RPE lipofuscin and its role in retinal pathobiology

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A2E, a byproduct of the visual cycle

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Age-related Macular Degeneration

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The 220-kDa Rim Protein of Retinal Rod Outer Segments Is a Member of the ABC Transporter Superfamily

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Photodamage to human RPE cells by A2-E, a retinoid component of lipofuscin.

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TheRpe65Leu450Met Variation Increases Retinal Resistance Against Light-Induced Degeneration by Slowing Rhodopsin Regeneration

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Retinal Pigment Epithelial Abnormalities in Fundus Flavimmaculatus

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Involvement of oxidative mechanisms in blue-light-induced damage to A2E-laden RPE.

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The lipofuscin component A2E selectively inhibits phagolysosomal degradation of photoreceptor phospholipid by the retinal pigment epithelium

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Inhibition of lysosomal degradative functions in RPE cells by a retinoid component of lipofuscin.

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A2E-epoxides Damage DNA in Retinal Pigment Epithelial Cells

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Fundus autofluorescence in age-related macular disease imaged with a laser scanning ophthalmoscope

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A comparative study of the photosensitizing characteristics of some cyanine dyes

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Blue light-induced apoptosis of A2E-containing RPE: involvement of caspase-3 and protection by Bcl-2.

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ABCR expression in foveal cone photoreceptors and its role in Stargardt macular dystrophy

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Do blue light filters confer protection against age-related macular degeneration?

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The biosynthesis of A2E, a fluorophore of aging retina, involves the formation of the precursor, A2-PE, in the photoreceptor outer segment membrane

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Stargardt's ABCR is localized to the disc membrane of retinal rod outer segments

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Histopathology of Best's Macular Dystrophy

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Blue Light-Induced Singlet Oxygen Generation by Retinal Lipofuscin in Non-Polar Media

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Formation of a Nonaoxirane from A2E, a Lipofuscin Fluorophore related to Macular Degeneration, and Evidence of Singlet Oxygen Involvement This work was supported by NIH grant GM 34509 (K.N.), NSF grant NSF-CHE-98-12676 (N.J.T. and S.J.), and NIH grant EY-12951 (J.R.S.).

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Untitled work

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Late-onset Stargardt disease is associated with missense mutations that map outside known functional regions of ABCR ( ABCA4 )

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