Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface. - Wikidata - wikimedia - TriplyDB

Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

http://www.wikidata.org/entity/Q34480194

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Dopamine D2 receptors form higher order oligomers at physiological expression levels Autosomal recessive retinitis pigmentosa and E150K mutation in the opsin gene Crystal structure of oligomeric β1-adrenergic G protein–coupled receptors in ligand-free basal state A G Protein-Coupled Receptor Dimerization Interface in Human Cone Opsins Three-dimensional architecture of murine rod outer segments determined by cryoelectron tomography.Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit.Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding Time-resolved fluorescence spectroscopy measures clustering and mobility of a G protein-coupled receptor opsin in live cell membranes Dynamic models of G-protein coupled receptor dimers: indications of asymmetry in the rhodopsin dimer from molecular dynamics simulations in a POPC bilayer.Complexes between photoactivated rhodopsin and transducin: progress and questions.Do crystal structures obviate the need for theoretical models of GPCRs for structure-based virtual screening?Rhodopsin self-associates in asolectin liposomes.Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding Role of membrane integrity on G protein-coupled receptors: Rhodopsin stability and function.Structural basis of M3 muscarinic receptor dimer/oligomer formation Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction.Misfolded opsin mutants display elevated β-sheet structure.Disruption of Rhodopsin Dimerization with Synthetic Peptides Targeting an Interaction Interface Mutations affecting the oligomerization interface of G-protein-coupled receptors revealed by a novel de novo protein design framework Ligand sensitivity in dimeric associations of the serotonin 5HT2c receptor Vertebrate membrane proteins: structure, function, and insights from biophysical approaches.G protein-coupled receptor oligomerization provides the framework for signal discrimination.GPCR monomers and oligomers: it takes all kinds.Monomeric rhodopsin is the minimal functional unit required for arrestin binding.Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex.GPCR dimers fall apart.Fluorescence spectroscopy of rhodopsins: insights and approaches.Dimers of G-protein coupled receptors as versatile storage and response units Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation.Instability of a class a G protein-coupled receptor oligomer interface.TRP1 interacting PDZ-domain protein GIPC forms oligomers and is localized to intracellular vesicles in human melanocytes.Molecular simulations of lipid-mediated protein-protein interactions Influence of oligomerization on the dynamics of G-protein coupled receptors as assessed by normal mode analysis.Wild-type opsin does not aggregate with a misfolded opsin mutant.Endoplasmic reticulum-associated degradation of a degron-containing polytopic membrane protein.Comparative fluorescence resonance energy transfer analysis of metabotropic glutamate receptors: implications about the dimeric arrangement and rearrangement upon ligand bindings.Quaternary structures of opsin in live cells revealed by FRET spectrometry.The molecular and cellular basis of rhodopsin retinitis pigmentosa reveals potential strategies for therapy.Molecular Dynamics Simulations of G Protein-Coupled Receptors.Molecular dynamics simulations and structure-based network analysis reveal structural and functional aspects of G-protein coupled receptor dimer interactions.

P2860

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P2860

Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface.

http://www.wikidata.org/entity/Q34480194

description

2006 nî lūn-bûn

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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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H Gobind Khorana

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P2860

Heterodimerization is required for the formation of a functional GABA(B) receptor

Crystal structure of rhodopsin: A G protein-coupled receptor

Subtypes of the somatostatin receptor assemble as functional homo- and heterodimers

Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells

Mammalian sweet taste receptors

Structure of a bacterial sensory receptor. A site-directed sulfhydryl study.

Sites of interaction in the complex between beta- and gamma-subunits of transducin.

Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping

Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation.

Oligomerization of G-protein-coupled transmitter receptors.

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