Binding of Transducin to Light-Activated Rhodopsin Prevents Transducin Interaction with the Rod cGMP Phosphodiesterase γ-Subunit
Author:
Affiliation:
1. Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi963002y
Reference40 articles.
1. Sites of interaction between rod G-protein alpha-subunit and cGMP-phosphodiesterase gamma-subunit. Implications for the phosphodiesterase activation mechanism.
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3. Mechanism of photoreceptor cGMP phosphodiesterase inhibition by its gamma-subunits.
4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
5. Functional regions of the inhibitory subunit of retinal rod cGMP phosphodiesterase identified by site-specific mutagenesis and fluorescence spectroscopy
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4. Computational Molecular Analysis of Human Rhodopsin, Transducin and Arrestin Interactions: An Insight into Signal Transduction for Ophthalmology;Advances in Intelligent Systems and Computing;2016-11-23
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