Internalization of the m2 Muscarinic Acetylcholine Receptor-Reference-Cited by-同舟云学术

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Internalization of the m2 Muscarinic Acetylcholine Receptor

Published:1997-09 Issue:38 Volume:272 Page:23682-23689
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pals-Rylaarsdam Robin,Gurevich Vsevolod V.,Lee Katharine B.,Ptasienski Judith A.,Benovic Jeffrey L.,Hosey M. Marlene

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference28 articles.

1. Regulation of Signal Transduction Pathways by Desensitization and Amplification;Liggett,1994

2. Role of β-Arrestin in Mediating Agonist-Promoted G Protein-Coupled Receptor Internalization

3. β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor

4. Two Homologous Phosphorylation Domains Differentially Contribute to Desensitization and Internalization of the m2 Muscarinic Acetylcholine Receptor

5. Desensitization and Internalization of the m2 Muscarinic Acetylcholine Receptor Are Directed by Independent Mechanisms

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1. Arrestins: A Small Family of Multi-Functional Proteins;International Journal of Molecular Sciences;2024-06-06

2. Arrestin‐centred interactions at the membrane and their conformational determinants;British Journal of Pharmacology;2024-03-13

3. Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors;Science;2024-01-05

4. Phosphorylation motif dictates GPCR C-terminal domain conformation and arrestin interaction;Structure;2023-11

5. Molecular insights into atypical modes of β-arrestin interaction with seven transmembrane receptors;2023-07-05

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