Enhanced Mutant Compensates for Defects in Rhodopsin Phosphorylation in the Presence of Endogenous Arrestin-1
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[1] Naomi R. Latorraca,et al. Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors , 2017, Cell.
[2] M. E. Burns,et al. cGMP in mouse rods: the spatiotemporal dynamics underlying single photon responses , 2015, Front. Mol. Neurosci..
[3] H. Stoy,et al. How genetic errors in GPCRs affect their function: Possible therapeutic strategies , 2015, Genes & diseases.
[4] Garth J. Williams,et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser , 2014, Nature.
[5] V. Arshavsky,et al. Current understanding of signal amplification in phototransduction , 2014, Cellular logistics.
[6] M. Palazzo,et al. Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant. , 2013, Cellular signalling.
[7] C. Jao,et al. Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina , 2013, Proceedings of the National Academy of Sciences.
[8] V. Gurevich,et al. Critical Role of the Central 139-Loop in Stability and Binding Selectivity of Arrestin-1* , 2013, The Journal of Biological Chemistry.
[9] M. Palazzo,et al. Engineering Visual Arrestin-1 with Special Functional Characteristics* , 2012, The Journal of Biological Chemistry.
[10] V. Gurevich,et al. The functional cycle of visual arrestins in photoreceptor cells , 2011, Progress in Retinal and Eye Research.
[11] Jeannie Chen,et al. Progressive Reduction of its Expression in Rods Reveals Two Pools of Arrestin-1 in the Outer Segment with Different Roles in Photoresponse Recovery , 2011, PloS one.
[12] W. Hubbell,et al. Robust self-association is a common feature of mammalian visual arrestin-1. , 2011, Biochemistry.
[13] V. Gurevich,et al. Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health , 2011, Neuroscience.
[14] E. Pugh,et al. Lessons from photoreceptors: turning off g-protein signaling in living cells. , 2010, Physiology.
[15] Marie E Burns,et al. Control of Rhodopsin's Active Lifetime by Arrestin-1 Expression in Mammalian Rods , 2010, The Journal of Neuroscience.
[16] Jeannie Chen,et al. Enhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation , 2009, Current Biology.
[17] Marie E. Burns,et al. Enhanced Arrestin Facilitates Recovery and Protects Rods Lacking Rhodopsin Phosphorylation , 2009, Current Biology.
[18] E. Pugh,et al. Mouse Cones Require an Arrestin for Normal Inactivation of Phototransduction , 2008, Neuron.
[19] J. Meiler,et al. A model for the solution structure of the rod arrestin tetramer. , 2008, Structure.
[20] W. W. Rubin,et al. Functional comparisons of visual arrestins in rod photoreceptors of transgenic mice. , 2007, Investigative ophthalmology & visual science.
[21] V. Arshavsky,et al. Structure and function of the visual arrestin oligomer , 2007, The EMBO journal.
[22] Vsevolod V. Gurevich,et al. Each rhodopsin molecule binds its own arrestin , 2007, Proceedings of the National Academy of Sciences.
[23] M. Sokolov,et al. Arrestin Translocation Is Induced at a Critical Threshold of Visual Signaling and Is Superstoichiometric to Bleached Rhodopsin , 2006, The Journal of Neuroscience.
[24] J. Hurley,et al. Light-Dependent Redistribution of Arrestin in Vertebrate Rods Is an Energy-Independent Process Governed by Protein-Protein Interactions , 2005, Neuron.
[25] Katrin Sangkuhl,et al. Mutant G-protein-coupled receptors as a cause of human diseases. , 2004, Pharmacology & therapeutics.
[26] Edward N. Pugh,et al. From candelas to photoisomerizations in the mouse eye by rhodopsin bleaching in situ and the light-rearing dependence of the major components of the mouse ERG , 2004, Vision Research.
[27] E. Pugh,et al. Functionally rodless mice: transgenic models for the investigation of cone function in retinal disease and therapy , 2002, Vision Research.
[28] Marie E. Burns,et al. Rapid and Reproducible Deactivation of Rhodopsin Requires Multiple Phosphorylation Sites , 2000, Neuron.
[29] M. Simon,et al. Increased susceptibility to light damage in an arrestin knockout mouse model of Oguchi disease (stationary night blindness) , 1999, Investigative ophthalmology & visual science.
[30] P B Sigler,et al. How Does Arrestin Respond to the Phosphorylated State of Rhodopsin?* , 1999, The Journal of Biological Chemistry.
[31] P. Sigler,et al. A Model for Arrestin’s Regulation: The 2.8 Å Crystal Structure of Visual Arrestin , 1999, Cell.
[32] J. Hetling,et al. Sensitivity and kinetics of mouse rod flash responses determined in vivo from paired‐flash electroretinograms , 1999, The Journal of physiology.
[33] J B Hurley,et al. Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[34] R L Sidman,et al. Morphological, physiological, and biochemical changes in rhodopsin knockout mice. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[35] V. Gurevich. The Selectivity of Visual Arrestin for Light-activated Phosphorhodopsin Is Controlled by Multiple Nonredundant Mechanisms* , 1998, The Journal of Biological Chemistry.
[36] G. Büldt,et al. X-ray crystal structure of arrestin from bovine rod outer segments , 1998, Nature.
[37] A. Cideciyan,et al. Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[38] Denis A. Baylor,et al. Prolonged photoresponses in transgenic mouse rods lacking arrestin , 1997, Nature.
[39] J. Benovic,et al. Mechanism of Quenching of Phototransduction , 1997, The Journal of Biological Chemistry.
[40] P. Detwiler,et al. Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion. , 1997, Biochemistry.
[41] D R Pepperberg,et al. Photoresponses of human rods in vivo derived from paired-flash electroretinograms , 1997, Visual Neuroscience.
[42] T. Dryja,et al. Transgenic mice carrying the dominant rhodopsin mutation P347S: evidence for defective vectorial transport of rhodopsin to the outer segments. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[43] E. Pugh,et al. Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings , 1996, The Journal of neuroscience : the official journal of the Society for Neuroscience.
[44] M. Tamai,et al. A homozygous 1–base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese , 1995, Nature Genetics.
[45] J. Benovic,et al. Visual Arrestin Binding to Rhodopsin , 1995, The Journal of Biological Chemistry.
[46] U Wilden,et al. Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding. , 1995, Biochemistry.
[47] David J. Baylor,et al. Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant , 1995, Science.
[48] E. Zrenner,et al. Ocular findings in a family with autosomal dominant retinitis pigmentosa and a frameshift mutation altering the carboxyl terminal sequence of rhodopsin. , 1993, The British journal of ophthalmology.
[49] J L Benovic,et al. Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. , 1993, The Journal of biological chemistry.
[50] J. Jin,et al. Light-dependent delay in the falling phase of the retinal rod photoresponse , 1992, Visual Neuroscience.
[51] D. Baylor,et al. Responses of retinal rods to single photons. , 1979, The Journal of physiology.
[52] L. Donoso,et al. Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina. , 1977, Journal of immunology.
[53] A. Mushegian,et al. G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. , 2012, Pharmacology & therapeutics.
[54] Jeannie Chen,et al. [11] Functional study of rhodopsin phosphorylation in vivo , 2000 .
[55] P. Demoly,et al. [Transgenic mice]. , 1992, Annales de dermatologie et de venereologie.
[56] S. B. Aronson. Experimental allergic uveitis. , 1968, Archives of ophthalmology.