scholarly article | Q13442814 |
P50 | author | Vsevolod V. Gurevich | Q42173663 |
P2093 | author name string | Sergey A Vishnivetskiy | |
Candice S Klug | |||
Ya Zhuo | |||
Xuanzhi Zhan | |||
P2860 | cites work | Arrestins: ubiquitous regulators of cellular signaling pathways | Q21184142 |
beta-Arrestin: a protein that regulates beta-adrenergic receptor function | Q24305145 | ||
Functional specialization of beta-arrestin interactions revealed by proteomic analysis | Q24318455 | ||
Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds | Q24605173 | ||
The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis | Q24651529 | ||
The structural basis of arrestin-mediated regulation of G-protein-coupled receptors | Q24657537 | ||
The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation | Q27618047 | ||
N-terminal and C-terminal domains of arrestin both contribute in binding to rhodopsin | Q38307271 | ||
Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. | Q40159254 | ||
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 | ||
Computer modeling of nitroxide spin labels on proteins | Q41844162 | ||
Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance. | Q41894869 | ||
How does arrestin respond to the phosphorylated state of rhodopsin? | Q42470664 | ||
Topographic study of arrestin using differential chemical modifications and hydrogen/deuterium exchange | Q42843987 | ||
DEER distance measurements on proteins | Q43666647 | ||
Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge | Q44127981 | ||
Helix formation in arrestin accompanies recognition of photoactivated rhodopsin | Q46625169 | ||
Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. | Q46804865 | ||
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 | ||
Crystal packing effects on protein loops. | Q51975331 | ||
Arrestin interaction with rhodopsin: conceptual models. | Q53589615 | ||
Structural properties of arrestin studied by chemical modification and circular dichroism | Q68099952 | ||
An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation | Q73054341 | ||
Arrestin/clathrin interaction. Localization of the clathrin binding domain of nonvisual arrestins to the carboxy terminus | Q73382665 | ||
Arrestin: mutagenesis, expression, purification, and functional characterization | Q73591654 | ||
Dynamics of arrestin-rhodopsin interactions: loop movement is involved in arrestin activation and receptor binding | Q80557418 | ||
Arrestin2 expression selectively increases during neural differentiation | Q81109121 | ||
Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin | Q82372903 | ||
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation | Q27634946 | ||
Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis | Q27638156 | ||
Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes | Q27666519 | ||
Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide | Q27677473 | ||
Crystal structure of pre-activated arrestin p44 | Q27684457 | ||
Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin | Q28190513 | ||
Transduction of receptor signals by beta-arrestins | Q28246395 | ||
The molecular acrobatics of arrestin activation | Q28257918 | ||
Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family | Q28264339 | ||
Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development | Q28576365 | ||
Structural diversity of G protein-coupled receptors and significance for drug discovery | Q29616716 | ||
Beta-arrestins and cell signaling | Q29616793 | ||
Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor | Q29618735 | ||
Seven-transmembrane receptors | Q29619896 | ||
Structure and dynamics of an imidazoline nitroxide side chain with strongly hindered internal motion in proteins | Q30430837 | ||
Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry | Q33220382 | ||
Global phosphorylation analysis of beta-arrestin-mediated signaling downstream of a seven transmembrane receptor (7TMR). | Q34093722 | ||
The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation | Q34103312 | ||
Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health | Q34486390 | ||
Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2. | Q34536660 | ||
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin | Q34596638 | ||
Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins | Q35085144 | ||
Rhodopsin phosphorylation: 30 years later | Q35125718 | ||
The new face of active receptor bound arrestin attracts new partners | Q35214608 | ||
The functional cycle of visual arrestins in photoreceptor cells | Q35387361 | ||
G protein-coupled receptor kinases: more than just kinases and not only for GPCRs | Q35621624 | ||
Each rhodopsin molecule binds its own arrestin | Q35652316 | ||
Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant | Q36003914 | ||
Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins | Q36215950 | ||
Conformation of receptor-bound visual arrestin | Q36389593 | ||
Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin | Q36545558 | ||
Stop that cell! Beta-arrestin-dependent chemotaxis: a tale of localized actin assembly and receptor desensitization | Q36604354 | ||
Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. | Q36796795 | ||
Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina | Q36915521 | ||
Regulation of arrestin binding by rhodopsin phosphorylation level | Q37089132 | ||
The role of arrestin alpha-helix I in receptor binding | Q37456291 | ||
P433 | issue | 30 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 20991-21002 | |
P577 | publication date | 2014-05-27 | |
P1433 | published in | Journal of Biological Chemistry | Q867727 |
P1476 | title | Identification of receptor binding-induced conformational changes in non-visual arrestins | |
P478 | volume | 289 |
Q26785358 | Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs |
Q42548477 | Arrestin expression in E. coli and purification. |
Q38521129 | Arrestins: Critical Players in Trafficking of Many GPCRs |
Q49908026 | Arrestins: structural disorder creates rich functionality. |
Q51739139 | Distinct Phosphorylation Clusters Determine the Signaling Outcome of Free Fatty Acid Receptor 4/G Protein-Coupled Receptor 120. |
Q64228935 | GPCR Signaling Regulation: The Role of GRKs and Arrestins |
Q47394219 | Heterologous phosphorylation-induced formation of a stability lock permits regulation of inactive receptors by β-arrestins |
Q104139733 | How GPCR Phosphorylation Patterns Orchestrate Arrestin-Mediated Signaling |
Q47255137 | Molecular Mechanisms of GPCR Signaling: A Structural Perspective |
Q64895618 | Molecular mechanism of modulating arrestin conformation by GPCR phosphorylation. |
Q64103540 | Not all arrestins are created equal: Therapeutic implications of the functional diversity of the β-arrestins in the heart |
Q94388687 | Paradigm Shift is the Normal State of Pharmacology |
Q64926886 | Structural Basis of Arrestin-Dependent Signal Transduction. |
Q47107777 | Structural basis of arrestin-3 activation and signaling. |
Q40383376 | Structural evidence for the role of polar core residue Arg175 in arrestin activation |
Q38716027 | Structural mechanism of GPCR-arrestin interaction: recent breakthroughs. |
Q50093625 | Structure and dynamics of GPCR signaling complexes. |
Q39381430 | The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling |
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