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Dr. Hideaki YOSHIMURA

Research and Professional Experience

1997–2001
 
Department of Industrial Chemistry, Faculty of Engineering, Kyoto University
2001–2003
 
Department of Molecular Engineering, Graduate School of Engineering, Kyoto University
2003–2007
 
 
Department of Structural Molecular Science, School of Physical Sciences, The Graduate University for Advanced Studies
2007–2009
 
Postdoctoral Researcher, JST-ICORP, Institute of Frontier Medical Sciences, Kyoto University
2009–2015
 
 
Project Assistant Professor, Department of Chemistry, School of Science, The University of Tokyo
2015–
 
 
Assistant Professor, Department of Chemistry, School of Science, The University of Tokyo

Awards

2016 Presentation Award (International Symposium on Pure and Applied Chemistry, Kuching, Malaysia)
2015 RSC Best Presentation Award (Royal Society of Chemistry Tokyo International Conference 2015)
2012 CSJ Presentation Award
2006 CSJ Student Presentation Award

 

Research Interests
   Biomolecular Science, Bioimaging


Research Subjects

  • Solve the signal transduction mechanism in live cell with bioimaging technique
  • Understand RNA functions based on its single-molecule dynamics

    Publications

    • Probing the role of the heme distal and proximal environment in ligand dynamics in the signal transducer protein HemAT by time-resolved step-scan FTIR and resonance Raman spectroscopy.
      A. Pavlou, A. Loullis, H. Yoshimura, S. Aono, E. Pinakoulaki,
      Biochemistry, in press

    • Real-time fluorescence imaging of single-molecule endogenous non-coding
      RNA in living cells.
      H. Yoshimura and T. Ozawa,
      Methods Mol. Biol., in press.

    • Monitoring of RNA dynamics in living cells using PUM-HD and fluorescent protein reconstitution technique.
      H. Yoshimura and T. Ozawa,
      Methods Enzymol., 572, 65-85 (2016).

    • Genetically Encoded Fluorescent Probe for Imaging Apoptosis in Vivo with Spontaneous GFP Complementation.
      Y. Nasu, Y. Asaoka, M. Namae, H. Nishina, H. Yoshimuar, T. Ozawa,
      Anal. Chem.
      , 88, 838-844 (2016).

    • Development of red-shifted mutants derived from luciferase of Brazilian click beetle Pyrearinus termitilluminans
      T. Nishiguchi, T. Yamada, Y. Nasu, M. Ito, H. Yoshimura, T. Ozawa
      J. Biomed. Opt., 20, 101205 (2015)

    • Simultaneous time-lamination imaging of protein association using a split fluorescent timer protein.
      A. Takamura, M Hattori, H. Yoshimura, T Ozawa
      Anal. Chem., 87, 3366-3372 (2015).

    • Method of split-reporter reconstitution for the analysis of biomolecules
      H. Yoshimura, T. Ozawa
      Chem. Record
      , 14, 492-501 (2014)

    • Bioluminescent Probes to Analyze Ligand-induced Phosphatidylinositol
      3,4,5-trisphosphate Production with Split Luciferase Complementation
      L.Z. Yang, Y. Nasu, M. Hattori, H. Yoshimura, A. Kanno, T. Ozawa,
      Anal. Chem., 85, 11352-11359 (2013).

    • Advances in fluorescence and bioluminescence imaging
      T. Ozawa, H. Yoshimura and S.B. Kim,
      Anal. Chem.,85, 590-609 (2013).

    • Fluorescent probes for imaging endogenous β-actin mRNA in living cells using fluorescent protein-tagged pumilio.
      H. Yoshimura, A. Inaguma, T. Yamada and T. Ozawa
      ACS Chem. Biol.7, 999-1005 (2012). 

    • Visualization of non-engineered single mRNAs in living cells using genetically encoded fluorescent probes.
      T. Yamada, H. Yoshimura, A. Inaguma and T. Ozawa,
      Anal. Chem., 83, 5708-5714 (2011).

    • Hydrogen bonding interaction on the heme-bound ligand in the heme-based O2 sensor protein,
      M. Nishimura, H. Yoshimura, K. Ozawa, S. Yoshioka, M. Kubo, T. Kitagawa and S. Aono,
      JPorphyrins Phthalocyanines12, 142-148 (2008).

    • Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy,
      S. F. EI-Mashtoly, Y. Gu, H. Yoshimura, S. Yoshioka, S. Aono, T. Kitagawa,
      JBiolChem., 283, 6942-6946 (2008).

    • The signal transduction mechanism of HemAT-Bs through the proximal heme pocket revealed by time-resolved resonance Raman spectroscopy,
      H. Yoshimura, S. Yoshioka, Y. Mizutani and S. Aono,
      BiochemBiophysResCommun., 307, 1053-1057 (2007).

    • Two ligand binding sites in the O2-sensing signal transducer HemAT: implications for ligand recognition/discrimination and signaling,
      E. Pinakoulaki, H. Yoshimura, V. Daskalakis, S. Yoshioka, S. Aono and C. Varotsis,
      ProcNatlAcadSciUSA103, 14796-14801 (2006).

    • Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis,
      H. Yoshimura, S. Yoshioka, K. Kobayashi, T. Ohta, T. Uchida, M. Kubo, T. Kitagawa and S. Aono,
      Biochemistry45, 8301-8307 (2006).

    • Recognition and discrimination of gases by the oxygen-sensing signal transducer protein HemAT as revealed by FTIR spectroscopy,
      E. Pinakoulaki, H. Yoshimura, S. Yoshioka, S. Aono and C. Varotsis,
      Biochemistry45, 7763-7766 (2006).

    • Non-covalent modification of the heme-pocket of apomyoglobin by a 1,10-phenanthroline derivative,
      Y. Hitomi, H. Mukai, H. Yoshimura, T. Tanaka and T. Funabiki,
      BioorgMedChemLett., 16, 248-251 (2006).

    • Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA,
      S. Yoshioka, K. Kobayashi, H. Yoshimura, T. Uchida, T. Kitagawa and S. Aono,
      Biochemistry, 44, 15406.-15413 (2005).

    • Oxygen-sensing mechanism of HemAT from Bacillus subtilis: a resonance Raman spectroscopic study,
      T. Ohta, H. Yoshimura, S. Yoshioka, S. Aono and Teizo Kitagawa,
      JAmChemSoc., 126, 15000-15001 (2004).