A Palmitoylation Switch Mechanism in the Regulation of the Visual Cycle
- 11 June 2004
- Vol. 117 (6) , 761-771
- https://doi.org/10.1016/j.cell.2004.05.016
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- RPE65 Operates in the Vertebrate Visual Cycle by Stereospecifically Binding All-trans-Retinyl Esters,Biochemistry, 2004
- Rpe65 Is a Retinyl Ester Binding Protein That Presents Insoluble Substrate to the Isomerase in Retinal Pigment Epithelial CellsPublished by Elsevier ,2004
- Lecithin Retinol Acyltransferase Is a Founder Member of a Novel Family of EnzymesBiochemistry, 2003
- A Cleavable Affinity Biotinylating Agent Reveals a Retinoid Binding Role for RPE65Biochemistry, 2003
- All-trans-retinyl Esters Are the Substrates for Isomerization in the Vertebrate Visual CycleBiochemistry, 2003
- Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptorsBiochemistry and Cell Biology, 1996
- Affinity labeling of lecithin retinol acyltransferaseBiochemistry, 1993
- Substrate specificities and mechanism in the enzymic processing of vitamin A into 11-cis-retinolBiochemistry, 1990
- Inhibitors of retinyl ester formation also prevent the biosynthesis of 11-cis-retinolBiochemistry, 1990
- The Biochemistry of VisionAnnual Review of Biochemistry, 1953