Rhodopsin Function
Published by Anonymous on 2007/9/30 (3689 reads)
1: Chembiochem. 2007 Jan 2;8(1):19-24.
The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors.
Pardo L, Deupi X, Dölker N, López-Rodríguez ML, Campillo M.
Laboratori de Medicina Computacional, Unitat de Bioestadística, Facultat de Medicina, Universitat Autňnoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Leonardo.Pardo@uab.es
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17173267 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Curr Opin Struct Biol. 2005 Aug;15(4):416-22.
Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin.
Feller SE, Gawrisch K.
Department of Chemistry, Wabash College, Crawfordsville, IN 47933, USA.
The importance of highly polyunsaturated fatty acids in health and development has been convincingly demonstrated by many studies over the past several decades. The mechanisms by which polyunsaturated lipid species might influence biological function at the molecular level are now attracting considerable attention. The G-protein-coupled receptor rhodopsin and docosahexaenoic acid, the dominant fatty acid in the retinal membrane, provide the best-studied example of protein function being influenced by lipid environment.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 16039844 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Biochim Biophys Acta. 2002 Oct 11;1565(2):196-205.
Structural basis for sensory rhodopsin function.
Pebay-Peyroula E, Royant A, Landau EM, Navarro J.
Institut de Biologie Structurale, UMR5075, CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, Grenoble, France.
The crystal structure of sensory rhodopsin II from Natronobacterium pharaonis was recently solved at 2.1 A resolution from lipidic cubic phase-grown crystals. A critical analysis of previous structure-function studies is possible within the framework of the high-resolution structure of this photoreceptor. Based on the structure, a molecular understanding emerges of the efficiency and selectivity of the photoisomerization reaction, of the interaction of the sensory receptor and its cognate transducer protein HtrII, and of the mechanism of spectral tuning in photoreceptors. The architecture of the retinal binding pocket is compact, representing a major determinant for the selective binding of the chromophore, all-trans retinal to the apoprotein, opsin. Several chromophore-protein interactions revealed by the structure were not predicted by previous mutagenesis and spectroscopic analyses. The structure suggests likely mechanisms by which photoisomerization triggers the activation of sensory rhodopsin II, and highlights the possibility of a unified mechanism of signaling mediated by sensory receptors, including visual rhodopsins. Future investigations using time-resolved crystallography, structural dynamics, and computational studies will provide the basis to unveil the molecular mechanisms of sensory receptors-mediated transmembrane signaling.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12409195 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Receptors Channels. 2002;8(1):33-50.
Rhodopsin and retinitis pigmentosa: shedding light on structure and function.
Stojanovic A, Hwa J.
Department of Pharmacology and Toxicology, Dartmouth Medical School, Dartmouth College, 7650 Remsen, Hanover, NH 03755, USA.
Rhodopsin is the dim-light activated photoreceptor located in the rod cells of the eye. It belongs to the large superfamily of G-protein-coupled receptors (GPCRs). Many consider it the proto-typical GPCR as numerous studies since its cloning in 1983 (Nathans and Hogness 1983) have established many fundamental principles of seven transmembrane-spanning GPCRs. Abundant expression in the rod's outer segment, constituting about 90% of the total membrane protein in the discs, and the development of techniques to purify large quantities of functional protein has facilitated this process. Another distinct feature is rhodopsin's ligand, 11-cis-retinal, which is covalently bound via a Schiff base to transmembrane seven (TM VII), allowing extensive spectroscopic studies. Exciting recent developments include the discovery of naturally occurring mutations that lead to retinal degeneration, the determination of transmembrane movements using electron paramagnetic resonance (EPR) and biochemical techniques, and the discovery of its 3D X-ray crystal structure, the first among GPCRs. The impact of these major advances will be discussed in this review.
Publication Types:
Review
PMID: 12402507 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Tanpakushitsu Kakusan Koso. 2002 Jun;47(8 Suppl):1123-30.
[Structure-function relationship in G protein-coupled receptors deduced from crystal structure of rhodopsin]
[Article in Japanese]
Okada T, Terakita A, Shichida Y.
t-okada@aist.go.jp
Publication Types:
Review
PMID: 12099033 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Mol Pharmacol. 2001 Jul;60(1):1-19.
Erratum in:
Mol Pharmacol 2002 Jan;61(1):247.
Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors.
Ballesteros JA, Shi L, Javitch JA.
Novasite Pharmaceuticals, Inc., San Diego, California, USA. jaj2@columbia.edu
The availability of a high-resolution structure of rhodopsin now allows us to reconsider research attempts to understand structure-function relationships in other G protein-coupled receptors (GPCRs). A comparison of the rhodopsin structure with the results of previous sequence analysis and molecular modeling that incorporated experimental results demonstrates a high degree of success for these methods in predicting the helix ends and protein-protein interface of GPCRs. Moreover, the amino acid residues inferred to form the surface of the binding-site crevice based on our application of the substituted-cysteine accessibility method in the dopamine D(2) receptor are in remarkable agreement with the rhodopsin structure, with the notable exception of some residues in the fourth transmembrane segment. Based on our analysis of the data reviewed, we propose that the overall structures of rhodopsin and of amine receptors are very similar, although we also identified localized regions where the structure of these receptors may diverge. We further propose that several of the highly unusual structural features of rhodopsin are also present in amine GPCRs, despite the absence of amino acids that might have thought to have been critical to the adoption of these features. Thus, different amino acids or alternate microdomains can support similar deviations from regular alpha-helical structure, thereby resulting in similar tertiary structure. Such structural mimicry is a mechanism by which a common ancestor could diverge sufficiently to develop the selectivity necessary to interact with diverse signals, while still maintaining a similar overall fold. Through this process, the core function of signaling activation through a conformational change in the transmembrane segments that alters the conformation of the cytoplasmic surface and subsequent interaction with G proteins is presumably shared by the entire Class A family of receptors, despite their selectivity for a diverse group of ligands.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11408595 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Invest Ophthalmol Vis Sci. 2001 Jan;42(1):3-9.
Rhodopsin structure, function, and topography the Friedenwald lecture.
Hargrave PA.
Department of Ophthalmology, School of Medicine, University of Florida, Gainesville, Florida 32610, USA. hargrave@ufl.edu
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11133841 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Vision Res. 1998 May;38(10):1341-52.
Rhodopsin phosphorylation and its role in photoreceptor function.
Hurley JB, Spencer M, Niemi GA.
Department of Biochemistry, University of Washington, Seattle 98195, USA. jbhhh@u.washington.edu
Light-stimulated phosphorylation of rhodopsin was first described 25 years ago. This paper reviews the progress that has been made towards (i) understanding the nature of the enzymes that phosphorylate and dephosphorylate rhodopsin (ii) identifying the sites of phosphorylation on rhodopsin and (iii) understanding the physiological importance of rhodopsin phosphorylation. Many important questions related to rhodopsin phosphorylation remain unanswered and new strategies and methods are needed to address issues such as the roles of Ca2+ and recoverin. We present one such method that uses mass spectrometry to quantitate rhodopsin phosphorylation in intact mouse retinas.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9667002 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Chem Phys Lipids. 1994 Sep 6;73(1-2):159-80.
Modulation of rhodopsin function by properties of the membrane bilayer.
Brown MF.
Department of Chemistry, University of Arizona, Tucson 85721.
A prevalent model for the function of rhodopsin centers on the metarhodopsin I (MI) to metarhodopsin II (MII) conformational transition as the triggering event for the visual process. Flash photolysis techniques enable one to determine the [MII]/[MI] ratio for rhodopsin in various recombinant membranes, and thus investigate the roles of the phospholipid head groups and the lipid acyl chains systematically. The results obtained to date clearly show that the pK for the acid-base MI-MII equilibrium of rhodopsin is modulated by the lipid environment. In bilayers of phosphatidylcholines the MI-MII equilibrium is shifted to the left; whereas in the native rod outer segment membranes it is shifted to the right, i.e., at neutral pH near physiological temperature. The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains. Yet such a native-like lipid mixture is not necessary for the MI-MII conformational transition of rhodopsin; one can substitute other lipid compositions having similar properties. The MI-MII transition is favored by relatively small head groups which produce a condensed bilayer surface, viz, a comparatively small interfacial area as in the case of PE, together with bulky acyl chains such as DHA which prefer a relatively large cross sectional area. The resulting force imbalance across the layer gives rise to a curvature elastic stress of the lipid/water interface, such that the lipid mixtures yielding native-like behavior form reverse hexagonal (HII) phases at slightly higher temperatures. A relatively unstable membrane is needed: lipids tending to form the lamellar phase do not support full native-like photochemical function of rhodopsin. Thus chemically specific properties of the various lipids are not required, but rather average or material properties of the entire assembly, which may involve the curvature free energy of the membrane-lipid water interface. These findings reveal that the membrane lipid bilayer has a direct influence on the energetics of the conformational states of rhodopsin in visual excitation.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8001180 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Biochemistry. 1992 Jun 2;31(21):4923-31.
Rhodopsin: structure, function, and genetics.
Nathans J.
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1599916 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: J Biol Chem. 1992 Jan 5;267(1):1-4.
Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function.
Khorana HG.
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1730574 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Kidney Int Suppl. 1987 Dec;23:S2-13.
Structure and function of the beta 2-adrenergic receptor--homology with rhodopsin.
Dohlman HG, Caron MG, Lefkowitz RJ.
Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2831423 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: FEBS Lett. 1982 Nov 8;148(2):179-91.
Rhodopsin and bacteriorhodopsin: structure-function relationships.
Ovchinnikov YuA .
Publication Types:
Review
PMID: 6759163 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Seikagaku. 1981;53(1):20-4.
[Rhodopsin kinase--with emphasis on function and immunopathogenicity (author's transl)]
[Article in Japanese]
Shichi H.
Publication Types:
Review
PMID: 6169774 [PubMed - indexed for MEDLINE]
The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors.
Pardo L, Deupi X, Dölker N, López-Rodríguez ML, Campillo M.
Laboratori de Medicina Computacional, Unitat de Bioestadística, Facultat de Medicina, Universitat Autňnoma de Barcelona, 08193 Bellaterra, Barcelona, Spain. Leonardo.Pardo@uab.es
Publication Types:
Research Support, Non-U.S. Gov't
Review
PMID: 17173267 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
2: Curr Opin Struct Biol. 2005 Aug;15(4):416-22.
Properties of docosahexaenoic-acid-containing lipids and their influence on the function of rhodopsin.
Feller SE, Gawrisch K.
Department of Chemistry, Wabash College, Crawfordsville, IN 47933, USA.
The importance of highly polyunsaturated fatty acids in health and development has been convincingly demonstrated by many studies over the past several decades. The mechanisms by which polyunsaturated lipid species might influence biological function at the molecular level are now attracting considerable attention. The G-protein-coupled receptor rhodopsin and docosahexaenoic acid, the dominant fatty acid in the retinal membrane, provide the best-studied example of protein function being influenced by lipid environment.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
PMID: 16039844 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
3: Biochim Biophys Acta. 2002 Oct 11;1565(2):196-205.
Structural basis for sensory rhodopsin function.
Pebay-Peyroula E, Royant A, Landau EM, Navarro J.
Institut de Biologie Structurale, UMR5075, CEA-CNRS-Université Joseph Fourier, 41 rue Jules Horowitz, Grenoble, France.
The crystal structure of sensory rhodopsin II from Natronobacterium pharaonis was recently solved at 2.1 A resolution from lipidic cubic phase-grown crystals. A critical analysis of previous structure-function studies is possible within the framework of the high-resolution structure of this photoreceptor. Based on the structure, a molecular understanding emerges of the efficiency and selectivity of the photoisomerization reaction, of the interaction of the sensory receptor and its cognate transducer protein HtrII, and of the mechanism of spectral tuning in photoreceptors. The architecture of the retinal binding pocket is compact, representing a major determinant for the selective binding of the chromophore, all-trans retinal to the apoprotein, opsin. Several chromophore-protein interactions revealed by the structure were not predicted by previous mutagenesis and spectroscopic analyses. The structure suggests likely mechanisms by which photoisomerization triggers the activation of sensory rhodopsin II, and highlights the possibility of a unified mechanism of signaling mediated by sensory receptors, including visual rhodopsins. Future investigations using time-resolved crystallography, structural dynamics, and computational studies will provide the basis to unveil the molecular mechanisms of sensory receptors-mediated transmembrane signaling.
Publication Types:
Comparative Study
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 12409195 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
4: Receptors Channels. 2002;8(1):33-50.
Rhodopsin and retinitis pigmentosa: shedding light on structure and function.
Stojanovic A, Hwa J.
Department of Pharmacology and Toxicology, Dartmouth Medical School, Dartmouth College, 7650 Remsen, Hanover, NH 03755, USA.
Rhodopsin is the dim-light activated photoreceptor located in the rod cells of the eye. It belongs to the large superfamily of G-protein-coupled receptors (GPCRs). Many consider it the proto-typical GPCR as numerous studies since its cloning in 1983 (Nathans and Hogness 1983) have established many fundamental principles of seven transmembrane-spanning GPCRs. Abundant expression in the rod's outer segment, constituting about 90% of the total membrane protein in the discs, and the development of techniques to purify large quantities of functional protein has facilitated this process. Another distinct feature is rhodopsin's ligand, 11-cis-retinal, which is covalently bound via a Schiff base to transmembrane seven (TM VII), allowing extensive spectroscopic studies. Exciting recent developments include the discovery of naturally occurring mutations that lead to retinal degeneration, the determination of transmembrane movements using electron paramagnetic resonance (EPR) and biochemical techniques, and the discovery of its 3D X-ray crystal structure, the first among GPCRs. The impact of these major advances will be discussed in this review.
Publication Types:
Review
PMID: 12402507 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
5: Tanpakushitsu Kakusan Koso. 2002 Jun;47(8 Suppl):1123-30.
[Structure-function relationship in G protein-coupled receptors deduced from crystal structure of rhodopsin]
[Article in Japanese]
Okada T, Terakita A, Shichida Y.
t-okada@aist.go.jp
Publication Types:
Review
PMID: 12099033 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
6: Mol Pharmacol. 2001 Jul;60(1):1-19.
Erratum in:
Mol Pharmacol 2002 Jan;61(1):247.
Structural mimicry in G protein-coupled receptors: implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors.
Ballesteros JA, Shi L, Javitch JA.
Novasite Pharmaceuticals, Inc., San Diego, California, USA. jaj2@columbia.edu
The availability of a high-resolution structure of rhodopsin now allows us to reconsider research attempts to understand structure-function relationships in other G protein-coupled receptors (GPCRs). A comparison of the rhodopsin structure with the results of previous sequence analysis and molecular modeling that incorporated experimental results demonstrates a high degree of success for these methods in predicting the helix ends and protein-protein interface of GPCRs. Moreover, the amino acid residues inferred to form the surface of the binding-site crevice based on our application of the substituted-cysteine accessibility method in the dopamine D(2) receptor are in remarkable agreement with the rhodopsin structure, with the notable exception of some residues in the fourth transmembrane segment. Based on our analysis of the data reviewed, we propose that the overall structures of rhodopsin and of amine receptors are very similar, although we also identified localized regions where the structure of these receptors may diverge. We further propose that several of the highly unusual structural features of rhodopsin are also present in amine GPCRs, despite the absence of amino acids that might have thought to have been critical to the adoption of these features. Thus, different amino acids or alternate microdomains can support similar deviations from regular alpha-helical structure, thereby resulting in similar tertiary structure. Such structural mimicry is a mechanism by which a common ancestor could diverge sufficiently to develop the selectivity necessary to interact with diverse signals, while still maintaining a similar overall fold. Through this process, the core function of signaling activation through a conformational change in the transmembrane segments that alters the conformation of the cytoplasmic surface and subsequent interaction with G proteins is presumably shared by the entire Class A family of receptors, despite their selectivity for a diverse group of ligands.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11408595 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
7: Invest Ophthalmol Vis Sci. 2001 Jan;42(1):3-9.
Rhodopsin structure, function, and topography the Friedenwald lecture.
Hargrave PA.
Department of Ophthalmology, School of Medicine, University of Florida, Gainesville, Florida 32610, USA. hargrave@ufl.edu
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 11133841 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
8: Vision Res. 1998 May;38(10):1341-52.
Rhodopsin phosphorylation and its role in photoreceptor function.
Hurley JB, Spencer M, Niemi GA.
Department of Biochemistry, University of Washington, Seattle 98195, USA. jbhhh@u.washington.edu
Light-stimulated phosphorylation of rhodopsin was first described 25 years ago. This paper reviews the progress that has been made towards (i) understanding the nature of the enzymes that phosphorylate and dephosphorylate rhodopsin (ii) identifying the sites of phosphorylation on rhodopsin and (iii) understanding the physiological importance of rhodopsin phosphorylation. Many important questions related to rhodopsin phosphorylation remain unanswered and new strategies and methods are needed to address issues such as the roles of Ca2+ and recoverin. We present one such method that uses mass spectrometry to quantitate rhodopsin phosphorylation in intact mouse retinas.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 9667002 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
9: Chem Phys Lipids. 1994 Sep 6;73(1-2):159-80.
Modulation of rhodopsin function by properties of the membrane bilayer.
Brown MF.
Department of Chemistry, University of Arizona, Tucson 85721.
A prevalent model for the function of rhodopsin centers on the metarhodopsin I (MI) to metarhodopsin II (MII) conformational transition as the triggering event for the visual process. Flash photolysis techniques enable one to determine the [MII]/[MI] ratio for rhodopsin in various recombinant membranes, and thus investigate the roles of the phospholipid head groups and the lipid acyl chains systematically. The results obtained to date clearly show that the pK for the acid-base MI-MII equilibrium of rhodopsin is modulated by the lipid environment. In bilayers of phosphatidylcholines the MI-MII equilibrium is shifted to the left; whereas in the native rod outer segment membranes it is shifted to the right, i.e., at neutral pH near physiological temperature. The lipid mixtures sufficient to yield full photochemical function of rhodopsin include a native-like head group composition, viz, comprising phosphatidylcholine (PC), phosphatidylethanolamine (PE), and phosphatidylserine (PS), in combination with polyunsaturated docosahexaenoic acid (DHA; 22:6 omega 3) chains. Yet such a native-like lipid mixture is not necessary for the MI-MII conformational transition of rhodopsin; one can substitute other lipid compositions having similar properties. The MI-MII transition is favored by relatively small head groups which produce a condensed bilayer surface, viz, a comparatively small interfacial area as in the case of PE, together with bulky acyl chains such as DHA which prefer a relatively large cross sectional area. The resulting force imbalance across the layer gives rise to a curvature elastic stress of the lipid/water interface, such that the lipid mixtures yielding native-like behavior form reverse hexagonal (HII) phases at slightly higher temperatures. A relatively unstable membrane is needed: lipids tending to form the lamellar phase do not support full native-like photochemical function of rhodopsin. Thus chemically specific properties of the various lipids are not required, but rather average or material properties of the entire assembly, which may involve the curvature free energy of the membrane-lipid water interface. These findings reveal that the membrane lipid bilayer has a direct influence on the energetics of the conformational states of rhodopsin in visual excitation.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 8001180 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
10: Biochemistry. 1992 Jun 2;31(21):4923-31.
Rhodopsin: structure, function, and genetics.
Nathans J.
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Publication Types:
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1599916 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
11: J Biol Chem. 1992 Jan 5;267(1):1-4.
Rhodopsin, photoreceptor of the rod cell. An emerging pattern for structure and function.
Khorana HG.
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Publication Types:
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 1730574 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
12: Kidney Int Suppl. 1987 Dec;23:S2-13.
Structure and function of the beta 2-adrenergic receptor--homology with rhodopsin.
Dohlman HG, Caron MG, Lefkowitz RJ.
Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, North Carolina.
Publication Types:
Research Support, U.S. Gov't, P.H.S.
Review
PMID: 2831423 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
13: FEBS Lett. 1982 Nov 8;148(2):179-91.
Rhodopsin and bacteriorhodopsin: structure-function relationships.
Ovchinnikov YuA .
Publication Types:
Review
PMID: 6759163 [PubMed - indexed for MEDLINE]
--------------------------------------------------------------------------------
14: Seikagaku. 1981;53(1):20-4.
[Rhodopsin kinase--with emphasis on function and immunopathogenicity (author's transl)]
[Article in Japanese]
Shichi H.
Publication Types:
Review
PMID: 6169774 [PubMed - indexed for MEDLINE]
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