The Two Non-Visual Arrestins Engage ERK2 Differently-Reference-Cited by-同舟云学术

The Two Non-Visual Arrestins Engage ERK2 Differently

Published:2022-04 Issue:7 Volume:434 Page:167465
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Perry-Hauser Nicole A.,Hopkins Jesse B.,Zhuo Ya,Zheng Chen,Perez Ivette,Schultz Kathryn M.,Vishnivetskiy Sergey A.,Kaya Ali I.,Sharma Pankaj,Dalby Kevin N.,Chung Ka Young,Klug Candice S.,Gurevich Vsevolod V.,Iverson T.M.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference87 articles.

1. Functional specialization of beta-arrestin interactions revealed by proteomic analysis;Xiao;Proc. Natl. Acad. Sci. USA,2007

2. Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling;Ferguson;Pharmacol Rev.,2001

3. Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor;Goodman;Nature.,1996

4. beta -Arrestin-mediated recruitment of the Src family kinase Yes mediates endothelin-1-stimulated glucose transport;Imamura;J. Biol. Chem.,2001

5. Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes;Luttrell;Science,1999

Cited by 10 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Molecular mechanism of β-arrestin-2 interaction with phosphatidylinositol 4,5-bisphosphate;2024-01-23

2. Electron Paramagnetic Resonance in Structural Biology;Integrated Structural Biology;2023-12-08

3. Molecular insights into intrinsic transducer-coupling bias in the CXCR4-CXCR7 system;Nature Communications;2023-08-09

4. Conformational flexibility of β‐arrestins – How these scaffolding proteins guide and transform the functionality of GPCRs;BioEssays;2023-05-31

5. β−Arrestins: Structure, Function, Physiology, and Pharmacological Perspectives;Pharmacological Reviews;2023-04-07