An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1-Reference-Cited by-同舟云学术

An arrestin-1 surface opposite of its interface with photoactivated rhodopsin engages with enolase-1

Published:2020-05 Issue:19 Volume:295 Page:6498-6508
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Miranda Connie Jaqueline,Fernandez Nicole,Kamel Nader,Turner Daniel,Benzenhafer Del,Bolch Susan N.,Andring Jacob T.^ORCID,McKenna Robert,Smith W. Clay

Funder

Research to Prevent Blindness

Foundation Fighting Blindness

Oxnard Foundation

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

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4. Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylatio of rhodopsin and by arrestin binding;Wilden;Biochemistry,1995

5. The diverse roles of arrestin scaffolds in G protein–coupled receptor signaling;Peterson;Pharmacol. Rev,2017

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