Published in Cell Signal on September 03, 2013
Overview of different mechanisms of arrestin-mediated signaling. Curr Protoc Pharmacol (2014) 0.82
Beyond traditional pharmacology: new tools and approaches. Br J Pharmacol (2015) 0.80
Self-association of arrestin family members. Handb Exp Pharmacol (2014) 0.78
Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs. Crit Rev Biochem Mol Biol (2015) 0.77
Arrestin expression in E. coli and purification. Curr Protoc Pharmacol (2014) 0.77
Enhanced phosphorylation-independent arrestins and gene therapy. Handb Exp Pharmacol (2014) 0.75
Arrestins in apoptosis. Handb Exp Pharmacol (2014) 0.75
The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling. Pharmacol Rev (2017) 0.75
Cell death: critical control points. Cell (2004) 22.56
Caspases: enemies within. Science (1998) 19.45
Retinitis pigmentosa. Lancet (2006) 13.62
Responses of retinal rods to single photons. J Physiol (1979) 7.47
A unified model for apical caspase activation. Mol Cell (2003) 6.12
Apoptosis in the nervous system. Nature (2000) 5.82
The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell (1999) 3.67
Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ (2003) 3.59
Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase. Proc Natl Acad Sci U S A (1999) 2.83
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation. Structure (2001) 2.66
Prolonged photoresponses in transgenic mouse rods lacking arrestin. Nature (1997) 2.64
Evidence for two apoptotic pathways in light-induced retinal degeneration. Nat Genet (2002) 2.49
The molecular acrobatics of arrestin activation. Trends Pharmacol Sci (2004) 2.44
Mechanisms of rhodopsin inactivation in vivo as revealed by a COOH-terminal truncation mutant. Science (1995) 2.39
Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron (2005) 2.21
Arrestins: ubiquitous regulators of cellular signaling pathways. Genome Biol (2006) 2.15
Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J Biol Chem (1993) 2.14
Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites. Neuron (2000) 2.13
A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila. Neuron (2000) 2.10
The relationship between opsin overexpression and photoreceptor degeneration. Invest Ophthalmol Vis Sci (2001) 1.98
Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin. J Neurosci (2006) 1.95
Photoreceptor cell death mechanisms in inherited retinal degeneration. Mol Neurobiol (2008) 1.94
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci U S A (2006) 1.94
Tissue-specific and developmental regulation of rod opsin chimeric genes in transgenic mice. Neuron (1991) 1.88
The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration. Neuron (2000) 1.88
Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol (2005) 1.82
Each rhodopsin molecule binds its own arrestin. Proc Natl Acad Sci U S A (2007) 1.73
Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins. J Biol Chem (2003) 1.67
Structure and function of the visual arrestin oligomer. EMBO J (2007) 1.66
Mouse cones require an arrestin for normal inactivation of phototransduction. Neuron (2008) 1.66
Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J Biol Chem (2010) 1.66
How does arrestin respond to the phosphorylated state of rhodopsin? J Biol Chem (1999) 1.65
Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding. J Biol Chem (2006) 1.54
An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation. J Biol Chem (2000) 1.53
Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. J Biol Chem (2006) 1.53
The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. J Biol Chem (1998) 1.53
Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashion. Biochemistry (1997) 1.49
Quantification of the cytoplasmic spaces of living cells with EGFP reveals arrestin-EGFP to be in disequilibrium in dark adapted rod photoreceptors. J Cell Sci (2004) 1.47
Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin. J Biol Chem (1997) 1.46
Arrestin: mutagenesis, expression, purification, and functional characterization. Methods Enzymol (2000) 1.45
Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. J Biol Chem (1995) 1.44
The differential engagement of arrestin surface charges by the various functional forms of the receptor. J Biol Chem (2005) 1.42
Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction. J Biol Chem (1992) 1.41
Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem (2006) 1.41
Homo- and hetero-oligomerization of beta-arrestins in living cells. J Biol Chem (2005) 1.39
Arrestin2 expression selectively increases during neural differentiation. J Neurochem (2004) 1.38
A model for the solution structure of the rod arrestin tetramer. Structure (2008) 1.37
Monomeric rhodopsin is the minimal functional unit required for arrestin binding. J Mol Biol (2010) 1.33
Visual arrestin activity may be regulated by self-association. J Biol Chem (1999) 1.31
Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol (2011) 1.31
Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J Biol Chem (2011) 1.30
Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development. Neuroscience (2002) 1.28
Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci U S A (2012) 1.27
Conformation of receptor-bound visual arrestin. Proc Natl Acad Sci U S A (2012) 1.24
Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors. J Biol Chem (2004) 1.23
The functional cycle of visual arrestins in photoreceptor cells. Prog Retin Eye Res (2011) 1.23
Arrestin-1 expression level in rods: balancing functional performance and photoreceptor health. Neuroscience (2010) 1.19
Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants. J Neurosci (2006) 1.16
Stable rhodopsin/arrestin complex leads to retinal degeneration in a transgenic mouse model of autosomal dominant retinitis pigmentosa. J Neurosci (2006) 1.16
Concentration-dependent tetramerization of bovine visual arrestin. Biophys J (2003) 1.15
Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation. Curr Biol (2009) 1.14
Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites. J Neurochem (2007) 1.13
Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nat Commun (2012) 1.12
The role of arrestin alpha-helix I in receptor binding. J Mol Biol (2009) 1.10
Functional comparisons of visual arrestins in rod photoreceptors of transgenic mice. Invest Ophthalmol Vis Sci (2007) 1.10
Flow of energy in the outer retina in darkness and in light. Proc Natl Acad Sci U S A (2010) 1.07
Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. J Biol Chem (2012) 1.01
Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association. Biochemistry (2007) 0.99
Visual Arrestin 1 acts as a modulator for N-ethylmaleimide-sensitive factor in the photoreceptor synapse. J Neurosci (2010) 0.99
Robust self-association is a common feature of mammalian visual arrestin-1. Biochemistry (2011) 0.97
Insights into congenital stationary night blindness based on the structure of G90D rhodopsin. EMBO Rep (2013) 0.95
Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. J Biol Chem (2013) 0.92
Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina. Proc Natl Acad Sci U S A (2013) 0.90
Engineering visual arrestin-1 with special functional characteristics. J Biol Chem (2012) 0.90
Interaction of arrestin with enolase1 in photoreceptors. Invest Ophthalmol Vis Sci (2011) 0.89
Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding. Cell Signal (2013) 0.87
Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery. PLoS One (2011) 0.82
Calmodulin kinase II inhibition protects against structural heart disease. Nat Med (2005) 5.87
High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc Natl Acad Sci U S A (2008) 5.06
A new spin on protein dynamics. Trends Biochem Sci (2002) 3.72
Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking. Adv Protein Chem (2003) 3.28
The structural basis of arrestin-mediated regulation of G-protein-coupled receptors. Pharmacol Ther (2006) 3.15
Dynamics of cyclic GMP synthesis in retinal rods. Neuron (2002) 3.03
Structure of membrane-bound alpha-synuclein from site-directed spin labeling and computational refinement. Proc Natl Acad Sci U S A (2008) 2.68
Mechanism of the receptor-catalyzed activation of heterotrimeric G proteins. Nat Struct Mol Biol (2006) 2.68
Sugar binding induces an outward facing conformation of LacY. Proc Natl Acad Sci U S A (2007) 2.66
Structural organization of alpha-synuclein fibrils studied by site-directed spin labeling. J Biol Chem (2003) 2.65
Downregulation of miR-133 and miR-590 contributes to nicotine-induced atrial remodelling in canines. Cardiovasc Res (2009) 2.54
Multiquantum EPR spectroscopy of spin-labeled arrestin K267C at 35 GHz. Biophys J (2005) 2.50
The molecular acrobatics of arrestin activation. Trends Pharmacol Sci (2004) 2.44
Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling. Proc Natl Acad Sci U S A (2004) 2.33
Investigation of alpha-synuclein fibril structure by site-directed spin labeling. J Biol Chem (2007) 2.30
Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron (2005) 2.21
Arrestins: ubiquitous regulators of cellular signaling pathways. Genome Biol (2006) 2.15
G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharmacol Ther (2011) 2.13
Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit. Proc Natl Acad Sci U S A (2011) 2.10
Structural determinants of nitroxide motion in spin-labeled proteins: tertiary contact and solvent-inaccessible sites in helix G of T4 lysozyme. Protein Sci (2007) 2.01
Mapping backbone dynamics in solution with site-directed spin labeling: GCN4-58 bZip free and bound to DNA. Biochemistry (2004) 2.00
Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study. Biochemistry (2002) 1.99
GPCR monomers and oligomers: it takes all kinds. Trends Neurosci (2008) 1.97
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci U S A (2006) 1.94
Structural determinants of nitroxide motion in spin-labeled proteins: solvent-exposed sites in helix B of T4 lysozyme. Protein Sci (2007) 1.87
Sequence of late molecular events in the activation of rhodopsin. Proc Natl Acad Sci U S A (2007) 1.85
Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol (2005) 1.82
Characterization of agonist stimulation of cAMP-dependent protein kinase and G protein-coupled receptor kinase phosphorylation of the beta2-adrenergic receptor using phosphoserine-specific antibodies. Mol Pharmacol (2004) 1.79
Each rhodopsin molecule binds its own arrestin. Proc Natl Acad Sci U S A (2007) 1.73
Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses. Science (2006) 1.70
Structural origin of weakly ordered nitroxide motion in spin-labeled proteins. Protein Sci (2009) 1.68
Identification of functional genetic variants in cyclooxygenase-2 and their association with risk of esophageal cancer. Gastroenterology (2005) 1.67
Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins. J Biol Chem (2003) 1.67
How and why do GPCRs dimerize? Trends Pharmacol Sci (2008) 1.67
Structure and function of the visual arrestin oligomer. EMBO J (2007) 1.66
Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding. J Biol Chem (2010) 1.66
Site-directed spin labeling of a genetically encoded unnatural amino acid. Proc Natl Acad Sci U S A (2009) 1.65
Comparative analysis of human mesenchymal stem cells from bone marrow, adipose tissue, and umbilical cord blood as sources of cell therapy. Int J Mol Sci (2013) 1.64
Motion of spin label side chains in cellular retinol-binding protein: correlation with structure and nearest-neighbor interactions in an antiparallel beta-sheet. Biochemistry (2004) 1.62
Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci (2009) 1.60
Site-directed spin labeling measurements of nanometer distances in nucleic acids using a sequence-independent nitroxide probe. Nucleic Acids Res (2006) 1.57
Recoverin improves rod-mediated vision by enhancing signal transmission in the mouse retina. Neuron (2005) 1.54
Regulation of arrestin binding by rhodopsin phosphorylation level. J Biol Chem (2007) 1.54
Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm. J Biol Chem (2006) 1.53
Multifrequency electron spin resonance study of the dynamics of spin labeled T4 lysozyme. J Phys Chem B (2010) 1.53
Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. J Mol Biol (2007) 1.52
Blockage by SP600125 of Fcepsilon receptor-induced degranulation and cytokine gene expression in mast cells is mediated through inhibition of phosphatidylinositol 3-kinase signalling pathway. J Biochem (2008) 1.52
Conformational states and dynamics of rhodopsin in micelles and bilayers. Biochemistry (2006) 1.51
Signaling properties of a short-wave cone visual pigment and its role in phototransduction. J Neurosci (2007) 1.49
The new face of active receptor bound arrestin attracts new partners. Structure (2003) 1.48
Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge. J Biol Chem (2002) 1.47
Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation EPR. Biophys J (2005) 1.44
Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers. J Clin Invest (2006) 1.43
Arrangement of subunits and ordering of beta-strands in an amyloid sheet. Nat Struct Biol (2002) 1.43
The differential engagement of arrestin surface charges by the various functional forms of the receptor. J Biol Chem (2005) 1.42
Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J Biol Chem (2002) 1.42
Visual arrestin binding to microtubules involves a distinct conformational change. J Biol Chem (2006) 1.41
Structure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy. Proc Natl Acad Sci U S A (2011) 1.41
Arrestin2 expression selectively increases during neural differentiation. J Neurochem (2004) 1.38
Light-dependent translocation of arrestin in the absence of rhodopsin phosphorylation and transducin signaling. J Neurosci (2003) 1.38
A model for the solution structure of the rod arrestin tetramer. Structure (2008) 1.37
Technological advances in site-directed spin labeling of proteins. Curr Opin Struct Biol (2013) 1.36
Monitoring RNA base structure and dynamics using site-directed spin labeling. Biochemistry (2003) 1.36
Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export. J Mol Biol (2005) 1.34
Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway. Proc Natl Acad Sci U S A (2006) 1.33
Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge. Proc Natl Acad Sci U S A (2004) 1.32
Retinoic acid and polyriboinosinic:polyribocytidylic acid stimulate robust anti-tetanus antibody production while differentially regulating type 1/type 2 cytokines and lymphocyte populations. J Immunol (2005) 1.32
Substrate-induced conformational changes of the periplasmic N-terminus of an outer-membrane transporter by site-directed spin labeling. Biochemistry (2003) 1.31
Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol (2011) 1.31
How does arrestin assemble MAPKs into a signaling complex? J Biol Chem (2008) 1.30
Altered sensitivity to rewarding and aversive drugs in mice with inducible disruption of cAMP response element-binding protein function within the nucleus accumbens. J Neurosci (2009) 1.30
Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J Biol Chem (2011) 1.30