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Physiological and microfluorometric studies of reduction and clearance of retinal in bleached rod photoreceptors.
Reduction of all-trans retinal to all-trans retinol in the outer segments of frog and mouse rod photoreceptors.
Visual cycle: Dependence of retinol production and removal on photoproduct decay and cell morphology.
Interphotoreceptor retinoid-binding protein is the physiologically relevant carrier that removes retinol from rod photoreceptor outer segments.
Rod outer segment retinol formation is independent of Abca4, arrestin, rhodopsin kinase, and rhodopsin palmitylation.
Reduction of all-trans-retinal in vertebrate rod photoreceptors requires the combined action of RDH8 and RDH12.
Formation of all-trans retinol after visual pigment bleaching in mouse photoreceptors.
Measurement of the mobility of all-trans-retinol with two-photon fluorescence recovery after photobleaching.
Microfluorometric measurement of the formation of all-trans-retinol in the outer segments of single isolated vertebrate photoreceptors.
2-Hydroxypropyl-beta-cyclodextrin removes all-trans retinol from frog rod photoreceptors in a concentration-dependent manner.
Rapid formation of all-trans retinol after bleaching in frog and mouse rod photoreceptor outer segments.
Kinetics of rhodopsin's chromophore monitored in a single photoreceptor.
Interphotoreceptor retinoid-binding protein removes all-trans-retinol and retinal from rod outer segments, preventing lipofuscin precursor formation.
Photooxidation mediated by 11-cis and all-trans retinal in single isolated mouse rod photoreceptors.