Two Point Mutations of RPE65 from Patients with Retinal Dystrophies Decrease the Stability of RPE65 Protein and Abolish Its Isomerohydrolase Activity

This publication has 32 references indexed in Scilit:

• Binding of RPE65 Fragments to Lipid Monolayers and Identification of Its Partners by Glutathione S-Transferase Pull-Down Assays
  Biochemistry, 2006
• Rpe65 Is the Retinoid Isomerase in Bovine Retinal Pigment Epithelium
  Cell, 2005
• Retinyl Esters Are the Substrate for Isomerohydrolase
  Biochemistry, 2003
• Genetic and genomic tools for Xenopus research: The NIH Xenopus initiative
  Developmental Dynamics, 2002
• Expression pattern and localization of β,β-carotene 15,15′-dioxygenase in different tissues
  Biochemical Journal, 2001
• Identification, Expression, and Substrate Specificity of a Mammalian β-Carotene 15,15′-Dioxygenase
  Journal of Biological Chemistry, 2001
• Vertebrate Photoreceptors
  Progress in Retinal and Eye Research, 2001
• Mutational analysis and clinical correlation in Leber congenital amaurosis
  Ophthalmic Genetics, 2000
• Mutational analysis and clinical correlation in Leber congenital amaurosis
  Ophthalmic Genetics, 2000
• Molecular characterization of the human gene encoding an abundant 61 kDa protein specific to the retinal pigment epithelium
  Human Molecular Genetics, 1995