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Quantitative biophysical life science(Chemistry)

Yoshida TakuyaAssociate professor

1995. M.Sc. Department of Chemistry, Graduate School of Science, Osaka University
1997. Assistant Professor, Faculty of Pharmaceutical Sciences, Osaka University
2004. Ph.D (Pharmaceutical Sciences, Osaka University)
I am engaged in drug discovery research through structural analysis and molecular interaction analysis of human disease-related protein complexes.

Research theme

Structural biology of proteins involved in human diseases

We are investigating the three-dimensional structures and molecular interactions of proteins involved in lifestyle-related diseases such as diabetes and dyslipidemia, as well as cancer, through structural and physico-chemical approaches, with the aim of making discoveries that will lead to the elucidation of their function. In addition, we design drug seed molecules based on structural analysis of protein complexes and docking studies.

Structural dynamics of proteins by NMR spectroscopy and molecular dynamics simulation

Dynamics in the conformation of proteins are important for their functions and molecular interactions such as recognition of drug compounds. We are elucidating the dynamic structures of protein molecules experimentally, mainly by using NMR spectroscopy, and clarify the relationship between dynamics and function through molecular dynamics simulations.

Representative achievements

Structural Basis for PPARα Activation by 1H-pyrazolo-[3,4-b]pyridine Derivatives., Yoshida T, Oki H, Doi M, Fukuda S, Yuzuriha T, Tabata R, Ishimoto K, Kawahara K, Ohkubo T, Miyachi H, Doi T, Tachibana K. Sci Rep. 2020;10(1):7623

Spatiotemporal regulation of PEDF signaling by type I collagen remodeling., Kawahara K, Yoshida T, Maruno T, Oki H, Ohkubo T, Koide T, Kobayashi Y. Proc Natl Acad Sci U S A. 2020;117(21):11450-11458

Ordered self-assembly of the collagenous domain of adiponectin with noncovalent interactions via glycosylated lysine residues., Takuwa A, Yoshida T, Maruno T, Kawahara K, Mochizuki M, Nishiuchi Y, Kobayashi Y, Ohkubo T. FEBS Lett. 2016;590(2):195-201

Structural basis for PPARγ transactivation by endocrine-disrupting organotin compounds., Harada S, Hiromori Y, Nakamura S, Kawahara K, Fukakusa S, Maruno T, Noda M, Uchiyama S, Fukui K, Nishikawa J, Nagase H, Kobayashi Y, Yoshida T, Ohkubo T, Nakanishi T. Sci Rep. 2015;5:8520

Thermodynamic and NMR analyses of NADPH binding to lipocalin-type prostaglandin D synthase., Qin S, Shimamoto S, Maruno T, Kobayashi Y, Kawahara K, Yoshida T, Ohkubo T. Biochem Biophys Res Commun. 2015;468(1-2):234-9

Solution structure of the variable-type domain of the receptor for advanced glycation end products: new insight into AGE-RAGE interaction., Matsumoto S, Yoshida T, Murata H, Harada S, Fujita N, Nakamura S, Yamamoto Y, Watanabe T, Yonekura H, Yamamoto H, Ohkubo T, Kobayashi Y. Biochemistry. 2008 ;47(47):12299-311

X-ray crystallography study on ribosome recycling: the mechanism of binding and action of RRF on the 50S ribosomal subunit., Wilson DN, Schluenzen F, Harms JM, Yoshida T, Ohkubo T, Albrecht R, Buerger J, Kobayashi Y, Fucini P. EMBO J. 2005;24(2):251-60.

NMR structure of transcription factor Sp1 DNA binding domain., Oka S, Shiraishi Y, Yoshida T, Ohkubo T, Sugiura Y, Kobayashi Y. Biochemistry. 2004;43(51):16027-35

Structure and binding mode of a ribosome recycling factor (RRF) from mesophilic bacterium., Nakano H, Yoshida T, Uchiyama S, Kawachi M, Matsuo H, Kato T, Ohshima A, Yamaichi Y, Honda T, Kato H, Yamagata Y, Ohkubo T, Kobayashi Y. J Biol Chem. 2003;278(5):3427-36

Solution structure of the ribosome recycling factor from Aquifex aeolicus., Yoshida T, Uchiyama S, Nakano H, Kashimori H, Kijima H, Ohshima T, Saihara Y, Ishino T, Shimahara H, Yoshida T, Yokose K, Ohkubo T, Kaji A, Kobayashi Y. Biochemistry. 2001;40(8):2387-96