scholarly article | Q13442814 |
P50 | author | Vsevolod V. Gurevich | Q42173663 |
P2093 | author name string | Matthew J Kennedy | |
Dayanidhi Raman | |||
Sergey A Vishnivetskiy | |||
James B Hurley | |||
Junhua Wei | |||
P2860 | cites work | Arrestins: ubiquitous regulators of cellular signaling pathways | Q21184142 |
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Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexes | Q24563320 | ||
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The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation | Q27618047 | ||
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation | Q27634946 | ||
Transduction of receptor signals by beta-arrestins | Q28246395 | ||
Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signaling | Q33819399 | ||
Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor | Q33819496 | ||
Structure and function in rhodopsin: asymmetric reconstitution of rhodopsin in liposomes | Q34159475 | ||
Origin of reproducibility in the responses of retinal rods to single photons | Q34169073 | ||
Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degeneration | Q34453852 | ||
Possible involvement of the endocannabinoid system in the actions of three clinically used drugs. | Q34547367 | ||
Stable rhodopsin/arrestin complex leads to retinal degeneration in a transgenic mouse model of autosomal dominant retinitis pigmentosa. | Q34581973 | ||
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin | Q34596638 | ||
Toward a unified model of vertebrate rod phototransduction | Q34693762 | ||
The new face of active receptor bound arrestin attracts new partners | Q35214608 | ||
Each rhodopsin molecule binds its own arrestin | Q35652316 | ||
Determinants of single photon response variability | Q36411526 | ||
Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylation | Q36639195 | ||
Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm | Q36726881 | ||
Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state | Q73030745 | ||
Use of bacteriophage RNA polymerase in RNA synthesis | Q73053443 | ||
An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation | Q73054341 | ||
Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion | Q73427926 | ||
Isolation of isoelectric species of phosphorylated rhodopsin | Q73591603 | ||
Arrestin: mutagenesis, expression, purification, and functional characterization | Q73591654 | ||
Visual arrestin activity may be regulated by self-association | Q78010480 | ||
Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses | Q80011647 | ||
Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin | Q82372903 | ||
The differential engagement of arrestin surface charges by the various functional forms of the receptor | Q36737719 | ||
Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions | Q37365027 | ||
Structure and function of the visual arrestin oligomer | Q38304145 | ||
Concentration-dependent tetramerization of bovine visual arrestin | Q40248090 | ||
Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins | Q40628650 | ||
The nature of the arrestin x receptor complex determines the ultimate fate of the internalized receptor | Q40678127 | ||
Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. | Q41079862 | ||
Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. | Q41099124 | ||
Constitutive activation of opsin: interaction of mutants with rhodopsin kinase and arrestin | Q41294623 | ||
How does arrestin respond to the phosphorylated state of rhodopsin? | Q42470664 | ||
Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. | Q42623057 | ||
Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptation | Q43702730 | ||
Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge | Q44127981 | ||
N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity | Q44211079 | ||
Light induced shift and binding of S-antigen in retinal rods | Q44722936 | ||
Visual pigment phosphorylation but not transducin translocation can contribute to light adaptation in zebrafish cones | Q44815991 | ||
Rhodopsin phosphorylation in rats exposed to intense light | Q45123488 | ||
Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events | Q45182666 | ||
Light dependent phosphorylation of rhodopsin by ATP. | Q46123273 | ||
Light causes phosphorylation of nonactivated visual pigments in intact mouse rod photoreceptor cells | Q46137947 | ||
RGS expression rate-limits recovery of rod photoresponses | Q46175317 | ||
Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites | Q46690154 | ||
Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. | Q46804865 | ||
G-protein-coupled receptors: turn-ons and turn-offs | Q47754228 | ||
The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms | Q47982269 | ||
Conservation of the phosphate-sensitive elements in the arrestin family of proteins | Q48871433 | ||
Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cells | Q48922901 | ||
Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors | Q50337370 | ||
Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin. | Q52078908 | ||
Variability in the time course of single photon responses from toad rods: termination of rhodopsin's activity. | Q52209745 | ||
The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration. | Q52584172 | ||
A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila. | Q52584174 | ||
Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. | Q54266642 | ||
The role of arrestin and retinoids in the regeneration pathway of rhodopsin | Q67901125 | ||
Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction | Q67907347 | ||
Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination | Q68905392 | ||
Differential immunogold-dextran labeling of bovine and frog rod and cone cells using monoclonal antibodies against bovine rhodopsin | Q68957656 | ||
Phosphorylation of frog photoreceptor membranes induced by light | Q68997021 | ||
Mechanism of rhodopsin kinase activation | Q70231775 | ||
Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin | Q70501789 | ||
Phosphorylation of non-bleached rhodopsin in intact retinas and living frogs | Q71245930 | ||
Light-dependent phosphorylation of rhodopsin: number of phosphorylation sites | Q72111974 | ||
Rhodopsin phosphorylation and dephosphorylation in vivo | Q72315710 | ||
Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin binding | Q72422681 | ||
Control of rhodopsin multiple phosphorylation | Q72767084 | ||
P433 | issue | 44 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | phosphorylation | Q242736 |
P1104 | number of pages | 9 | |
P304 | page(s) | 32075-32083 | |
P577 | publication date | 2007-09-11 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Regulation of arrestin binding by rhodopsin phosphorylation level | |
P478 | volume | 282 |
Q46913447 | A comprehensive model of the phototransduction cascade in mouse rod cells |
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Q42668381 | Arrestin competition influences the kinetics and variability of the single-photon responses of mammalian rod photoreceptors |
Q61444237 | Arrestin-1 engineering facilitates complex stabilization with native rhodopsin |
Q34486390 | Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health |
Q41981772 | Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains. |
Q34606311 | Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors |
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Q90575731 | Biased GPCR signaling: Possible mechanisms and inherent limitations |
Q99571920 | Biological role of arrestin-1 oligomerization |
Q35626307 | C-terminal threonines and serines play distinct roles in the desensitization of rhodopsin, a G protein-coupled receptor |
Q36673993 | Calcium feedback to cGMP synthesis strongly attenuates single-photon responses driven by long rhodopsin lifetimes |
Q90357054 | Cleavage of arrestin-3 by caspases attenuates cell death by precluding arrestin-dependent JNK activation |
Q27023938 | Constitutively active rhodopsin and retinal disease |
Q37174339 | Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding |
Q33736656 | Control of rhodopsin's active lifetime by arrestin-1 expression in mammalian rods |
Q36796795 | Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. |
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Q61800782 | Determination of basal phosphodiesterase activity in mouse rod photoreceptors with cGMP clamp |
Q34787383 | Differential temporal and spatial regulation of somatostatin receptor phosphorylation and dephosphorylation |
Q36538241 | Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction. |
Q64077238 | Distinct G protein-coupled receptor phosphorylation motifs modulate arrestin affinity and activation and global conformation |
Q33845194 | Effect of g protein-coupled receptor kinase 1 (Grk1) overexpression on rod photoreceptor cell viability |
Q41894869 | Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance. |
Q42553690 | Engineered hyperphosphorylation of the β2-adrenoceptor prolongs arrestin-3 binding and induces arrestin internalization. |
Q36579557 | Engineering visual arrestin-1 with special functional characteristics |
Q42159390 | Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation |
Q42394084 | Enhanced phosphorylation-independent arrestins and gene therapy |
Q43063154 | Exploring the rate-limiting steps in visual phototransduction recovery by bottom-up kinetic modeling |
Q35085144 | Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins |
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Q36181935 | Functional characterization of an arrestin gene on insecticide resistance of Culex pipiens pallens |
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Q35536256 | G Protein-coupled Receptor Kinases of the GRK4 Protein Subfamily Phosphorylate Inactive G Protein-coupled Receptors (GPCRs). |
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Q36238782 | How rods respond to single photons: Key adaptations of a G-protein cascade that enable vision at the physical limit of perception |
Q38429586 | Identification of Phosphorylation Codes for Arrestin Recruitment by G Protein-Coupled Receptors. |
Q33566969 | Identification of critical phosphorylation sites on the carboxy tail of melanopsin |
Q34482298 | Identification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptor |
Q33947214 | Identification of receptor binding-induced conformational changes in non-visual arrestins |
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Q28476555 | Kinetics of rhodopsin deactivation and its role in regulating recovery and reproducibility of rod photoresponse |
Q36946699 | Kinetics of turn-offs of frog rod phototransduction cascade |
Q33892087 | Lessons from photoreceptors: turning off g-protein signaling in living cells |
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Q37209196 | Location, location, location...site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling |
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Q33983455 | Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery |
Q34715589 | Protein kinase C-mediated phosphorylation of the μ-opioid receptor and its effects on receptor signaling |
Q37036865 | Quantitative modeling of the molecular steps underlying shut-off of rhodopsin activity in rod phototransduction |
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Q37178682 | Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms |
Q34708925 | Robust self-association is a common feature of mammalian visual arrestin-1. |
Q35841895 | Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. |
Q36197653 | Role of rhodopsin and arrestin phosphorylation in retinal degeneration of Drosophila |
Q37041964 | Signal transducing membrane complexes of photoreceptor outer segments |
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Q38114211 | Structural determinants of arrestin functions |
Q50093625 | Structure and dynamics of GPCR signaling complexes. |
Q38016028 | Synthetic biology with surgical precision: targeted reengineering of signaling proteins |
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Q34103312 | The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation |
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Q36083423 | ßarrestin1-biased agonism at human δ-opioid receptor by peptidic and alkaloid ligands. |
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