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Crystal structure of rhodopsin: a G-protein-coupled receptor.
Heterotrimeric guanine nucleotide–binding protein (G protein)–coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structuralExpand
Crystal Structure of Rhodopsin: A G‐Protein‐Coupled Receptor
Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors (GPCRs) respond to a variety of different external stimuli and activate G proteins. GPCRs share many structuralExpand
Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin.
G-protein-coupled receptors 1 constitute a large superfamily of receptor proteins responsible for signal transduction, with family A being by far the largest and more closely related to each other within a few functional domains than those of the other families. Expand
Five Members of a Novel Ca2+-binding Protein (CABP) Subfamily with Similarity to Calmodulin*
Five members of a novel Ca2+-binding protein subfamily (CaBP), with 46–58% sequence similarity to calmodulin (CaM), were identified in the vertebrate retina, suggesting that these novel CaBPs are an important component of Ca2-mediated cellular signal transduction in the central nervous system where they may augment or substitute for CaM. Expand
Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs).
The further refinement of rhodopsin is described and some clues about how the receptor could be activated by light are provided, to allow models, firmly based on the atomic-resolution structural information, to be further tested as to the conformational changes that these receptors undergo in going from the quiescent to the signaling state. Expand
Essential role of Ca2+-binding protein 4, a Cav1.4 channel regulator, in photoreceptor synaptic function
Observations indicate that CaBP4 is important for normal synaptic function, probably through regulation of Ca2+ influx and neurotransmitter release in photoreceptor synaptic terminals. Expand
Atomic-force microscopy: Rhodopsin dimers in native disc membranes
In vertebrate retinal photoreceptors, the rod outer-segment disc membranes contain densely packed rhodopsin molecules for optimal light absorption and subsequent amplification by the visualExpand
Organization of the G Protein-coupled Receptors Rhodopsin and Opsin in Native Membranes*
This is the first semi-empirical model of a higher order structure of a GPCR in native membranes, and it has profound implications for the understanding of how this receptor interacts with partner proteins. Expand
Diseases caused by defects in the visual cycle: retinoids as potential therapeutic agents.
Gene therapy has been successfully used in animal models of these diseases to rescue the function of enzymes involved in chromophore regeneration, restoring vision and hope that multiple inherited retinal diseases will soon be treated by pharmaceutical intervention. Expand
Role of guanylate cyclase-activating proteins (GCAPs) in setting the flash sensitivity of rod photoreceptors
It is concluded that GCAPs strongly regulate GC activity in mouse rods, decreasing the flash sensitivity in darkness and increasing the incrementalflash sensitivity in bright steady light, thereby extending the rod's operating range. Expand