Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding.
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International Union of Basic and Clinical Pharmacology. LXXIII. Nomenclature for the formyl peptide receptor (FPR) familyThe two neutrophil members of the formylpeptide receptor family activate the NADPH-oxidase through signals that differ in sensitivity to a gelsolin derived phosphoinositide-binding peptideN-formyl peptide receptor 3 (FPR3) departs from the homologous FPR2/ALX receptor with regard to the major processes governing chemoattractant receptor regulation, expression at the cell surface, and phosphorylationActin dynamics rapidly reset chemoattractant receptor sensitivity following adaptation in neutrophilsThe chemoattractant receptors FPR and C5aR: same functions--different fates.Formyl peptide receptor-mediated ERK1/2 activation occurs through G(i) and is not dependent on beta-arrestin1/2.Arrestin binds to different phosphorylated regions of the thyrotropin-releasing hormone receptor with distinct functional consequences.Deletion of the COOH-terminal domain of CXC chemokine receptor 4 leads to the down-regulation of cell-to-cell contact, enhanced motility and proliferation in breast carcinoma cells.Phosphorylation of key serine residues is required for internalization of the complement 5a (C5a) anaphylatoxin receptor via a beta-arrestin, dynamin, and clathrin-dependent pathway.Twenty years of the G protein-coupled estrogen receptor GPER: Historical and personal perspectives.Phosphorylation-independent beta-arrestin translocation and internalization of leukotriene B4 receptors.N-formyl peptide receptors internalize but do not recycle in the absence of arrestins.Beta-arrestin binding to CC chemokine receptor 5 requires multiple C-terminal receptor phosphorylation sites and involves a conserved Asp-Arg-Tyr sequence motif.Identification of a novel recycling sequence in the C-tail of FPR2/ALX receptor: association with cell protection from apoptosis.N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity.Real-time analysis of ternary complex on particles: direct evidence for partial agonism at the agonist-receptor-G protein complex assembly step of signal transduction.Arrestins block G protein-coupled receptor-mediated apoptosis.Inhibition of chemoattractant N-formyl peptide receptor trafficking by active arrestins.Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons.
P2860
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P2860
Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding.
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2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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name
Partial phosphorylation of the ...... dependent of arrestin binding.
@en
type
label
Partial phosphorylation of the ...... dependent of arrestin binding.
@en
prefLabel
Partial phosphorylation of the ...... dependent of arrestin binding.
@en
P2093
P2860
P356
P1476
Partial phosphorylation of the ...... ndependent of arrestin binding
@en
P2093
P2860
P304
49195-49203
P356
10.1074/JBC.M106414200
P407
P577
2001-10-15T00:00:00Z