Flavonoids enhance rod opsin stability, folding, and self-association by directly binding to ligand-free opsin and modulating its conformation [PDF]
Journal of Biological Chemistry, 2019 Rhodopsin (Rho) is a visual G protein-coupled receptor expressed in the rod photoreceptors of the eye, where it mediates transmission of a light signal into a cell and converts this signal into a nerve impulse. More than 100 mutations in Rho are linked to various ocular impairments, including retinitis pigmentosa (RP). Accordingly, much effort has been
Joseph T. Ortega +2 more
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Calcium‐activated Opsin Phosphatase Activity in Retinal Rod Outer Segments [PDF]
European Journal of Biochemistry, 1996 We describe the presence in bovine retinal rod outer segments of a phosphatase which dephosphorylates phosphoopsin with an efficiency similar to that of PP2A, and which is stimulated by submicromolar levels of Ca2+ (half‐maximal activation, 0.4–0.5 μM). This enzyme is designated Ca2+‐activated opsin phosphatase (CAOP).
M A, Kutuzov, N, Bennett
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BMC Biology, 2018 Background Animal opsins are light-sensitive G-protein-coupled receptors (GPCRs) that enable optogenetic control over the major heterotrimeric G-protein signaling pathways in animal cells.
Edward R. Ballister +3 more
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Retinoids in the visual cycle: role of the retinal G protein-coupled receptor
Journal of Lipid Research, 2021 Driven by the energy of a photon, the visual pigments in rod and cone photoreceptor cells isomerize 11-cis-retinal to the all-trans configuration.
Elliot H. Choi +4 more
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Variations in photoreceptor throughput to mouse visual cortex and the unique effects on tuning
Scientific Reports, 2021 Visual input to primary visual cortex (V1) depends on highly adaptive filtering in the retina. In turn, isolation of V1 computations requires experimental control of retinal adaptation to infer its spatio-temporal-chromatic output.
I. Rhim, G. Coello-Reyes, I. Nauhaus
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Blue light regenerates functional visual pigments in mammals through a retinyl-phospholipid intermediate. [PDF]
, 2017 The light absorbing chromophore in opsin visual pigments is the protonated Schiff base of 11-cis-retinaldehyde (11cRAL). Absorption of a photon isomerizes 11cRAL to all-trans-retinaldehyde (atRAL), briefly activating the pigment before it dissociates ...
Fain, Gordon L +6 more
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Rpgrip1 is required for rod outer segment development and ciliary protein trafficking in zebrafish [PDF]
, 2017 The authors would like to thank the Royal Society of London, the National Eye Research Centre, the Visual Research Trust, Fight for Sight, the W.H. Ross Foundation, the Rosetrees Trust, and the Glasgow Children’s Hospital Charity for supporting this work.
A Eblimit +54 more
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P23H opsin knock-in mice reveal a novel step in retinal rod disc morphogenesis [PDF]
Human Molecular Genetics, 2013 Abstract Retinal rod photoreceptor cells have double membrane discs located in their outer segments (ROS) that are continuously formed proximally from connecting cilia (CC) and phagocytized distally by the retinal pigmented epithelium. The major component of these rod discs, the light-sensitive visual pigment rhodopsin (Rho), consists of
Sanae Sakami +3 more
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Abnormal photoreceptor outer segment development and early retinal degeneration in kif3a mutant zebrafish [PDF]
, 2016 Photoreceptors are highly specialized sensory neurons that possess a modified primary cilium called the outer segment. Photoreceptor outer segment formation and maintenance require highly active protein transport via a process known as intraflagellar ...
Akhtar +44 more
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A dual role for EDEM1 in the processing of rod opsin [PDF]
Journal of Cell Science, 2009 Mutations in rod opsin, the archetypal G-protein-coupled receptor, cause retinitis pigmentosa. The majority of mutations, e.g. P23H, cause protein misfolding, resulting in ER retention, induction of the unfolded protein response and degradation by ERAD.
Kosmaoglou, Maria +4 more
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