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Three cytoplasmic loops of rhodopsin interact with transducin.
Rhodopsin is a member of an ancient class of receptors that transduce signals through their interaction with guanine nucleotide-binding proteins (G proteins). We have mapped the sites of interactionExpand
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Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides.
The binding sites for four monoclonal antibodies, rho 1D4, rho 3C2, rho 3A6, and rho 1C5, have been localized within the C-terminal region of bovine rhodopsin:Expand
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Retinoids Assist the Cellular Folding of the Autosomal Dominant Retinitis Pigmentosa Opsin Mutant P23H*
The clinically common mutant opsin P23H, associated with autosomal dominant retinitis pigmentosa, yields low levels of rhodopsin when retinal is added following induction of the protein in stablyExpand
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Crystals of native and modified bovine rhodopsins and their heavy atom derivatives.
Rhodopsin, the pigment protein responsible for dim-light vision, is a G protein-coupled receptor that converts light absorption into the activation of a G protein, transducin, to initiate the visualExpand
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The structure of bovine rhodopsin
We have isolated 16 peptides from a cyanogen bromide digest of rhodopsin. These cyanogen bromide peptides account for the complete composition of the protein. Methionine-containing peptides fromExpand
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Retinal degeneration 12 (rd12): a new, spontaneously arising mouse model for human Leber congenital amaurosis (LCA).
PURPOSE To report the phenotype and characterization of a new, naturally occurring mouse model of hereditary retinal degeneration (rd12). METHODS The retinal phenotype of rd12 mice were studiedExpand
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Arrestin migrates in photoreceptors in response to light: a study of arrestin localization using an arrestin-GFP fusion protein in transgenic frogs.
Subcellular translocation of phototransduction proteins in response to light has previously been detected by immunocytochemistry. This movement is consistent with the hypothesis that migration isExpand
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Regulation of rhodopsin dephosphorylation by arrestin.
We have characterized the opsin phosphatase activities in extracts of rod outer segments and determined their relationship to known protein phosphatases. The opsin phosphatase activity in theExpand
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Dynamics of Arrestin-Rhodopsin Interactions
In this study we investigate conformational changes in Loop V-VI of visual arrestin during binding to light-activated, phosphorylated rhodopsin (Rho*-P) using a combination of site-specific cysteineExpand
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Binding pattern of anti-rhodopsin monoclonal antibodies to photoreceptor cells: an immunocytochemical study.
A panel of anti-rhodopsin monoclonal antibodies (MAbs) of defined epitope specificity has been evaluated by immunocytochemistry. Most of the IgG class MAbs (23/27) gave positive results, but only aExpand
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