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Chemical Compound Review

AG-E-65304     3,7-dimethyl-9-(2,6,6- trimethyl-1...

Synonyms: AG-E-65305, AG-G-36171, KBioGR_001555, KBioSS_001753, CHEBI:50211, ...
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Disease relevance of Vitamin A


High impact information on Vitamin A


Biological context of Vitamin A


Anatomical context of Vitamin A


Associations of Vitamin A with other chemical compounds


Gene context of Vitamin A


Analytical, diagnostic and therapeutic context of Vitamin A


  1. Characterization of a dehydrogenase activity responsible for oxidation of 11-cis-retinol in the retinal pigment epithelium of mice with a disrupted RDH5 gene. A model for the human hereditary disease fundus albipunctatus. Jang, G.F., Van Hooser, J.P., Kuksa, V., McBee, J.K., He, Y.G., Janssen, J.J., Driessen, C.A., Palczewski, K. J. Biol. Chem. (2001) [Pubmed]
  2. Mutation of the gene encoding cellular retinaldehyde-binding protein in autosomal recessive retinitis pigmentosa. Maw, M.A., Kennedy, B., Knight, A., Bridges, R., Roth, K.E., Mani, E.J., Mukkadan, J.K., Nancarrow, D., Crabb, J.W., Denton, M.J. Nat. Genet. (1997) [Pubmed]
  3. Membranes as the energy source in the endergonic transformation of vitamin A to 11-cis-retinol. Deigner, P.S., Law, W.C., Cañada, F.J., Rando, R.R. Science (1989) [Pubmed]
  4. Visual cycle impairment in cellular retinaldehyde binding protein (CRALBP) knockout mice results in delayed dark adaptation. Saari, J.C., Nawrot, M., Kennedy, B.N., Garwin, G.G., Hurley, J.B., Huang, J., Possin, D.E., Crabb, J.W. Neuron (2001) [Pubmed]
  5. Mutation of key residues of RPE65 abolishes its enzymatic role as isomerohydrolase in the visual cycle. Redmond, T.M., Poliakov, E., Yu, S., Tsai, J.Y., Lu, Z., Gentleman, S. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro. Bernstein, P.S., Law, W.C., Rando, R.R. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  7. Delayed dark adaptation in 11-cis-retinol dehydrogenase-deficient mice: a role of RDH11 in visual processes in vivo. Kim, T.S., Maeda, A., Maeda, T., Heinlein, C., Kedishvili, N., Palczewski, K., Nelson, P.S. J. Biol. Chem. (2005) [Pubmed]
  8. Properties of an interphotoreceptor retinoid-binding protein from bovine retina. Saari, J.C., Teller, D.C., Crabb, J.W., Bredberg, L. J. Biol. Chem. (1985) [Pubmed]
  9. 11-cis-Acyl-CoA:Retinol O-Acyltransferase Activity in the Primary Culture of Chicken Muller Cells. Muniz, A., Villazana-Espinoza, E.T., Thackeray, B., Tsin, A.T. Biochemistry (2006) [Pubmed]
  10. Membrane phospholipids as an energy source in the operation of the visual cycle. Rando, R.R. Biochemistry (1991) [Pubmed]
  11. Substrate specificities and mechanism in the enzymatic processing of vitamin A into 11-cis-retinol. Cañada, F.J., Law, W.C., Rando, R.R., Yamamoto, T., Derguini, F., Nakanishi, K. Biochemistry (1990) [Pubmed]
  12. Dual-substrate specificity short chain retinol dehydrogenases from the vertebrate retina. Haeseleer, F., Jang, G.F., Imanishi, Y., Driessen, C.A., Matsumura, M., Nelson, P.S., Palczewski, K. J. Biol. Chem. (2002) [Pubmed]
  13. Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. Stecher, H., Gelb, M.H., Saari, J.C., Palczewski, K. J. Biol. Chem. (1999) [Pubmed]
  14. Rpe65 is a retinyl ester binding protein that presents insoluble substrate to the isomerase in retinal pigment epithelial cells. Mata, N.L., Moghrabi, W.N., Lee, J.S., Bui, T.V., Radu, R.A., Horwitz, J., Travis, G.H. J. Biol. Chem. (2004) [Pubmed]
  15. Retinoids and butyrate modulate fibroblast growth and contraction of collagen matrices. Kim, R.Y., Stern, W.H. Invest. Ophthalmol. Vis. Sci. (1990) [Pubmed]
  16. Retinoid- and carotenoid-enriched diets influence the ontogenesis of the immune system in mice. Garcia, A.L., Rühl, R., Herz, U., Koebnick, C., Schweigert, F.J., Worm, M. Immunology (2003) [Pubmed]
  17. Purification of cellular retinaldehyde-binding protein from bovine retina and retinal pigment epithelium. Saari, J.C., Bredberg, D.L. Exp. Eye Res. (1988) [Pubmed]
  18. Mapping the ligand binding pocket in the cellular retinaldehyde binding protein. Wu, Z., Yang, Y., Shaw, N., Bhattacharya, S., Yan, L., West, K., Roth, K., Noy, N., Qin, J., Crabb, J.W. J. Biol. Chem. (2003) [Pubmed]
  19. Lack of effect of RPE65 removal on the enzymatic processing of all-trans-retinol into 11-cis-retinol in vitro. Choo, D.W., Cheung, E., Rando, R.R. FEBS Lett. (1998) [Pubmed]
  20. Topological and epitope mapping of the cellular retinaldehyde-binding protein from retina. Crabb, J.W., Gaur, V.P., Garwin, G.G., Marx, S.V., Chapline, C., Johnson, C.M., Saari, J.C. J. Biol. Chem. (1991) [Pubmed]
  21. Support for a proposed retinoid-processing protein complex in apical retinal pigment epithelium. Bonilha, V.L., Bhattacharya, S.K., West, K.A., Crabb, J.S., Sun, J., Rayborn, M.E., Nawrot, M., Saari, J.C., Crabb, J.W. Exp. Eye Res. (2004) [Pubmed]
  22. Identification of the endogenous retinoids associated with three cellular retinoid-binding proteins from bovine retina and retinal pigment epithelium. Saari, J.C., Bredberg, L., Garwin, G.G. J. Biol. Chem. (1982) [Pubmed]
  23. Size and shape of bovine interphotoreceptor retinoid-binding protein by electron microscopy and hydrodynamic analysis. Adler, A.J., Stafford, W.F., Slayter, H.S. J. Biol. Chem. (1987) [Pubmed]
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