Takumi Takata (Assistant Professor)

Field of Expertise:

Biochemistry, Protein Folding, Life Science

Research Interests:

1. Mechanisms of spontaneous racemization and isomerization of amino acids in proteins during aging.
2. The post-translational modifications such as deamidation, racemization, stereoinversion, isomerization, truncation, oxidation in proteins and age-related diseases.
3. 3. The mechanisms of proteins folding and protein misfolding with aging.

Selected Papers:

1. 1. Inoue,　R., Takata, T., Fujii, N., Ishii, K., Uchiyama, S., Sato, N., Oba, Y., Wood, K., Kato, K., Fujii, N. and Sugiyama, M. New insight into the dynamical system of αB-crystallin oligomers. Scientific Reports 6, 29208 (2016).
2. Serebryany, E., Takata, T., Erickson, E., Schafheimer, N., Wang, Y., and King, J. A. Aggregation of Trp>Glu Point Mutants of Human Gamma-D Crystallin Provides a Model for Hereditary or UV-Induced Cataract. Protein Sci. 25, 1115-1128 (2016).
3. Takata, T., and Fujii, N. Isomerization of Asp residues plays an important role in αA-crystallin dissociation. FEBS J. 283, 850-859 (2016)
4. Takata, T., and Fujii, N. Effect of Asp 96 isomerization on the properties of a lens αB-crystallin-derived short peptide. J. Pharm. Biomed Anal. 116, 139-144 (2015).
5. Maeda, H., Takata,T., Fujii, N., Sakaue, H., Nirasawa, S., Takahashi, S., Sasaki, H., and Fujii, N. Rapid Survey of Four Asp Isomers in Disease-Related Proteins by LC-MS combined with Commercial Enzymes. Anal Chem, 87, 561-568 (2015).
6. Sakaue, H., Takata, T., Fujii, N., Sasaki, H., and Fujii, N. Alpha B- and βA3-crystallins containing d-Aspartic acids exist in a monomeric state. Biochim Biophys Acta, 1854, 1-9 (2015).
7. Takata, T., Haase-Pettingell, C., and King, J. The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly. Bacteriophage, 2, 36-49 (2012).
8. Takata, T., Smith, J. P., Arbogast, B., David, L. L., and Lampi, K. J. Solvent accessibility of betaB2-crystallin and local structural changes due to deamidation at the dimer interface. Exp. Eye Res, 91, 336-346 (2010).
9. Takata, T., Woodbury, L. G., and Lampi, K. J. Deamidation alters interactions of beta-crystallins in hetero-oligomers. Molecular Vision, 15, 241-249 (2009).
10. Takata, T., Oxford, J. T., Demeler, B., and Lampi, K. J. Deamidation destabilizes and triggers aggregation of a lens protein, betaA3-crystallin. Protein Science, 17, 1565-1575 (2008).
11. Takata, T., Oxford, J. T., Brandon, T. R., and Lampi, K. J. Deamidation alters the structure and decreases the stability of human lens betaA3-crystallin. Biochemistry, 46, 8861-8871 (2007).

Education:

2006 Ph.D. of Science, Kyoto University, Kyoto.
2003 M.S. of Science, Kyoto University, Kyoto.
2001 B.S. of Engineering, Ritsumeikan University, Shiga.

Professional experience:

2016- Assistant Professor, Department of Chemistry, Kyoto University
2015-2016 Assistant Professor, Department of Biochemistry, Tokyo University of Pharmacy and Life Sciences
2013-2015 Postdoctoral Associate, Department of Radiation Life Science and Radiation Medical Science. Research Reactor Institute, Kyoto University,
2009-2013 Postdoctoral Associate, Department of Biology, Massachusetts Institute of Technology
2006-2009 Postdoctoral Associate, Department of Integrative Biosciences, Oregon Health & Science University

Awards:

2014 The Outstanding Presentation Award in Japanese Society for Crystallin Lens Research.
2015 The D-amino Acid Conference Encouragement Prize.
2015 Travel Award of International Conference on the Lens 2015
2015 The Outstanding Poster Presentation Award in the ¹¹⁵th Annual Meeting of the Japanese Dermatological Association.

Contact Information:

Office: Kyoto University Research Reactor Institute 2, Asashiro-Nishi, Kumatori-cho, Sennan-gun, Osaka 590-0494
Phone: 81(Japan)-72-451-2378
E-mail: takumi 　＋　@rri.kyoto-u.ac.jp

Link:

Radiation Biochemistry and Biological Function Laboratory (internal link)
FUJII Noriko lab.

This page was last modified on 05 April 2018.