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Department of Chemistry, Graduate School of Science, Kyoto University

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

This page was last modified on 20 September 2016.

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