Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. - Wikidata - awgldk - TriplyDB

Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.

Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.

http://www.wikidata.org/entity/Q37365027

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Arrestins: ubiquitous regulators of cellular signaling pathways SARA-regulated vesicular targeting underlies formation of the light-sensing organelle in mammalian rods Photoreceptor Sensory Cilium: Traversing the Ciliary Gate Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs 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.Trafficking to the ciliary membrane: how to get across the periciliary diffusion barrier?Ablation of retinal ciliopathy protein RPGR results in altered photoreceptor ciliary composition Expression of hydroxyindole-O-methyltransferase enzyme in the human central nervous system and in pineal parenchymal cell tumors Mechanisms underlying stage-1 TRPL channel translocation in Drosophila photoreceptors Three-dimensional architecture of the rod sensory cilium and its disruption in retinal neurodegeneration Spatial distribution of intraflagellar transport proteins in vertebrate photoreceptors Immunocytochemical evidence of Tulp1-dependent outer segment protein transport pathways in photoreceptor cells Interaction of glyceraldehyde-3-phosphate dehydrogenase in the light-induced rod alpha-transducin translocation Transport and localization of signaling proteins in ciliated cells Arrestin translocation is stoichiometric to rhodopsin isomerization and accelerated by phototransduction in Drosophila photoreceptors An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier Chemically inducible diffusion trap at cilia reveals molecular sieve-like barrier.Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.Diffusion of a soluble protein, photoactivatable GFP, through a sensory cilium GAP-independent termination of photoreceptor light response by excess gamma subunit of the cGMP-phosphodiesterase.Relationships among visual cycle retinoids, rhodopsin phosphorylation, and phototransduction in mouse eyes during light and dark adaptation.Visual Arrestin 1 contributes to cone photoreceptor survival and light adaptation.Arrestin can act as a regulator of rhodopsin photochemistry.Lessons from photoreceptors: turning off g-protein signaling in living cells.Functional analysis of retinitis pigmentosa 2 (RP2) protein reveals variable pathogenic potential of disease-associated missense variants Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.A component of retinal light adaptation mediated by the thyroid hormone cascade.Diffusion and light-dependent compartmentalization of transducin.Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health.Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors.Robust self-association is a common feature of mammalian visual arrestin-1.Modeling the role of incisures in vertebrate phototransduction Interaction of arrestin with enolase1 in photoreceptors.Development of an MRI biomarker sensitive to tetrameric visual arrestin 1 and its reduction via light-evoked translocation in vivo.A role for cytoskeletal elements in the light-driven translocation of proteins in rod photoreceptors.Identification of arrestin-3-specific residues necessary for JNK3 kinase activation Accumulation of the Raf-1 kinase inhibitory protein (Rkip) is associated with Cep290-mediated photoreceptor degeneration in ciliopathies.Interaction of transducin with uncoordinated 119 protein (UNC119): implications for the model of transducin trafficking in rod photoreceptors.The functional cycle of visual arrestins in photoreceptor cells.

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Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.

http://www.wikidata.org/entity/Q37365027

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on May 2005

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Light-dependent redistribution ...... protein-protein interactions.

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Light-dependent redistribution ...... protein-protein interactions.

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Light-dependent redistribution ...... protein-protein interactions.

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Light-dependent redistribution ...... protein-protein interactions.

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Light-dependent redistribution ...... protein-protein interactions.

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Light-dependent redistribution ...... protein-protein interactions.

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J.NEURON.2005.03.023

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Light-dependent redistribution ...... protein-protein interactions.

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Ana Mendez

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Eugenia V Gurevich

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James B Hurley

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Jeannie Chen

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K Saidas Nair

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Matthew J Kennedy

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Sergey A Vishnivetskiy

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Susan M Hanson

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Valery I Shestopalov

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Vladlen Z Slepak

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P2860

Mutations in the inosine monophosphate dehydrogenase 1 gene (IMPDH1) cause the RP10 form of autosomal dominant retinitis pigmentosa.

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

The molecular acrobatics of arrestin activation

Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin

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

Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase

Prolonged photoresponses in transgenic mouse rods lacking arrestin.

Protein translocation in photoreceptor light adaptation: a common theme in vertebrate and invertebrate vision.

Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation

Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.

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555-567

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10.1016/J.NEURON.2005.03.023

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4

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Vsevolod V. Gurevich

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2005-05-01T00:00:00Z

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7798520

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