|Yusuke Takahashi, PhD
Instructor of Research
941 Stanton L. Young Blvd., BSEB 302C
Oklahoma City, OK 73104-5020
(405) 271-5896 ext 48493
- The retinoid cycle in vertebrate vision. Particularly RPE65, a key enzyme (isomerohydrolase) in the visual cycle.
- Molecular basis of spectral tuning in visual pigments and adaptive evolution of color vision.
||PhD - Information Science, Tohoku University, Miyagi, Japan
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.