Quantification of Arrestin–Rhodopsin Binding Stoichiometry
Author:
Publisher
Springer New York
Link
http://link.springer.com/content/pdf/10.1007/978-1-4939-2330-4_16
Reference17 articles.
1. Schleicher A, Kühn H, Hofmann KP (1989) Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II. Biochemistry 28:1770–1775
2. Wilden U, Hall SW, Kuhn H (1986) Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci U S A 83:1174–1178
3. Sommer ME, Hofmann KP, Heck M (2012) Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin. Nat Commun 3:995
4. Zhuang T, Chen Q, Cho MK et al (2013) Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci U S A 110:942–947
5. Sommer ME, Hofmann KP, Heck M (2014) Not just signal shutoff: the protective role of arrestin-1 in rod cells. Handb Exp Pharmacol 219:101–116
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