Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. - sprookjes - yvandenbroek - TriplyDB

Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.

Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.

http://www.wikidata.org/entity/Q35085144

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The chemokine receptor CCR1 is constitutively active, which leads to G protein-independent, β-arrestin-mediated internalization Analyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKs How genetic errors in GPCRs affect their function: Possible therapeutic strategies Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin binding Identification of receptor binding-induced conformational changes in non-visual arrestins.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activation G protein-coupled receptors--recent advances Identification of arrestin-3-specific residues necessary for JNK3 kinase activation A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding.The functional cycle of visual arrestins in photoreceptor cells.G Protein-coupled Receptor Kinases of the GRK4 Protein Subfamily Phosphorylate Inactive G Protein-coupled Receptors (GPCRs).GPCR structure, function, drug discovery and crystallography: report from Academia-Industry International Conference (UK Royal Society) Chicheley Hall, 1-2 September 2014.Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Quantitative Signaling and Structure-Activity Analyses Demonstrate Functional Selectivity at the Nociceptin/Orphanin FQ Opioid Receptor.Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins Spinophilin as a novel regulator of M3 muscarinic receptor-mediated insulin release in vitro and in vivo.Design and functional characterization of a novel, arrestin-biased designer G protein-coupled receptor.Conformation of receptor-bound visual arrestin.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin Engineering visual arrestin-1 with special functional characteristics Evidence for Noncanonical Neurotransmitter Activation: Norepinephrine as a Dopamine D2-Like Receptor Agonist A G Protein-biased Designer G Protein-coupled Receptor Useful for Studying the Physiological Relevance of Gq/11-dependent Signaling Pathways.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.Constitutively active rhodopsin mutants causing night blindness are effectively phosphorylated by GRKs but differ in arrestin-1 binding Functional and structural characterization of axonal opioid receptors as targets for analgesia.Synthetic biology with surgical precision: targeted reengineering of signaling proteins.Structural determinants of arrestin functions β-arrestins and G protein-coupled receptor trafficking.Extensive shape shifting underlies functional versatility of arrestins.Uncovering missing pieces: duplication and deletion history of arrestins in deuterostomes.β-Arrestin biosensors reveal a rapid, receptor-dependent activation/deactivation cycle Mutations in arrestin-3 differentially affect binding to neuropeptide Y receptor subtypes The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.Nonvisual arrestins function as simple scaffolds assembling the MKK4-JNK3α2 signaling complex Unraveling the molecular architecture of a G protein-coupled receptor/β-arrestin/Erk module complex.Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors.Targeting individual GPCRs with redesigned nonvisual arrestins.Self-association of arrestin family members.

P2860

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P2860

Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.

http://www.wikidata.org/entity/Q35085144

description

2011 nî lūn-bûn

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2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Few residues within an extensi ...... cificity of arrestin proteins.

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Few residues within an extensi ...... cificity of arrestin proteins.

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Few residues within an extensi ...... cificity of arrestin proteins.

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Few residues within an extensi ...... cificity of arrestin proteins.

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JBC.M110.213835

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Journal of Biological Chemistry

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Few residues within an extensi ...... cificity of arrestin proteins.

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P2093

Candice S Klug

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Derek J Francis

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Luis E Gimenez

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Sergey A Vishnivetskiy

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Susan M Hanson

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Vsevolod V Gurevich

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P2860

Arrestins: ubiquitous regulators of cellular signaling pathways

Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments

The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis

The structural basis of arrestin-mediated regulation of G-protein-coupled receptors

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

Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane Translocation

Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis

Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking

Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes

Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking

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scholarly article

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10.1074/JBC.M110.213835

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27

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286

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Wayne L. Hubbell

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2011-04-06T00:00:00Z

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21471193

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3129209

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