Researcher Database

（Last updated : 2025-07-03 12:41:06）　

KITAHARA Ryo

Department / Course College of Pharmaceutical Sciences Department of Pharmaceutical Sciences

Title / Position Professor

Click to view the Scopus page. The data was downloaded from Scopus API on Jul 07, 2025. via http://api.elsevier.com and http://www.scopus.com .

Other Affiliations
1.	Graduate School of Life Sciences
2.	Research Organization of Science and Technology Research Center for Drug Discovery and Development Scieces
3.	Graduate School of Pharmacy

Academic background
1.	2002/03 Degree Acquisition	│ Kobe University Ph.D. (Science)
2.	～2002/03	Doctoral Program (2nd Semester) │ Department of Molecular Science │ Graduate School of Science and Technology │ Kobe University │ Completed
3.	～1997/03	Department of Chemistry │ Faculty of Science and Engineering │ Ritsumeikan University │ Graduated
4.	～1999/03	Doctoral Program (1st Semester) │ Graduate School, Division of Science and Engineering │ Ritsumeikan University │ Completed

Business career
1.	2011/04/01 ～ 2017/03/31	│ Colleges of PharmaceuticalScience │ Ritsumeikan University,
2.	2008/04/01 ～ 2011/03/31	│ Colleges of PharmaceuticalScience │ Ritsumeikan University,

Research activities
1.		American Chemical Society
2.		Biophysical Society
3.		The NMR Society of Japan
4.		The Japan SOciety of High Pressure Science and Technology
5.		The Biophysical Society of Japan
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Subject of research
1.	A new design strategy of functional biomolecules based on high-energy conformers of proteins

Research summary
High pressure structural biology Conventional X-ray and NMR approaches, widely applied to protein structural determination, do not serve to elucidate structures of high-energy conformers in proteins. Therefore, the conventional design strategy widely used in the field of the rational drug design is based only on the basic "native" structure of proteins. The study of structure and dynamics of high-energy conformers would provide new information for a wide range of problems in protein science, such as protein folding and function, conformational disease and design of biomolecules. The high pressure NMR approach using a pressure-resisting cell on a commercial high frequency NMR spectrometer has made it possible to investigate higher energy conformers of proteins basically at atomic resolution under high pressure. The strategy is simple. Pressure shifts the water-protein system to a smaller volume, and shifts the protein conformation within the range of its fluctuation since the volume is strongly coupled to the conformation.

Present specialized field
Biophysics, Structural Biochemistry, Basic chemistry (Keyword：protein, pressure, structure, semi-stable conformer, conformational fluctuation)

Books
1.	2016/03	Molecular Science of Fluctuations toward Biological Functions/M. Terazima, M. Kataoka, R. Ueoka, Y. Okamoto eds. │ ,pp.87-103
2.	2015/08	High Pressure Bioscience, Akasaka K. and Matsuki H. Eds │ ,pp.199-214

Papers
1.	2025/06/16	ATP as a key modulator of fused-in-sarcoma phase separation and aggregation: Insights into amyotrophic lateral sclerosis pathogenesis │ Journal of molecular biology │ 437 (169295)
2.	2024/10/24	Raman Spectroscopic Algorithms for Assessing Virulence in Oral Candidiasis: The Fight-or-Flight Response │ International Journal o f Molecular Sciences │ 25 (21),pp.11410
3.	2024/07/30	Galantamine suppresses α-synuclein aggregation by inducing autophagy via the activation of α7 nicotinic acetylcholine receptors │ Journal of Pharmacological Sciences │ 156,pp.102-114
4.	2024/07/19	Modulation of Biomolecular Liquid–Liquid Phase Separation by Preferential Hydration and Interaction of Small Osmolytes with Proteins │ The Journal of Physical Chemistry Letters │ 15,pp.7620-7627
5.	2024/04/17	An aberrant FUS liquid droplet of amyotrophic lateral sclerosis pathological variant, R495X, accelerates liquid–solid phase transition │ Scientific Reports │ 14,pp.8914
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Academic conference presentation
1.	2025/05/17	ATP as a Dual-Mode Suppressor of FUS Phase Separation and Aggregation in ALS
2.	2025/02/16	An aberrant fused in sarcoma liquid droplet of amyotrophic lateral sclerosis pathological variant, R495X, accelerates liquid-solid phase transition.
3.	2024/10/03	Effects of pressure, temperature, salts, and osmolytes on biomolecular liquid-liquid phase separation
4.	2024/09/25	Pressure, temperature, and osmolyte effects on protein liquid-liquid phase separation
5.	2024/06/28	Pressure and temperature effects on FUS liquid droplet of amyotrophic lateral sclerosis pathlogical variant, R495X
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Other research achievements
1.	2006/02	seminar: A new paradigm of protein structures (University of Utah)
2.	2004/07	seminar:Exploring the entire conformational space of proteins by high pressure NMR (High Pressure Research Center, Poland)