholipids are formed by the osmotic lysis of reconstituted membrane vesicles.	Water	4-9	rhodopsin	Bos taurus	45-54
719068-1	1978	The rate of rhodopsin regeneration in decolorized rod outer segments ROS of pollock and ruff in the presence of exogenous 11Z-retinal is found to depend slightly on the temperature.	ros	69-72	rhodopsin	Bos taurus	12-21
719068-1	1978	The rate of rhodopsin regeneration in decolorized rod outer segments ROS of pollock and ruff in the presence of exogenous 11Z-retinal is found to depend slightly on the temperature.	11z	122-125	rhodopsin	Bos taurus	12-21
719068-7	1978	Trimethylcyclohexene derivatives with a side chain of about 7 carbon atoms and 13Z-retinal competitively inhibited the rhodopsin regeneration in pollock and bovine ROS, while 13E-11, 12-dehydroretinal and all-E-retinal did not effect this process.	1,5,5-Trimethylcyclohexene	0-20	rhodopsin	Bos taurus	119-128
719068-7	1978	Trimethylcyclohexene derivatives with a side chain of about 7 carbon atoms and 13Z-retinal competitively inhibited the rhodopsin regeneration in pollock and bovine ROS, while 13E-11, 12-dehydroretinal and all-E-retinal did not effect this process.	13Z	79-82	rhodopsin	Bos taurus	119-128
719068-7	1978	Trimethylcyclohexene derivatives with a side chain of about 7 carbon atoms and 13Z-retinal competitively inhibited the rhodopsin regeneration in pollock and bovine ROS, while 13E-11, 12-dehydroretinal and all-E-retinal did not effect this process.	ros	164-167	rhodopsin	Bos taurus	119-128
25681-0	1978	[Accessibility of sulfhydryl groups to 5,5"-dithiobis-2-nitrobenzoic acid and acid-base properties of bovine and walleye pollock rhodopsin preparations].	acid-base	78-87	rhodopsin	Bos taurus	129-138
661987-0	1978	Photochemical cis-trans isomerisation of bovine rhodopsin at liquid helium temperatures.	Helium	68-74	rhodopsin	Bos taurus	48-57
699918-3	1978	The infrared peptide exchange data show that the highly hydrophobic nature of rhodopsin is conserved in the presence of the two detergents used: Cemulsol LA 90 and Ammonyx LO.	cemulsol	145-153	rhodopsin	Bos taurus	78-87
699918-3	1978	The infrared peptide exchange data show that the highly hydrophobic nature of rhodopsin is conserved in the presence of the two detergents used: Cemulsol LA 90 and Ammonyx LO.	dodecyldimethylamine oxide	164-174	rhodopsin	Bos taurus	78-87
699918-5	1978	The conformational stability of rhodopsin in these two detergents is also demonstrated by the similarity of the tritium exchange-out kinetics and the infrared amide I band frequencies for both membrane-bound and detergent-solubilised rhodopsin.	Tritium	112-119	rhodopsin	Bos taurus	32-41
699918-5	1978	The conformational stability of rhodopsin in these two detergents is also demonstrated by the similarity of the tritium exchange-out kinetics and the infrared amide I band frequencies for both membrane-bound and detergent-solubilised rhodopsin.	Amides	159-164	rhodopsin	Bos taurus	32-41
699918-6	1978	Upon illumination of rhodopsin (bleaching) in the presence of detergents, the hydrogen exchange rates are greatly increased and shifts in the amide I band frequencies are observed, indicative of a large conformation change.	Hydrogen	78-86	rhodopsin	Bos taurus	21-30
699918-6	1978	Upon illumination of rhodopsin (bleaching) in the presence of detergents, the hydrogen exchange rates are greatly increased and shifts in the amide I band frequencies are observed, indicative of a large conformation change.	Amides	142-147	rhodopsin	Bos taurus	21-30
647004-8	1978	Simple addition of amphipathic lipids, without the use of detergent, restores the rhodopsin properties only in the case of rod outer segment lipids and of didecanoylphosphatidylcholine, and even then only occasionally.	didecanoylphosphatidylcholine	155-184	rhodopsin	Bos taurus	82-91
647004-12	1978	Presumably, the uniquely high phospholipid unsaturation of rod outer segment membranes is important for another, as yet unassessed, function of rhodopsin or the photoreceptor membrane.	Phospholipids	30-42	rhodopsin	Bos taurus	144-153
25681-9	1978	After proteolysis of ROS with papain, a fragment with molecular weight 24500 +/- 1000 was detected, which contained the same number of SH-groups and cysteine residues as in the case of intact rhodopsin.	ros	21-24	rhodopsin	Bos taurus	192-201
25681-2	1978	The preparations studied can be arranged in the order of increase of these parameters as follows: ROS less than rhodopsin extracted by digitonin less than triton X-100 less than cetyltrimethylammonium bromide (CTAB) less than sodium dodecylsulphate (SDS).	Digitonin	135-144	rhodopsin	Bos taurus	112-121
25681-3	1978	After illumination of ROS and digitonin, triton X-100 and CTAB-solubilized rhodopsin, and increase was observed in the number of modified SH-groups.	ros	22-25	rhodopsin	Bos taurus	75-84
25681-3	1978	After illumination of ROS and digitonin, triton X-100 and CTAB-solubilized rhodopsin, and increase was observed in the number of modified SH-groups.	Digitonin	30-39	rhodopsin	Bos taurus	75-84
25681-3	1978	After illumination of ROS and digitonin, triton X-100 and CTAB-solubilized rhodopsin, and increase was observed in the number of modified SH-groups.	Cetrimonium	58-62	rhodopsin	Bos taurus	75-84
41159-1	1978	Reactions of the sulfhydryl groups of bovine rhodopsin in rod outer segment membranes have been investigated using 4,4"-dithiopyridine.	4,4'-dipyridyl disulfide	115-134	rhodopsin	Bos taurus	45-54
27004-0	1978	Kinetics of cryanoborohydride reduction of bovine rhodopsin.	cryanoborohydride	12-29	rhodopsin	Bos taurus	50-59
901803-7	1977	When ammonium sulfate is added to the sonicated disk membranes suspended in cholic acid solution, the alpha-band CD of rhodopsin decreases to about a third and the gamma-band CD increases remarkably.	Ammonium Sulfate	5-21	rhodopsin	Bos taurus	119-128
588586-0	1977	Fractionation of rhodopsin and other components in the rod outer segment membrane by ammonium sulfate salting-out.	Ammonium Sulfate	85-101	rhodopsin	Bos taurus	17-26
21189-0	1977	Hydrogen exchange study of membrane-bound rhodopsin.	Hydrogen	0-8	rhodopsin	Bos taurus	42-51
21189-5	1977	The results show that about 70% of rhodopsin"s peptide group protons are exposed to water.	Water	84-89	rhodopsin	Bos taurus	35-44
21189-9	1977	Our results together with available information on rhodopsin suggest that a considerable length of its polypeptide chain is arranged at the surface of a channel of water penetrating into the membrane.	Water	164-169	rhodopsin	Bos taurus	51-60
563728-0	1978	Effect of digitonin concentration on regeneration of cattle rhodopsin.	Digitonin	10-19	rhodopsin	Bos taurus	60-69
901803-2	1977	This tendency of CD change is most prominent in the purified rhodopsin in cholic acid obtained by the ammonium sulfate fractionation of disk membranes, and the gamma-band CD is three times larger than the alpha-band CD.	Cadmium	17-19	rhodopsin	Bos taurus	61-70
901803-7	1977	When ammonium sulfate is added to the sonicated disk membranes suspended in cholic acid solution, the alpha-band CD of rhodopsin decreases to about a third and the gamma-band CD increases remarkably.	Cholic Acid	76-87	rhodopsin	Bos taurus	119-128
901803-2	1977	This tendency of CD change is most prominent in the purified rhodopsin in cholic acid obtained by the ammonium sulfate fractionation of disk membranes, and the gamma-band CD is three times larger than the alpha-band CD.	Cholic Acid	74-85	rhodopsin	Bos taurus	61-70
901803-7	1977	When ammonium sulfate is added to the sonicated disk membranes suspended in cholic acid solution, the alpha-band CD of rhodopsin decreases to about a third and the gamma-band CD increases remarkably.	Cadmium	113-115	rhodopsin	Bos taurus	119-128
901803-2	1977	This tendency of CD change is most prominent in the purified rhodopsin in cholic acid obtained by the ammonium sulfate fractionation of disk membranes, and the gamma-band CD is three times larger than the alpha-band CD.	Ammonium Sulfate	102-118	rhodopsin	Bos taurus	61-70
901803-9	1977	However, the purified rhodopsin recovers native CD spectrum on addition of lipids extracted from disk membranes.	Cadmium	48-50	rhodopsin	Bos taurus	22-31
901803-2	1977	This tendency of CD change is most prominent in the purified rhodopsin in cholic acid obtained by the ammonium sulfate fractionation of disk membranes, and the gamma-band CD is three times larger than the alpha-band CD.	Cadmium	171-173	rhodopsin	Bos taurus	61-70
901803-2	1977	This tendency of CD change is most prominent in the purified rhodopsin in cholic acid obtained by the ammonium sulfate fractionation of disk membranes, and the gamma-band CD is three times larger than the alpha-band CD.	Cadmium	171-173	rhodopsin	Bos taurus	61-70
618334-5	1977	Fluorescence increase rate is controlled by the rate of chemical reaction of rhodopsin with hydroxylamine.	Hydroxylamine	92-105	rhodopsin	Bos taurus	77-86
901803-5	1977	Both in rhodopsin and isorhodopsin the gamma-band CD is lost by light irradiation.	Cadmium	50-52	rhodopsin	Bos taurus	8-17
890058-2	1977	It was found that the incorporated phosphate is not uniformly distributed in a population of rhodopsin molecules.	Phosphates	35-44	rhodopsin	Bos taurus	93-102
890058-3	1977	In a preparation with an average phosphorylation extent of 2.4 moles of phosphate per mole of rhodopsin, most of the 32P-phosphate was found in fractions where 4-5 phosphates are bound per rhodopsin, whereas a large fraction of the total rhodopsin was not phosphorylated at all.	32p-phosphate	117-130	rhodopsin	Bos taurus	94-103
890058-4	1977	The maximum number os phosphate binding sites in rhodopsin appears to be at least five.	Phosphates	19-31	rhodopsin	Bos taurus	49-58
857949-1	1977	Transient electric birefringence studies have been made on bovine rhodopsin solubilized in the detergent lauryldimethylamine oxide from glutaraldehyde fixed rod outer segment (ROS) membranes.	dodecyldimethylamine oxide	105-130	rhodopsin	Bos taurus	66-75
861254-0	1977	The amino-terminal tryptic peptide of bovine rhodopsin.	Peptides	27-34	rhodopsin	Bos taurus	45-54
861254-5	1977	When a method specific for isolating amino-terminal tryptic peptides from proteins is applied to rhodopsin, peptide T1 is demonstrated to be the amino-terminal peptide of rhodopsin.	Peptides	60-68	rhodopsin	Bos taurus	97-106
861254-5	1977	When a method specific for isolating amino-terminal tryptic peptides from proteins is applied to rhodopsin, peptide T1 is demonstrated to be the amino-terminal peptide of rhodopsin.	Peptides	60-68	rhodopsin	Bos taurus	171-180
893355-1	1977	Cattle and squid opsins were found to be associated with phospholipids after extensive dialysis of the salt-free digitonin extract of rhodopsin against 30% aqueous 2-chloroethanol (v/v) at pH  2.5.	Phospholipids	57-70	rhodopsin	Bos taurus	134-143
893355-1	1977	Cattle and squid opsins were found to be associated with phospholipids after extensive dialysis of the salt-free digitonin extract of rhodopsin against 30% aqueous 2-chloroethanol (v/v) at pH  2.5.	Salts	103-107	rhodopsin	Bos taurus	134-143
893355-1	1977	Cattle and squid opsins were found to be associated with phospholipids after extensive dialysis of the salt-free digitonin extract of rhodopsin against 30% aqueous 2-chloroethanol (v/v) at pH  2.5.	Digitonin	113-122	rhodopsin	Bos taurus	134-143
14680-1	1977	Calcium trapped within sonicated and resealed bovine rod outer segment disks is released upon light exposure with a stoichiometry of 0.75 +/- 0.05 calcium for each rhodopsin bleached.	Calcium	0-7	rhodopsin	Bos taurus	164-173
266718-3	1977	The slowly relaxing component of each disc membrane resonance is most likely due to phospholipids whose motion is affected by rhodopsin.	Phospholipids	84-97	rhodopsin	Bos taurus	126-135
266718-5	1977	These observations suggest that the interaction of rhodopsin with the more fluid membrane phospholipids predominantly affects relatively high frequency segmental motions, which determine T1, while having minimal effects on the lower frequency segmental motions, which influence T2.	Phospholipids	90-103	rhodopsin	Bos taurus	51-60
14680-9	1977	The resluts suggest a model for the disk in which each bleached rhodopsin functions as a "one-shot carrier" to transport a single calcium ion across the membrane.	Calcium	130-137	rhodopsin	Bos taurus	64-73
857949-1	1977	Transient electric birefringence studies have been made on bovine rhodopsin solubilized in the detergent lauryldimethylamine oxide from glutaraldehyde fixed rod outer segment (ROS) membranes.	Glutaral	136-150	rhodopsin	Bos taurus	66-75
843524-0	1977	Differential effects of puromycin on the incorporation of precursors of rhodopsin in bovine retina.	Puromycin	24-33	rhodopsin	Bos taurus	72-81
843524-1	1977	Bovine retinas incubated in vitro sustain the synthesis of opsin and rhodopsin as monitored by the incorporation of labeled leucine, mannose, and glucosamine.	Leucine	124-131	rhodopsin	Bos taurus	69-78
843524-2	1977	Puromycin, an inhibitor of protein synthesis, effectively blocks the incorporation of leucine and mannose into opsin and rhodopsin of rod outer segments.	Puromycin	0-9	rhodopsin	Bos taurus	121-130
843587-9	1977	(4) The detergents, Emulphogene, cetyltrimethylammonium salts, and digitonin, significantly decrease the conformational stability of rhodopsin as compared to the in situ conditions.	Digitonin	67-76	rhodopsin	Bos taurus	133-142
843524-5	1977	Galactose, not normally found in rhodopsin, is also incorporated into both opsin and rhodopsin.	Galactose	0-9	rhodopsin	Bos taurus	33-42
843587-9	1977	(4) The detergents, Emulphogene, cetyltrimethylammonium salts, and digitonin, significantly decrease the conformational stability of rhodopsin as compared to the in situ conditions.	cetyltrimethylammonium salts	33-61	rhodopsin	Bos taurus	133-142
843524-5	1977	Galactose, not normally found in rhodopsin, is also incorporated into both opsin and rhodopsin.	Galactose	0-9	rhodopsin	Bos taurus	85-94
592823-1	1977	The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment.	CAV protocol	81-84	rhodopsin	Bos taurus	29-38
24271845-3	1977	However, bleached rhodopsin could activate it in the presence of a very low concentration of ATP, strongly suggesting the mediation of rhodopsin in the light activation of the enzyme in ROS.	Adenosine Triphosphate	93-96	rhodopsin	Bos taurus	18-27
24271845-3	1977	However, bleached rhodopsin could activate it in the presence of a very low concentration of ATP, strongly suggesting the mediation of rhodopsin in the light activation of the enzyme in ROS.	Adenosine Triphosphate	93-96	rhodopsin	Bos taurus	135-144
592823-1	1977	The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment.	CAV protocol	138-141	rhodopsin	Bos taurus	29-38
592823-1	1977	The amino terminus of bovine rhodopsin is blocked and has the sequence x-Met-Asn(CHO)-Gly-Thr-Glu-Gly-Pro-Asn-Phe-Tyr-Val-Pro-Phe-Ser-Asn(CHO)-Lys-Thr-Gly-Val-Val-Arg, where CHO represents sites of carbohydrate attachment.	Carbohydrates	198-210	rhodopsin	Bos taurus	29-38
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	val-ser-lys-thr	47-62	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Glutamic Acid	63-66	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Threonine	59-62	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Serine	51-54	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Glutamine	75-78	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Valine	47-50	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Alanine	83-86	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Proline	87-90	rhodopsin	Bos taurus	34-43
592823-2	1977	The carboxyl-terminal sequence of rhodopsin is Val-Ser-Lys-Thr-Glu-Thr-Ser-Gln-Val-Ala-Pro-Ala.	Alanine	91-94	rhodopsin	Bos taurus	34-43
1254583-5	1976	After treatment of the rhodopsin with chloroform/methanol (2/1) to remove lipids and detergents, the carbohydrate content was measured by gas-liquid chromatography, colorimetric and enzymatic analyses, paper chromatography, and electrophoresis.	Methanol	49-57	rhodopsin	Bos taurus	23-32
999895-2	1976	Relation between sulfhydryl groups and properties of rhodopsin studied by means of methylmercuric iodide.	methylmercuric iodide	83-104	rhodopsin	Bos taurus	53-62
999895-4	1976	Treatment of isolated bovine rod outer segment membranes with the very reactive, small and uncharged sulfhydryl reagent methylmercuric iodide shows all six SH groups of rhodopsin can be modified without loss of its typical absorbance spectrum.	sulfhydryl reagent methylmercuric iodide	101-141	rhodopsin	Bos taurus	169-178
938731-2	1976	The use of this inversion technique is illustrated by application to the proteins: lysozyme, bovine serum albumin, human transferrin, and bovine rhodopsin solubilized in digitonin.	Digitonin	170-179	rhodopsin	Bos taurus	145-154
949475-6	1976	Bilayers prepared from extracted disk lipids had a microviscosity which was about one-fourth that of the intact disk membrane, demonstrating that rhodopsin hinders the mobility of the hydrocarbon chains of the disk phospholipids or egg phosphatidylcholine had identical microviscosities despite the much higher degree of unsaturation of the disk phospholipids.	Hydrocarbons	184-195	rhodopsin	Bos taurus	146-155
949475-6	1976	Bilayers prepared from extracted disk lipids had a microviscosity which was about one-fourth that of the intact disk membrane, demonstrating that rhodopsin hinders the mobility of the hydrocarbon chains of the disk phospholipids or egg phosphatidylcholine had identical microviscosities despite the much higher degree of unsaturation of the disk phospholipids.	Phospholipids	215-228	rhodopsin	Bos taurus	146-155
949475-6	1976	Bilayers prepared from extracted disk lipids had a microviscosity which was about one-fourth that of the intact disk membrane, demonstrating that rhodopsin hinders the mobility of the hydrocarbon chains of the disk phospholipids or egg phosphatidylcholine had identical microviscosities despite the much higher degree of unsaturation of the disk phospholipids.	Phosphatidylcholines	236-255	rhodopsin	Bos taurus	146-155
949475-6	1976	Bilayers prepared from extracted disk lipids had a microviscosity which was about one-fourth that of the intact disk membrane, demonstrating that rhodopsin hinders the mobility of the hydrocarbon chains of the disk phospholipids or egg phosphatidylcholine had identical microviscosities despite the much higher degree of unsaturation of the disk phospholipids.	Phospholipids	346-359	rhodopsin	Bos taurus	146-155
178349-5	1976	In intact, light-bleached outer segments, GTP appears to specifically phosphorylate rhodopsin.	Guanosine Triphosphate	42-45	rhodopsin	Bos taurus	84-93
178349-7	1976	Histone appears to block rhodopsin phosphorylation by GTP while histone and, to some extent, phosvitin, both act as substrates for ATP-kinase activity.	Guanosine Triphosphate	54-57	rhodopsin	Bos taurus	25-34
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	c-me	160-164	rhodopsin	Bos taurus	72-81
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	c-me	160-164	rhodopsin	Bos taurus	315-324
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	Sulfur	31-32	rhodopsin	Bos taurus	72-81
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	Sulfur	31-32	rhodopsin	Bos taurus	315-324
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	Sulfur	47-48	rhodopsin	Bos taurus	72-81
1268187-7	1976	Due to the fact that the Raman spectra of 11-cis-retinal (solution) and rhodopsin show bands near 998 and 1018 cm(-1), a spectral region previously assigned to C-Me stretching motions, it is suggested that 11-cis-retinal in solution is compased of a mixture of 12-s-trans and 12-s-cis, and that the conformation of rhodopsin is (perhaps distorted) 12-s-trans.	Sulfur	47-48	rhodopsin	Bos taurus	315-324
1083249-1	1976	Phosphorylation of rhodopsin has been measured in isolated retinas incubated with 32P-phosphate under physiological conditions.	32p-phosphate	82-95	rhodopsin	Bos taurus	19-28
1254583-0	1976	Carbohydrate composition of bovine rhodopsin.	Carbohydrates	0-12	rhodopsin	Bos taurus	35-44
1254583-1	1976	The carbohydrate content of bovine rhodopsin was investigated and found to be different from previously reported values.	Carbohydrates	4-16	rhodopsin	Bos taurus	35-44
1254583-6	1976	Rhodopsin was found to have about 9 mol of mannose and 5 mol of glucosamine per mol of visual pigment.	Mannose	43-50	rhodopsin	Bos taurus	0-9
1254583-6	1976	Rhodopsin was found to have about 9 mol of mannose and 5 mol of glucosamine per mol of visual pigment.	Glucosamine	64-75	rhodopsin	Bos taurus	0-9
1254583-3	1976	Rhodopsin was extracted with detergents and purified by chromatographic procedures involving calcium phosphate/celite chromatography followed by affinity chromatograpy on concanavalin A-Sepharose (or in some cases, gel filtration on agarose).	calcium phosphate	93-110	rhodopsin	Bos taurus	0-9
1254583-7	1976	A molar ratio of mannose/glucosamine of about 2 was also found in samples of rhodopsin obtained from two other laboratories.	Mannose	17-24	rhodopsin	Bos taurus	77-86
1254583-3	1976	Rhodopsin was extracted with detergents and purified by chromatographic procedures involving calcium phosphate/celite chromatography followed by affinity chromatograpy on concanavalin A-Sepharose (or in some cases, gel filtration on agarose).	Diatomaceous Earth	111-117	rhodopsin	Bos taurus	0-9
1254583-7	1976	A molar ratio of mannose/glucosamine of about 2 was also found in samples of rhodopsin obtained from two other laboratories.	Glucosamine	25-36	rhodopsin	Bos taurus	77-86
1254583-3	1976	Rhodopsin was extracted with detergents and purified by chromatographic procedures involving calcium phosphate/celite chromatography followed by affinity chromatograpy on concanavalin A-Sepharose (or in some cases, gel filtration on agarose).	Sepharose	186-195	rhodopsin	Bos taurus	0-9
172116-4	1975	The phosphorylation reaction apparently requires a specific conformation of the rhodopsin molecule since it is abolished by heat denaturation of rhodopsin, and it is greatly reduced or abolished by treatment of the visual pigment protein with potassium alum after the rhodopsin has been "bleached" by light.	aluminum sulfate	243-257	rhodopsin	Bos taurus	80-89
1254583-3	1976	Rhodopsin was extracted with detergents and purified by chromatographic procedures involving calcium phosphate/celite chromatography followed by affinity chromatograpy on concanavalin A-Sepharose (or in some cases, gel filtration on agarose).	Sepharose	233-240	rhodopsin	Bos taurus	0-9
1254583-5	1976	After treatment of the rhodopsin with chloroform/methanol (2/1) to remove lipids and detergents, the carbohydrate content was measured by gas-liquid chromatography, colorimetric and enzymatic analyses, paper chromatography, and electrophoresis.	Chloroform	38-48	rhodopsin	Bos taurus	23-32
1276263-0	1976	[Electrophoresis and electrofocusing of rhodopsin solubilized by triton X-100].	Octoxynol	65-77	rhodopsin	Bos taurus	40-49
1276263-2	1976	Treatment of ROS by alum caused a complete disappearance of non-rhodopsin proteins and the appearance of slow migrating band (component II).	aluminum sulfate	20-24	rhodopsin	Bos taurus	64-73
55959-7	1976	Rhodopsin, extracted using cetyltrimethylammonium bromide from pure washed ROS, induced prominent chorio-retinal damage at the dose of 500 mug.	Cetrimonium	27-57	rhodopsin	Bos taurus	0-9
1260100-4	1976	Studies on bleached rhodopsin showed a large increase in axial ratio in 0.02% Ammonyx LO.	dodecyldimethylamine oxide	78-88	rhodopsin	Bos taurus	20-29
1247624-0	1976	Alkyl glucosides as effective solubilizing agents for bovine rhodopsin.	alkyl glucosides	0-16	rhodopsin	Bos taurus	61-70
1203446-0	1975	The electric dipole moment of rhodopsin solubilized in Triton X-100.	Octoxynol	55-67	rhodopsin	Bos taurus	30-39
1203446-2	1975	Rhodopsin was extracted from disc membranes of cattle rod outer segments with the nonionic detergent Triton X-100.	Octoxynol	101-113	rhodopsin	Bos taurus	0-9
1203446-5	1975	Flash irradiation of the rhodopsin results in an increase in the dipole moment of about 25 D (5 charge-A).	dipole	65-71	rhodopsin	Bos taurus	25-34
1203446-6	1975	The light-induced increase in dipole moment appears to be composed of two parts--a faster component related to a change in the number of protons bound by rhodopsin and a slower component apparently independent of the change in proton binding.	dipole	30-36	rhodopsin	Bos taurus	154-163
172116-4	1975	The phosphorylation reaction apparently requires a specific conformation of the rhodopsin molecule since it is abolished by heat denaturation of rhodopsin, and it is greatly reduced or abolished by treatment of the visual pigment protein with potassium alum after the rhodopsin has been "bleached" by light.	aluminum sulfate	243-257	rhodopsin	Bos taurus	145-154
172116-4	1975	The phosphorylation reaction apparently requires a specific conformation of the rhodopsin molecule since it is abolished by heat denaturation of rhodopsin, and it is greatly reduced or abolished by treatment of the visual pigment protein with potassium alum after the rhodopsin has been "bleached" by light.	aluminum sulfate	243-257	rhodopsin	Bos taurus	145-154
1148250-4	1975	On the basis of their reactivity towards rho-chloromercuribenzoate and rho-chloromercuribenzene sulfonate in suspensions of outer segment membranes, the sulfhydryl groups of rhodopsin can be divided into three pairs.	rho-chloromercuribenzoate	41-66	rhodopsin	Bos taurus	174-183
1148250-4	1975	On the basis of their reactivity towards rho-chloromercuribenzoate and rho-chloromercuribenzene sulfonate in suspensions of outer segment membranes, the sulfhydryl groups of rhodopsin can be divided into three pairs.	rho-chloromercuribenzene sulfonate	71-105	rhodopsin	Bos taurus	174-183
1148250-10	1975	The differences between these results and those obtained by modification with dithiobis-(2-nitrobenzoic acid) or N-ethylmaleimide in suspension, where even upon prolonged exposure to light as well as in darkness only two sulfhydryl groups of rhodopsin are modified, is explained by the detergent-like character of the rho-chloromercuri-derivatives.	dithiobis-(2-nitrobenzoic acid)	78-109	rhodopsin	Bos taurus	242-251
1138949-3	1975	Phototransformations of digitonin extracts of rhodopsin and suspensions of outer segments of frog rods at minus 22 degrees C under the effect of light with lambda 579 and 435  nm are studied.	Digitonin	24-33	rhodopsin	Bos taurus	46-55
4139160-3	1974	Bovine rhodopsin in emulphogene was purified on an hydroxyapatite column.	Durapatite	51-65	rhodopsin	Bos taurus	7-16
1152468-2	1975	The glutaraldehyde-fixed mouse retina was treated first with rabbit antibodies specific against bovine rhodopsin and then with hemocyanin-labeled goat antibodies specific against rabbit antibody.	Glutaral	4-18	rhodopsin	Bos taurus	103-112
4417532-1	1974	Bovine photoreceptor membranes have been treated with proteases to determine the accessibility of rhodopsin to these large, water soluble molecules.	Water	124-129	rhodopsin	Bos taurus	98-107
4139160-7	1974	Papain-digested univalent antibodies (Fab) coupled with peroxidase were used to label rhodopsin in formaldehyde-fixed bovine and murine retinas.	Formaldehyde	99-111	rhodopsin	Bos taurus	86-95
5127425-2	1971	Phospholipid requirement and opsin conformation for regeneration of bovine rhodopsin.	Phospholipids	0-12	rhodopsin	Bos taurus	75-84
4751384-1	1973	Cattle rhodopsin can be highly oriented by shearing a wet paste of digitonin micelles of this visual pigment between two quartz slides.	Digitonin	67-76	rhodopsin	Bos taurus	7-16
4751384-7	1973	These experiments show the rhodopsin-digitonin micelle to be markedly asymmetric, with the chromophore lying parallel to its long axis.	Digitonin	37-46	rhodopsin	Bos taurus	27-36
4504322-1	1972	Energy transfer was used as a spectroscopic ruler to deduce proximity relationships within bovine rhodopsin in digitonin solution.	Digitonin	111-120	rhodopsin	Bos taurus	98-107
4838675-0	1974	Bovine rhodopsin: characterization of the complex formed with Triton X-100.	Octoxynol	62-74	rhodopsin	Bos taurus	7-16
4702002-0	1973	The binding site of retinaldehyde in cattle rhodopsin.	Retinaldehyde	20-33	rhodopsin	Bos taurus	44-53
5001225-2	1971	The role of phospholipids in cattle rhodopsin studied with phospholipase C.	Phospholipids	12-25	rhodopsin	Bos taurus	36-45
13346044-7	1956	It involves the exposure of 1 new acid-binding group per mole of rhodopsin with pK about 6.6, close therefore to that of the imidazole group of histidine.	imidazole	125-134	rhodopsin	Bos taurus	65-74
24174154-4	1970	The concentration of alpha-tocopherol in the ROS preparations was about 0.1 mole alpha-tocopherol per mole rhodopsin, or about 1 nmole/mg, protein.	alpha-Tocopherol	21-37	rhodopsin	Bos taurus	107-116
4309188-0	1969	Isolation and identification of phospholipids of bovine rhodopsin.	Phospholipids	32-45	rhodopsin	Bos taurus	56-65
4309188-1	1969	Phospholipids present in digitonin solutions of bovine rhodopsin have been identified and assayed.	Phospholipids	0-13	rhodopsin	Bos taurus	55-64
4309188-1	1969	Phospholipids present in digitonin solutions of bovine rhodopsin have been identified and assayed.	Digitonin	25-34	rhodopsin	Bos taurus	55-64
4309188-4	1969	The rhodopsin residue (free from digitonin) was extracted with chloroform-methanol 2:1; this extract contained the rest of the phospholipid, which consisted only of choline and ethanolamine phosphoglycerides.	chloroform methanol	63-82	rhodopsin	Bos taurus	4-13
5786898-0	1969	Amino acids near the binding site of retinaldehyde in cattle rhodopsin.	Retinaldehyde	37-50	rhodopsin	Bos taurus	61-70
13587911-1	1958	Rhodopsin, the red photosensitive pigment of rod vision, is composed of a specific cis isomer of retinene, neo-b (11-cis), joined as chromophore to a colorless protein, opsin.	Retinaldehyde	97-105	rhodopsin	Bos taurus	0-9
13587911-1	1958	Rhodopsin, the red photosensitive pigment of rod vision, is composed of a specific cis isomer of retinene, neo-b (11-cis), joined as chromophore to a colorless protein, opsin.	neo-b	107-112	rhodopsin	Bos taurus	0-9
13587911-6	1958	This is true whether rhodopsin is extracted from dark-adapted retinas, or synthesized in vitro from neo-b retinene and opsin.	neo-b retinene	100-114	rhodopsin	Bos taurus	21-30
13587919-1	1958	The effects have been examined of chymotrypsin, pepsin, trypsin, and pancreatic lipase on cattle rhodopsin in digitonin solution.	Digitonin	110-119	rhodopsin	Bos taurus	97-106
13587919-2	1958	The digestion of rhodopsin by chymotrypsin was measured by the hydrolysis of peptide bonds (formol titration), changes in pH, and bleaching.	Formaldehyde	92-98	rhodopsin	Bos taurus	17-26
13587919-7	1958	In digitonin solution each rhodopsin molecule is associated in a micelle with about 200 molecules of digitonin; yet the latter do not appear to hinder enzyme action.	Digitonin	3-12	rhodopsin	Bos taurus	27-36
13587919-7	1958	In digitonin solution each rhodopsin molecule is associated in a micelle with about 200 molecules of digitonin; yet the latter do not appear to hinder enzyme action.	Digitonin	101-110	rhodopsin	Bos taurus	27-36
4101657-0	1971	Sedimentation of bovine rhodopsin--digitonin micelles.	Digitonin	35-44	rhodopsin	Bos taurus	24-33
5439041-0	1970	Phospholipid composition and extractability of bovine rod outer segments and rhodopsin micelles.	Phospholipids	0-12	rhodopsin	Bos taurus	77-86
13346044-7	1956	It involves the exposure of 1 new acid-binding group per mole of rhodopsin with pK about 6.6, close therefore to that of the imidazole group of histidine.	Histidine	144-153	rhodopsin	Bos taurus	65-74
13346044-11	1956	Such frank denaturation procedures as the exposure of rhodopsin to alkali or heat in the dark result in comparable acid-base changes.	base	120-124	rhodopsin	Bos taurus	54-63
13346046-1	1956	Rhodopsin is formed by the condensation of opsin with a cis isomer of retinene, called neo-b.	Retinaldehyde	70-78	rhodopsin	Bos taurus	0-9
13346046-1	1956	Rhodopsin is formed by the condensation of opsin with a cis isomer of retinene, called neo-b.	neo-b	87-92	rhodopsin	Bos taurus	0-9
13346046-2	1956	The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate.	Retinaldehyde	36-54	rhodopsin	Bos taurus	17-26
13346046-2	1956	The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate.	Retinaldehyde	36-54	rhodopsin	Bos taurus	107-116
13346046-2	1956	The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate.	neo-b	88-93	rhodopsin	Bos taurus	17-26
13346046-2	1956	The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate.	neo-b	88-93	rhodopsin	Bos taurus	107-116
13346046-8	1956	With opsin present to trap neo-b, the isomerase catalyzes the synthesis of rhodopsin from all-trans retinene.	Retinaldehyde	90-108	rhodopsin	Bos taurus	75-84
32497171-0	2020	Cross-linking of bovine rhodopsin with sulfosuccinimidyl 4-(N maleimidomethyl)cyclohexane-1-carboxylate affects its functionality.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	39-103	rhodopsin	Bos taurus	24-33
13118108-0	1954	The molecular weight of rhodopsin and the nature of the rhodopsin-digitonin complex.	Digitonin	66-75	rhodopsin	Bos taurus	24-33
13118108-0	1954	The molecular weight of rhodopsin and the nature of the rhodopsin-digitonin complex.	Digitonin	66-75	rhodopsin	Bos taurus	56-65
13118108-1	1954	The sedimentation behavior of aqueous solutions of digitonin and of cattle rhodopsin in digitonin has been examined in the ultracentrifuge.	Digitonin	88-97	rhodopsin	Bos taurus	75-84
13118108-3	1954	The rhodopsin solutions sediment as a stoichiometric complex of rhodopsin with digitonin (RD-1) with an s(20) of about 9.77 Svedberg units.	Digitonin	79-88	rhodopsin	Bos taurus	4-13
13118108-3	1954	The rhodopsin solutions sediment as a stoichiometric complex of rhodopsin with digitonin (RD-1) with an s(20) of about 9.77 Svedberg units.	Digitonin	79-88	rhodopsin	Bos taurus	64-73
13118108-9	1954	Comparison of the relative concentrations of RD-1 and retinene in solutions of rhodopsin-digitonin shows that RD-1 contains only one retinene equivalent.	Retinaldehyde	54-62	rhodopsin	Bos taurus	79-88
13118108-9	1954	Comparison of the relative concentrations of RD-1 and retinene in solutions of rhodopsin-digitonin shows that RD-1 contains only one retinene equivalent.	Digitonin	89-98	rhodopsin	Bos taurus	79-88
13118108-11	1954	Cattle rhodopsin therefore contains only one chromophore consisting of a single molecule of retinene.	Retinaldehyde	92-100	rhodopsin	Bos taurus	7-16
33159335-4	2021	This interaction is driven by two factors, rhodopsin activation and rhodopsin-attached phosphates.	Phosphates	87-97	rhodopsin	Bos taurus	68-77
32761024-7	2020	We found that a proper choice of hydration algorithms and setups is needed to predict functionally important water molecules in the chromophore-binding cavity of rhodopsins, such as the water cluster in the N-H region of bacteriorhodopsin or two water molecules in the binding pocket of bovine visual rhodopsin.	Water	109-114	rhodopsin	Bos taurus	162-171
32761024-7	2020	We found that a proper choice of hydration algorithms and setups is needed to predict functionally important water molecules in the chromophore-binding cavity of rhodopsins, such as the water cluster in the N-H region of bacteriorhodopsin or two water molecules in the binding pocket of bovine visual rhodopsin.	Water	186-191	rhodopsin	Bos taurus	162-171
32761024-7	2020	We found that a proper choice of hydration algorithms and setups is needed to predict functionally important water molecules in the chromophore-binding cavity of rhodopsins, such as the water cluster in the N-H region of bacteriorhodopsin or two water molecules in the binding pocket of bovine visual rhodopsin.	Water	186-191	rhodopsin	Bos taurus	162-171
13109155-2	1953	(2) per mole equivalent of retinene; i.e., this is the extinction of a solution of rhodopsin which is produced by, or yields on bleaching, a molar solution of retinene.	Retinaldehyde	27-35	rhodopsin	Bos taurus	83-92
13109155-2	1953	(2) per mole equivalent of retinene; i.e., this is the extinction of a solution of rhodopsin which is produced by, or yields on bleaching, a molar solution of retinene.	Retinaldehyde	159-167	rhodopsin	Bos taurus	83-92
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	94-102	rhodopsin	Bos taurus	50-59
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	94-102	rhodopsin	Bos taurus	165-174
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	94-102	rhodopsin	Bos taurus	165-174
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	94-102	rhodopsin	Bos taurus	165-174
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	282-290	rhodopsin	Bos taurus	50-59
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	282-290	rhodopsin	Bos taurus	165-174
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	282-290	rhodopsin	Bos taurus	165-174
13109155-4	1953	On the assumption that each chromophoric group of rhodopsin is made from a single molecule of retinene, it is concluded that the primary photochemical conversion of rhodopsin to lumi-rhodopsin has a quantum efficiency of 1; though the over-all bleaching of rhodopsin in solution to retinene and opsin may have a quantum efficiency as low as one-half.	Retinaldehyde	282-290	rhodopsin	Bos taurus	165-174
13109155-5	1953	On bleaching cattle rhodopsin, about two sulfhydryl groups appear for each molecule of retinene liberated.	Retinaldehyde	87-95	rhodopsin	Bos taurus	20-29
13109155-6	1953	In frog rhodopsin the -SH:retinene ratio appears to be higher, 5:2 or perhaps even 3:1.	Retinaldehyde	26-34	rhodopsin	Bos taurus	8-17
14955620-1	1952	The condensation of retinene(1) with opsin to form rhodopsin is optimal at pH about 6, a pH which favors the condensation of retinene(1) with sulfhydryl rather than with amino groups.	Retinaldehyde	20-28	rhodopsin	Bos taurus	51-60
14955620-1	1952	The condensation of retinene(1) with opsin to form rhodopsin is optimal at pH about 6, a pH which favors the condensation of retinene(1) with sulfhydryl rather than with amino groups.	Retinaldehyde	125-133	rhodopsin	Bos taurus	51-60
14955620-2	1952	The synthesis of rhodopsin, though unaffected by the less powerful sulfhydryl reagents, monoiodoacetic acid and its amide, is inhibited completely by p-chloromercuribenzoate (PCMB).	Iodoacetic Acid	88-107	rhodopsin	Bos taurus	17-26
14955620-2	1952	The synthesis of rhodopsin, though unaffected by the less powerful sulfhydryl reagents, monoiodoacetic acid and its amide, is inhibited completely by p-chloromercuribenzoate (PCMB).	Amides	116-121	rhodopsin	Bos taurus	17-26
14955620-2	1952	The synthesis of rhodopsin, though unaffected by the less powerful sulfhydryl reagents, monoiodoacetic acid and its amide, is inhibited completely by p-chloromercuribenzoate (PCMB).	p-chloromercuribenzoate	150-173	rhodopsin	Bos taurus	17-26
14955620-2	1952	The synthesis of rhodopsin, though unaffected by the less powerful sulfhydryl reagents, monoiodoacetic acid and its amide, is inhibited completely by p-chloromercuribenzoate (PCMB).	p-Chloromercuribenzoic Acid	175-179	rhodopsin	Bos taurus	17-26
14955620-6	1952	Under some conditions the synthesis of rhodopsin is aided by the presence of such a sulfhydryl compound as glutathione, which helps to keep the -SH groups of opsin free and reduced.	Glutathione	107-118	rhodopsin	Bos taurus	39-48
14955620-7	1952	By means of the amperometric silver titration of Kolthoff and Harris, it is shown that sulfhydryl groups are liberated in the bleaching of rhodopsin, two such groups for each retinene(1) molecule that appears.	Sulfhydryl Compounds	87-97	rhodopsin	Bos taurus	139-148
14955620-7	1952	By means of the amperometric silver titration of Kolthoff and Harris, it is shown that sulfhydryl groups are liberated in the bleaching of rhodopsin, two such groups for each retinene(1) molecule that appears.	Retinaldehyde	175-183	rhodopsin	Bos taurus	139-148
32497171-2	2020	The functionality of bovine rhodopsin was determined following treatment with sulfosuccinimidyl 4-(N maleimidomethyl)cyclohexane-1-carboxylate (sulfo-SMCC), a bifunctional reagent capable of forming covalent cross-links between suitable placed lysines and cysteines.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	78-142	rhodopsin	Bos taurus	28-37
32497171-2	2020	The functionality of bovine rhodopsin was determined following treatment with sulfosuccinimidyl 4-(N maleimidomethyl)cyclohexane-1-carboxylate (sulfo-SMCC), a bifunctional reagent capable of forming covalent cross-links between suitable placed lysines and cysteines.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	144-154	rhodopsin	Bos taurus	28-37
32497171-2	2020	The functionality of bovine rhodopsin was determined following treatment with sulfosuccinimidyl 4-(N maleimidomethyl)cyclohexane-1-carboxylate (sulfo-SMCC), a bifunctional reagent capable of forming covalent cross-links between suitable placed lysines and cysteines.	Lysine	244-251	rhodopsin	Bos taurus	28-37
32497171-2	2020	The functionality of bovine rhodopsin was determined following treatment with sulfosuccinimidyl 4-(N maleimidomethyl)cyclohexane-1-carboxylate (sulfo-SMCC), a bifunctional reagent capable of forming covalent cross-links between suitable placed lysines and cysteines.	Cysteine	256-265	rhodopsin	Bos taurus	28-37
32497171-3	2020	Denaturing polyacrylamide gel electrophoresis showed that rhodopsin incubated with sulfo-SMCC generated intermolecular dimers, trimers, and higher oligomers, although most of the sulfo-SMCC-treated protein remained as a monomer.	polyacrylamide	11-25	rhodopsin	Bos taurus	58-67
32497171-3	2020	Denaturing polyacrylamide gel electrophoresis showed that rhodopsin incubated with sulfo-SMCC generated intermolecular dimers, trimers, and higher oligomers, although most of the sulfo-SMCC-treated protein remained as a monomer.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	83-93	rhodopsin	Bos taurus	58-67
32497171-3	2020	Denaturing polyacrylamide gel electrophoresis showed that rhodopsin incubated with sulfo-SMCC generated intermolecular dimers, trimers, and higher oligomers, although most of the sulfo-SMCC-treated protein remained as a monomer.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	179-189	rhodopsin	Bos taurus	58-67
32497171-4	2020	Minor alterations on the absorption spectrum of light-activated sulfo-SMCC-treated rhodopsin were observed.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	64-74	rhodopsin	Bos taurus	83-92
32497171-5	2020	However, only about 2% stimulation of the guanine nucleotide binding activity of transducin was measured in the presence of sulfo-SMCC-cross-linked photolyzed rhodopsin.	Guanine Nucleotides	42-60	rhodopsin	Bos taurus	159-168
32497171-5	2020	However, only about 2% stimulation of the guanine nucleotide binding activity of transducin was measured in the presence of sulfo-SMCC-cross-linked photolyzed rhodopsin.	sulfosuccinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate	124-134	rhodopsin	Bos taurus	159-168
32497171-7	2020	Rhodopsin was purified in the presence of either 0.1% or 1% n-dodecyl beta-D-maltoside, to obtain dimeric and monomeric forms of the protein, respectively.	dodecyl maltoside	60-86	rhodopsin	Bos taurus	0-9
32497171-9	2020	Structural analysis of the rhodopsin three-dimensional structure suggested that the following lysine and cysteine pairs: Lys66/Lys67 and Cys316, Cys140 and Lys141, Cys140 and Lys248, Lys311 and Cys316, and/or Cys316 and Lys325 are potential candidates to generate intramolecular cross-links in the protein.	Lysine	94-100	rhodopsin	Bos taurus	27-36
32497171-9	2020	Structural analysis of the rhodopsin three-dimensional structure suggested that the following lysine and cysteine pairs: Lys66/Lys67 and Cys316, Cys140 and Lys141, Cys140 and Lys248, Lys311 and Cys316, and/or Cys316 and Lys325 are potential candidates to generate intramolecular cross-links in the protein.	Cysteine	105-113	rhodopsin	Bos taurus	27-36
30582615-2	2019	Fluorescence and 1 H NMR spectroscopy studies with the bovine dim-light photoreceptor, rhodopsin, indicate that Ce6 weakly binds to it with mum affinity.	phytochlorin	112-115	rhodopsin	Bos taurus	87-96
32225143-5	2020	Dark-state rhodopsin was prepared in classical and neopentyl glycol (NPG) detergents, followed by complex formation with mini-Go under light exposure.	2,2-dimethyl-1,3-propanediol	51-67	rhodopsin	Bos taurus	11-20
32225143-5	2020	Dark-state rhodopsin was prepared in classical and neopentyl glycol (NPG) detergents, followed by complex formation with mini-Go under light exposure.	2,2-dimethyl-1,3-propanediol	69-72	rhodopsin	Bos taurus	11-20
32225143-8	2020	SDS-polyacrylamide electrophoresis (SDS-PAGE) confirmed the formation of the complex by identifying a 1:1 molar ratio between rhodopsin and mini-Go after staining the gel with Coomassie blue.	Sodium Dodecyl Sulfate	0-3	rhodopsin	Bos taurus	126-135
32225143-8	2020	SDS-polyacrylamide electrophoresis (SDS-PAGE) confirmed the formation of the complex by identifying a 1:1 molar ratio between rhodopsin and mini-Go after staining the gel with Coomassie blue.	polyacrylamide	4-18	rhodopsin	Bos taurus	126-135
32225143-8	2020	SDS-polyacrylamide electrophoresis (SDS-PAGE) confirmed the formation of the complex by identifying a 1:1 molar ratio between rhodopsin and mini-Go after staining the gel with Coomassie blue.	Sodium Dodecyl Sulfate	36-39	rhodopsin	Bos taurus	126-135
32225143-8	2020	SDS-polyacrylamide electrophoresis (SDS-PAGE) confirmed the formation of the complex by identifying a 1:1 molar ratio between rhodopsin and mini-Go after staining the gel with Coomassie blue.	Coomassie blue	176-190	rhodopsin	Bos taurus	126-135
32225143-11	2020	Heterologously-expressed rhodopsin was observed on SDS-PAGE to have two different N-glycosylated populations, which would probably have hindered crystallogenesis.	Sodium Dodecyl Sulfate	51-54	rhodopsin	Bos taurus	25-34
32225143-11	2020	Heterologously-expressed rhodopsin was observed on SDS-PAGE to have two different N-glycosylated populations, which would probably have hindered crystallogenesis.	Nitrogen	82-83	rhodopsin	Bos taurus	25-34
30582615-6	2019	Chemical shift changes in 1 H-15 N NMR spectroscopy of 15 N-Trp labeled bovine rhodopsin reveal that Ce6 binding perturbs the entire structure.	15 n-trp	55-63	rhodopsin	Bos taurus	79-88
30582615-6	2019	Chemical shift changes in 1 H-15 N NMR spectroscopy of 15 N-Trp labeled bovine rhodopsin reveal that Ce6 binding perturbs the entire structure.	phytochlorin	101-104	rhodopsin	Bos taurus	79-88
30582615-7	2019	These results provide experimental evidence that Ce6 is an allosteric modulator of rhodopsin.	phytochlorin	49-52	rhodopsin	Bos taurus	83-92
26633591-3	2016	We report here a charge-interaction-directed reconstitution mechanism that induces spontaneous insertion of bovine rhodopsin, the eukaryotic GPCR, into both lipid- and polymer-based artificial membranes.	Polymers	168-175	rhodopsin	Bos taurus	115-124
29730301-1	2018	In order to monitor conformational changes following photoactivation and phosphorylation of bovine rhodopsin, the two reactive sulfhydryl groups at Cys140 and Cys316 were specifically labeled with the monobromobimane (mBBr) fluorophore.	monobromobimane	218-222	rhodopsin	Bos taurus	99-108
29730301-6	2018	Apparently, amino acid residues that are buried in the interior of the inactive protein become accessible following illumination and phosphorylation of rhodopsin, quenching in turn the fluorescence excitation signal of mBBr-modified rhodopsin.	monobromobimane	219-223	rhodopsin	Bos taurus	152-161
29730301-6	2018	Apparently, amino acid residues that are buried in the interior of the inactive protein become accessible following illumination and phosphorylation of rhodopsin, quenching in turn the fluorescence excitation signal of mBBr-modified rhodopsin.	monobromobimane	219-223	rhodopsin	Bos taurus	233-242
27486845-0	2016	Relocating the Active-Site Lysine in Rhodopsin: 2.	Lysine	27-33	rhodopsin	Bos taurus	37-46
27486845-2	2016	The visual pigment rhodopsin is a G protein-coupled receptor that covalently binds its retinal chromophore via a Schiff base linkage to an active-site Lys residue in the seventh transmembrane helix.	Schiff Bases	113-124	rhodopsin	Bos taurus	19-28
27486845-2	2016	The visual pigment rhodopsin is a G protein-coupled receptor that covalently binds its retinal chromophore via a Schiff base linkage to an active-site Lys residue in the seventh transmembrane helix.	Lysine	151-154	rhodopsin	Bos taurus	19-28
27486845-3	2016	Although this residue is strictly conserved among all type II retinylidene proteins, we found previously that the active-site Lys in bovine rhodopsin (Lys296) can be moved to three other locations (G90K, T94K, S186K) while retaining the ability to form a pigment with retinal and to activate transducin in a light-dependent manner [ Devine et al.	Lysine	126-129	rhodopsin	Bos taurus	140-149
27486845-13	2016	These results demonstrate that rhodopsin can tolerate a second Lys in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys could allow migration of the Schiff base Lys to a position other than the observed, highly conserved location in the seventh TM helix.	Lysine	63-66	rhodopsin	Bos taurus	31-40
27486845-13	2016	These results demonstrate that rhodopsin can tolerate a second Lys in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys could allow migration of the Schiff base Lys to a position other than the observed, highly conserved location in the seventh TM helix.	Lysine	152-155	rhodopsin	Bos taurus	31-40
27486845-13	2016	These results demonstrate that rhodopsin can tolerate a second Lys in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys could allow migration of the Schiff base Lys to a position other than the observed, highly conserved location in the seventh TM helix.	Schiff Bases	185-196	rhodopsin	Bos taurus	31-40
27486845-13	2016	These results demonstrate that rhodopsin can tolerate a second Lys in the retinal binding pocket and suggest that an evolutionary intermediate with two Lys could allow migration of the Schiff base Lys to a position other than the observed, highly conserved location in the seventh TM helix.	Lysine	152-155	rhodopsin	Bos taurus	31-40
28289214-3	2017	Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C11=C12 double bond locked in its cis conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11-cis to an 11,13-dicis configuration for prolonged Gt activation.	Carbon	62-68	rhodopsin	Bos taurus	27-29
28289214-3	2017	Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C11=C12 double bond locked in its cis conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11-cis to an 11,13-dicis configuration for prolonged Gt activation.	rh6mr	158-163	rhodopsin	Bos taurus	27-29
28289214-3	2017	Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C11=C12 double bond locked in its cis conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11-cis to an 11,13-dicis configuration for prolonged Gt activation.	11-cis	224-230	rhodopsin	Bos taurus	27-29
28289214-3	2017	Here we report that bovine Rh, regenerated instead with a six-carbon-ring retinal chromophore featuring a C11=C12 double bond locked in its cis conformation (Rh6mr), employs an atypical isomerization mechanism by converting 11-cis to an 11,13-dicis configuration for prolonged Gt activation.	11,13-dicis	237-248	rhodopsin	Bos taurus	27-29
28289214-6	2017	Overall, these comprehensive structure-function studies unveil a unique photocyclic mechanism of Rh activation by an 11-cis-to-11,13-dicis isomerization.	11-cis-to-11,13-dicis	117-138	rhodopsin	Bos taurus	97-99
27376589-4	2016	The free backbone C=O groups on helices H5 and H7 stabilize the inactive rhodopsin structure through hydrogen-bonds to residues on adjacent helices.	Hydrogen	101-109	rhodopsin	Bos taurus	73-82
27410736-2	2016	In the bovine photoreceptor rhodopsin, this is accompanied by proton uptake at Glu(134) in the class-conserved D(E)RY motif.	Glutamic Acid	79-82	rhodopsin	Bos taurus	28-37
26074351-0	2015	Impacts of retinal polyene (de)methylation on the photoisomerization mechanism and photon energy storage of rhodopsin.	Polyenes	19-26	rhodopsin	Bos taurus	108-117
26098991-7	2015	An Arrhenius plot of zebrafish rhodopsin was consistent with this model, inferring that the activation energy for Schiff base hydrolysis is similar to that of bovine rhodopsin.	Schiff Bases	114-125	rhodopsin	Bos taurus	166-175
26383645-5	2015	Here, the interaction of pre-activated truncated bovine visual arrestin (Arr(Tr)) with rhodopsin in 1,2-diheptanoyl-sn-glycero-3-phosphocholine (DHPC) micelles is investigated by solution NMR techniques and flash photolysis spectroscopy.	1,2-heptanoylphosphatidylcholine	100-143	rhodopsin	Bos taurus	87-96
26383645-5	2015	Here, the interaction of pre-activated truncated bovine visual arrestin (Arr(Tr)) with rhodopsin in 1,2-diheptanoyl-sn-glycero-3-phosphocholine (DHPC) micelles is investigated by solution NMR techniques and flash photolysis spectroscopy.	1,2-heptanoylphosphatidylcholine	145-149	rhodopsin	Bos taurus	87-96
24911398-0	2014	Mercury-induced dark-state instability and photobleaching alterations of the visual g-protein coupled receptor rhodopsin.	Mercury	0-7	rhodopsin	Bos taurus	111-120
25514632-4	2015	We found that these rates were significantly faster in the UV pigment than in rhodopsin due to the difference in the structural and electrostatic effects surrounding the unprotonated Schiff base (USB) retinyl chromophore in the UV pigment.	Schiff Bases	183-194	rhodopsin	Bos taurus	78-87
25857788-9	2015	This chapter describes a protocol for using the PB-based system for inducible expression of bovine rhodopsin in HEK293S GnTI(-) cells.	pladienolide B	48-50	rhodopsin	Bos taurus	99-108
25772009-9	2015	Overall, the oxidative stress caused by the prolonged intense illumination of retina might affect rhodopsin desensitization via concerted disulfide dimerization of recoverin and arrestin.	Disulfides	138-147	rhodopsin	Bos taurus	98-107
24911398-2	2014	We have analyzed the effect of mercuric chloride on the structure and stability of the dim light vision photoreceptor rhodopsin.	Chlorides	40-48	rhodopsin	Bos taurus	118-127
24911398-3	2014	For this purpose, we have used both native rhodopsin immunopurified from bovine retinas and a recombinant mutant rhodopsin carrying several Cys to Ser substitutions in order to investigate the potential binding site of mercury on the receptor.	Serine	147-150	rhodopsin	Bos taurus	113-122
24911398-3	2014	For this purpose, we have used both native rhodopsin immunopurified from bovine retinas and a recombinant mutant rhodopsin carrying several Cys to Ser substitutions in order to investigate the potential binding site of mercury on the receptor.	Mercury	219-226	rhodopsin	Bos taurus	43-52
24911398-3	2014	For this purpose, we have used both native rhodopsin immunopurified from bovine retinas and a recombinant mutant rhodopsin carrying several Cys to Ser substitutions in order to investigate the potential binding site of mercury on the receptor.	Mercury	219-226	rhodopsin	Bos taurus	113-122
24911398-4	2014	Our results show that mercuric chloride dramatically reduces the stability of dark-state rhodopsin and alters the molecular features of the photoactived conformation obtained upon illumination by eliciting the formation of an altered photointermediate.	Mercuric Chloride	22-39	rhodopsin	Bos taurus	89-98
24911398-5	2014	The thermal bleaching kinetics of native and mutant rhodopsin is markedly accelerated by mercury in a concentration-dependent manner, and its chromophore regeneration ability is severely reduced without significantly affecting its G-protein activation capacity.	Mercury	89-96	rhodopsin	Bos taurus	52-61
24911398-7	2014	Our results provide further support for the capacity of mercury as a hazardous metal ion with reported deleterious effect on vision and provide a molecular explanation for such an effect at the rhodopsin photoreceptor level.	Mercury	56-63	rhodopsin	Bos taurus	194-203
24911398-8	2014	We suggest that mercury could alter vision by acting in a specific manner on the molecular components of the retinoid cycle, particularly by modifying the ability of the visual photoreceptor protein rhodopsin to be regenerated and to be normally photoactivated by light.	Mercury	16-23	rhodopsin	Bos taurus	199-208
24911398-8	2014	We suggest that mercury could alter vision by acting in a specific manner on the molecular components of the retinoid cycle, particularly by modifying the ability of the visual photoreceptor protein rhodopsin to be regenerated and to be normally photoactivated by light.	Retinoids	109-117	rhodopsin	Bos taurus	199-208
23553533-5	2013	The method was validated by construction of the beta1 adrenergic receptor model in complex with (S)-cyanopindolol using bovine rhodopsin as template.	cyanopindolol	96-113	rhodopsin	Bos taurus	127-136
23638692-2	2013	PURPOSE: In a previous paper, we showed that chemiluminescence from radical recombination (initiated by lipid peroxidation and propagated by polyunsaturated fatty acids [PUFA]) has a bleaching effect comparable to that caused by light on the rhodopsin of retinal rod outer segment (RdOS) prepared from bovine eyes.	Fatty Acids, Unsaturated	141-168	rhodopsin	Bos taurus	242-251
23904486-0	2013	Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins.	Lysine	27-33	rhodopsin	Bos taurus	37-46
23904486-0	2013	Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins.	retinylidene	81-93	rhodopsin	Bos taurus	37-46
23570417-2	2013	Here we measured the activation efficiencies of chicken green-sensitive cone visual pigment (cG) and bovine rhodopsin (bRh) in real time by monitoring the intrinsic fluorescence of tryptophan residues in the pigments and Gt.	Tryptophan	181-191	rhodopsin	Bos taurus	108-117
26579920-0	2014	Generalized QM/MM Force Matching Approach Applied to the 11-cis Protonated Schiff Base Chromophore of Rhodopsin.	Schiff Bases	75-86	rhodopsin	Bos taurus	102-111
26579920-2	2014	We applied this approach to the challenging case of the retinal protonated Schiff base in dark state bovine rhodopsin.	Schiff Bases	75-86	rhodopsin	Bos taurus	108-117
23805751-0	2013	Elastic properties of polyunsaturated phosphatidylethanolamines influence rhodopsin function.	polyunsaturated phosphatidylethanolamines	22-63	rhodopsin	Bos taurus	74-83
23805751-1	2013	Membranes with a high content of polyunsaturated phosphatidylethanolamines (PE) facilitate formation of metarhodopsin-II (M(II)), the photointermediate of bovine rhodopsin that activates the G protein transducin.	polyunsaturated phosphatidylethanolamines	33-74	rhodopsin	Bos taurus	108-117
23805751-1	2013	Membranes with a high content of polyunsaturated phosphatidylethanolamines (PE) facilitate formation of metarhodopsin-II (M(II)), the photointermediate of bovine rhodopsin that activates the G protein transducin.	Phosphatidylethanolamines	76-78	rhodopsin	Bos taurus	108-117
22634396-3	2012	Rod outer segments of photoreceptors are characterized by rhodopsin, a membrane protein surrounded by phospholipids containing a very high concentration of polyunsaturated fatty acids.	Phospholipids	102-115	rhodopsin	Bos taurus	58-67
24143992-5	2013	For bovine rhodopsin, we developed a new purification strategy including a (NH4)2SO4-induced phase separation that proved essential to obtain crystals of photoactivated rhodopsin containing parallel dimers.	Ammonium Sulfate	75-84	rhodopsin	Bos taurus	11-20
24143992-5	2013	For bovine rhodopsin, we developed a new purification strategy including a (NH4)2SO4-induced phase separation that proved essential to obtain crystals of photoactivated rhodopsin containing parallel dimers.	Ammonium Sulfate	75-84	rhodopsin	Bos taurus	169-178
22634396-3	2012	Rod outer segments of photoreceptors are characterized by rhodopsin, a membrane protein surrounded by phospholipids containing a very high concentration of polyunsaturated fatty acids.	Fatty Acids, Unsaturated	156-183	rhodopsin	Bos taurus	58-67
22127612-4	2012	In the present work, we report comparative docking studies of 2-(benzimidazol-2-ylthio)-N-phenylacetamide derived FPR1 agonists, identified here and previously, with several known FPR1 peptide agonists in a FPR1 homology model that is based on the crystal structure of bovine rhodopsin.	2-(1H-Benzimidazol-2-ylthio)-N-phenylacetamide	62-105	rhodopsin	Bos taurus	276-285
22303823-3	2012	Our mutational analysis revealed that the counterion in parietopsin is the glutamic acid (Glu) in the second extracellular loop, corresponding to Glu181 in bovine rhodopsin.	Glutamic Acid	75-88	rhodopsin	Bos taurus	163-172
22303823-3	2012	Our mutational analysis revealed that the counterion in parietopsin is the glutamic acid (Glu) in the second extracellular loop, corresponding to Glu181 in bovine rhodopsin.	Glutamic Acid	90-93	rhodopsin	Bos taurus	163-172
21995315-6	2011	We demonstrate the following: that rhodopsin has a covalently bound all-trans-retinal chromophore and therefore corresponds to the active metarhodopin II state; that transducin has an empty nucleotide-binding pocket; that the isolated complex is active and dissociates upon addition of guanine nucleotide; and finally that the stoichiometry corresponds reproducibly to a 1/1 molar ratio of rhodopsin to transducin.	Guanine Nucleotides	286-304	rhodopsin	Bos taurus	35-44
20964383-0	2010	QM/MM study of dehydro and dihydro beta-ionone retinal analogues in squid and bovine rhodopsins: implications for vision in salamander rhodopsin.	beta-ionone	35-46	rhodopsin	Bos taurus	85-94
21689528-3	2011	Rhodopsin kinetic stability was examined under subsolubilizing (rhodopsin in a bilayer environment perturbed by octyl-beta-D-glucopyranoside) and under fully solubilizing conditions (rhodopsin in a micelle with cosolubilized phospholipids).	octyl-beta-D-glucoside	112-140	rhodopsin	Bos taurus	0-9
21689528-6	2011	However, once the rhodopsin was in a micelle environment there was little change of the T(m) as the phospholipid/rhodopsin ratio in the mixed micelles decreased during the fully solubilized stage.	Phospholipids	100-112	rhodopsin	Bos taurus	18-27
21539361-6	2011	At the temperatures and pHs studied, photointermediates formed after photoexcitation of rhodopsin in nanodiscs are extremely similar to those that form in native membrane, in particular displaying the normal forward shift of the Meta I(480)   Meta II equilibrium with increased temperature and reduced pH which occurs in native membrane but which is not observed in lauryl maltoside detergent suspensions.	lauryl	366-372	rhodopsin	Bos taurus	88-97
21539361-6	2011	At the temperatures and pHs studied, photointermediates formed after photoexcitation of rhodopsin in nanodiscs are extremely similar to those that form in native membrane, in particular displaying the normal forward shift of the Meta I(480)   Meta II equilibrium with increased temperature and reduced pH which occurs in native membrane but which is not observed in lauryl maltoside detergent suspensions.	Maltoside	373-382	rhodopsin	Bos taurus	88-97
21510671-4	2011	In squid rhodopsin, an extended hydrogen bond network that spans ~13 A to Tyr315 on the cytoplasmic site is present regardless of the protonation state of Asp80.	Hydrogen	32-40	rhodopsin	Bos taurus	9-18
21510671-5	2011	In contrast, the extended hydrogen bond network is interrupted at Tyr306 in bovine rhodopsin.	Hydrogen	26-34	rhodopsin	Bos taurus	83-92
21510671-8	2011	Together with the interhelical hydrogen bonds, the salt bridges between TM6 and H9 stabilize the protein conformation of squid rhodopsin and may hinder the occurrence of large conformational changes that are observed upon activation of bovine rhodopsin.	Hydrogen	31-39	rhodopsin	Bos taurus	127-136
20886156-2	2010	In rhodopsin, ECL2 forms a rigid structure including a beta-sheet and interacts with the transmembrane region via a disulfide bond, hydrogen bonds, and hydrophobic interactions.	Disulfides	116-125	rhodopsin	Bos taurus	3-12
20886156-2	2010	In rhodopsin, ECL2 forms a rigid structure including a beta-sheet and interacts with the transmembrane region via a disulfide bond, hydrogen bonds, and hydrophobic interactions.	Hydrogen	132-140	rhodopsin	Bos taurus	3-12
20886156-6	2010	Split rhodopsin was resistant to hydroxylamine and activated transducin upon light absorption similarly to wild-type rhodopsin, but was readily disassembled by photobleaching.	Hydroxylamine	33-46	rhodopsin	Bos taurus	6-15
20923672-2	2010	Microspectrophotometric measurements on isolated, dark-adapted, salamander photoreceptors indicated that the truncated retinal analog, beta-ionone, partitioned into the membranes of green-sensitive rods; however, in blue-sensitive rod outer segments, there was an enhanced uptake of four or more beta-ionones per rhodopsin.	beta-ionone	135-146	rhodopsin	Bos taurus	313-322
20923672-3	2010	X-ray crystallography revealed binding of one beta-ionone to bovine green-sensitive rod rhodopsin.	beta-ionone	46-57	rhodopsin	Bos taurus	88-97
20923672-5	2010	Salamander green-sensitive rod rhodopsin is also expected to bind beta-ionone at sufficiently high concentrations because the binding site is present on its surface.	salamander green	0-16	rhodopsin	Bos taurus	31-40
20923672-5	2010	Salamander green-sensitive rod rhodopsin is also expected to bind beta-ionone at sufficiently high concentrations because the binding site is present on its surface.	beta-ionone	66-77	rhodopsin	Bos taurus	31-40
20923672-6	2010	Therefore, both blue- and green-sensitive rod rhodopsins have at least one allosteric binding site for retinoid, but beta-ionone binds to the latter type of rhodopsin with low affinity and low efficacy.	Retinoids	103-111	rhodopsin	Bos taurus	46-55
20544957-8	2010	The protocol is applied to model the human beta(2)-adrenergic receptor (beta(2)AR) bound to carazolol, using contacts derived from the template structure of bovine rhodopsin.	carazolol	92-101	rhodopsin	Bos taurus	164-173
20030396-1	2010	Bovine rhodopsin contains 11-cis-retinal as a light-absorbing chromophore that binds to a lysine residue of the apoprotein opsin via a protonated Schiff base linkage.	Lysine	90-96	rhodopsin	Bos taurus	7-16
20557105-0	2010	FTIR study of the photoreaction of bovine rhodopsin in the presence of hydroxylamine.	Hydroxylamine	71-84	rhodopsin	Bos taurus	42-51
20557105-1	2010	In bovine rhodopsin, 11-cis-retinal forms a Schiff base linkage with Lys296.	Schiff Bases	44-55	rhodopsin	Bos taurus	10-19
20557105-4	2010	This suggests that activation of rhodopsin creates a specific reaction channel for hydroxylamine or loosens the chromophore binding pocket.	Hydroxylamine	83-96	rhodopsin	Bos taurus	33-42
20042594-4	2010	Here we show the pivotal role of the covalent bond between the retinal chromophore and the lysine residue at position 296 in the activation pathway of bovine rhodopsin, by use of a rhodopsin mutant K296G reconstituted with retinylidene Schiff bases.	Lysine	91-97	rhodopsin	Bos taurus	158-167
20042594-4	2010	Here we show the pivotal role of the covalent bond between the retinal chromophore and the lysine residue at position 296 in the activation pathway of bovine rhodopsin, by use of a rhodopsin mutant K296G reconstituted with retinylidene Schiff bases.	Lysine	91-97	rhodopsin	Bos taurus	181-190
20042594-4	2010	Here we show the pivotal role of the covalent bond between the retinal chromophore and the lysine residue at position 296 in the activation pathway of bovine rhodopsin, by use of a rhodopsin mutant K296G reconstituted with retinylidene Schiff bases.	retinylidene schiff bases	223-248	rhodopsin	Bos taurus	158-167
20030396-1	2010	Bovine rhodopsin contains 11-cis-retinal as a light-absorbing chromophore that binds to a lysine residue of the apoprotein opsin via a protonated Schiff base linkage.	Schiff Bases	146-157	rhodopsin	Bos taurus	7-16
26609989-0	2009	How Does the Relocation of Internal Water Affect Resonance Raman Spectra of Rhodopsin?	Water	36-41	rhodopsin	Bos taurus	76-85
19905009-4	2009	The circular dichroism spectrum of lumirhodopsin, obtained after correcting the 5 micros difference CD data for the bleached rhodopsin, was in reasonable agreement with the lumirhodopsin CD spectrum obtained previously by thermal trapping at -76 degrees C. Similarly, the metarhodopsin II spectrum obtained with a 500 micros delay was also in agreement with the results of previous work on the temperature-trapped form of metarhodopsin II.	Cadmium	100-102	rhodopsin	Bos taurus	39-48
19955366-6	2009	Together, these results indicate that the structure of the rhodopsin N terminus must be maintained by an appropriate amino acid sequence surrounding N2 and may require a carbohydrate moiety at N15.	Carbohydrates	170-182	rhodopsin	Bos taurus	59-68
26609989-2	2009	The effect of relocation of the W2 crystallographic water in bovine rhodopsin has been investigated by comparing and analyzing simulated resonance Raman spectra of 1HZX- and 1U19-based quantum mechanics/molecular mechanics (CASSCF/MM) models.	Water	52-57	rhodopsin	Bos taurus	68-77
26609989-4	2009	In particular, we focus on a quantitative investigation of the changes in the vibrational activity of rhodopsin induced by modifications in the protein cavity structure and in the water position.	Water	180-185	rhodopsin	Bos taurus	102-111
19433801-0	2009	Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors.	Water	10-16	rhodopsin	Bos taurus	75-84
19706606-6	2009	The free enthalpies of helix stabilization and hydrophobic burial of the neutral carboxyl shift the side chain pK(a) into the range typical of Glu-134 in photoactivated rhodopsin.	Glutamic Acid	143-146	rhodopsin	Bos taurus	169-178
19413332-0	2009	Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex.	Phospholipids	0-13	rhodopsin	Bos taurus	97-106
19192200-5	2009	Rhodopsin, a member of the GPCR or seven-transmembrane spanning receptor superfamily, is composed of a chromophore, 11-cis-retinal that is covalently bound by a protonated Schiff base linkage to the apo-protein opsin at Lys(296) (in bovine opsin).	Schiff Bases	172-183	rhodopsin	Bos taurus	0-9
19192200-5	2009	Rhodopsin, a member of the GPCR or seven-transmembrane spanning receptor superfamily, is composed of a chromophore, 11-cis-retinal that is covalently bound by a protonated Schiff base linkage to the apo-protein opsin at Lys(296) (in bovine opsin).	Lysine	220-223	rhodopsin	Bos taurus	0-9
19192200-6	2009	Upon absorption of a photon, isomerization of the chromophore to an all-trans-retinylidene conformation induces changes in the rhodopsin structure, ultimately converting it from an inactive to an activated state.	all-trans-retinylidene	68-90	rhodopsin	Bos taurus	127-136
18984904-7	2009	Phylogenetic analyses and the presence of a lysine residue corresponding to position 90 in bovine rhodopsin suggested that three of the branchiopod opsins comprise UV-sensitive pigments.	Lysine	44-50	rhodopsin	Bos taurus	98-107
19126545-3	2009	Here we describe a serine/alanine (S/A) substitution in long wavelength-absorbing Drosophila visual pigments that occurs at a site corresponding to Ala-292 in bovine rhodopsin.	Serine	19-25	rhodopsin	Bos taurus	166-175
19126545-3	2009	Here we describe a serine/alanine (S/A) substitution in long wavelength-absorbing Drosophila visual pigments that occurs at a site corresponding to Ala-292 in bovine rhodopsin.	Alanine	26-33	rhodopsin	Bos taurus	166-175
19126545-3	2009	Here we describe a serine/alanine (S/A) substitution in long wavelength-absorbing Drosophila visual pigments that occurs at a site corresponding to Ala-292 in bovine rhodopsin.	Alanine	148-151	rhodopsin	Bos taurus	166-175
19166361-4	2009	Here, we report comparative docking studies of anibamine with several other known CCR5 antagonists in two CCR5 homology models built based on the crystal structures of bovine rhodopsin and human beta(2)-adrenergic receptor.	anibamine	47-56	rhodopsin	Bos taurus	175-184
18847221-1	2008	The transient changes of the tryptophan fluorescence of bovine rhodopsin in ROS membranes were followed in time from 1 micros to 10 s after flash excitation of the photoreceptor.	Tryptophan	29-39	rhodopsin	Bos taurus	63-72
18847221-1	2008	The transient changes of the tryptophan fluorescence of bovine rhodopsin in ROS membranes were followed in time from 1 micros to 10 s after flash excitation of the photoreceptor.	ros	76-79	rhodopsin	Bos taurus	63-72
18847221-2	2008	Up to about 100 micros the fluorescence did not change, suggesting that the tryptophan lifetimes in rhodopsin and the M(I) intermediate are similar.	Tryptophan	76-86	rhodopsin	Bos taurus	100-109
18847221-7	2008	Similar results were obtained at other temperatures and with monomeric rhodopsin in dodecyl maltoside micelles.	dodecyl maltoside	84-101	rhodopsin	Bos taurus	71-80
18712874-4	2008	Purified bovine rhodopsin was reconstituted into a series of mono-unsaturated phosphatidylcholines with 14-20 carbons per hydrocarbon chain.	mono-unsaturated phosphatidylcholines	61-98	rhodopsin	Bos taurus	16-25
18676678-7	2008	Homology modeling studies based on the structure of bovine rhodopsin indicated a potential intracellular antagonist binding pocket involving lysine 320.	Lysine	141-147	rhodopsin	Bos taurus	59-68
18712874-4	2008	Purified bovine rhodopsin was reconstituted into a series of mono-unsaturated phosphatidylcholines with 14-20 carbons per hydrocarbon chain.	Carbon	110-117	rhodopsin	Bos taurus	16-25
18712874-4	2008	Purified bovine rhodopsin was reconstituted into a series of mono-unsaturated phosphatidylcholines with 14-20 carbons per hydrocarbon chain.	Hydrocarbons	122-133	rhodopsin	Bos taurus	16-25
18712874-10	2008	The increases of bilayer thickness and helicity of rhodopsin are accompanied by higher metarhodopsin II/metarhodopsin I ratios, faster rates of metarhodopsin II formation, an increase of tryptophan fluorescence, and higher temperatures of rhodopsin denaturation.	Tryptophan	187-197	rhodopsin	Bos taurus	51-60
18399914-1	2008	The regeneration of bovine rhodopsin from its apoprotein opsin and the prosthetic group 11-cis retinal involves the formation of a retinylidene Schiff base with the epsilon-amino group of the active lysine residue of opsin.	retinylidene schiff base	131-155	rhodopsin	Bos taurus	27-36
18424497-0	2008	Regulation of membrane proteins by dietary lipids: effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function.	Cholesterol	62-73	rhodopsin	Bos taurus	138-147
18424497-0	2008	Regulation of membrane proteins by dietary lipids: effects of cholesterol and docosahexaenoic acid acyl chain-containing phospholipids on rhodopsin stability and function.	docosahexaenoic acid acyl chain-containing phospholipids	78-134	rhodopsin	Bos taurus	138-147
18424497-1	2008	Purified bovine rhodopsin was reconstituted into vesicles consisting of 1-stearoyl-2-oleoyl phosphatidylcholine or 1-stearoyl-2-docosahexaenoyl phosphatidylcholine with and without 30 mol % cholesterol.	1-stearoyl-2-oleoyl phosphatidylcholine	72-111	rhodopsin	Bos taurus	16-25
18424497-1	2008	Purified bovine rhodopsin was reconstituted into vesicles consisting of 1-stearoyl-2-oleoyl phosphatidylcholine or 1-stearoyl-2-docosahexaenoyl phosphatidylcholine with and without 30 mol % cholesterol.	1-stearoyl-2-docosahexaenoyl phosphatidylcholine	115-163	rhodopsin	Bos taurus	16-25
18424497-1	2008	Purified bovine rhodopsin was reconstituted into vesicles consisting of 1-stearoyl-2-oleoyl phosphatidylcholine or 1-stearoyl-2-docosahexaenoyl phosphatidylcholine with and without 30 mol % cholesterol.	Cholesterol	190-201	rhodopsin	Bos taurus	16-25
18399914-1	2008	The regeneration of bovine rhodopsin from its apoprotein opsin and the prosthetic group 11-cis retinal involves the formation of a retinylidene Schiff base with the epsilon-amino group of the active lysine residue of opsin.	Lysine	199-205	rhodopsin	Bos taurus	27-36
18399914-4	2008	These results are interpreted by the Matsumoto and Yoshizawa (Nature 258 [1975] 523) model of rhodopsin regeneration in which the 11-cis retinal chromophore binds first to opsin through the beta-ionone ring, followed by the slow formation of the retinylidene Schiff base in a restricted space.	beta-ionone	190-201	rhodopsin	Bos taurus	94-103
18399914-4	2008	These results are interpreted by the Matsumoto and Yoshizawa (Nature 258 [1975] 523) model of rhodopsin regeneration in which the 11-cis retinal chromophore binds first to opsin through the beta-ionone ring, followed by the slow formation of the retinylidene Schiff base in a restricted space.	retinylidene schiff base	246-270	rhodopsin	Bos taurus	94-103
18399914-8	2008	The acceleration of the Schiff base formation in rhodopsin is explained by stabilization of the deprotonated form of the lysyl epsilon-NH(2) group which might be induced when the beta-ionone ring binding site is occupied through the noncovalent binding of 11-cis retinal to opsin at the initial stage of rhodopsin regeneration, followed by the proximity and orientation effect rendered by the formation of noncovalent 11-cis retinal-opsin complex.	Schiff Bases	24-35	rhodopsin	Bos taurus	49-58
18399914-8	2008	The acceleration of the Schiff base formation in rhodopsin is explained by stabilization of the deprotonated form of the lysyl epsilon-NH(2) group which might be induced when the beta-ionone ring binding site is occupied through the noncovalent binding of 11-cis retinal to opsin at the initial stage of rhodopsin regeneration, followed by the proximity and orientation effect rendered by the formation of noncovalent 11-cis retinal-opsin complex.	Schiff Bases	24-35	rhodopsin	Bos taurus	304-313
18399914-8	2008	The acceleration of the Schiff base formation in rhodopsin is explained by stabilization of the deprotonated form of the lysyl epsilon-NH(2) group which might be induced when the beta-ionone ring binding site is occupied through the noncovalent binding of 11-cis retinal to opsin at the initial stage of rhodopsin regeneration, followed by the proximity and orientation effect rendered by the formation of noncovalent 11-cis retinal-opsin complex.	beta-ionone	179-190	rhodopsin	Bos taurus	49-58
18399914-8	2008	The acceleration of the Schiff base formation in rhodopsin is explained by stabilization of the deprotonated form of the lysyl epsilon-NH(2) group which might be induced when the beta-ionone ring binding site is occupied through the noncovalent binding of 11-cis retinal to opsin at the initial stage of rhodopsin regeneration, followed by the proximity and orientation effect rendered by the formation of noncovalent 11-cis retinal-opsin complex.	beta-ionone	179-190	rhodopsin	Bos taurus	304-313
18399918-0	2008	Quantitation of the effect of hydroxylamine on rhodopsin palmitylation.	Hydroxylamine	30-43	rhodopsin	Bos taurus	47-56
18399918-2	2008	The two palmitate groups attached to cysteines 322 and 323 are thought to serve as membrane anchors for the rhodopsin C-terminus, but the absence of the palmitates does not alter membrane localization.	Palmitates	8-17	rhodopsin	Bos taurus	108-117
18399918-2	2008	The two palmitate groups attached to cysteines 322 and 323 are thought to serve as membrane anchors for the rhodopsin C-terminus, but the absence of the palmitates does not alter membrane localization.	Cysteine	37-46	rhodopsin	Bos taurus	108-117
18399918-3	2008	However, removal of the palmitates affects rhodopsin function.	Palmitates	24-34	rhodopsin	Bos taurus	43-52
18399918-4	2008	Therefore, it is important to quantitate the stability of rhodopsin palmitates to hydroxylamine, which is a widely utilized reagent in biochemical preparations of the apoprotein.	Hydroxylamine	82-95	rhodopsin	Bos taurus	58-67
18399918-6	2008	Our data show that both of the bovine rhodopsin palmitates are labile to hydroxylamine, with significant depalmitylation occurring at concentrations of >or=100 mM, with an EC(50) of 220 mM L(-1).	Hydroxylamine	73-86	rhodopsin	Bos taurus	38-47
17034041-2	2006	To understand the molecular interactions of these antagonists, such as losartan and telmisartan, with the AT(1) receptor, a homology model of the human AT(1) (hAT(1)) receptor with all connecting loops was constructed from the 2.6 A resolution crystal structure (PDB i.d., 1L9H) of bovine rhodopsin.	Telmisartan	84-95	rhodopsin	Bos taurus	289-298
18480818-1	2008	Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a G(q)-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cbeta.	Inositol 1,4,5-Trisphosphate	39-67	rhodopsin	Bos taurus	111-120
18480818-1	2008	Invertebrate phototransduction uses an inositol-1,4,5-trisphosphate signalling cascade in which photoactivated rhodopsin stimulates a G(q)-type G protein, that is, a class of G protein that stimulates membrane-bound phospholipase Cbeta.	cbeta	230-235	rhodopsin	Bos taurus	111-120
18396152-4	2008	Results reveal surprisingly rapid conformational transitions of polyunsaturated chains and existence of weakly specific interactions of DHAn3 with spatially distinct sites on rhodopsin.	dhan3	136-141	rhodopsin	Bos taurus	175-184
17900762-1	2008	Ligand-supported homology models of the human histamine H4 receptor (hH4R) were developed based on the crystal structure of bovine rhodopsin and different known H4 ligands (histamine, OUP-16, JNJ7777120).	Histamine	46-55	rhodopsin	Bos taurus	131-140
18033822-0	2008	Efficient coupling of transducin to monomeric rhodopsin in a phospholipid bilayer.	Phospholipids	61-73	rhodopsin	Bos taurus	46-55
18033822-4	2008	Here we report the reconstitution of bovine rhodopsin, a GPCR expressed in the retina, into an apolipoprotein A-I phospholipid particle, derived from high density lipoprotein (HDL).	Phospholipids	114-126	rhodopsin	Bos taurus	44-53
17591774-3	2007	We developed a homology model based on the crystal structure of bovine rhodopsin and predicted novel cysteine substitutions that should dramatically reduce E2 loop flexibility via disulfide bond formation and significantly inhibit the binding of both types of ligands.	Cysteine	101-109	rhodopsin	Bos taurus	71-80
17591774-3	2007	We developed a homology model based on the crystal structure of bovine rhodopsin and predicted novel cysteine substitutions that should dramatically reduce E2 loop flexibility via disulfide bond formation and significantly inhibit the binding of both types of ligands.	Disulfides	180-189	rhodopsin	Bos taurus	71-80
17668276-4	2007	For this purpose, a strategy was pursued in which a homology model of the hH(3)R based on the crystal structure of bovine rhodopsin was generated and refined by molecular dynamics simulations in a dipalmitoylphosphatidylcholine (DPPC)/water membrane mimic before the resulting binding pocket was used for high-throughput docking using the program GOLD.	1,2-Dipalmitoylphosphatidylcholine	197-227	rhodopsin	Bos taurus	122-131
17668276-4	2007	For this purpose, a strategy was pursued in which a homology model of the hH(3)R based on the crystal structure of bovine rhodopsin was generated and refined by molecular dynamics simulations in a dipalmitoylphosphatidylcholine (DPPC)/water membrane mimic before the resulting binding pocket was used for high-throughput docking using the program GOLD.	1,2-Dipalmitoylphosphatidylcholine	229-233	rhodopsin	Bos taurus	122-131
17668276-4	2007	For this purpose, a strategy was pursued in which a homology model of the hH(3)R based on the crystal structure of bovine rhodopsin was generated and refined by molecular dynamics simulations in a dipalmitoylphosphatidylcholine (DPPC)/water membrane mimic before the resulting binding pocket was used for high-throughput docking using the program GOLD.	Water	235-240	rhodopsin	Bos taurus	122-131
17269123-0	2007	Effect of different treatments of long-range interactions and sampling conditions in molecular dynamic simulations of rhodopsin embedded in a dipalmitoyl phosphatidylcholine bilayer.	1,2-Dipalmitoylphosphatidylcholine	142-173	rhodopsin	Bos taurus	118-127
17269123-2	2007	Accordingly, the present work reports the analysis of different simulations of bovine rhodopsin embedded in a dipalmitoyl phosphatidylcholine (DPPC) lipid bilayer using two different sampling conditions and two different approaches for the treatment of long-range electrostatic interactions.	1,2-Dipalmitoylphosphatidylcholine	110-141	rhodopsin	Bos taurus	86-95
17269123-2	2007	Accordingly, the present work reports the analysis of different simulations of bovine rhodopsin embedded in a dipalmitoyl phosphatidylcholine (DPPC) lipid bilayer using two different sampling conditions and two different approaches for the treatment of long-range electrostatic interactions.	1,2-Dipalmitoylphosphatidylcholine	143-147	rhodopsin	Bos taurus	86-95
17303564-0	2007	Stabilizing effect of Zn2+ in native bovine rhodopsin.	Zinc	22-26	rhodopsin	Bos taurus	44-53
17303564-2	2007	We applied SMFS to understand the effect of Zn2+ on the molecular interactions underlying the structure of rhodopsin.	Zinc	44-48	rhodopsin	Bos taurus	107-116
17303564-6	2007	Thus, Zn2+ stabilizes the structure of rhodopsin in a specific manner.	Zinc	6-10	rhodopsin	Bos taurus	39-48
17318366-0	2007	Combined solid state and solution NMR studies of alpha,epsilon-15N labeled bovine rhodopsin.	alpha,epsilon-15n	49-66	rhodopsin	Bos taurus	82-91
17318366-2	2007	Towards the study of dynamics in rhodopsin, we report NMR-spectroscopic investigations of alpha,epsilon-15N-tryptophan labeled rhodopsin in detergent micelles and reconstituted in phospholipids.	alpha,epsilon-15n-tryptophan	90-118	rhodopsin	Bos taurus	33-42
17318366-2	2007	Towards the study of dynamics in rhodopsin, we report NMR-spectroscopic investigations of alpha,epsilon-15N-tryptophan labeled rhodopsin in detergent micelles and reconstituted in phospholipids.	alpha,epsilon-15n-tryptophan	90-118	rhodopsin	Bos taurus	127-136
17213190-1	2007	Recent studies suggest that the second extracellular loop (o2 loop) of bovine rhodopsin and other class I G protein-coupled receptors (GPCRs) targeted by biogenic amine ligands folds deeply into the transmembrane receptor core where the binding of cis-retinal and biogenic amine ligands is known to occur.	Amines	163-168	rhodopsin	Bos taurus	78-87
17213190-1	2007	Recent studies suggest that the second extracellular loop (o2 loop) of bovine rhodopsin and other class I G protein-coupled receptors (GPCRs) targeted by biogenic amine ligands folds deeply into the transmembrane receptor core where the binding of cis-retinal and biogenic amine ligands is known to occur.	Amines	273-278	rhodopsin	Bos taurus	78-87
17196983-0	2007	Linkage between the intramembrane H-bond network around aspartic acid 83 and the cytosolic environment of helix 8 in photoactivated rhodopsin.	Aspartic Acid	56-69	rhodopsin	Bos taurus	132-141
17196983-3	2007	Using FTIR/fluorescence cross-correlation we show specifically that surface alterations monitored by emission changes of fluorescein bound to Cys316 in helix 8 of rhodopsin are highly correlated with (i) H-bonding to Asp83 proximal of the retinal Schiff base but not to Glu122 close to the beta-ionone and (ii) with a metarhodopsin II (MII)-specific 1643 cm(-1) IR absorption change, indicative of a partial loss of secondary structure in helix 8 upon MII formation.	Fluorescein	121-132	rhodopsin	Bos taurus	163-172
17196983-3	2007	Using FTIR/fluorescence cross-correlation we show specifically that surface alterations monitored by emission changes of fluorescein bound to Cys316 in helix 8 of rhodopsin are highly correlated with (i) H-bonding to Asp83 proximal of the retinal Schiff base but not to Glu122 close to the beta-ionone and (ii) with a metarhodopsin II (MII)-specific 1643 cm(-1) IR absorption change, indicative of a partial loss of secondary structure in helix 8 upon MII formation.	Schiff Bases	247-258	rhodopsin	Bos taurus	163-172
17196983-3	2007	Using FTIR/fluorescence cross-correlation we show specifically that surface alterations monitored by emission changes of fluorescein bound to Cys316 in helix 8 of rhodopsin are highly correlated with (i) H-bonding to Asp83 proximal of the retinal Schiff base but not to Glu122 close to the beta-ionone and (ii) with a metarhodopsin II (MII)-specific 1643 cm(-1) IR absorption change, indicative of a partial loss of secondary structure in helix 8 upon MII formation.	(2-benzoylethyl)trimethylammonium	290-294	rhodopsin	Bos taurus	163-172
17196983-3	2007	Using FTIR/fluorescence cross-correlation we show specifically that surface alterations monitored by emission changes of fluorescein bound to Cys316 in helix 8 of rhodopsin are highly correlated with (i) H-bonding to Asp83 proximal of the retinal Schiff base but not to Glu122 close to the beta-ionone and (ii) with a metarhodopsin II (MII)-specific 1643 cm(-1) IR absorption change, indicative of a partial loss of secondary structure in helix 8 upon MII formation.	Norisoprenoids	295-301	rhodopsin	Bos taurus	163-172
18393486-9	2008	2005, 127, 5320-5321) showed that rhodopsin retains photoactivity after incorporation into UV-polymerized bis-SorbPC, but did not address how the protein is associated with the bilayer.	bis-sorbpc	106-116	rhodopsin	Bos taurus	34-43
18393486-10	2008	In this study, we show that rhodopsin is retained in supported bilayers of poly(bis-SorbPC) under ultra-high-vacuum conditions, on the basis of the increase in the XPS nitrogen concentration and the presence of characteristic amino acid peaks in the ToF-SIMS data.	poly(bis-sorbyl phosphatidylcholine)	75-91	rhodopsin	Bos taurus	28-37
18393486-10	2008	In this study, we show that rhodopsin is retained in supported bilayers of poly(bis-SorbPC) under ultra-high-vacuum conditions, on the basis of the increase in the XPS nitrogen concentration and the presence of characteristic amino acid peaks in the ToF-SIMS data.	Nitrogen	168-176	rhodopsin	Bos taurus	28-37
17474760-6	2007	The quantum yield of the bovine rhodopsin E113Q mutant at pH 8.2, where the Schiff base is unprotonated, was significantly lower than that of wild-type rhodopsin, whereas the mutant gave a quantum yield almost identical to that of the wild type at pH 5.5, where the Schiff base is protonated.	Schiff Bases	76-87	rhodopsin	Bos taurus	32-41
17474760-6	2007	The quantum yield of the bovine rhodopsin E113Q mutant at pH 8.2, where the Schiff base is unprotonated, was significantly lower than that of wild-type rhodopsin, whereas the mutant gave a quantum yield almost identical to that of the wild type at pH 5.5, where the Schiff base is protonated.	Schiff Bases	266-277	rhodopsin	Bos taurus	32-41
17576343-3	2007	After complete bleaching of the membranes and subsequent regeneration with the exogenous retinal, 9-cis-rhodopsin is selectively extracted from the membranes using combination of zinc and heptylthioglucoside.	heptylthioglucoside	188-207	rhodopsin	Bos taurus	104-113
17576343-5	2007	The X-ray diffraction from 9-cis-rhodopsin crystals was examined and the electron density map at 2.9 angstroms resolution in the chromophore region can be fitted well with the model of 9-cis-retinal Schiff base.	Schiff Bases	199-210	rhodopsin	Bos taurus	33-42
17176079-5	2006	The rhodopsin in AAO pores is G-protein binding competent as shown by a [35S]GTPgammaS binding assay.	Sulfur-35	73-76	rhodopsin	Bos taurus	4-13
17176079-6	2006	The lipid-rhodopsin interaction was investigated by 2H NMR on sn-1- or sn-2-chain perdeuterated 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phospholine as a matrix lipid.	Deuterium	52-54	rhodopsin	Bos taurus	10-19
17176079-6	2006	The lipid-rhodopsin interaction was investigated by 2H NMR on sn-1- or sn-2-chain perdeuterated 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phospholine as a matrix lipid.	sn-1- or sn-2-chain perdeuterated 1-stearoyl-2-docosahexaenoyl-sn-glycero-3-phospholine	62-149	rhodopsin	Bos taurus	10-19
16959786-1	2006	The interaction of bovine rhodopsin with poly- and monounsaturated lipids was studied by (1)H MAS NMR with magnetization transfer from rhodopsin to lipid.	poly- and monounsaturated lipids	41-73	rhodopsin	Bos taurus	26-35
17098868-6	2006	These peptide surfactants not only enhance the stability of bovine rhodopsin in the presence of lipids and the common surfactants n-dodecyl-beta-D-maltoside and octyl-D-glucoside, but they also significantly stabilize rhodopsin under thermal denaturation conditions, even after lipids are removed.	dodecyl maltoside	130-156	rhodopsin	Bos taurus	67-76
17098868-6	2006	These peptide surfactants not only enhance the stability of bovine rhodopsin in the presence of lipids and the common surfactants n-dodecyl-beta-D-maltoside and octyl-D-glucoside, but they also significantly stabilize rhodopsin under thermal denaturation conditions, even after lipids are removed.	octyl-beta-D-glucoside	161-178	rhodopsin	Bos taurus	67-76
16959786-1	2006	The interaction of bovine rhodopsin with poly- and monounsaturated lipids was studied by (1)H MAS NMR with magnetization transfer from rhodopsin to lipid.	poly- and monounsaturated lipids	41-73	rhodopsin	Bos taurus	135-144
16959786-3	2006	Poly- and monounsaturated lipids interact specifically with different sites on the rhodopsin surface.	poly- and monounsaturated lipids	0-32	rhodopsin	Bos taurus	83-92
16959786-6	2006	All rhodopsin photointermediates transferred magnetization preferentially to DHA-containing lipids, but highest rates were observed for Meta-III rhodopsin.	Dihydroalprenolol	77-80	rhodopsin	Bos taurus	4-13
16731966-2	2006	We applied this approach to the G-protein-coupled receptor bovine rhodopsin in its native membrane using lysine- and cysteine-targeted bifunctional cross-linking reagents.	Lysine	105-111	rhodopsin	Bos taurus	66-75
16815918-0	2006	Bacteriorhodopsin chimeras containing the third cytoplasmic loop of bovine rhodopsin activate transducin for GTP/GDP exchange.	Guanosine Triphosphate	109-112	rhodopsin	Bos taurus	8-17
16815918-0	2006	Bacteriorhodopsin chimeras containing the third cytoplasmic loop of bovine rhodopsin activate transducin for GTP/GDP exchange.	Guanosine Diphosphate	113-116	rhodopsin	Bos taurus	8-17
16895762-1	2006	Transducin is a heterotrimeric GTP-binding protein found in the outer segment of vertebrate retinas that links the photoactivation of rhodopsin (R*) with activation of a robust type VI cGMP phosphodiesterase (PDE6).	Guanosine Triphosphate	31-34	rhodopsin	Bos taurus	134-143
16948780-2	2006	Rhodopsin, the major integral protein of ROSg, is surrounded by phospholipids highly enriched in docosahexaenoic acid (22:6 n3).	Phospholipids	64-77	rhodopsin	Bos taurus	0-9
16948780-2	2006	Rhodopsin, the major integral protein of ROSg, is surrounded by phospholipids highly enriched in docosahexaenoic acid (22:6 n3).	Docosahexaenoic Acids	97-117	rhodopsin	Bos taurus	0-9
16948780-16	2006	In the SDS-PAGE we observed a decrease in the content of all the proteins, mainly rhodopsin, as a consequence of peroxidation.	Sodium Dodecyl Sulfate	7-10	rhodopsin	Bos taurus	82-91
16731966-2	2006	We applied this approach to the G-protein-coupled receptor bovine rhodopsin in its native membrane using lysine- and cysteine-targeted bifunctional cross-linking reagents.	Cysteine	117-125	rhodopsin	Bos taurus	66-75
16634624-8	2006	These results show that several ionizable groups besides the Schiff base imine are affected by the structural changes involved in rhodopsin activation.	schiff base imine	61-78	rhodopsin	Bos taurus	130-139
16634624-9	2006	At least two proton uptake groups and probably at least one proton release group in addition to the Schiff base are present in rhodopsin.	Schiff Bases	100-111	rhodopsin	Bos taurus	127-136
16519899-5	2006	One class corresponded to the unfolding of rhodopsin with the highly conserved Cys110-Cys187 disulfide bond remaining intact and the other class corresponded to the unfolding of the entire rhodopsin polypeptide chain.	Disulfides	93-102	rhodopsin	Bos taurus	43-52
16271145-1	2005	BACKGROUND: Prostacyclin receptor (IP) and thromboxane A2 receptor (TP) belong to rhodopsin-type G protein-coupling receptors and respectively bind to prostacyclin and thromboxane A2 derived from arachidonic acid.	Epoprostenol	151-163	rhodopsin	Bos taurus	82-91
16509586-1	2006	We derived homology models for all human catecholamine-binding GPCRs (CABRs; the alpha-1, alpha-2, and beta-adrenoceptors and the D1-type and D2-type dopamine receptor) using the bovine rhodopsin-11-cis-retinal X-ray structure.	Catecholamines	41-54	rhodopsin	Bos taurus	186-195
16503639-0	2006	Structural changes in the Schiff base region of squid rhodopsin upon photoisomerization studied by low-temperature FTIR spectroscopy.	Schiff Bases	26-37	rhodopsin	Bos taurus	54-63
16503639-1	2006	Low-temperature Fourier transform infrared (FTIR) spectroscopy is used to study squid rhodopsin at 77 K in investigating structural changes in the Schiff base region upon photoisomerization.	Schiff Bases	147-158	rhodopsin	Bos taurus	86-95
16503639-2	2006	The analysis of O-D stretching vibrations in D(2)O revealed that there are more internal water molecules near the retinal chromophore in squid rhodopsin than in bovine rhodopsin.	Water	89-94	rhodopsin	Bos taurus	143-152
16503639-3	2006	Among nine O-D stretching vibrations of water in squid rhodopsin, eight peaks are identical between rhodopsin and 9-cis-rhodopsin (Iso).	Water	40-45	rhodopsin	Bos taurus	55-64
16503639-3	2006	Among nine O-D stretching vibrations of water in squid rhodopsin, eight peaks are identical between rhodopsin and 9-cis-rhodopsin (Iso).	Water	40-45	rhodopsin	Bos taurus	100-109
16503639-3	2006	Among nine O-D stretching vibrations of water in squid rhodopsin, eight peaks are identical between rhodopsin and 9-cis-rhodopsin (Iso).	Water	40-45	rhodopsin	Bos taurus	100-109
16503639-4	2006	On the other hand, the isomer-specific O-D stretch of water was observed for rhodopsin (2451 cm(-)(1)) and Iso (2382 cm(-)(1)).	Water	54-59	rhodopsin	Bos taurus	77-86
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Hydrogen	39-47	rhodopsin	Bos taurus	91-100
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Hydrogen	39-47	rhodopsin	Bos taurus	117-126
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Hydrogen	39-47	rhodopsin	Bos taurus	117-126
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Hydrogen	39-47	rhodopsin	Bos taurus	117-126
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Schiff Bases	60-71	rhodopsin	Bos taurus	91-100
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Schiff Bases	60-71	rhodopsin	Bos taurus	117-126
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Schiff Bases	60-71	rhodopsin	Bos taurus	117-126
16503639-6	2006	In addition, it was suggested that the hydrogen bond of the Schiff base is weaker in squid rhodopsin than in bacteriorhodopsin and bovine rhodopsin, and squid rhodopsin possessed similar hydrogen bonding strength for the Schiff base among rhodopsin, Iso, and bathorhodopsin.	Schiff Bases	60-71	rhodopsin	Bos taurus	117-126
16503639-7	2006	Most vibrational bands in the X-D stretch region originate from water O-D or the Schiff base N-D stretches, suggesting that the hydrogen bonding network in the Schiff base region of squid rhodopsin is composed of only water molecules.	Water	64-69	rhodopsin	Bos taurus	188-197
16503639-7	2006	Most vibrational bands in the X-D stretch region originate from water O-D or the Schiff base N-D stretches, suggesting that the hydrogen bonding network in the Schiff base region of squid rhodopsin is composed of only water molecules.	Schiff Bases	81-92	rhodopsin	Bos taurus	188-197
16503639-7	2006	Most vibrational bands in the X-D stretch region originate from water O-D or the Schiff base N-D stretches, suggesting that the hydrogen bonding network in the Schiff base region of squid rhodopsin is composed of only water molecules.	Hydrogen	128-136	rhodopsin	Bos taurus	188-197
16503639-7	2006	Most vibrational bands in the X-D stretch region originate from water O-D or the Schiff base N-D stretches, suggesting that the hydrogen bonding network in the Schiff base region of squid rhodopsin is composed of only water molecules.	Schiff Bases	160-171	rhodopsin	Bos taurus	188-197
16503639-7	2006	Most vibrational bands in the X-D stretch region originate from water O-D or the Schiff base N-D stretches, suggesting that the hydrogen bonding network in the Schiff base region of squid rhodopsin is composed of only water molecules.	Water	218-223	rhodopsin	Bos taurus	188-197
16548507-2	2006	The reviewed studies provide fundamental insight on long-standing problems regarding the assembly and function of the individual residues and bound water molecules that form the rhodopsin active site, a center that catalyzes the 11-cis/all-trans isomerization of the retinyl chromophore in the primary step of the phototransduction mechanism.	Water	148-153	rhodopsin	Bos taurus	178-187
16293613-11	2006	His-216 occupies a position similar to that of Tyr-136 in bovine rhodopsin, part of the DRY motif of the latter receptor.	Histidine	0-3	rhodopsin	Bos taurus	65-74
16293613-11	2006	His-216 occupies a position similar to that of Tyr-136 in bovine rhodopsin, part of the DRY motif of the latter receptor.	Tyrosine	47-50	rhodopsin	Bos taurus	65-74
16271145-1	2005	BACKGROUND: Prostacyclin receptor (IP) and thromboxane A2 receptor (TP) belong to rhodopsin-type G protein-coupling receptors and respectively bind to prostacyclin and thromboxane A2 derived from arachidonic acid.	Thromboxane A2	43-57	rhodopsin	Bos taurus	82-91
16271145-1	2005	BACKGROUND: Prostacyclin receptor (IP) and thromboxane A2 receptor (TP) belong to rhodopsin-type G protein-coupling receptors and respectively bind to prostacyclin and thromboxane A2 derived from arachidonic acid.	Arachidonic Acid	196-212	rhodopsin	Bos taurus	82-91
16085419-3	2005	In the present work, a 3D model of the rat histamine H(3) receptor, built by comparative modeling from the crystallographic coordinates of bovine rhodopsin, is presented with the discussion of its ability to predict the potency of known and new H(3) antagonists.	HS 3	53-57	rhodopsin	Bos taurus	146-155
15927400-3	2005	Quantitative immobilization of the membrane-bound rhodopsin either non-specifically on a carboxylated dextran surface grafted with long alkyl groups, or specifically on a surface coated with anti-rhodopsin antibody was demonstrated by surface plasmon resonance.	Dextrans	102-109	rhodopsin	Bos taurus	50-59
16097745-2	2005	Bovine rhodopsin (Rho) in its dark-adapted state was intramolecularly cross-linked with lysine-cysteine (K-C) or lysine-lysine (K-K) cross-linkers to obtain interatomic distance information.	lysine-cysteine	88-103	rhodopsin	Bos taurus	7-16
16097745-2	2005	Bovine rhodopsin (Rho) in its dark-adapted state was intramolecularly cross-linked with lysine-cysteine (K-C) or lysine-lysine (K-K) cross-linkers to obtain interatomic distance information.	lysine-lysine	113-126	rhodopsin	Bos taurus	7-16
16026166-0	2005	Direct observation of the complex formation of GDP-bound transducin with the rhodopsin intermediate having a visible absorption maximum in rod outer segment membranes.	Guanosine Diphosphate	47-50	rhodopsin	Bos taurus	77-86
16026166-1	2005	Rhodopsin is a photoreceptive protein that is present in rod photoreceptor cells, inducing a GDP-GTP exchange reaction on the retinal G-protein transducin (Gt) upon light absorption.	gdp-gtp	93-100	rhodopsin	Bos taurus	0-9
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Diphosphate	119-122	rhodopsin	Bos taurus	106-115
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Diphosphate	119-122	rhodopsin	Bos taurus	166-175
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Diphosphate	153-156	rhodopsin	Bos taurus	106-115
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Diphosphate	153-156	rhodopsin	Bos taurus	166-175
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Triphosphate	207-210	rhodopsin	Bos taurus	106-115
16026166-2	2005	This exchange reaction proceeds through at least three steps, which include the binding of photoactivated rhodopsin to GDP-bound Gt, the dissociation of GDP from the rhodopsin-Gt complex, and the binding of GTP to the nucleotide-unbound Gt.	Guanosine Triphosphate	207-210	rhodopsin	Bos taurus	166-175
16026166-3	2005	These steps have been thought to occur after the formation of the rhodopsin intermediate, meta-II; however, the extra formation of meta-II, which reflects the formation of a complex with Gt, was inhibited in the presence of excess GDP.	GT	187-189	rhodopsin	Bos taurus	66-75
16026166-3	2005	These steps have been thought to occur after the formation of the rhodopsin intermediate, meta-II; however, the extra formation of meta-II, which reflects the formation of a complex with Gt, was inhibited in the presence of excess GDP.	Guanosine Diphosphate	231-234	rhodopsin	Bos taurus	66-75
15924417-6	2005	The analysis of N-D and O-D stretching vibrations in D(2)O revealed that the hydrogen bond of the Schiff base is weaker in retinochrome than in bovine rhodopsin and bacteriorhodopsin, while retinochrome has a water molecule under strongly hydrogen-bonded conditions (O-D stretch at 2334 cm(-)(1)).	Hydrogen	77-85	rhodopsin	Bos taurus	151-160
15819603-0	2005	Effect of digitonin on the rhodopsin meta I-meta II equilibrium.	Digitonin	10-19	rhodopsin	Bos taurus	27-36
15819603-4	2005	The possibility that digitonin induced large-scale aggregation of rhodopsin in the disk membrane that could be reversed by azolectin was tested using time-resolved linear dichroism.	Digitonin	21-30	rhodopsin	Bos taurus	66-75
15819603-4	2005	The possibility that digitonin induced large-scale aggregation of rhodopsin in the disk membrane that could be reversed by azolectin was tested using time-resolved linear dichroism.	asolectin	123-132	rhodopsin	Bos taurus	66-75
15924417-6	2005	The analysis of N-D and O-D stretching vibrations in D(2)O revealed that the hydrogen bond of the Schiff base is weaker in retinochrome than in bovine rhodopsin and bacteriorhodopsin, while retinochrome has a water molecule under strongly hydrogen-bonded conditions (O-D stretch at 2334 cm(-)(1)).	Schiff Bases	98-109	rhodopsin	Bos taurus	151-160
15826160-7	2005	In this study, we have examined the effects of UV polymerization of bis-Sorbylphosphatidylcholine (bis-SorbPC) on the photoactivation of reconstituted bovine rhodopsin (Rho), a model G-protein-coupled receptor.	bis-sorbylphosphatidylcholine	68-97	rhodopsin	Bos taurus	158-167
15826160-7	2005	In this study, we have examined the effects of UV polymerization of bis-Sorbylphosphatidylcholine (bis-SorbPC) on the photoactivation of reconstituted bovine rhodopsin (Rho), a model G-protein-coupled receptor.	bis-sorbpc	99-109	rhodopsin	Bos taurus	158-167
15449951-0	2004	Time-resolved photointermediate changes in rhodopsin glutamic acid 181 mutants.	Glutamic Acid	53-66	rhodopsin	Bos taurus	43-52
15764373-3	2004	In this work we demonstrate by electron microscopy of negatively stained samples, blue native- and sodium dodecyl sulphate-polyacrylamide gel electrophoresis, chemical crosslinking, and by proteolysis that native bovine rhodopsin exists mainly as dimers and higher oligomers.	Sodium Dodecyl Sulfate	99-122	rhodopsin	Bos taurus	220-229
15764373-3	2004	In this work we demonstrate by electron microscopy of negatively stained samples, blue native- and sodium dodecyl sulphate-polyacrylamide gel electrophoresis, chemical crosslinking, and by proteolysis that native bovine rhodopsin exists mainly as dimers and higher oligomers.	polyacrylamide	123-137	rhodopsin	Bos taurus	220-229
15449951-1	2004	The role of glutamic acid 181 in the bovine rhodopsin retinylidene chromophore pocket was studied by expressing E181 mutants in COS cells and measuring, as a function of time, the absorbance changes produced after excitation of lauryl maltoside pigment suspensions with 7 ns laser pulses.	Glutamic Acid	12-25	rhodopsin	Bos taurus	44-53
15449951-1	2004	The role of glutamic acid 181 in the bovine rhodopsin retinylidene chromophore pocket was studied by expressing E181 mutants in COS cells and measuring, as a function of time, the absorbance changes produced after excitation of lauryl maltoside pigment suspensions with 7 ns laser pulses.	retinylidene	54-66	rhodopsin	Bos taurus	44-53
15480300-7	2004	RESULTS: A synthetic peptide phosphorylated on residues corresponding to Ser-338, Thr-340, Thr-342 and Ser-343 of bovine rhodopsin was sufficient for direct binding to visual arrestin.	Serine	73-76	rhodopsin	Bos taurus	121-130
15480300-7	2004	RESULTS: A synthetic peptide phosphorylated on residues corresponding to Ser-338, Thr-340, Thr-342 and Ser-343 of bovine rhodopsin was sufficient for direct binding to visual arrestin.	Threonine	82-85	rhodopsin	Bos taurus	121-130
15480300-7	2004	RESULTS: A synthetic peptide phosphorylated on residues corresponding to Ser-338, Thr-340, Thr-342 and Ser-343 of bovine rhodopsin was sufficient for direct binding to visual arrestin.	Threonine	91-94	rhodopsin	Bos taurus	121-130
15480300-7	2004	RESULTS: A synthetic peptide phosphorylated on residues corresponding to Ser-338, Thr-340, Thr-342 and Ser-343 of bovine rhodopsin was sufficient for direct binding to visual arrestin.	Serine	103-106	rhodopsin	Bos taurus	121-130
15258159-0	2004	The hydrodynamic properties of dark- and light-activated states of n-dodecyl beta-D-maltoside-solubilized bovine rhodopsin support the dimeric structure of both conformations.	dodecyl maltoside	67-93	rhodopsin	Bos taurus	113-122
15258159-1	2004	Rhodopsin (Rho) has been extracted in n-dodecyl beta-D-maltoside (DM) from bovine retinal rod outer segments and purified to homogeneity by affinity chromatography on concanavalin A-Sepharose.	dodecyl maltoside	38-64	rhodopsin	Bos taurus	0-9
15258159-1	2004	Rhodopsin (Rho) has been extracted in n-dodecyl beta-D-maltoside (DM) from bovine retinal rod outer segments and purified to homogeneity by affinity chromatography on concanavalin A-Sepharose.	Sepharose	182-191	rhodopsin	Bos taurus	0-9
15303842-4	2004	These mechanisms suggest that rhodopsin possesses a pocket, proximal to the Schiff base so that porphyrins act as photosensitizers.	Schiff Bases	76-87	rhodopsin	Bos taurus	30-39
15461454-0	2004	Deuterium NMR structure of retinal in the ground state of rhodopsin.	Deuterium	0-9	rhodopsin	Bos taurus	58-67
15461454-2	2004	Site-directed deuterium ((2)H) NMR spectroscopy was used to investigate the structure of retinal within the binding pocket of bovine rhodopsin.	Deuterium	14-23	rhodopsin	Bos taurus	133-142
15303842-4	2004	These mechanisms suggest that rhodopsin possesses a pocket, proximal to the Schiff base so that porphyrins act as photosensitizers.	Porphyrins	96-106	rhodopsin	Bos taurus	30-39
15041637-5	2004	The crystal structure of bovine rhodopsin has the second extracellular (EC-II) loop closed over the transmembrane regions by making a disulfide linkage between Cys-110 and Cys-187, but we speculate that opening this loop may play a role in the activation process of the receptor through the cysteine linkage with helix 3.	Disulfides	134-143	rhodopsin	Bos taurus	32-41
15041637-5	2004	The crystal structure of bovine rhodopsin has the second extracellular (EC-II) loop closed over the transmembrane regions by making a disulfide linkage between Cys-110 and Cys-187, but we speculate that opening this loop may play a role in the activation process of the receptor through the cysteine linkage with helix 3.	Cysteine	160-163	rhodopsin	Bos taurus	32-41
15041637-5	2004	The crystal structure of bovine rhodopsin has the second extracellular (EC-II) loop closed over the transmembrane regions by making a disulfide linkage between Cys-110 and Cys-187, but we speculate that opening this loop may play a role in the activation process of the receptor through the cysteine linkage with helix 3.	Cysteine	172-175	rhodopsin	Bos taurus	32-41
15041637-5	2004	The crystal structure of bovine rhodopsin has the second extracellular (EC-II) loop closed over the transmembrane regions by making a disulfide linkage between Cys-110 and Cys-187, but we speculate that opening this loop may play a role in the activation process of the receptor through the cysteine linkage with helix 3.	Cysteine	291-299	rhodopsin	Bos taurus	32-41
15041637-10	2004	We validate HierDock by predicting the binding site of 11-cis-retinal in the crystal structure of bovine rhodopsin.	Retinaldehyde	55-69	rhodopsin	Bos taurus	105-114
15041682-1	2004	The deactivation of the bovine G-protein-coupled receptor, rhodopsin, is a two-step process consisting of the phosphorylation of specific serine and threonine residues in the cytoplasmic tail of rhodopsin by rhodopsin kinase.	Serine	138-144	rhodopsin	Bos taurus	59-68
15041682-1	2004	The deactivation of the bovine G-protein-coupled receptor, rhodopsin, is a two-step process consisting of the phosphorylation of specific serine and threonine residues in the cytoplasmic tail of rhodopsin by rhodopsin kinase.	Serine	138-144	rhodopsin	Bos taurus	195-204
15041682-1	2004	The deactivation of the bovine G-protein-coupled receptor, rhodopsin, is a two-step process consisting of the phosphorylation of specific serine and threonine residues in the cytoplasmic tail of rhodopsin by rhodopsin kinase.	Threonine	149-158	rhodopsin	Bos taurus	59-68
15041682-1	2004	The deactivation of the bovine G-protein-coupled receptor, rhodopsin, is a two-step process consisting of the phosphorylation of specific serine and threonine residues in the cytoplasmic tail of rhodopsin by rhodopsin kinase.	Threonine	149-158	rhodopsin	Bos taurus	195-204
15038749-1	2004	We have obtained carbon-carbon bond length data for the functional retinylidene chromophore of rhodopsin, with a spatial resolution of 3 pm.	Carbon	17-23	rhodopsin	Bos taurus	95-104
15038749-1	2004	We have obtained carbon-carbon bond length data for the functional retinylidene chromophore of rhodopsin, with a spatial resolution of 3 pm.	Carbon	24-30	rhodopsin	Bos taurus	95-104
15038749-1	2004	We have obtained carbon-carbon bond length data for the functional retinylidene chromophore of rhodopsin, with a spatial resolution of 3 pm.	retinylidene	67-79	rhodopsin	Bos taurus	95-104
15056918-4	2004	In this paper, we report the large scale preparation of a stable, homogenous species, truncated octopus rhodopsin (t-rhodopsin) in which proteolysis has removed the proline-rich C-terminal; this species retains the spectral properties and the ability for light-induced G-protein activation of unproteolyzed octopus rhodopsin.	Proline	165-172	rhodopsin	Bos taurus	104-113
15056918-4	2004	In this paper, we report the large scale preparation of a stable, homogenous species, truncated octopus rhodopsin (t-rhodopsin) in which proteolysis has removed the proline-rich C-terminal; this species retains the spectral properties and the ability for light-induced G-protein activation of unproteolyzed octopus rhodopsin.	Proline	165-172	rhodopsin	Bos taurus	117-126
15056918-4	2004	In this paper, we report the large scale preparation of a stable, homogenous species, truncated octopus rhodopsin (t-rhodopsin) in which proteolysis has removed the proline-rich C-terminal; this species retains the spectral properties and the ability for light-induced G-protein activation of unproteolyzed octopus rhodopsin.	Proline	165-172	rhodopsin	Bos taurus	117-126
15056918-6	2004	Photoisomerization of t-Acid Metarhodopsin leads back to the inactive form, t-rhodopsin with the inverse agonist 11-cis-retinal.	11-cis-Retinal	116-127	rhodopsin	Bos taurus	33-42
14660595-7	2004	To test the predictive power of ET, we introduced novel mutations in bovine rhodopsin at a globally important position, Leu-79, and at an opsin-specific position, Trp-175.	Leucine	120-123	rhodopsin	Bos taurus	76-85
14704269-1	2004	The binding site of the dopamine D(2) receptor (D2R), like those of homologous rhodopsin-like G protein-coupled receptors (GPCRs) that bind small molecules, is contained within a water-accessible crevice formed among its seven transmembrane segments (TMs).	Water	179-184	rhodopsin	Bos taurus	79-88
14981504-1	2004	The counterion, a negatively charged amino acid residue that stabilizes a positive charge on the retinylidene chromophore, is essential for rhodopsin to receive visible light.	retinylidene	97-109	rhodopsin	Bos taurus	140-149
14704269-6	2004	The pattern of accessibility in E2 is consistent with a structure similar to that of bovine rhodopsin, in which the region C-terminal to the conserved disulfide bond is deeper in the binding-site crevice than is the N-terminal part of E2.	Disulfides	151-160	rhodopsin	Bos taurus	92-101
12911303-0	2003	Structural changes of water molecules during the photoactivation processes in bovine rhodopsin.	Water	22-27	rhodopsin	Bos taurus	85-94
14500738-6	2003	To visualize these experimental findings, we have constructed a homology model based on the X-ray crystal of bovine rhodopsin and have suggested a possible binding mode of MPEP.	6-methyl-2-(phenylethynyl)pyridine	172-176	rhodopsin	Bos taurus	116-125
14499593-1	2003	The endergonic trans-->cis isomerization of retinoids is an essential element in rhodopsin regeneration in vertebrates.	Retinoids	47-56	rhodopsin	Bos taurus	84-93
14611941-2	2003	The effect of dodecyl maltoside detergent on the thermal stability of dark-state rhodopsin, and upon formation of the different intermediates after rhodopsin photobleaching (metarhodopsin II and metarhodopsin III), and upon transducin activation has been studied.	dodecyl maltoside	14-31	rhodopsin	Bos taurus	81-90
14621981-0	2003	Conformational similarities in the beta-ionone ring region of the rhodopsin chromophore in its ground state and after photoactivation to the metarhodopsin-I intermediate.	beta-ionone	35-46	rhodopsin	Bos taurus	66-75
14621981-3	2003	Indirect photoconversion via the primary intermediate, bathorhodopin, was adopted as the preferred method since approximately 44% conversion to the metarhodopsin-I component could be achieved, with only low levels (approximately 18%) of ground-state rhodopsin remaining.	bathorhodopin	55-68	rhodopsin	Bos taurus	152-161
14645481-4	2003	This residue (UV: lysine vs blue:asparagine or glutamate) corresponds to amino acid position glycine 90 (G90) in bovine rhodopsin, a site affected in autosomal dominant human congenital night blindness.	Lysine	18-24	rhodopsin	Bos taurus	120-129
14645481-4	2003	This residue (UV: lysine vs blue:asparagine or glutamate) corresponds to amino acid position glycine 90 (G90) in bovine rhodopsin, a site affected in autosomal dominant human congenital night blindness.	Asparagine	33-43	rhodopsin	Bos taurus	120-129
14645481-4	2003	This residue (UV: lysine vs blue:asparagine or glutamate) corresponds to amino acid position glycine 90 (G90) in bovine rhodopsin, a site affected in autosomal dominant human congenital night blindness.	Glutamic Acid	47-56	rhodopsin	Bos taurus	120-129
14645481-4	2003	This residue (UV: lysine vs blue:asparagine or glutamate) corresponds to amino acid position glycine 90 (G90) in bovine rhodopsin, a site affected in autosomal dominant human congenital night blindness.	Glycine	93-100	rhodopsin	Bos taurus	120-129
12370420-2	2002	Rhodopsin purified from rod outer segments of bovine retinae by immunoaffinity chromatography in octyl glucoside was reconstituted into liposomes prepared from soybean phospholipids by detergent dialysis.	octyl-beta-D-glucoside	97-112	rhodopsin	Bos taurus	0-9
12902330-7	2003	From mutational studies and three-dimensional modeling based on the structure of bovine rhodopsin, we conclude that the helix 8 of LTB4 receptor 1 plays an important role in the conformational change of the receptor to the low affinity state after G-protein activation, possibly by sensing the status of coupling Galpha subunits as GTP-bound.	Guanosine Triphosphate	332-335	rhodopsin	Bos taurus	88-97
12718552-8	2003	The results are discussed in the context of possibly related processes on the same time scale that have been observed recently in artificial visual pigments with synthetic retinylidene chromophores and in a related rhodopsin mutant.	retinylidene	172-184	rhodopsin	Bos taurus	215-224
12601023-4	2003	The decay of photoactivated rhodopsin (R*) and inactivation of transducin by guanosine triphosphate (GTP) hydrolysis are the leading candidates for limiting the rate of phototransduction turn-off.	Guanosine Triphosphate	77-99	rhodopsin	Bos taurus	28-37
12601023-4	2003	The decay of photoactivated rhodopsin (R*) and inactivation of transducin by guanosine triphosphate (GTP) hydrolysis are the leading candidates for limiting the rate of phototransduction turn-off.	Guanosine Triphosphate	101-104	rhodopsin	Bos taurus	28-37
12482872-3	2003	A specific effect of Zn(2+) on the thermal stability of rhodopsin, obtained from bovine retinas and solubilized in dodecyl maltoside detergent, in the dark is reported.	Zinc	21-23	rhodopsin	Bos taurus	56-65
12482872-4	2003	The thermal stability of rhodopsin in its ground state (dark state) is clearly reduced with increasing Zn(2+) concentrations (0-50 microm Zn(2+)).	Zinc	103-109	rhodopsin	Bos taurus	25-34
12482872-4	2003	The thermal stability of rhodopsin in its ground state (dark state) is clearly reduced with increasing Zn(2+) concentrations (0-50 microm Zn(2+)).	Zinc	103-105	rhodopsin	Bos taurus	25-34
12482872-9	2003	These effects, specific for zinc, are also seen for rhodopsin in native disc membranes, and may be relevant to the suggested role of Zn(2+) in normal and pathological retinal function.	Zinc	133-135	rhodopsin	Bos taurus	52-61
12710180-2	2003	Digitonin extract of bovine rhodopsin was irradiated at -155 degrees C with blue light (436 nm).	Digitonin	0-9	rhodopsin	Bos taurus	28-37
12471166-1	2003	Rhodopsin is a retinal photoreceptor protein of bipartite structure consisting of the transmembrane protein opsin and a light-sensitive chromophore 11-cis-retinal, linked to opsin via a protonated Schiff base.	Schiff Bases	197-208	rhodopsin	Bos taurus	0-9
12479925-4	2003	With this work we demonstrated, by means of an NMR-based and a computational conformational analysis, that 8-alkynyladenosines, differently from 2-alkynyladenosines, cannot adopt the sugar-base anti conformation required for adenosine receptor activation.Furthermore, using the recently reported X-ray crystal structure of bovine rhodopsin as template, we built a 3D model of the seven transmembrane domains of the human adenosine A(3) receptor with the homology modeling.	8-alkynyladenosines	107-126	rhodopsin	Bos taurus	330-339
12370420-2	2002	Rhodopsin purified from rod outer segments of bovine retinae by immunoaffinity chromatography in octyl glucoside was reconstituted into liposomes prepared from soybean phospholipids by detergent dialysis.	Phospholipids	168-181	rhodopsin	Bos taurus	0-9
12370420-3	2002	The orientation of rhodopsin in the liposomes was determined by susceptibility of its C terminus to papain and the endoproteinase, Asp-N, followed by SDS/PAGE, which showed that the cytoplasmic domain in at least 90% of rhodopsin faced the exterior of the proteoliposomes.	Sodium Dodecyl Sulfate	150-153	rhodopsin	Bos taurus	19-28
12093898-0	2002	(1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin.	Norisoprenoids	89-95	rhodopsin	Bos taurus	136-145
12093898-0	2002	(1)H and (13)C MAS NMR evidence for pronounced ligand-protein interactions involving the ionone ring of the retinylidene chromophore in rhodopsin.	retinylidene	108-120	rhodopsin	Bos taurus	136-145
12130792-3	2002	An antigenic peptide obtained by a cyanogene bromide cleavage of rhodopsin was purified and determined as residues 2-39 in the amino acid sequence.	cyanogene bromide	35-52	rhodopsin	Bos taurus	65-74
12069576-1	2002	Bovine rhodopsin was specifically labeled on the cytoplasmic surface at cysteine 140 (the first residue of the loop connecting helices III and IV) or at cysteine 316 (in the loop connecting helix VII and the palmitoylation sites) with the fluorescent labels fluorescein and Texas Red.	Cysteine	72-80	rhodopsin	Bos taurus	7-16
12069576-1	2002	Bovine rhodopsin was specifically labeled on the cytoplasmic surface at cysteine 140 (the first residue of the loop connecting helices III and IV) or at cysteine 316 (in the loop connecting helix VII and the palmitoylation sites) with the fluorescent labels fluorescein and Texas Red.	Cysteine	153-161	rhodopsin	Bos taurus	7-16
12069576-1	2002	Bovine rhodopsin was specifically labeled on the cytoplasmic surface at cysteine 140 (the first residue of the loop connecting helices III and IV) or at cysteine 316 (in the loop connecting helix VII and the palmitoylation sites) with the fluorescent labels fluorescein and Texas Red.	Fluorescein	258-269	rhodopsin	Bos taurus	7-16
12069576-1	2002	Bovine rhodopsin was specifically labeled on the cytoplasmic surface at cysteine 140 (the first residue of the loop connecting helices III and IV) or at cysteine 316 (in the loop connecting helix VII and the palmitoylation sites) with the fluorescent labels fluorescein and Texas Red.	Texas red	274-283	rhodopsin	Bos taurus	7-16
12056885-0	2002	Relative orientation between the beta-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes.	beta-ionone	33-44	rhodopsin	Bos taurus	95-104
12056885-0	2002	Relative orientation between the beta-ionone ring and the polyene chain for the chromophore of rhodopsin in native membranes.	Polyenes	58-65	rhodopsin	Bos taurus	95-104
12056885-1	2002	Rotational resonance solid state nuclear magnetic resonance has been used to determine the relative orientation of the beta-ionone ring and the polyene chain of the chromophore 11-Z-retinylidene of rhodopsin in rod outer segment membranes from bovine retina.	Polyenes	144-151	rhodopsin	Bos taurus	198-207
12056885-1	2002	Rotational resonance solid state nuclear magnetic resonance has been used to determine the relative orientation of the beta-ionone ring and the polyene chain of the chromophore 11-Z-retinylidene of rhodopsin in rod outer segment membranes from bovine retina.	11-z-retinylidene	177-194	rhodopsin	Bos taurus	198-207
12056885-6	2002	The resulting distance constraints, C8 to C16 and C17 (4.05 +/- 0.25 A) and from C8 to C18 (2.95 +/- 0.15 A), show that the major portion of retinylidene in rhodopsin has a twisted 6-s-cis conformation.	retinylidene	141-153	rhodopsin	Bos taurus	157-166
12009897-5	2002	Here we have investigated the relation of nonlamellar-forming lipids, such as dioleoylphosphatidylethanolamine (DOPE), together with dioleoylphosphatidylcholine (DOPC), to the photochemistry of membrane-bound rhodopsin.	dioleoyl phosphatidylethanolamine	78-110	rhodopsin	Bos taurus	209-218
12009897-5	2002	Here we have investigated the relation of nonlamellar-forming lipids, such as dioleoylphosphatidylethanolamine (DOPE), together with dioleoylphosphatidylcholine (DOPC), to the photochemistry of membrane-bound rhodopsin.	1,2-oleoylphosphatidylcholine	133-160	rhodopsin	Bos taurus	209-218
11968076-5	2002	The titled retinoid was synthesized for study of the absolute conformation of the retinal pigment in rhodopsin.	Retinoids	11-19	rhodopsin	Bos taurus	101-110
11806921-0	2002	Suramin affects coupling of rhodopsin to transducin.	Suramin	0-7	rhodopsin	Bos taurus	28-37
11961111-3	2002	We report herein the location of the binding site for the inhaled anesthetic halothane at the amino acid residue level of resolution in the ligand binding cavity in a prototypical G protein-coupled receptor, bovine rhodopsin.	Halothane	77-86	rhodopsin	Bos taurus	215-224
11961111-4	2002	Tryptophan fluorescence quenching and direct photoaffinity labeling with [(14)C]halothane suggested an interhelical location of halothane with a stoichiometry of 1 (halothane/rhodopsin molar ratio).	Halothane	128-137	rhodopsin	Bos taurus	175-184
11961111-5	2002	Radiosequence analysis of [(14)C]halothane-labeled rhodopsin revealed that halothane contacts an amino acid residue (Trp265) lining the ligand binding cavity in the transmembrane core of the receptor.	Halothane	33-42	rhodopsin	Bos taurus	51-60
11961111-5	2002	Radiosequence analysis of [(14)C]halothane-labeled rhodopsin revealed that halothane contacts an amino acid residue (Trp265) lining the ligand binding cavity in the transmembrane core of the receptor.	Halothane	75-84	rhodopsin	Bos taurus	51-60
11801601-3	2002	Alanine-scanning mutagenesis of residues close to the intracellular end of H6 of the 5-HT2A receptor implicated glutamate Glu-318(6.30) in receptor activation, as also predicted by a newly constructed molecular model of the 5-HT2A receptor, which was based on the x-ray structure of bovine rhodopsin.	Alanine	0-7	rhodopsin	Bos taurus	290-299
11801601-3	2002	Alanine-scanning mutagenesis of residues close to the intracellular end of H6 of the 5-HT2A receptor implicated glutamate Glu-318(6.30) in receptor activation, as also predicted by a newly constructed molecular model of the 5-HT2A receptor, which was based on the x-ray structure of bovine rhodopsin.	Glutamic Acid	122-125	rhodopsin	Bos taurus	290-299
11888278-0	2002	Function of extracellular loop 2 in rhodopsin: glutamic acid 181 modulates stability and absorption wavelength of metarhodopsin II.	Glutamic Acid	47-60	rhodopsin	Bos taurus	36-45
11888278-1	2002	The second extracellular loop of rhodopsin folds back into the membrane-embedded domain of the receptor to form part of the binding pocket for the 11-cis-retinylidene chromophore.	11-cis-retinylidene	147-166	rhodopsin	Bos taurus	33-42
11827550-5	2002	Large increases were seen in the amount of metarhodopsin I which appeared after photolysis of 5-ethylisorhodopsin and the bicyclic isorhodopsin analogue, while 5-demethyl-8-methylisorhodopsin more closely followed native rhodopsin in decaying through meta I380, a 380 nm absorbing precursor to metarhodopsin II.	5-ethylisorhodopsin	94-113	rhodopsin	Bos taurus	47-56
11827550-5	2002	Large increases were seen in the amount of metarhodopsin I which appeared after photolysis of 5-ethylisorhodopsin and the bicyclic isorhodopsin analogue, while 5-demethyl-8-methylisorhodopsin more closely followed native rhodopsin in decaying through meta I380, a 380 nm absorbing precursor to metarhodopsin II.	5-demethyl-8-methylisorhodopsin	160-191	rhodopsin	Bos taurus	47-56
11972040-0	2002	Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography.	Water	28-33	rhodopsin	Bos taurus	47-56
11972040-2	2002	In rhodopsin, a prototypical GPCR, the helical bundle accommodates an intrinsic inverse-agonist 11-cis-retinal, which undergoes photo-isomerization to the all-trans form upon light absorption.	Retinaldehyde	96-110	rhodopsin	Bos taurus	3-12
11972040-4	2002	Here we have explored the functional role of water molecules in the transmembrane region of bovine rhodopsin by using x-ray diffraction to 2.6 A.	Water	45-50	rhodopsin	Bos taurus	99-108
11972040-5	2002	The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively.	Water	35-40	rhodopsin	Bos taurus	169-178
11806921-3	2002	Here, we have investigated the influence of suramin on coupling of bovine rhodopsin to G(t), where G-protein activation and receptor structure can be monitored by spectroscopic in vitro assays.	Suramin	44-51	rhodopsin	Bos taurus	74-83
11806921-4	2002	G(t) fluorescence changes in response to rhodopsin-catalyzed nucleotide exchange reveal that suramin inhibits G(t) activation by slowing down the rate of complex formation between metarhodopsin-II and G(t).	Suramin	93-100	rhodopsin	Bos taurus	41-50
11602594-8	2001	Furthermore, dimers containing chimeric Ggamma chains with identical geranylgeranyl modification displayed rhodopsin affinities largely determined by the carboxyl-terminal one-third of the protein.	geranylgeranyl	69-83	rhodopsin	Bos taurus	107-116
12596915-3	2002	(6-9) Because rhodopsin phosphorylation is the quench mechanism of light-activated rhodopsin (R*), (10,11) the inhibition of the phosphorylation by S-modulin probably contributes to increase the lifetime of R* to result in sustained hydrolysis of cGMP5.	cgmp5	247-252	rhodopsin	Bos taurus	14-23
12596915-3	2002	(6-9) Because rhodopsin phosphorylation is the quench mechanism of light-activated rhodopsin (R*), (10,11) the inhibition of the phosphorylation by S-modulin probably contributes to increase the lifetime of R* to result in sustained hydrolysis of cGMP5.	cgmp5	247-252	rhodopsin	Bos taurus	83-92
11551216-1	2001	The G-protein coupled receptor, rhodopsin, consists of seven transmembrane helices which are buried in the lipid bilayer and are connected by loop domains extending out of the hydrophobic core.	Lipid Bilayers	107-120	rhodopsin	Bos taurus	32-41
11743865-2	2001	Rhodopsin has an 11-cis retinal as the chromophore, which binds covalently with a lysine residue through a protonated Schiff base linkage.	Lysine	82-88	rhodopsin	Bos taurus	0-9
11743865-2	2001	Rhodopsin has an 11-cis retinal as the chromophore, which binds covalently with a lysine residue through a protonated Schiff base linkage.	Schiff Bases	118-129	rhodopsin	Bos taurus	0-9
11743870-5	2001	Similar internal water molecules were shown to be present in bovine rhodopsin.	Water	17-22	rhodopsin	Bos taurus	68-77
11743873-0	2001	Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: possible coupling to proton uptake and formation of the active form of Meta II.	Schiff Bases	65-76	rhodopsin	Bos taurus	80-89
11743873-2	2001	We then go on to compare the processes that lead to the deprotonation of the Schiff base in bacteriorhodopsin with rhodopsin.	Schiff Bases	77-88	rhodopsin	Bos taurus	100-109
11743873-6	2001	We concluded that the pKa of the counter-ion to the Schiff base of bovine rhodopsin and of a surface residue that takes up a proton upon photolysis are both less than 4 in the unphotolyzed state.	Schiff Bases	52-63	rhodopsin	Bos taurus	74-83
11743873-8	2001	Finally we examined the evidence that, like in bacteriorhodopsin, the protonation of the Schiff bases"s counter-ion (Glu113) is coupled to the changing of the pKa of a protonatable surface group, called Z for rhodopsin and tentatively assigned to Glu134.	Schiff Bases	89-101	rhodopsin	Bos taurus	55-64
12020081-7	2001	Squid rhodopsin phosphorylation by purified SQRK was sensitive to both Mg2+ and GTPgammaS but was insensitive to Ca2+/CaM regulation.	magnesium ion	71-75	rhodopsin	Bos taurus	6-15
12020081-7	2001	Squid rhodopsin phosphorylation by purified SQRK was sensitive to both Mg2+ and GTPgammaS but was insensitive to Ca2+/CaM regulation.	Guanosine 5'-O-(3-Thiotriphosphate)	80-89	rhodopsin	Bos taurus	6-15
11592880-0	2001	Steric barrier to bathorhodopsin decay in 5-demethyl and mesityl analogues of rhodopsin.	mesityl	57-64	rhodopsin	Bos taurus	23-32
11513737-4	2001	Synergistic binding of the retinal G-protein subunits to rhodopsin was not observed for guanosine 5"-[gamma-thio]triphosphate-bound Galpha(t), nor was binding observed with squid retinal Galpha(q), which is not activated by bovine rhodopsin.	Guanosine 5'-O-(3-Thiotriphosphate)	88-125	rhodopsin	Bos taurus	57-66
11343699-3	2001	Using a combination of enzymatic and manual Edman degradation in conjunction with G-protein coupled receptor mass spectrometry, the structure and sites of O-glycans in octopus rhodopsin are determined.	o-glycans	155-164	rhodopsin	Bos taurus	176-185
11381044-0	2001	Activation of arrestin: requirement of phosphorylation as the negative charge on residues in synthetic peptides from the carboxyl-terminal region of rhodopsin.	Peptides	103-111	rhodopsin	Bos taurus	149-158
11381044-1	2001	PURPOSE: To determine whether substitution of the potential phosphorylation sites of bovine rhodopsin"s carboxyl-terminal region with the acidic residues aspartic acid, glutamic acid, or cysteic acid promotes the activation of arrestin.	Aspartic Acid	154-167	rhodopsin	Bos taurus	92-101
11381044-1	2001	PURPOSE: To determine whether substitution of the potential phosphorylation sites of bovine rhodopsin"s carboxyl-terminal region with the acidic residues aspartic acid, glutamic acid, or cysteic acid promotes the activation of arrestin.	Glutamic Acid	169-182	rhodopsin	Bos taurus	92-101
11381044-1	2001	PURPOSE: To determine whether substitution of the potential phosphorylation sites of bovine rhodopsin"s carboxyl-terminal region with the acidic residues aspartic acid, glutamic acid, or cysteic acid promotes the activation of arrestin.	Cysteic Acid	187-199	rhodopsin	Bos taurus	92-101
11381044-2	2001	METHODS: Three peptide analogues of the 19-residue carboxyl-terminal region of rhodopsin (330-348) were synthesized: the fully phosphorylated peptide (7P-peptide), the peptide with all potential phosphorylation sites substituted with glutamic acid (7E-peptide), and the peptide with the phosphorylation sites substituted with cysteic acid (7Cya-peptide).	Glutamic Acid	234-247	rhodopsin	Bos taurus	79-88
11381044-2	2001	METHODS: Three peptide analogues of the 19-residue carboxyl-terminal region of rhodopsin (330-348) were synthesized: the fully phosphorylated peptide (7P-peptide), the peptide with all potential phosphorylation sites substituted with glutamic acid (7E-peptide), and the peptide with the phosphorylation sites substituted with cysteic acid (7Cya-peptide).	Cysteic Acid	326-338	rhodopsin	Bos taurus	79-88
11381044-2	2001	METHODS: Three peptide analogues of the 19-residue carboxyl-terminal region of rhodopsin (330-348) were synthesized: the fully phosphorylated peptide (7P-peptide), the peptide with all potential phosphorylation sites substituted with glutamic acid (7E-peptide), and the peptide with the phosphorylation sites substituted with cysteic acid (7Cya-peptide).	7cya-peptide	340-352	rhodopsin	Bos taurus	79-88
11381044-4	2001	Rhodopsin with glutamic acid (Etail) or aspartic acid (Dtail) substituted for the phosphorylation sites in rhodopsin were constructed and expressed in COS-7 cells and tested in an in vitro assay.	Glutamic Acid	15-28	rhodopsin	Bos taurus	0-9
11381044-4	2001	Rhodopsin with glutamic acid (Etail) or aspartic acid (Dtail) substituted for the phosphorylation sites in rhodopsin were constructed and expressed in COS-7 cells and tested in an in vitro assay.	etail	30-35	rhodopsin	Bos taurus	0-9
11381044-4	2001	Rhodopsin with glutamic acid (Etail) or aspartic acid (Dtail) substituted for the phosphorylation sites in rhodopsin were constructed and expressed in COS-7 cells and tested in an in vitro assay.	dtail	55-60	rhodopsin	Bos taurus	0-9
11381044-4	2001	Rhodopsin with glutamic acid (Etail) or aspartic acid (Dtail) substituted for the phosphorylation sites in rhodopsin were constructed and expressed in COS-7 cells and tested in an in vitro assay.	carbonyl sulfide	151-154	rhodopsin	Bos taurus	0-9
11381044-4	2001	Rhodopsin with glutamic acid (Etail) or aspartic acid (Dtail) substituted for the phosphorylation sites in rhodopsin were constructed and expressed in COS-7 cells and tested in an in vitro assay.	carbonyl sulfide	151-154	rhodopsin	Bos taurus	107-116
11381044-10	2001	CONCLUSIONS: These results, taken together, suggest that the negative charge due to phosphates in the carboxyl-terminal region of rhodopsin are required for the full activation of arrestin and that acidic amino acids (carboxyl and sulfonic) do not mimic the negative charge of phosphorylated residues.	Phosphates	84-94	rhodopsin	Bos taurus	130-139
11319820-0	2001	Mass spectrometric analysis of cyanogen bromide fragments of integral membrane proteins at the picomole level: application to rhodopsin.	Cyanogen Bromide	31-47	rhodopsin	Bos taurus	126-135
11319820-8	2001	We present a MALDI MS method that quickly and reliably identifies the cyanogen bromide fragments and posttranslational modifications of reduced and alkylated bovine rhodopsin from as little as 30 pmol of rhodopsin in detergent-solubilized retinal rod disk membranes, using 1-5 pmol of digest per sample.	Cyanogen Bromide	70-86	rhodopsin	Bos taurus	165-174
11319820-8	2001	We present a MALDI MS method that quickly and reliably identifies the cyanogen bromide fragments and posttranslational modifications of reduced and alkylated bovine rhodopsin from as little as 30 pmol of rhodopsin in detergent-solubilized retinal rod disk membranes, using 1-5 pmol of digest per sample.	Cyanogen Bromide	70-86	rhodopsin	Bos taurus	204-213
11343699-4	2001	Two N-acetylgalactosamine residues are O-linked to Thr4 and Thr5 in the N-terminus of octopus rhodopsin.	Acetylgalactosamine	4-25	rhodopsin	Bos taurus	94-103
11045439-2	2000	In the case of bovine rhodopsin, the best studied of the visual pigments, the chromophore is 11-cis retinal attached to the terminal amino group of Lys296 through a protonated Schiff base linkage.	Schiff Bases	176-187	rhodopsin	Bos taurus	22-31
11106382-0	2000	Highly conserved glutamic acid in the extracellular IV-V loop in rhodopsins acts as the counterion in retinochrome, a member of the rhodopsin family.	Glutamic Acid	17-30	rhodopsin	Bos taurus	65-74
11106382-4	2000	Our results showed that the counterion is the glutamic acid at position 181, at which almost all the pigments in the rhodopsin family, including vertebrate and invertebrate rhodopsins, have a glutamic or aspartic acid.	Glutamic Acid	46-59	rhodopsin	Bos taurus	117-126
11106382-4	2000	Our results showed that the counterion is the glutamic acid at position 181, at which almost all the pigments in the rhodopsin family, including vertebrate and invertebrate rhodopsins, have a glutamic or aspartic acid.	glutamic	46-54	rhodopsin	Bos taurus	117-126
11106382-4	2000	Our results showed that the counterion is the glutamic acid at position 181, at which almost all the pigments in the rhodopsin family, including vertebrate and invertebrate rhodopsins, have a glutamic or aspartic acid.	Aspartic Acid	204-217	rhodopsin	Bos taurus	117-126
11106382-6	2000	Replacement of Glu-181 of bovine rhodopsin with Gln caused a 10-nm red-shift of absorption maximum.	Glutamic Acid	15-18	rhodopsin	Bos taurus	33-42
11106382-6	2000	Replacement of Glu-181 of bovine rhodopsin with Gln caused a 10-nm red-shift of absorption maximum.	Glutamine	48-51	rhodopsin	Bos taurus	33-42
10930404-5	2000	Systematic chimeric and point mutational studies indicate that three amino acids (Glu(134), Val(138), and Cys(140)) in the N-terminal region of the second loop of rhodopsin are crucial for efficient G protein activation.	Glutamic Acid	82-85	rhodopsin	Bos taurus	163-172
10930404-5	2000	Systematic chimeric and point mutational studies indicate that three amino acids (Glu(134), Val(138), and Cys(140)) in the N-terminal region of the second loop of rhodopsin are crucial for efficient G protein activation.	Valine	92-95	rhodopsin	Bos taurus	163-172
10930404-5	2000	Systematic chimeric and point mutational studies indicate that three amino acids (Glu(134), Val(138), and Cys(140)) in the N-terminal region of the second loop of rhodopsin are crucial for efficient G protein activation.	Cysteine	106-109	rhodopsin	Bos taurus	163-172
11087361-12	2000	We conclude that the binding site of Drosophila rhodopsin is similar to that of bovine rhodopsin and is characterized by a protonated Schiff base chromophore stabilized via a single negatively charged counterion.	Schiff Bases	134-145	rhodopsin	Bos taurus	87-96
11053136-1	2000	Bovine rhodopsin was reconstituted into mixtures of didocosahexaenoylphosphatidylcholine (di22:6-PC), dipalmitoylphosphatidylcholine (di16:0-PC), sn-1-palmitoyl-sn-2-docosahexaenoylphosphatidylcholine (16:0, 22:6-PC) and cholesterol.	didocosahexaenoylphosphatidylcholine	52-88	rhodopsin	Bos taurus	7-16
11053136-1	2000	Bovine rhodopsin was reconstituted into mixtures of didocosahexaenoylphosphatidylcholine (di22:6-PC), dipalmitoylphosphatidylcholine (di16:0-PC), sn-1-palmitoyl-sn-2-docosahexaenoylphosphatidylcholine (16:0, 22:6-PC) and cholesterol.	didocosahexaenoylphosphatidylcholine	90-99	rhodopsin	Bos taurus	7-16
11053136-1	2000	Bovine rhodopsin was reconstituted into mixtures of didocosahexaenoylphosphatidylcholine (di22:6-PC), dipalmitoylphosphatidylcholine (di16:0-PC), sn-1-palmitoyl-sn-2-docosahexaenoylphosphatidylcholine (16:0, 22:6-PC) and cholesterol.	1,2-Dipalmitoylphosphatidylcholine	102-132	rhodopsin	Bos taurus	7-16
11053136-1	2000	Bovine rhodopsin was reconstituted into mixtures of didocosahexaenoylphosphatidylcholine (di22:6-PC), dipalmitoylphosphatidylcholine (di16:0-PC), sn-1-palmitoyl-sn-2-docosahexaenoylphosphatidylcholine (16:0, 22:6-PC) and cholesterol.	di16:0-pc	134-143	rhodopsin	Bos taurus	7-16
11053136-1	2000	Bovine rhodopsin was reconstituted into mixtures of didocosahexaenoylphosphatidylcholine (di22:6-PC), dipalmitoylphosphatidylcholine (di16:0-PC), sn-1-palmitoyl-sn-2-docosahexaenoylphosphatidylcholine (16:0, 22:6-PC) and cholesterol.	6-pc	95-99	rhodopsin	Bos taurus	7-16
11053136-7	2000	Higher FRET efficiencies detected for di22:6-PE-Py, compared to di16:0-PE-Py, in mixed di22:6-PC-di16:0-PC-cholesterol bilayers, indicate preferential segregation of rhodopsin with polyunsaturated lipids.	-pe	44-47	rhodopsin	Bos taurus	166-175
11045439-3	2000	Photoaffinity labeling with a 3-diazo-4-oxo-retinoid shows that C-3 of the ionone ring moiety is close to Trp265 in helix F (VI) in dark inactivated rhodopsin.	3-diazo-4-oxo-retinoid	30-52	rhodopsin	Bos taurus	149-158
11045439-3	2000	Photoaffinity labeling with a 3-diazo-4-oxo-retinoid shows that C-3 of the ionone ring moiety is close to Trp265 in helix F (VI) in dark inactivated rhodopsin.	Norisoprenoids	75-81	rhodopsin	Bos taurus	149-158
11045439-6	2000	Photoaffinity labeling performed with 3-diazo-4-oxoretinal at -196 degrees C for batho-, -80 degrees C for lumi-, -40 degrees C for meta-I, and 0 degrees C for meta-II rhodopsin showed that in bathorhodopsin the ring is still close to Trp265.	3-Diazo-4-oxoretinal	38-58	rhodopsin	Bos taurus	168-177
10891063-0	2000	Structural constraints imposed by a non-native disulfide cause reversible changes in rhodopsin photointermediate kinetics.	Disulfides	47-56	rhodopsin	Bos taurus	85-94
10920009-4	2000	Rotational correlation times of 1-2 micros for purified spin-labeled bovine rhodopsin in lipid membranes led to viscosities of 2.2 poise for bilayers of dimyristoylphosphatidylcholine (28 degrees C) and 3.0 poise for the specific mixture of lipids used to reconstitute LacS (30 degrees C).	Lactose	269-273	rhodopsin	Bos taurus	76-85
10920009-4	2000	Rotational correlation times of 1-2 micros for purified spin-labeled bovine rhodopsin in lipid membranes led to viscosities of 2.2 poise for bilayers of dimyristoylphosphatidylcholine (28 degrees C) and 3.0 poise for the specific mixture of lipids used to reconstitute LacS (30 degrees C).	Dimyristoylphosphatidylcholine	153-183	rhodopsin	Bos taurus	76-85
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	cu(phen)(3)	83-94	rhodopsin	Bos taurus	22-31
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Disulfides	109-118	rhodopsin	Bos taurus	22-31
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Disulfides	109-118	rhodopsin	Bos taurus	192-201
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Cysteine	134-143	rhodopsin	Bos taurus	22-31
10891063-1	2000	Suspensions of bovine rhodopsin in 2% lauryl maltoside detergent were treated with Cu(phen)(3)(2+) to form a disulfide bridge between cysteines 140 and 222 which occur naturally in the bovine rhodopsin sequence.	Cysteine	134-143	rhodopsin	Bos taurus	192-201
10891063-3	2000	Only two exponentials could be fit to data from the Cu(phen)(3)(2+)-treated rhodopsin, while three exponentials were needed to fit data either from untreated rhodopsin or from Cu(phen)(3)(2+)-oxidized rhodopsin after further dithiothreitol reduction.	1,10-phenanthroline	55-59	rhodopsin	Bos taurus	76-85
10891063-5	2000	Since the 140-222 disulfide has previously been shown to block transducin activation, its effects on rhodopsin activation are of considerable interest.	Disulfides	18-27	rhodopsin	Bos taurus	101-110
10891063-8	2000	These results show that formation of disulfides in rhodopsin has potential as a tool for discriminating between the three isochromic, 380 nm absorbing intermediates involved in rhodopsin activation and for gaining insight into how their structures differ.	Disulfides	37-47	rhodopsin	Bos taurus	51-60
10891063-8	2000	These results show that formation of disulfides in rhodopsin has potential as a tool for discriminating between the three isochromic, 380 nm absorbing intermediates involved in rhodopsin activation and for gaining insight into how their structures differ.	Disulfides	37-47	rhodopsin	Bos taurus	177-186
10691986-8	2000	We reason that the solubilization zone around the photoreceptor rhodopsin may be the locus of rapid redistribution of the highly unsaturated disc phospholipid.	Phospholipids	146-158	rhodopsin	Bos taurus	64-73
10806093-1	2000	Rhodopsin, a prototypic G protein-coupled receptor responsible for absorption of photons in retinal rod photoreceptor cells, was selectively extracted from bovine rod outer segment membranes, employing mixed micelles of nonyl beta-d-glucoside and heptanetriol.	beta-d-glucoside	226-242	rhodopsin	Bos taurus	0-9
10806093-1	2000	Rhodopsin, a prototypic G protein-coupled receptor responsible for absorption of photons in retinal rod photoreceptor cells, was selectively extracted from bovine rod outer segment membranes, employing mixed micelles of nonyl beta-d-glucoside and heptanetriol.	Heptanetriol	247-259	rhodopsin	Bos taurus	0-9
10614053-0	1999	Calcium-dependent regulation of rhodopsin phosphorylation.	Calcium	0-7	rhodopsin	Bos taurus	32-41
10984085-6	2000	Therefore, the putrescine enhancing LDH-5 activity appeared to be capable of stimulating NAD-mediated rhodopsin regeneration.	Putrescine	15-25	rhodopsin	Bos taurus	102-111
10984085-6	2000	Therefore, the putrescine enhancing LDH-5 activity appeared to be capable of stimulating NAD-mediated rhodopsin regeneration.	NAD	89-92	rhodopsin	Bos taurus	102-111
10387033-1	1999	Eleven single-cysteine substitution mutants have been prepared in the sequence 325-340 of rhodopsin, corresponding to the C-terminal domain.	Cysteine	14-22	rhodopsin	Bos taurus	90-99
10320338-5	1999	The arrestin mutant R175Q bound to light-activated, unphosphorylated rhodopsin in ROS disk membranes.	ros	82-85	rhodopsin	Bos taurus	69-78
10213616-3	1999	Several studies in which synthetic peptides were used have suggested that sites on the rhodopsin cytoplasmic loops are involved in this interaction.	Peptides	35-43	rhodopsin	Bos taurus	87-96
10090766-0	1999	Rhodopsin"s carboxyl-terminal threonines are required for wild-type arrestin-mediated quench of transducin activation in vitro.	Threonine	30-40	rhodopsin	Bos taurus	0-9
10090766-1	1999	Many recent reports have demonstrated that rhodopsin"s carboxyl-terminal serine residues are the main targets for phosphorylation by rhodopsin kinase.	Serine	73-79	rhodopsin	Bos taurus	43-52
10090766-3	1999	We have examined the roles of the carboxyl serine and threonine residues during arrestin-mediated deactivation of rhodopsin using an in vitro transducin activation assay.	carboxyl serine	34-49	rhodopsin	Bos taurus	114-123
10090766-4	1999	Mutations were introduced into a synthetic bovine rhodopsin gene and expressed in COS-7 cells.	carbonyl sulfide	82-85	rhodopsin	Bos taurus	50-59
10090766-8	1999	A rhodopsin mutant lacking the carboxyl serine and threonine residues was not phosphorylated by rhodopsin kinase, demonstrating that phosphorylation is restricted to the seven putative phosphorylation sites.	carboxyl serine	31-46	rhodopsin	Bos taurus	2-11
10090766-8	1999	A rhodopsin mutant lacking the carboxyl serine and threonine residues was not phosphorylated by rhodopsin kinase, demonstrating that phosphorylation is restricted to the seven putative phosphorylation sites.	Threonine	51-60	rhodopsin	Bos taurus	2-11
10090766-9	1999	A rhodopsin mutant possessing a single phosphorylatable serine at 338 demonstrated no phosphorylation-dependent quench by arrestin.	Serine	56-62	rhodopsin	Bos taurus	2-11
10090766-11	1999	Analysis of additional mutants revealed that the presence of threonine in the carboxyl tail of rhodopsin provides for greater arrestin-mediated quench than does serine.	Threonine	61-70	rhodopsin	Bos taurus	95-104
10090766-11	1999	Analysis of additional mutants revealed that the presence of threonine in the carboxyl tail of rhodopsin provides for greater arrestin-mediated quench than does serine.	Serine	161-167	rhodopsin	Bos taurus	95-104
10642185-1	2000	Glutamic acid at position 113 in bovine rhodopsin ionizes to form the counterion to the protonated Schiff base (PSB), which links the 11-cis-retinylidene chromophore to opsin.	Glutamic Acid	0-13	rhodopsin	Bos taurus	40-49
10642185-1	2000	Glutamic acid at position 113 in bovine rhodopsin ionizes to form the counterion to the protonated Schiff base (PSB), which links the 11-cis-retinylidene chromophore to opsin.	Schiff Bases	99-110	rhodopsin	Bos taurus	40-49
10642185-1	2000	Glutamic acid at position 113 in bovine rhodopsin ionizes to form the counterion to the protonated Schiff base (PSB), which links the 11-cis-retinylidene chromophore to opsin.	psb	112-115	rhodopsin	Bos taurus	40-49
10642185-2	2000	Photoactivation of rhodopsin requires both Schiff base deprotonation and neutralization of Glu-113.	Schiff Bases	43-54	rhodopsin	Bos taurus	19-28
10642185-2	2000	Photoactivation of rhodopsin requires both Schiff base deprotonation and neutralization of Glu-113.	Glutamic Acid	91-94	rhodopsin	Bos taurus	19-28
10718607-2	2000	The H-C10-C11-H torsional angles of the retinylidene chromophore in bovine rhodopsin and metarhodopsin-I were determined simultaneously in the photo-activated membrane-bound state, using double-quantum heteronuclear local field spectroscopy.	retinylidene	40-52	rhodopsin	Bos taurus	75-84
10455014-1	1999	Here we describe a generic procedure for the expression and purification of milligram quantities of functional recombinant eukaryotic integral membrane proteins, exemplified by hexahistidine-tagged bovine rhodopsin.	His-His-His-His-His-His	177-190	rhodopsin	Bos taurus	205-214
10455014-4	1999	The recombinant rhodopsin could be purified with high overall yield by using immobilized-metal-affinity chromatography on Ni(2+)-agarose.	Metals	89-94	rhodopsin	Bos taurus	16-25
10455014-4	1999	The recombinant rhodopsin could be purified with high overall yield by using immobilized-metal-affinity chromatography on Ni(2+)-agarose.	Nickel(2+)	122-128	rhodopsin	Bos taurus	16-25
10455014-4	1999	The recombinant rhodopsin could be purified with high overall yield by using immobilized-metal-affinity chromatography on Ni(2+)-agarose.	Sepharose	129-136	rhodopsin	Bos taurus	16-25
10471281-0	1999	Retinylidene ligand structure in bovine rhodopsin, metarhodopsin-I, and 10-methylrhodopsin from internuclear distance measurements using 13C-labeling and 1-D rotational resonance MAS NMR.	retinylidene	0-12	rhodopsin	Bos taurus	40-49
9844007-0	1998	Phosphorylation of photolyzed rhodopsin is calcium-insensitive in retina permeabilized by alpha-toxin.	Calcium	43-50	rhodopsin	Bos taurus	30-39
9760262-1	1998	Purified bovine rhodopsin solubilized in dodecyl maltoside was photolyzed at 20 degreesC with 477 nm light, and difference spectra were collected at time delays ranging from 10 micros to 10 ms after photolysis.	dodecyl maltoside	41-58	rhodopsin	Bos taurus	16-25
9860835-0	1998	The hydrogen-bonding network of water molecules and the peptide backbone in the region connecting Asp83, Gly120, and Glu113 in bovine rhodopsin.	Hydrogen	4-12	rhodopsin	Bos taurus	134-143
9860835-0	1998	The hydrogen-bonding network of water molecules and the peptide backbone in the region connecting Asp83, Gly120, and Glu113 in bovine rhodopsin.	Water	32-37	rhodopsin	Bos taurus	134-143
9760262-2	1998	Bromocresol purple was added to the samples to detect pH changes in the aqueous environment due to changes in the protonation state of rhodopsin.	Bromcresol Purple	0-18	rhodopsin	Bos taurus	135-144
9767084-1	1998	Our recent finding of the co-localization of 11-cis retinyl esters and 11-cis retinyl ester hydrolase (11-cis REH) activity in bovine retinal pigment epithelium (RPE) plasma membrane (PM) has led us to explore the possibility that the PM may provide 11-cis retinal for rhodopsin regeneration.	11-cis retinyl esters	45-66	rhodopsin	Bos taurus	269-278
9767130-2	1998	PAT incorporates fatty acid into rhodopsin with higher efficiency (10 times higher initial rate), as compared to autoacylation.	Fatty Acids	17-27	rhodopsin	Bos taurus	33-42
9767130-4	1998	The presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT.	Cysteine	33-41	rhodopsin	Bos taurus	67-76
9562631-7	1998	In addition, we incubated purified rhodopsin and phospholipids extracted from ROS with 11-cis-retinol.	Vitamin A	87-101	rhodopsin	Bos taurus	35-44
9726932-5	1998	Reconstitution of rhodopsin into phosphatidylcholine vesicles has little influence on the spectral properties of the rhodopsin-transducin complex, whereas pH affects the intensity of the carbonyl stretching band.	Phosphatidylcholines	33-52	rhodopsin	Bos taurus	18-27
9726932-8	1998	The 1735 cm-1 vibration is also seen in the complex with C-terminal peptides devoid of free carboxylic acid groups, indicating that the corresponding carbonyl group is located on rhodopsin.	Carboxylic Acids	92-107	rhodopsin	Bos taurus	179-188
9562631-8	1998	Rhodopsin was found to isomerize 11-cis-retinol to all-trans-retinol as well as ROS, but phospholipids did not.	Vitamin A	33-47	rhodopsin	Bos taurus	0-9
9562631-8	1998	Rhodopsin was found to isomerize 11-cis-retinol to all-trans-retinol as well as ROS, but phospholipids did not.	Vitamin A	51-68	rhodopsin	Bos taurus	0-9
9562631-9	1998	In contrast, the phospholipids inhibited the isomerization of 11-cis-retinol to all-trans-retinol by the purified rhodopsin.	Phospholipids	17-30	rhodopsin	Bos taurus	114-123
9562631-9	1998	In contrast, the phospholipids inhibited the isomerization of 11-cis-retinol to all-trans-retinol by the purified rhodopsin.	Vitamin A	62-76	rhodopsin	Bos taurus	114-123
9562631-9	1998	In contrast, the phospholipids inhibited the isomerization of 11-cis-retinol to all-trans-retinol by the purified rhodopsin.	Vitamin A	80-97	rhodopsin	Bos taurus	114-123
9562631-11	1998	Our results suggest that rhodopsin has activity for the isomerization of 11-cis-retinol to all-trans-retinol and may play an important role in the detoxification of 11-cis-retinol in the ROS.	Vitamin A	73-87	rhodopsin	Bos taurus	25-34
9562631-11	1998	Our results suggest that rhodopsin has activity for the isomerization of 11-cis-retinol to all-trans-retinol and may play an important role in the detoxification of 11-cis-retinol in the ROS.	Vitamin A	91-108	rhodopsin	Bos taurus	25-34
9562631-11	1998	Our results suggest that rhodopsin has activity for the isomerization of 11-cis-retinol to all-trans-retinol and may play an important role in the detoxification of 11-cis-retinol in the ROS.	Vitamin A	165-179	rhodopsin	Bos taurus	25-34
9613234-0	1998	Highly selective separation of rhodopsin from bovine rod outer segment membranes using combination of divalent cation and alkyl(thio)glucoside.	alkyl(thio)glucoside	122-142	rhodopsin	Bos taurus	31-40
9613234-2	1998	It is found that when alkyl(thio)glucosides with an appropriate hydrophillic-lipophilic balance (e.g. octylthioglucoside) are used in combination with a divalent cation, rhodopsin is selectively extracted from ROS membranes at a specific detergent-to-membrane ratio.	alkyl(thio)glucosides	22-43	rhodopsin	Bos taurus	170-179
9613234-2	1998	It is found that when alkyl(thio)glucosides with an appropriate hydrophillic-lipophilic balance (e.g. octylthioglucoside) are used in combination with a divalent cation, rhodopsin is selectively extracted from ROS membranes at a specific detergent-to-membrane ratio.	n-octyl-beta-D-thioglucopyranoside	102-120	rhodopsin	Bos taurus	170-179
9421960-0	1997	Absorbance changes by aromatic amino acid side chains in early rhodopsin photointermediates.	Amino Acids, Aromatic	22-41	rhodopsin	Bos taurus	63-72
9526110-6	1998	These results imply that GTP[S]-dependent interaction of NDP kinase with the membranes in the presence of bleached visual pigment rhodopsin is mediated by Gt.	Guanosine Triphosphate	25-28	rhodopsin	Bos taurus	130-139
9490006-0	1998	Photoreceptor rhodopsin: structural and conformational study of its chromophore 11-cis retinal in oriented membranes by deuterium solid state NMR.	Deuterium	120-129	rhodopsin	Bos taurus	14-23
9490006-3	1998	Bovine rhodopsin containing 11-cis retinal, specifically deuterated at its methyl groups at the C19 or C20 position, was uniaxially oriented in DMPC bilayers.	Dimyristoylphosphatidylcholine	144-148	rhodopsin	Bos taurus	7-16
9421967-0	1997	Transmembrane signaling mediated by water in bovine rhodopsin.	Water	36-41	rhodopsin	Bos taurus	52-61
9129801-0	1997	The transmembrane 7-alpha-bundle of rhodopsin: distance geometry calculations with hydrogen bonding constraints.	Hydrogen	83-91	rhodopsin	Bos taurus	36-45
9305971-0	1997	Properties of early photolysis intermediates of rhodopsin are affected by glycine 121 and phenylalanine 261.	Glycine	74-81	rhodopsin	Bos taurus	48-57
9305971-0	1997	Properties of early photolysis intermediates of rhodopsin are affected by glycine 121 and phenylalanine 261.	Phenylalanine	90-103	rhodopsin	Bos taurus	48-57
9305971-1	1997	Glycine 121 in transmembrane (TM) helix 3 and phenylalanine 261 in TM helix 6 of bovine rhodopsin have been shown to be critical residues for creating an appropriate chromophore binding pocket for 11-cis-retinal [Han, M., Lin, S. W., Smith, S. O., and Sakmar, T. P. (1996) J. Biol.	Glycine	0-7	rhodopsin	Bos taurus	88-97
9305971-1	1997	Glycine 121 in transmembrane (TM) helix 3 and phenylalanine 261 in TM helix 6 of bovine rhodopsin have been shown to be critical residues for creating an appropriate chromophore binding pocket for 11-cis-retinal [Han, M., Lin, S. W., Smith, S. O., and Sakmar, T. P. (1996) J. Biol.	Phenylalanine	46-59	rhodopsin	Bos taurus	88-97
9298947-4	1997	Rhodopsin was labeled with a nuclear spin label (31P) by limited phosphorylation with rhodopsin kinase.	ET bromodomain inhibitor	49-52	rhodopsin	Bos taurus	0-9
9298947-4	1997	Rhodopsin was labeled with a nuclear spin label (31P) by limited phosphorylation with rhodopsin kinase.	ET bromodomain inhibitor	49-52	rhodopsin	Bos taurus	86-95
9298947-6	1997	The phosphorylated rhodopsin was then specifically labeled on cysteine 140 with an electron spin label.	Cysteine	62-70	rhodopsin	Bos taurus	19-28
9290215-3	1997	This protein migrates slightly behind bovine rhodopsin during sodium-dodecyl-sulfate polyacrylamide gel electrophoresis, suggesting that its molecular weight is slightly larger.	polyacrylamide gels	85-103	rhodopsin	Bos taurus	45-54
9166788-0	1997	Water and peptide backbone structure in the active center of bovine rhodopsin.	Water	0-5	rhodopsin	Bos taurus	68-77
9166788-3	1997	Water molecules in rhodopsin that change upon formation of bathorhodopsin are detected by a change in frequency of the O-H stretching vibration from 3538 to 3525 cm(-1).	Water	0-5	rhodopsin	Bos taurus	19-28
9166788-9	1997	On the other hand, the E113Q protein shows shifts of the N-H+ stretching vibrational band, that is probably due to the protonated Schiff base, upon conversion of rhodopsin to bathorhodopsin.	Schiff Bases	130-141	rhodopsin	Bos taurus	162-171
9129801-1	1997	A 3D model of the transmembrane 7-alpha-bundle of rhodopsin-like G-protein-coupled receptors (GPCRs) was calculated using an iterative distance geometry refinement with an evolving system of hydrogen bonds, formed by intramembrane polar side chains in various proteins of the family and collectively applied as distance constraints.	Hydrogen	191-199	rhodopsin	Bos taurus	50-59
9129801-5	1997	The bovine rhodopsin model thus determined is closely packed, but has a few small polar cavities, presumably filled by water, and has a binding pocket that is complementary to 11-cis (6-s-cis, 12-s-trans, C = N anti)-retinal or to all-trans-retinal, depending on conformations of the Lys296 and Trp265 side chains.	Water	119-124	rhodopsin	Bos taurus	11-20
8948474-0	1996	Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes.	Cholesterol	10-21	rhodopsin	Bos taurus	0-9
9099669-1	1997	The protein kinase C phosphorylation sites on bovine rhodopsin were identified using proteolytic, phosphoamino acid, mass spectrometric, and peptide sequencing analyses.	Phosphoamino Acids	98-115	rhodopsin	Bos taurus	53-62
9099669-2	1997	Tryptic removal of the 9 carboxyl-terminal residues of rhodopsin revealed that a major fraction of the phosphates incorporated by protein kinase C are in a region containing Ser334, Thr335, and Thr336.	Phosphates	103-113	rhodopsin	Bos taurus	55-64
9099669-4	1997	Analysis of the endoproteinase Asp-N-generated carboxyl terminus of rhodopsin by mass spectrometry and peptide sequencing revealed that Ser338 is also a primary phosphorylation site, with minor phosphorylation of Ser343.	asp-n	31-36	rhodopsin	Bos taurus	68-77
9098891-0	1997	Identification of transmembrane tryptic peptides of rhodopsin using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.	Peptides	40-48	rhodopsin	Bos taurus	52-61
9098891-2	1997	In this work, we present the accurate mass determination of transmembrane tryptic peptides of bovine rhodopsin using matrix-assisted laser desorption ionization time-of-flight mass spectrometry.	Peptides	82-90	rhodopsin	Bos taurus	101-110
9098891-7	1997	Four of the six transmembrane tryptic peptides of rhodopsin were identified, ranging in mass from 3,260 Da to 6,528 Da.	Peptides	38-46	rhodopsin	Bos taurus	50-59
9098891-9	1997	In addition, heterogeneity in the glycosylation of the N-terminal tryptic peptide of rhodopsin was identified by MALDI MS, without modifying the carbohydrate prior to analysis.	Peptides	74-81	rhodopsin	Bos taurus	85-94
9133606-0	1997	Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin.	Hydrogen	36-44	rhodopsin	Bos taurus	93-102
9133606-0	1997	Intramembrane signaling mediated by hydrogen-bonding of water and carboxyl groups in bacteriorhodopsin and rhodopsin.	Water	56-61	rhodopsin	Bos taurus	93-102
9133606-6	1997	Similar interactions, through internal water molecules and the peptide bonds in helices B and C, take place in bovine rhodopsin.	Water	39-44	rhodopsin	Bos taurus	118-127
8995408-3	1997	Light-exposed VCOP stimulated [35S]guanosine 5"-(gamma-thio)triphosphate nucleotide exchange on bovine rod transducin in a time-dependent manner with a half-time for activation of 0.75 min, similar to that of bovine rhodopsin.	Sulfur-35	31-34	rhodopsin	Bos taurus	216-225
9066300-0	1997	Steric hindrance between chromophore substituents as the driving force of rhodopsin photoisomerization: 10-methyl-13-demethyl retinal containing rhodopsin.	10-methyl-13-demethyl retinal	104-133	rhodopsin	Bos taurus	74-83
9066300-0	1997	Steric hindrance between chromophore substituents as the driving force of rhodopsin photoisomerization: 10-methyl-13-demethyl retinal containing rhodopsin.	10-methyl-13-demethyl retinal	104-133	rhodopsin	Bos taurus	145-154
9066300-1	1997	A visual chromophore analogue, 10-methyl-13-demethyl (dm) retinal, was synthesized and reconstituted with bleached bovine rhodopsin to form a visual pigment derivative with absorbance maximum at 505 nm.	10-methyl-13-demethyl	31-52	rhodopsin	Bos taurus	122-131
9066300-1	1997	A visual chromophore analogue, 10-methyl-13-demethyl (dm) retinal, was synthesized and reconstituted with bleached bovine rhodopsin to form a visual pigment derivative with absorbance maximum at 505 nm.	dm	54-56	rhodopsin	Bos taurus	122-131
9066301-1	1997	We determined the structure and site of fatty acid incorporated in octopus rhodopsin using a combination of fluorescence label and enzymatic cleavage methods in conjunction with fast-atom bombardment (FAB) mass spectrometry.	Fatty Acids	40-50	rhodopsin	Bos taurus	75-84
8943296-2	1996	Replacement of a highly conserved glycine residue on transmembrane (TM) helix 3 of bovine rhodopsin (Gly121) by amino acid residues with larger side chains causes a progressive blue-shift in the lambdamax value of the pigment, a decrease in thermal stability, and an increase in reactivity with hydroxylamine.	Glycine	34-41	rhodopsin	Bos taurus	90-99
8943296-2	1996	Replacement of a highly conserved glycine residue on transmembrane (TM) helix 3 of bovine rhodopsin (Gly121) by amino acid residues with larger side chains causes a progressive blue-shift in the lambdamax value of the pigment, a decrease in thermal stability, and an increase in reactivity with hydroxylamine.	Hydroxylamine	295-308	rhodopsin	Bos taurus	90-99
8961950-5	1996	Light-dependent binding of GTP gamma S was observed when the purified octopus Gq was reconstituted with octopus rhodopsin that had been integrated into phospholipid vesicles.	Guanosine Triphosphate	27-30	rhodopsin	Bos taurus	112-121
8961950-5	1996	Light-dependent binding of GTP gamma S was observed when the purified octopus Gq was reconstituted with octopus rhodopsin that had been integrated into phospholipid vesicles.	Phospholipids	152-164	rhodopsin	Bos taurus	112-121
8961950-7	1996	Finally, light- and GTP-dependent activation of PLC beta 1 was observed in a reconstitution system consisting of octopus rhodopsin, Gq, and bovine PLC beta 1.	Guanosine Triphosphate	20-23	rhodopsin	Bos taurus	121-130
8977115-2	1996	This finding excludes the possibility that Tyr-112 serves as the counter anion to the protonated Schiff base as does Glu-113 in bovine rhodopsin.	Glutamic Acid	117-120	rhodopsin	Bos taurus	135-144
8977115-3	1996	Upon photoconversion from rhodopsin to acid metarhodopsin, Trp and Tyr Raman bands decrease in intensity and concomitantly a Trp band shifts in frequency.	Tryptophan	59-62	rhodopsin	Bos taurus	26-35
8977115-3	1996	Upon photoconversion from rhodopsin to acid metarhodopsin, Trp and Tyr Raman bands decrease in intensity and concomitantly a Trp band shifts in frequency.	Tyrosine	67-70	rhodopsin	Bos taurus	26-35
8977115-3	1996	Upon photoconversion from rhodopsin to acid metarhodopsin, Trp and Tyr Raman bands decrease in intensity and concomitantly a Trp band shifts in frequency.	Tryptophan	125-128	rhodopsin	Bos taurus	26-35
8977115-4	1996	The changes of Trp Raman bands are ascribed to changes in hydrophobic interactions and conformation, suggesting a possible role of Trp in the photoconversion process of octopus rhodopsin.	Tryptophan	15-18	rhodopsin	Bos taurus	177-186
8977115-4	1996	The changes of Trp Raman bands are ascribed to changes in hydrophobic interactions and conformation, suggesting a possible role of Trp in the photoconversion process of octopus rhodopsin.	Tryptophan	131-134	rhodopsin	Bos taurus	177-186
9043648-1	1997	An attempt was made to reveal the mode of action of protons and salts on the recently discovered GTP gamma S-dependent interaction of bovine retinal rod outer segments (ROS)1 nucleoside diphosphate kinase (NDP kinase) with the complex between bleached visual receptor rhodopsin and retinal G-protein transducin in bovine ROS membranes.	Guanosine Triphosphate	97-100	rhodopsin	Bos taurus	268-277
9043648-1	1997	An attempt was made to reveal the mode of action of protons and salts on the recently discovered GTP gamma S-dependent interaction of bovine retinal rod outer segments (ROS)1 nucleoside diphosphate kinase (NDP kinase) with the complex between bleached visual receptor rhodopsin and retinal G-protein transducin in bovine ROS membranes.	ros	169-172	rhodopsin	Bos taurus	268-277
8948474-1	1996	Cholesterol modulates the function of rhodopsin in the retinal rod outer segment (ROS) disk membranes.	Cholesterol	0-11	rhodopsin	Bos taurus	38-47
8948474-5	1996	In this study, the fluorescent sterol, cholestatrienol, was used to probe interactions between cholesterol and rhodopsin in bovine ROS disk membranes.	Sterols	31-37	rhodopsin	Bos taurus	111-120
8948474-5	1996	In this study, the fluorescent sterol, cholestatrienol, was used to probe interactions between cholesterol and rhodopsin in bovine ROS disk membranes.	cholesta-5,7,9-trien-3 beta-ol	39-54	rhodopsin	Bos taurus	111-120
8948474-11	1996	The effect of increasing membrane cholesterol on the ability of cholestatrienol to quench rhodopsin tryptophan fluorescence was determined.	Cholesterol	34-45	rhodopsin	Bos taurus	90-99
8948474-11	1996	The effect of increasing membrane cholesterol on the ability of cholestatrienol to quench rhodopsin tryptophan fluorescence was determined.	cholesta-5,7,9-trien-3 beta-ol	64-79	rhodopsin	Bos taurus	90-99
8948474-11	1996	The effect of increasing membrane cholesterol on the ability of cholestatrienol to quench rhodopsin tryptophan fluorescence was determined.	Tryptophan	100-110	rhodopsin	Bos taurus	90-99
8948474-17	1996	The ability of cholesterol to compete with cholestatrienol for that interaction suggests a "site" at which cholesterol contacts rhodopsin.	Cholesterol	15-26	rhodopsin	Bos taurus	128-137
8948474-17	1996	The ability of cholesterol to compete with cholestatrienol for that interaction suggests a "site" at which cholesterol contacts rhodopsin.	cholesta-5,7,9-trien-3 beta-ol	43-58	rhodopsin	Bos taurus	128-137
8948474-17	1996	The ability of cholesterol to compete with cholestatrienol for that interaction suggests a "site" at which cholesterol contacts rhodopsin.	Cholesterol	107-118	rhodopsin	Bos taurus	128-137
8780519-0	1996	Specific tryptophan UV-absorbance changes are probes of the transition of rhodopsin to its active state.	Tryptophan	9-19	rhodopsin	Bos taurus	74-83
8823182-1	1996	Thirty consecutive single cysteine substitution mutants in the amino acids Q225-I256 of bovine rhodopsin have been prepared and modified with a sulfhydryl specific nitroxide reagent.	Cysteine	26-34	rhodopsin	Bos taurus	95-104
8823182-1	1996	Thirty consecutive single cysteine substitution mutants in the amino acids Q225-I256 of bovine rhodopsin have been prepared and modified with a sulfhydryl specific nitroxide reagent.	Sulfhydryl Compounds	144-154	rhodopsin	Bos taurus	95-104
8823182-1	1996	Thirty consecutive single cysteine substitution mutants in the amino acids Q225-I256 of bovine rhodopsin have been prepared and modified with a sulfhydryl specific nitroxide reagent.	Hydroxylamine	164-173	rhodopsin	Bos taurus	95-104
8823182-7	1996	Judging from nitroxide mobilities, the putative extension of helix E in the aqueous phase is more dynamic than that of helix F. Changes in the electron paramagnetic resonance characteristics of the spin-labeled rhodopsin upon photoactivation indicate that chromophore isomerization results in patterns of structural changes that can be interpreted in terms of movements of helices that extend into the aqueous loop regions.	Hydroxylamine	13-22	rhodopsin	Bos taurus	211-220
8702792-1	1996	Rapid transport of retinoids across the interphotoreceptor matrix is a critical part of the visual cycle, since it serves to replenish bleached rhodopsin with its chromophore 11-cis-retinal.	Retinoids	19-28	rhodopsin	Bos taurus	144-153
8865065-14	1996	From the slope of the linear regression of EC50CaM plotted vs. the rhodopsin concentration, the molar ratio of rhodopsin to externally accessible Ca(2+)-CaM binding sites of fused ROS membranes was determined to be 1439 +/- 109.	cafestol palmitate	47-50	rhodopsin	Bos taurus	111-120
8865065-15	1996	Therefore, there are about 720 molecules of rhodopsin per Ca(2+)-CaM binding site present in ROS.	cafestol palmitate	65-68	rhodopsin	Bos taurus	44-53
8679611-8	1996	Since the C14-C15 stretch mode frequency is relatively high in the spectra of octopus rhodopsin and bathorhodopsin (> 1200 cm-1) and since the normal mode pattern near the Schiff base is similar to the model, we suggest that the C=N configuration in these two species is anti.	Carbon	10-11	rhodopsin	Bos taurus	86-95
8679611-9	1996	The different responses of the C14-C15 stretch mode to the Schiff base nitrogen deuteration in bovine and octopus pigments are due to the fact that the coupled C14-C15 stretch and the C12-C13 stretch motions in the model compound or in bovine rhodopsin are altered in octopus rhodopsin so that the stretch motion of the C14-15 bond is more localized, similar to the C-C stretch motion in the small Schiff base model compound.	Schiff Bases	59-70	rhodopsin	Bos taurus	243-252
8679611-9	1996	The different responses of the C14-C15 stretch mode to the Schiff base nitrogen deuteration in bovine and octopus pigments are due to the fact that the coupled C14-C15 stretch and the C12-C13 stretch motions in the model compound or in bovine rhodopsin are altered in octopus rhodopsin so that the stretch motion of the C14-15 bond is more localized, similar to the C-C stretch motion in the small Schiff base model compound.	Schiff Bases	59-70	rhodopsin	Bos taurus	276-285
8679611-9	1996	The different responses of the C14-C15 stretch mode to the Schiff base nitrogen deuteration in bovine and octopus pigments are due to the fact that the coupled C14-C15 stretch and the C12-C13 stretch motions in the model compound or in bovine rhodopsin are altered in octopus rhodopsin so that the stretch motion of the C14-15 bond is more localized, similar to the C-C stretch motion in the small Schiff base model compound.	Nitrogen	71-79	rhodopsin	Bos taurus	243-252
8679611-9	1996	The different responses of the C14-C15 stretch mode to the Schiff base nitrogen deuteration in bovine and octopus pigments are due to the fact that the coupled C14-C15 stretch and the C12-C13 stretch motions in the model compound or in bovine rhodopsin are altered in octopus rhodopsin so that the stretch motion of the C14-15 bond is more localized, similar to the C-C stretch motion in the small Schiff base model compound.	Nitrogen	71-79	rhodopsin	Bos taurus	276-285
8804611-2	1996	Here we have used SPR spectroscopy for the first time to monitor the binding and activation of G-protein (transducin or Gt) by bovine rhodopsin incorporated into an egg phosphatidylcholine bilayer deposited on a silver film.	Phosphatidylcholines	169-188	rhodopsin	Bos taurus	134-143
8776886-3	1996	Two-dimensional crystals of C-terminally truncated rhodopsin reconstituted from octyl glucoside solution formed in a p222(1) lattice (a = 44 A, b = 131 A).	octyl-beta-D-glucoside	80-95	rhodopsin	Bos taurus	51-60
8780519-4	1996	Each of the five tryptophan residues in bovine rhodopsin was replaced by either a phenylalanine or a tyrosine.	Tryptophan	17-27	rhodopsin	Bos taurus	47-56
8780519-4	1996	Each of the five tryptophan residues in bovine rhodopsin was replaced by either a phenylalanine or a tyrosine.	Phenylalanine	82-95	rhodopsin	Bos taurus	47-56
8780519-4	1996	Each of the five tryptophan residues in bovine rhodopsin was replaced by either a phenylalanine or a tyrosine.	Tyrosine	101-109	rhodopsin	Bos taurus	47-56
8626592-13	1996	We find that rDrosNCa is capable of inhibiting bovine rhodopsin phosphorylation in vitro in a Ca2+-dependent manner.	rdrosnca	13-21	rhodopsin	Bos taurus	54-63
8830030-1	1996	Pure bovine rhodopsin pellets were prepared by removal of cholic acid from rhodopsin-cholic acid complex, and X-ray diffraction patterns from the internal structure of rhodopsin were obtained for the first time using wet and dry pellet samples.	Cholic Acid	85-96	rhodopsin	Bos taurus	75-84
8596913-2	1996	Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T).	Glutamic Acid	13-26	rhodopsin	Bos taurus	129-138
8596913-2	1996	Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T).	Alanine	33-40	rhodopsin	Bos taurus	129-138
8596913-2	1996	Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T).	gtp-guanosine diphosphate	143-168	rhodopsin	Bos taurus	129-138
8596913-2	1996	Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T).	Guanosine Diphosphate	170-173	rhodopsin	Bos taurus	129-138
8596913-2	1996	Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T).	Guanosine Triphosphate	143-146	rhodopsin	Bos taurus	129-138
8830030-1	1996	Pure bovine rhodopsin pellets were prepared by removal of cholic acid from rhodopsin-cholic acid complex, and X-ray diffraction patterns from the internal structure of rhodopsin were obtained for the first time using wet and dry pellet samples.	Cholic Acid	85-96	rhodopsin	Bos taurus	75-84
8554325-0	1995	Phospholipid solubilization during detergent extraction of rhodopsin from photoreceptor disk membranes.	Phospholipids	0-12	rhodopsin	Bos taurus	59-68
8554325-4	1995	The higher the CMC, the larger the amount of lipid associated to the solubilized rhodopsin and the larger the amount of lipid reassociated to rhodopsin upon surfactant dilution.	cmc	15-18	rhodopsin	Bos taurus	81-90
8554325-4	1995	The higher the CMC, the larger the amount of lipid associated to the solubilized rhodopsin and the larger the amount of lipid reassociated to rhodopsin upon surfactant dilution.	cmc	15-18	rhodopsin	Bos taurus	142-151
8554325-6	1995	The lipid which tended to be associated with rhodopsin in protein-lipid-detergent mixed micelles was also consistently richer in PC than that present in lipid-detergent micelles.	Phosphatidylcholines	129-131	rhodopsin	Bos taurus	45-54
8554325-8	1995	Rhodopsin photolytic transitions were faster in nonionic than in bile salt-related detergents.	Bile Acids and Salts	65-74	rhodopsin	Bos taurus	0-9
7578021-5	1995	The water structure is identical in rhodopsin and isorhodopsin.	Water	4-9	rhodopsin	Bos taurus	36-45
7612819-2	1995	Electron cryo-microscopy was used to determine the three-dimensional structure of bovine rhodopsin from tilted two-dimensional crystals embedded in vitrified water.	Water	158-163	rhodopsin	Bos taurus	89-98
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	11-cis-ene	74-84	rhodopsin	Bos taurus	35-44
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	Tryptophan	113-116	rhodopsin	Bos taurus	35-44
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	Leucine	121-124	rhodopsin	Bos taurus	35-44
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	beta-ionone c	158-171	rhodopsin	Bos taurus	35-44
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	Schiff Bases	277-288	rhodopsin	Bos taurus	35-44
7662862-1	1995	Photoaffinity labeling with bovine rhodopsin using a retinal with a fixed 11-cis-ene cross-linked exclusively to Trp-265/Leu-266 in helix F, showing that the beta-ionone C-3 is close to helix F. Moreover, since these labeled amino acids are in the middle of helix F, while the Schiff-base linkage to Lys-296 at the other terminus of the chromophore is also in the middle of helix G, the chromophore lies horizontally near the center of the lipid bilayer.	Lysine	300-303	rhodopsin	Bos taurus	35-44
7662871-0	1995	Changes in structure of the chromophore in the photochemical process of bovine rhodopsin as revealed by FTIR spectroscopy for hydrogen out-of-plane vibrations.	Hydrogen	126-134	rhodopsin	Bos taurus	79-88
7626602-1	1995	In rhodopsin, 11-cis-retinal is bound by a protonated Schiff base and acts as a strong antagonist, which holds the receptor in its inactive ground state conformation.	Schiff Bases	54-65	rhodopsin	Bos taurus	3-12
7626602-7	1995	The slow pathway regenerates rhodopsin (9- or 11-cis) via Schiff base reprotonation and proton release.	Schiff Bases	58-69	rhodopsin	Bos taurus	29-38
7626602-11	1995	The complex dissociates with GTP gamma S, and rhodopsin relaxes to the ground state.	Guanosine Triphosphate	29-32	rhodopsin	Bos taurus	46-55
7626602-11	1995	The complex dissociates with GTP gamma S, and rhodopsin relaxes to the ground state.	Sulfur	39-40	rhodopsin	Bos taurus	46-55
7629115-6	1995	RK, purified using immobilized Rv as an affinity matrix, catalyzed the light-dependent and Ca(2+)-independent incorporation of phosphates into rhodopsin when reconstituted with urea-stripped rod outer segment membranes.	Phosphates	127-137	rhodopsin	Bos taurus	143-152
7629115-6	1995	RK, purified using immobilized Rv as an affinity matrix, catalyzed the light-dependent and Ca(2+)-independent incorporation of phosphates into rhodopsin when reconstituted with urea-stripped rod outer segment membranes.	Urea	177-181	rhodopsin	Bos taurus	143-152
7629115-7	1995	When only a small fraction (0.04%) of rhodopsin was photolyzed, as many as 700 phosphates were incorporated per photolyzed rhodopsin, a phenomenon known as "high gain" phosphorylation.	Phosphates	79-89	rhodopsin	Bos taurus	38-47
7629115-7	1995	When only a small fraction (0.04%) of rhodopsin was photolyzed, as many as 700 phosphates were incorporated per photolyzed rhodopsin, a phenomenon known as "high gain" phosphorylation.	Phosphates	79-89	rhodopsin	Bos taurus	123-132
7612622-1	1995	All 20 single cysteine substitution mutants in the sequence Y136-M155 of bovine rhodopsin have been prepared and modified with a sulfhydryl-specific nitroxide reagent.	Cysteine	14-22	rhodopsin	Bos taurus	80-89
7612622-1	1995	All 20 single cysteine substitution mutants in the sequence Y136-M155 of bovine rhodopsin have been prepared and modified with a sulfhydryl-specific nitroxide reagent.	Sulfhydryl Compounds	129-139	rhodopsin	Bos taurus	80-89
7612622-1	1995	All 20 single cysteine substitution mutants in the sequence Y136-M155 of bovine rhodopsin have been prepared and modified with a sulfhydryl-specific nitroxide reagent.	Hydroxylamine	149-158	rhodopsin	Bos taurus	80-89
7744755-0	1995	Histidine tagging both allows convenient single-step purification of bovine rhodopsin and exerts ionic strength-dependent effects on its photochemistry.	Histidine	0-9	rhodopsin	Bos taurus	76-85
7720869-3	1995	Unlike heparin, the phosphopeptide also induced light-activated binding of arrestin to both unphosphorylated rhodopsin in disk membranes as well as to endoproteinase Asp-N-treated rhodopsin (des 330-348).	asp-n	166-171	rhodopsin	Bos taurus	180-189
7737995-0	1995	Characterization of rhodopsin mutants that bind transducin but fail to induce GTP nucleotide uptake.	gtp nucleotide	78-92	rhodopsin	Bos taurus	20-29
7737995-9	1995	Three types of assays were carried out: 1) a fluorescence assay of photoactivated rhodopsin (R*)-dependent guanosine 5"-O-(3-thiotriphosphate) uptake by transducin, 2) an assay of R*-dependent release of labeled GDP from the alpha-subunit of transducin holoenzyme (Gt alpha).GDP, and 3) a light-scattering assay of R*.Gt complex formation and dissociation.	Guanosine 5'-O-(3-Thiotriphosphate)	107-142	rhodopsin	Bos taurus	82-91
7890732-8	1995	Arg-175 also appears to function as a phosphorylation-sensitive trigger since charge neutralization by mutagenesis enables arrestin-R175N to bind to light-activated rhodopsin as well as wild-type arrestin binds to phosphorylated light-activated rhodopsin.	Arginine	0-3	rhodopsin	Bos taurus	165-174
7706043-0	1995	Rhodopsin from the fish, Astyanax: role of tyrosine 261 in the red shift.	Tyrosine	43-51	rhodopsin	Bos taurus	0-9
7706043-1	1995	PURPOSE: To isolate and characterize the rhodopsin cDNA from the fish, Astyanax fasciatus, and to determine the effect of tyrosine 261 on its spectral tuning.	Tyrosine	122-130	rhodopsin	Bos taurus	41-50
7706043-7	1995	In contrast to all known rhodopsins, this rhodopsin contains a tyrosine instead of a phenylalanine at amino acid position 261.	Tyrosine	63-71	rhodopsin	Bos taurus	25-34
7896814-4	1995	The phosphorylation of rhodopsin by protein kinase C is inhibited by the protein kinase C-selective inhibitor sangivamycin.	sangivamycin	110-122	rhodopsin	Bos taurus	23-32
7890732-8	1995	Arg-175 also appears to function as a phosphorylation-sensitive trigger since charge neutralization by mutagenesis enables arrestin-R175N to bind to light-activated rhodopsin as well as wild-type arrestin binds to phosphorylated light-activated rhodopsin.	Arginine	0-3	rhodopsin	Bos taurus	245-254
7827093-0	1995	Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding.	Cyclic GMP	44-48	rhodopsin	Bos taurus	134-143
7890614-5	1995	An extrinsic fluorescence reporter group, pyrene maleimide, attached to bovine rhodopsin also shows an increase in pyrene fluorescence on illumination.	pyrene-maleimide	42-58	rhodopsin	Bos taurus	79-88
7890614-5	1995	An extrinsic fluorescence reporter group, pyrene maleimide, attached to bovine rhodopsin also shows an increase in pyrene fluorescence on illumination.	pyrene	42-48	rhodopsin	Bos taurus	79-88
7890614-8	1995	An Arrhenius plot derived from the fluorescence assay shows the energy of activation barrier for retinal release from rhodopsin to be 20.2 kcal/mol in 0.1% dodecyl maltoside at pH 6.0.	dodecyl maltoside	156-173	rhodopsin	Bos taurus	118-127
7880821-2	1995	Previous mutagenesis studies have indicated the requirement of a tertiary structure in the intradiscal region with a disulfide bond between Cys-110 and Cys-187 for the correct assembly and/or function of rhodopsin.	Disulfides	117-126	rhodopsin	Bos taurus	204-213
7880821-2	1995	Previous mutagenesis studies have indicated the requirement of a tertiary structure in the intradiscal region with a disulfide bond between Cys-110 and Cys-187 for the correct assembly and/or function of rhodopsin.	Cysteine	140-143	rhodopsin	Bos taurus	204-213
7880821-2	1995	Previous mutagenesis studies have indicated the requirement of a tertiary structure in the intradiscal region with a disulfide bond between Cys-110 and Cys-187 for the correct assembly and/or function of rhodopsin.	Cysteine	152-155	rhodopsin	Bos taurus	204-213
7880821-3	1995	We have now studied a rhodopsin mutant in which only the natural intradiscal cysteines at positions 110, 185, and 187 are present while all the remaining seven cysteines in the wild-type bovine rhodopsin have been replaced by serines.	Cysteine	77-86	rhodopsin	Bos taurus	22-31
7880821-3	1995	We have now studied a rhodopsin mutant in which only the natural intradiscal cysteines at positions 110, 185, and 187 are present while all the remaining seven cysteines in the wild-type bovine rhodopsin have been replaced by serines.	Serine	226-233	rhodopsin	Bos taurus	22-31
8172594-2	1994	Since we have found tht the binding of rhodopsin to the alpha subunit of transducin (alpha T) increases the susceptibility of alpha T to phosphorylation by protein kinase C-beta 1, we used this phosphorylation reaction as an initial screen for peptides that mimic the actions of rhodopsin.	tetrahydrothiophene	20-23	rhodopsin	Bos taurus	39-48
8903933-4	1995	The recombinant mutants were tested for their ability to phosphorylate rhodopsin present in purified bovine ROS membranes which serves as a substrate for betaARK1.	ros	108-111	rhodopsin	Bos taurus	71-80
7947780-1	1994	Surface plasmon resonance (SPR) spectroscopy has been used to follow incorporation and light-induced conformational changes in bovine rhodopsin reconstituted into an egg phosphatidylcholine bilayer deposited on a thin silver film.	Phosphatidylcholines	170-189	rhodopsin	Bos taurus	134-143
7947717-4	1994	The amino acid sequence of the opsin-related protein in humans is 86% identical to that of bovine RGR, and a lysine residue, analogous to the retinaldehyde attachment site of rhodopsin, is conserved in the seventh transmembrane domain of RGR in both species.	Lysine	109-115	rhodopsin	Bos taurus	175-184
7947717-4	1994	The amino acid sequence of the opsin-related protein in humans is 86% identical to that of bovine RGR, and a lysine residue, analogous to the retinaldehyde attachment site of rhodopsin, is conserved in the seventh transmembrane domain of RGR in both species.	Retinaldehyde	142-155	rhodopsin	Bos taurus	175-184
7916209-10	1994	These results show that the Schiff base counterion of rhodopsin, the carboxylate side chain of Glu113, becomes protonated during MII formation.	carboxylate	69-80	rhodopsin	Bos taurus	54-63
8051070-3	1994	It is activated by photoexcited rhodopsin which catalyzes the exchange of transducin-bound GDP for GTP and then stays active until bound GTP is hydrolyzed by an intrinsic GTPase activity.	Guanosine Diphosphate	91-94	rhodopsin	Bos taurus	32-41
8051070-3	1994	It is activated by photoexcited rhodopsin which catalyzes the exchange of transducin-bound GDP for GTP and then stays active until bound GTP is hydrolyzed by an intrinsic GTPase activity.	Guanosine Triphosphate	99-102	rhodopsin	Bos taurus	32-41
8051070-3	1994	It is activated by photoexcited rhodopsin which catalyzes the exchange of transducin-bound GDP for GTP and then stays active until bound GTP is hydrolyzed by an intrinsic GTPase activity.	Guanosine Triphosphate	137-140	rhodopsin	Bos taurus	32-41
8027053-11	1994	This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage.	NADP	13-18	rhodopsin	Bos taurus	174-183
8027053-11	1994	This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage.	NADP	117-122	rhodopsin	Bos taurus	174-183
8027053-11	1994	This rate of NADPH production is sufficient to support both the reduction of retinal to retinol (1.2 +/- 0.2 nmol of NADPH/min/mg of protein) following the photobleaching of rhodopsin and glutathione reduction (1.1 +/- 0.1 nmol of NADPH/min/mg of protein) for the protection of rod outer segments from oxidative damage.	NADP	117-122	rhodopsin	Bos taurus	174-183
8180206-1	1994	Two tandem cysteine residues in the carboxyl-terminal region of rhodopsin have been shown to be covalently linked to palmitate via thioester bonds (Ovchinnikov, Y.	Cysteine	11-19	rhodopsin	Bos taurus	64-73
8180206-1	1994	Two tandem cysteine residues in the carboxyl-terminal region of rhodopsin have been shown to be covalently linked to palmitate via thioester bonds (Ovchinnikov, Y.	Palmitates	117-126	rhodopsin	Bos taurus	64-73
8180206-1	1994	Two tandem cysteine residues in the carboxyl-terminal region of rhodopsin have been shown to be covalently linked to palmitate via thioester bonds (Ovchinnikov, Y.	Cy5-benzyl thioester	131-140	rhodopsin	Bos taurus	64-73
8180206-8	1994	Treatment of SDS-solubilized, labeled rod outer segments with 10% beta-mercaptoethanol provided evidence that partial depalmitoylation may induce the formation of rhodopsin aggregates.	Sodium Dodecyl Sulfate	13-16	rhodopsin	Bos taurus	163-172
8180206-8	1994	Treatment of SDS-solubilized, labeled rod outer segments with 10% beta-mercaptoethanol provided evidence that partial depalmitoylation may induce the formation of rhodopsin aggregates.	Mercaptoethanol	66-86	rhodopsin	Bos taurus	163-172
8180206-9	1994	Labeled, unbleached rhodopsin was purified by chromatography over hydroxyapatite and concanavalin A-agarose and reconstituted into dimyristoylphosphatidylcholine vesicles.	Durapatite	66-80	rhodopsin	Bos taurus	20-29
8180206-9	1994	Labeled, unbleached rhodopsin was purified by chromatography over hydroxyapatite and concanavalin A-agarose and reconstituted into dimyristoylphosphatidylcholine vesicles.	concanavalin a-agarose	85-107	rhodopsin	Bos taurus	20-29
8180206-9	1994	Labeled, unbleached rhodopsin was purified by chromatography over hydroxyapatite and concanavalin A-agarose and reconstituted into dimyristoylphosphatidylcholine vesicles.	Dimyristoylphosphatidylcholine	131-161	rhodopsin	Bos taurus	20-29
8180206-10	1994	SDS gels of the rhodopsin vesicle preparation verified that all unbound fluorescent label had been removed and that the thioester bond linking probe to protein was not labile.	Sodium Dodecyl Sulfate	0-3	rhodopsin	Bos taurus	16-25
8053944-5	1994	Increase in ADP-ribosylation of 22 and 24 kDa substrates and their interaction with photoexcited rhodopsin in squid photoreceptors was found.	Adenosine Diphosphate	12-15	rhodopsin	Bos taurus	97-106
8171029-0	1994	Structure and function in rhodopsin: the role of asparagine-linked glycosylation.	Asparagine	49-59	rhodopsin	Bos taurus	26-35
8171029-1	1994	Rhodopsin, the dim light photoreceptor of the rod cell, is an integral membrane protein that is glycosylated at Asn-2 and Asn-15.	Asparagine	112-115	rhodopsin	Bos taurus	0-9
8171029-1	1994	Rhodopsin, the dim light photoreceptor of the rod cell, is an integral membrane protein that is glycosylated at Asn-2 and Asn-15.	Asparagine	122-125	rhodopsin	Bos taurus	0-9
8161500-1	1994	By suspending bovine rhodopsin in trehalose-water glass films, it is possible to trap photostates in the light-activation process.	Trehalose	34-43	rhodopsin	Bos taurus	21-30
8161500-1	1994	By suspending bovine rhodopsin in trehalose-water glass films, it is possible to trap photostates in the light-activation process.	Water	44-49	rhodopsin	Bos taurus	21-30
8161500-1	1994	By suspending bovine rhodopsin in trehalose-water glass films, it is possible to trap photostates in the light-activation process.	photostates	86-97	rhodopsin	Bos taurus	21-30
7813632-7	1995	Rhodopsin-mediated inhibition of adenylyl cyclase is pertussis toxin-sensitive, whereas inhibition by the purinergic receptor is calcium-sensitive but not pertussis toxin-sensitive.	Calcium	129-136	rhodopsin	Bos taurus	0-9
7916209-0	1994	Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin.	Glutamic Acid	18-31	rhodopsin	Bos taurus	82-91
7916209-0	1994	Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin.	Schiff Bases	43-54	rhodopsin	Bos taurus	82-91
7916209-2	1994	Rhodopsin mutants E113D and E113A were prepared in which the retinylidene Schiff base counterion, Glu113, was replaced by Asp and Ala, respectively.	retinylidene schiff base	61-85	rhodopsin	Bos taurus	0-9
7916209-2	1994	Rhodopsin mutants E113D and E113A were prepared in which the retinylidene Schiff base counterion, Glu113, was replaced by Asp and Ala, respectively.	Alanine	130-133	rhodopsin	Bos taurus	0-9
7916209-6	1994	A positive band at 1712 cm-1 caused by the protonation of an internal carboxylic acid in rhodopsin was shifted slightly to 1709 cm-1 in mutant E113D.	Carboxylic Acids	70-85	rhodopsin	Bos taurus	89-98
7916209-10	1994	These results show that the Schiff base counterion of rhodopsin, the carboxylate side chain of Glu113, becomes protonated during MII formation.	Schiff Bases	28-39	rhodopsin	Bos taurus	54-63
8050563-0	1994	Recoverin mediates the calcium effect upon rhodopsin phosphorylation and cGMP hydrolysis in bovine retina rod cells.	Calcium	23-30	rhodopsin	Bos taurus	43-52
8050563-1	1994	Rhodopsin phosphorylation and in consequence cGMP hydrolysis in bovine rod outer segments are Ca2+ dependent in the presence of ATP.	Cyclic GMP	45-49	rhodopsin	Bos taurus	0-9
8050563-1	1994	Rhodopsin phosphorylation and in consequence cGMP hydrolysis in bovine rod outer segments are Ca2+ dependent in the presence of ATP.	Adenosine Triphosphate	128-131	rhodopsin	Bos taurus	0-9
8172594-2	1994	Since we have found tht the binding of rhodopsin to the alpha subunit of transducin (alpha T) increases the susceptibility of alpha T to phosphorylation by protein kinase C-beta 1, we used this phosphorylation reaction as an initial screen for peptides that mimic the actions of rhodopsin.	tetrahydrothiophene	20-23	rhodopsin	Bos taurus	279-288
8172594-3	1994	The results of this screen indicated that a peptide from the C-terminal tail of rhodopsin (amino acids 325-338; KNPLGDDEASTTVS-amide; designated as peptide 3) was capable of interacting with the alpha T subunit.	Amides	127-132	rhodopsin	Bos taurus	80-89
8258527-6	1993	A lysine residue, analogous to the retinaldehyde attachment site in rhodopsin, is conserved in the seventh hydrophobic segment of the novel sequence.	Lysine	2-8	rhodopsin	Bos taurus	68-77
8110772-7	1994	The amide I band profile of rhodopsin indicates an extensive alpha-helical (53%) peptide chain, with little beta-sheet (21%) and beta-turns (18%) in ROS membranes.	Amides	4-9	rhodopsin	Bos taurus	28-37
8110772-7	1994	The amide I band profile of rhodopsin indicates an extensive alpha-helical (53%) peptide chain, with little beta-sheet (21%) and beta-turns (18%) in ROS membranes.	Peptides	81-88	rhodopsin	Bos taurus	28-37
8260505-11	1993	The higher pKa of the meta I to meta II transition in gecko P521 compared to a rod pigment like bovine rhodopsin (pKa = 6.4) probably is due to a cysteine residue at position 211 in gecko rather than a histidine residue in bovine rhodopsin.	Cysteine	146-154	rhodopsin	Bos taurus	103-112
8258527-6	1993	A lysine residue, analogous to the retinaldehyde attachment site in rhodopsin, is conserved in the seventh hydrophobic segment of the novel sequence.	Retinaldehyde	35-48	rhodopsin	Bos taurus	68-77
8218280-0	1993	Water structural changes in lumirhodopsin, metarhodopsin I, and metarhodopsin II upon photolysis of bovine rhodopsin: analysis by Fourier transform infrared spectroscopy.	Water	0-5	rhodopsin	Bos taurus	32-41
7901852-0	1993	Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin II: a Fourier-transform infrared spectroscopy study of site-directed mutants.	Carboxylic Acids	40-55	rhodopsin	Bos taurus	66-75
7901852-9	1993	These results show that Asp-83 and Glu-122 are protonated both in rhodopsin and in metarhodopsin II, in agreement with the isotope effects observed in spectra measured in 2H2O.	Aspartic Acid	24-27	rhodopsin	Bos taurus	66-75
7901852-9	1993	These results show that Asp-83 and Glu-122 are protonated both in rhodopsin and in metarhodopsin II, in agreement with the isotope effects observed in spectra measured in 2H2O.	Glutamic Acid	35-38	rhodopsin	Bos taurus	66-75
7901852-9	1993	These results show that Asp-83 and Glu-122 are protonated both in rhodopsin and in metarhodopsin II, in agreement with the isotope effects observed in spectra measured in 2H2O.	2h2o	171-175	rhodopsin	Bos taurus	66-75