Noncatalytic cGMP-binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory gamma-subunits. A putative regulatory mechanism of the rod photoresponse.-Reference-Cited by-同舟云学术

Noncatalytic cGMP-binding sites of amphibian rod cGMP phosphodiesterase control interaction with its inhibitory gamma-subunits. A putative regulatory mechanism of the rod photoresponse.

Published:1992-12 Issue:34 Volume:267 Page:24501-24507
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Arshavsky V.Y.,Dumke C.L.,Bownds M.D.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference67 articles.

1. Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP

2. cGMP suppresses GTPase activity of a portion of transducin equimolar to phosphodiesterase in frog rod outer segments. Light-induced cGMP decreases as a putative feedback mechanism of the photoresponse.

3. Two-site high-affinity interaction between inhibitory and catalytic subunits of rod cyclic GMP phosphodiesterase

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