Structure and function of the visual arrestin oligomer. - Wikidata - awgldk - TriplyDB

Structure and function of the visual arrestin oligomer.

Structure and function of the visual arrestin oligomer.

http://www.wikidata.org/entity/Q38304145

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Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser Structural origin of weakly ordered nitroxide motion in spin-labeled proteins Site-directed spin labeling of a genetically encoded unnatural amino acid Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes Photoreceptor signaling: supporting vision across a wide range of light intensities.Beta-arrestins: multifunctional cellular mediators Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors Probing Protein Secondary Structure using EPR: Investigating a Dynamic Region of Visual Arrestin.Transport and localization of signaling proteins in ciliated cells Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling.Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding Control of rhodopsin's active lifetime by arrestin-1 expression in mammalian rods.Visual Arrestin 1 contributes to cone photoreceptor survival and light adaptation.beta-Arrestin-dependent activation of Ca(2+)/calmodulin kinase II after beta(1)-adrenergic receptor stimulation.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health.Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding Robust self-association is a common feature of mammalian visual arrestin-1.Interaction of arrestin with enolase1 in photoreceptors.Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.The functional cycle of visual arrestins in photoreceptor cells.Redox proteomic identification of visual arrestin dimerization in photoreceptor degeneration after photic injury.ßarrestin1-biased agonism at human δ-opioid receptor by peptidic and alkaloid ligands.Arrestin 1 and Cone Arrestin 4 Have Unique Roles in Visual Function in an All-Cone Mouse Retina.Conformation of receptor-bound visual arrestin.Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin Engineering visual arrestin-1 with special functional characteristics Measuring nanometer distances in nucleic acids using a sequence-independent nitroxide probe.Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.The β-Arrestins: Multifunctional Regulators of G Protein-coupled Receptors GPCR monomers and oligomers: it takes all kinds.Regulation of arrestin binding by rhodopsin phosphorylation level.How and why do GPCRs dimerize?Protein sorting, targeting and trafficking in photoreceptor cells Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding

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Structure and function of the visual arrestin oligomer.

http://www.wikidata.org/entity/Q38304145

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Structure and function of the visual arrestin oligomer.

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Structure and function of the visual arrestin oligomer.

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Structure and function of the visual arrestin oligomer.

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SJ.EMBOJ.7601614

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Structure and function of the visual arrestin oligomer.

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Candice S Klug

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Christian Altenbach

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Derek J Francis

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Ned Van Eps

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Sergey A Vishnivetskiy

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Susan M Hanson

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Vadim Y Arshavsky

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Vsevolod V Gurevich

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P2860

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

Flow of information in the light-triggered cyclic nucleotide cascade of vision

The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

X-ray crystal structure of arrestin from bovine rod outer segments

Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation

Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure.

Estimation of inter-residue distances in spin labeled proteins at physiological temperatures: experimental strategies and practical limitations.

Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme.

New methods for measuring macromolecular interactions in solution via static light scattering: basic methodology and application to nonassociating and self-associating proteins.

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Wayne L. Hubbell

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2007-03-01T00:00:00Z

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6473473

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