Changes in interhelical hydrogen bonding upon rhodopsin activation. - Wikidata - wikimedia - TriplyDB

Changes in interhelical hydrogen bonding upon rhodopsin activation.

Changes in interhelical hydrogen bonding upon rhodopsin activation.

http://www.wikidata.org/entity/Q30984908

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Hydrogen bond dynamics in membrane protein function Cation Diffusion Facilitators Transport Initiation and Regulation Is Mediated by Cation Induced Conformational Changes of the Cytoplasmic Domain Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptor Structural waters define a functional channel mediating activation of the GPCR, rhodopsin.Unraveling the structure and function of G protein-coupled receptors through NMR spectroscopy.Membrane protein structure and dynamics from NMR spectroscopy.G-protein-coupled receptor structure, ligand binding and activation as studied by solid-state NMR spectroscopy.Internal hydration increases during activation of the G-protein-coupled receptor rhodopsin.Development and application of hybrid structure based method for efficient screening of ligands binding to G-protein coupled receptors.Modeling activated states of GPCRs: the rhodopsin template.Sequential rearrangement of interhelical networks upon rhodopsin activation in membranes: the Meta II(a) conformational substate.Structure and function of G protein-coupled receptors using NMR spectroscopy.A minimal ligand binding pocket within a network of correlated mutations identified by multiple sequence and structural analysis of G protein coupled receptors.Highly conserved tyrosine stabilizes the active state of rhodopsin.Comparison of class A and D G protein-coupled receptors: common features in structure and activation.Dynamic behavior of fully solvated beta2-adrenergic receptor, embedded in the membrane with bound agonist or antagonist.Glutamic acid 181 is negatively charged in the bathorhodopsin photointermediate of visual rhodopsin.Energy landscapes as a tool to integrate GPCR structure, dynamics, and function.Location of the retinal chromophore in the activated state of rhodopsin*.Evolution of opsins and phototransduction.G protein-coupled receptor rhodopsin.Atypical signaling and functional desensitization response of MAS receptor to peptide ligands.Frequency-selective homonuclear dipolar recoupling in solid state NMR Role of group-conserved residues in the helical core of beta2-adrenergic receptor Evidence from Chlamydomonas on the photoactivation of rhodopsins without isomerization of their chromophore.Polar transmembrane interactions drive formation of ligand-specific and signal pathway-biased family B G protein-coupled receptor conformations.Proton movement and photointermediate kinetics in rhodopsin mutants Atomistic insights into rhodopsin activation from a dynamic model Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation.6-s-cis Conformation and polar binding pocket of the retinal chromophore in the photoactivated state of rhodopsin Amino acid conservation and interactions in rhodopsin: probing receptor activation by NMR spectroscopy.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Insights into the activation mechanism of the visual receptor rhodopsin.G-protein-coupled receptor dynamics: dimerization and activation models compared with experiment.Light-induced photoreceptor and RPE degeneration involve zinc toxicity and are attenuated by pyruvate, nicotinamide, or cyclic light.High-resolution NMR spectroscopy of a GPCR in aligned bicelles.Systematic analysis of the entire second extracellular loop of the V(1a) vasopressin receptor: key residues, conserved throughout a G-protein-coupled receptor family, identified.The synthesis and high-level expression of a beta2-adrenergic receptor gene in a tetracycline-inducible stable mammalian cell line.Isotope labeling in mammalian cells.Differential activation of polymorphisms of the formyl peptide receptor by formyl peptides.

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P2860

Changes in interhelical hydrogen bonding upon rhodopsin activation.

http://www.wikidata.org/entity/Q30984908

description

2005 nî lūn-bûn

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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Changes in interhelical hydrogen bonding upon rhodopsin activation.

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Changes in interhelical hydrogen bonding upon rhodopsin activation.

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Changes in interhelical hydrogen bonding upon rhodopsin activation.

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Changes in interhelical hydrogen bonding upon rhodopsin activation.

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Changes in interhelical hydrogen bonding upon rhodopsin activation.

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Elena V Getmanova

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