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Pigment Epithelium of Eye
RPE65 is the isomerohydrolase in the retinoid visual cycle.
RPE65 gene delivery restores isomerohydrolase activity and prevents early cone loss in Rpe65-/- mice.
RPE65 from cone-dominant chicken is a more efficient isomerohydrolase compared with that from rod-dominant species.
Comparison of ocular pathologies in vitamin A-deficient mice and RPE65 gene knockout mice.
Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium.
The roles of three palmitoylation sites of RPE65 in its membrane association and isomerohydrolase activity.
Identification of a novel palmitylation site essential for membrane association and isomerohydrolase activity of RPE65.
The 11-cis-retinol dehydrogenase activity of RDH10 and its interaction with visual cycle proteins.
Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane.
Negative charge of the glutamic acid 417 residue is crucial for isomerohydrolase activity of RPE65.
RPE65 is an iron(II)-dependent isomerohydrolase in the retinoid visual cycle.
Two point mutations of RPE65 from patients with retinal dystrophies decrease the stability of RPE65 protein and abolish its isomerohydrolase activity.
Impacts of two point mutations of RPE65 from Leber's congenital amaurosis on the stability, subcellular localization and isomerohydrolase activity of RPE65.
An enzymatic mechanism for generating the precursor of endogenous 13-cis retinoic acid in the brain.
Identification of the key residues determining the product specificity of isomerohydrolase.
Inhibition of the visual cycle by A2E through direct interaction with RPE65 and implications in Stargardt disease.
The interplay of environmental luminance and genetics in the retinal dystrophy induced by the dominant RPE65 mutation.