Yusuke Takahashi, PhD Instructor of Research
Mailing Address: 941 Stanton L. Young Blvd., BSEB 302C Oklahoma City, OK 73104-5020	Telephone: (405) 271-5896 ext 48493 Fax: (405) 271-3973
Email: yusuke-takahashi@ouhsc.edu

Research Interests

1. The retinoid cycle in vertebrate vision. Particularly RPE65, a key enzyme (isomerohydrolase) in the visual cycle.
2. Molecular basis of spectral tuning in visual pigments and adaptive evolution of color vision.

Education

Nikolaeva O, Takahashi Y, Moiseyev G, and Ma J-x. Negative charge of the glutamic acid 417 residue is crucial for isomerohydrolase activity of RPE65., Biochem Biophys Res Commun, 2010, 391, 1757-1761.

Nikolaeva O, Takahashi Y, Moiseyev G, and Ma J-x. Purified RPE65 shows isomerohydrolase activity after reassociation with a phospholipid membrane., FEBS J, 2009, 276, 3020-3030.

Farjo K, Moiseyev G, Takahashi Y, Crouch RK, and Ma J-x. RDH10 has 11-cis-Retinol Dehydrogenase Activity and Interacts with Visual Cycle Proteins., Invest Ophtalmol Vis Sci, 2009, 50, 5089-5097.

Takahashi Y, Moiseyev G, Farjo K, and Ma J-x. Characterization of key residues and membrane association domains in RDH10., Biochem J, 2009, 419, 113-122.

Takahashi Y, Moiseyev G, Ablonczy Z, Chen Y, Crouch RK, and Ma J-x. Identification of a Novel Palmitylation Site Essential for Membrane Association and Isomerohydrolase Activity of RPE65., J Biol Chem, 2009, 284, 3211-3218

Moiseyev G, Takahashi Y, Chen Y, Kim S, and Ma, J-x. RPE65 from Cone-dominant Chicken Is a More Efficient Isomerohydrolase Compared with That from Rod-dominant Species. J Biol Chem 283: 8110-7, 2008.

Takahashi Y, Moiseyev G, Chen Y, and Ma J-x. The roles of three palmitoylation sites of RPE65 in its membrane association and isomerohydrolase activity. Invest Ophtalmol Vis Sci, 47:5191-5196, 2006.

Chen Y, Moiseyev G, Takahashi Y, and Ma J-x. Impacts of two point mutations of RPE65 from Leber's congenital amaurosis on the stability, subcellular localization and isomerohydrolase activity of RPE65. FEBS Lett., 580:4200-4204, 2006.

Takahashi Y, Chen Y, Moiseyev G, and Ma J-x. Two point mutations of RPE65 from patients with retinal dystrophies decrease the stability of RPE65 protein and abolish its isomerohydrolase activity. J Biol Chem, 281:21820-21826, 2006.

Chen Y, Moiseyev G, Takahashi Y, and Ma J-x. RPE65 Gene Delivery Restores Isomerohydrolase Activity and Prevents Early Cone Loss in Rpe65-/- Mice. Invest Ophtalmol Vis Sci, 47:1177-1184, 2006.

Moiseyev G, Takahashi Y, Chen Y, Gentleman S, Redmond TM, Crouch RK, and Ma J-x. RPE65 is an Iron(II)-dependent isomerohydrolase in the retinoid visual cycle. J Biol Chem, 281:2835-2840, 2006.

Takahashi Y, Moiseyev G, Chen Y, and Ma J-x. Identification of conserved histidines and glutamic acid as key residues for isomerohydrolase activity of RPE65, an enzyme of the visual cycle in the retinal pigment epithelium. FEBS Lett., 579:5414-5418, 2005.

Moiseyev G, Chen Y, Takahashi Y, Wu B, and Ma J-x. RPE65 is the isomerohydrolase in the visual cycle. Proceedings of the National Academy of Science U.S.A., 102:12413-12418, 2005.

Takahashi Y, and Yokoyama S. Genetic basis of spectral tuning in the violet-sensitive visual pigment of African clawed frog. Xenopus laevis., Genetics, 171:1153-1160, 2005.

Yokoyama S, Starmer WT, Takahashi Y, and Tada T. Tertiary structure and spectral tuning of UV and violet pigments in vertebrates. Gene, 365:95-103, 2005.