Molecular evidence suggests that each retina expresses a different visualpigment.
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A new high-resolution structure is reported for bovine rhodopsin, the visualpigment in rod photoreceptor cells.
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Goldfish has a UV-sensitive visualpigment (S group) localized in miniature single cone cells.
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Activation of the visualpigment by light in rod and cone photoreceptors initiates our visual perception.
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The visual cycle is a chain of biochemical reactions that regenerate visualpigment following exposure to light.
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The retinoid profile is altered as judged by biochemical analysis, arguing for a partial block in visualpigment regeneration.
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Activation of the visualpigment by light triggers a transduction cascade that produces experimentally measurable electrical responses in photoreceptors.
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Rhodopsin has been intensively characterized in its role as a visualpigment and G protein-coupled receptor responsible for dim-light vision.
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The 9-methyl group of 11-cis-retinal plays a crucial role in photoexcitation of the visualpigment rhodopsin.
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These data support the premise that rods and cones have mechanisms for handling retinoids and regenerating visualpigment that are specific to photoreceptor type.
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Both RPE65 isomerase of the visual cycle and the rhodopsin visualpigment have recently been identified as critical players in mediating light-induced retinal degeneration.
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We report experiments designed to test the hypothesis that the aqueous solubility of 11-cis-retinoids plays a significant role in the rate of visualpigment regeneration.
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Frogs have a violet-sensitive visualpigment (S group) in small single cone cells and a blue-sensitive visualpigment (MS group) in green rod cells.
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The retinal pigmented epithelium (RPE) forms the outer blood-retinal barrier and provides nutrients and recycling of visualpigment to the photoreceptors, among many other functions.
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Vision relies on photoactivation of visualpigments in rod and cone photoreceptor cells of the retina.
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For example, rod and cone visualpigments couple to distinct variants of the heterotrimeric G protein transducin.