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Molecular evidence suggests that each retina expresses a different visualpigment.
2
A new high-resolution structure is reported for bovine rhodopsin, the visualpigment in rod photoreceptor cells.
3
Goldfish has a UV-sensitive visualpigment (S group) localized in miniature single cone cells.
4
Activation of the visualpigment by light in rod and cone photoreceptors initiates our visual perception.
5
The visual cycle is a chain of biochemical reactions that regenerate visualpigment following exposure to light.
6
The retinoid profile is altered as judged by biochemical analysis, arguing for a partial block in visualpigment regeneration.
7
Activation of the visualpigment by light triggers a transduction cascade that produces experimentally measurable electrical responses in photoreceptors.
8
Rhodopsin has been intensively characterized in its role as a visualpigment and G protein-coupled receptor responsible for dim-light vision.
9
The 9-methyl group of 11-cis-retinal plays a crucial role in photoexcitation of the visualpigment rhodopsin.
10
These data support the premise that rods and cones have mechanisms for handling retinoids and regenerating visualpigment that are specific to photoreceptor type.
11
Both RPE65 isomerase of the visual cycle and the rhodopsin visualpigment have recently been identified as critical players in mediating light-induced retinal degeneration.
12
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.
13
Frogs have a violet-sensitive visualpigment (S group) in small single cone cells and a blue-sensitive visualpigment (MS group) in green rod cells.
14
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.
15
Vision relies on photoactivation of visualpigments in rod and cone photoreceptor cells of the retina.
16
For example, rod and cone visualpigments couple to distinct variants of the heterotrimeric G protein transducin.