Surveying nonvisual arrestins reveals allosteric interactions between functional sites-Reference-Cited by-同舟云学术

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Surveying nonvisual arrestins reveals allosteric interactions between functional sites

Published:2022-08-27 Issue:1 Volume:91 Page:99-107
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Seckler James M.¹^ORCID,Robinson Emily N.²,Lewis Stephen J.³,Grossfield Alan²

Affiliation:

1. Department of Biomedical Engineering Case Western Reserve University Cleveland Ohio USA

2. Department of Biochemistry and Biophysics University of Rochester Rochester New York USA

3. Department of Pediatrics Case Western Reserve University Cleveland Ohio USA

Funder

National Institute on Drug Abuse

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.26413

Reference67 articles.

1. The structural basis of the arrestin binding to GPCRs

2. β-Arrestin Based Receptor Signaling Paradigms: Potential Therapeutic Targets for Complex Age-Related Disorders

3. -Arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors

4. ERK and β-Arrestin Interaction

5. G Protein regulation of MAPK networks

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