N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity (Q44211079)

30 November 2017

title

N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinity (English)

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30 November 2017

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30 November 2017

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30 November 2017

Larry A Sklar

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30 November 2017

T Alexander Key

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30 November 2017

Terry D Foutz

series ordinal

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30 November 2017

language of work or name

English

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publication date

6 November 2002

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Journal of Biological Chemistry

30 November 2017

published in

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30 November 2017

volume

278

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30 November 2017

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30 November 2017

page(s)

4041-4047

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Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein)

30 November 2017

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Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence

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Internalization of the human N-formyl peptide and C5a chemoattractant receptors occurs via clathrin-independent mechanisms

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Differential phosphorylation paradigms dictate desensitization and internalization of the N-formyl peptide receptor

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Real-time analysis of G protein-coupled receptor reconstitution in a solubilized system

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Partial phosphorylation of the N-formyl peptide receptor inhibits G protein association independent of arrestin binding.

21 January 2018

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Two homologous phosphorylation domains differentially contribute to desensitization and internalization of the m2 muscarinic acetylcholine receptor

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21 January 2018

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21 January 2018

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Arrestin Variants Display Differential Binding Characteristics for the PhosphorylatedN-Formyl Peptide Receptor Carboxyl Terminus

21 January 2018

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An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation

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21 January 2018

Identifiers

DOI

10.1074/JBC.M204687200

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30 November 2017

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