Agonist-directed interactions with specific beta-arrestins determine mu-opioid receptor trafficking, ubiquitination, and dephosphorylation. - Wikidata - awgldk - TriplyDB

Agonist-directed interactions with specific beta-arrestins determine mu-opioid receptor trafficking, ubiquitination, and dephosphorylation.

Agonist-directed interactions with specific beta-arrestins determine mu-opioid receptor trafficking, ubiquitination, and dephosphorylation.

http://www.wikidata.org/entity/Q35213193

about

MOR is not enough: identification of novel mu-opioid receptor interacting proteins using traditional and modified membrane yeast two-hybrid screens Regulation of G protein-coupled receptors by allosteric ligands Activation of mu opioid receptors sensitizes transient receptor potential vanilloid type 1 (TRPV1) via β-arrestin-2-mediated cross-talk Opiate pharmacology and relief of pain.Putative kappa opioid heteromers as targets for developing analgesics free of adverse effects.Synthetic Studies of Neoclerodane Diterpenes from Salvia divinorum: Identification of a Potent and Centrally Acting μ Opioid Analgesic with Reduced Abuse Liability.Opioid receptor desensitization: mechanisms and its link to tolerance Neuropsychological Functions of μ- and δ-Opioid Systems.Potent Anti-HIV Chemokine Analogs Direct Post-Endocytic Sorting of CCR5 Differential Regulation of 6- and 7-Transmembrane Helix Variants of μ-Opioid Receptor in Response to Morphine Stimulation GRK2 protein-mediated transphosphorylation contributes to loss of function of μ-opioid receptors induced by neuropeptide FF (NPFF2) receptors.Evidence that behavioral phenotypes of morphine in β-arr2-/- mice are due to the unmasking of JNK signaling.Endomorphin-2: a biased agonist at the μ-opioid receptor.Ubiquitination of G protein-coupled receptors: functional implications and drug discovery.Regulation of endocytic clathrin dynamics by cargo ubiquitination Ligand-directed signalling within the opioid receptor family.Serine 363 is required for nociceptin/orphanin FQ opioid receptor (NOPR) desensitization, internalization, and arrestin signaling.Regulation of μ-opioid receptors: desensitization, phosphorylation, internalization, and tolerance.Ubiquitin-dependent regulation of G protein-coupled receptor trafficking and signaling Agonist-Specific Recruitment of Arrestin Isoforms Differentially Modify Delta Opioid Receptor Function Molecular mechanisms of opioid receptor-dependent signaling and behavior.Mu opioids and their receptors: evolution of a concept.Class B β-arrestin2-dependent CCR5 signalosome retention with natural antibodies to CCR5.Biased G Protein-Coupled Receptor Signaling: New Player in Modulating Physiology and Pathology Isolating and characterizing three alternatively spliced mu opioid receptor variants: mMOR-1A, mMOR-1O, and mMOR-1P.Morphine-induced trafficking of a mu-opioid receptor interacting protein in rat locus coeruleus neurons.Ligand- and cell-dependent determinants of internalization and cAMP modulation by delta opioid receptor (DOR) agonists.Ligand bias at the μ-opioid receptor.Efficacy and ligand bias at the μ-opioid receptor.β-arrestins: regulatory role and therapeutic potential in opioid and cannabinoid receptor-mediated analgesia.The μ-opioid receptor: an electrophysiologist's perspective from the sharp end.Functional selectivity of GPCR signaling in animals.Biased agonism: An emerging paradigm in GPCR drug discovery.Regulation of GPCR Trafficking by Ubiquitin.Morphine activation of mu opioid receptors causes disinhibition of neurons in the ventral tegmental area mediated by β-arrestin2 and c-Src.Ubiquitin-Related Roles of β-Arrestins in Endocytic Trafficking and Signal Transduction.Arresting the Development of Addiction: The Role of β-Arrestin 2 in Drug Abuse.GABA(B) receptors do not internalize after baclofen treatment, possibly due to a lack of β-arrestin association: study with a real-time visualizing assay.A comparison of the antinociceptive and temperature responses to morphine and fentanyl derivatives in rats.Morphine-induced internalization of the L83I mutant of the rat μ-opioid receptor

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P2860

Agonist-directed interactions with specific beta-arrestins determine mu-opioid receptor trafficking, ubiquitination, and dephosphorylation.

http://www.wikidata.org/entity/Q35213193

description

2011 nî lūn-bûn

@nan

2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին 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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name

Agonist-directed interactions ...... nation, and dephosphorylation.

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Agonist-directed interactions ...... nation, and dephosphorylation.

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type

label

Agonist-directed interactions ...... nation, and dephosphorylation.

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Agonist-directed interactions ...... nation, and dephosphorylation.

@en

prefLabel

Agonist-directed interactions ...... nation, and dephosphorylation.

@ast

Agonist-directed interactions ...... nation, and dephosphorylation.

@en

P1433

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JBC.M111.248310

P1433

Journal of Biological Chemistry

P1476

Agonist-directed interactions ...... ination, and dephosphorylation

@en

P2093

Alex M Jaeger

http://www.w3.org/2001/XMLSchema#string

Chad E Groer

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Cullen L Schmid

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P2860

{beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase

Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor

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

The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits

Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin

beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: identification of a beta-arrestin binging site in beta 2-adaptin

Transduction of receptor signals by beta-arrestins

Enhanced morphine analgesia in mice lacking beta-arrestin 2

Morphine promotes rapid, arrestin-dependent endocytosis of mu-opioid receptors in striatal neurons

Receptor heterodimerization leads to a switch in signaling: beta-arrestin2-mediated ERK activation by mu-delta opioid receptor heterodimers

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21757712

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protein ubiquitination

P932

3173119

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