T. Michael Redmond
Laboratory of Retinal Cell and Molecular Biology
NEI, National Institutes of Health
Bethesda
USA
Name/email consistency: high
- RPE65, visual cycle retinol isomerase, is not inherently 11-cis-specific: support for a carbocation mechanism of retinol isomerization. Redmond, T.M., Poliakov, E., Kuo, S., Chander, P., Gentleman, S. J. Biol. Chem. (2010)
- Focus on Molecules: RPE65, the visual cycle retinol isomerase. Redmond, T.M. Exp. Eye Res. (2009)
- Effect of Leu/Met variation at residue 450 on isomerase activity and protein expression of RPE65 and its modulation by variation at other residues. Redmond, T.M., Weber, C.H., Poliakov, E., Yu, S., Gentleman, S. Mol. Vis. (2007)
- 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)
- Identification, expression, and substrate specificity of a mammalian beta-carotene 15,15'-dioxygenase. Redmond, T.M., Gentleman, S., Duncan, T., Yu, S., Wiggert, B., Gantt, E., Cunningham, F.X. J. Biol. Chem. (2001)
- Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle. Redmond, T.M., Yu, S., Lee, E., Bok, D., Hamasaki, D., Chen, N., Goletz, P., Ma, J.X., Crouch, R.K., Pfeifer, K. Nat. Genet. (1998)
