2018
2017
2016
2015
2014
2013
2012
2011
2010
2009
2008
2007
2006
2005
2004
2003
2002
2001
before 2000

Refereed papers

 2018

• Circadian BMAL1–HSF1–p53 interplay regulates UV-triggered synchronization to promote stress protection.
  G. Kawamura, M. Hattori, K. Takamatsu, T. Tsukada, Y. Ninomiya, I. Benjamin, P. Sassone-Corsi, T. Ozawa and T. Tamaru,
  Commun. Biol., in press.
  
  
• A split luciferase-based probe for quantitative proximal determination of Gαq signalling in live cells.
  T. Littmann, T. Ozawa, C. Hoffmann, A. Buschauer, and G. Bernhardt,
  Sci Rep., 8, 17179 (2018). doi: 10.1038/s41598-018-35615-w.
  
  
• A Preferential Photoreaction in a Porous Crystal, Metal-Macrocycle Framework (MMF): PdII-Mediated Olefin Migration over [2+2] Cycloaddition.
  H. Yonezawa, S. Tashiro, T. Shiraogawa, M. Ehara, R. Shimada, T. Ozawa and M. Shionoya,
  J. Am. Chem. Soc., in press. doi: 10.1021/jacs.8b08534.
  
  
• A Robust Split-Luciferase-Based Cell Fusion Screening for Discovering Myogenesis-Promoting Molecules
  Q. Li, H. Yoshimura, M. Komiya, K. Tajiri, M. Uesugi, Y. Hata, T. Ozawa
  Analyst, 143, 3472-3480 (2018).
  
  
• Light-controllable Transcription System by Nucleocytoplasmic Shuttling of a Truncated Phytochrome B.
  N. Noda, T. Ozawa
  Photochem Photobiol.,94, 1071-1076 (2018). doi: 10.1111/php.12955.
  
  
• Soft and Robust Identification of Body Fluid Using Fourier Transform
  Infrared Spectroscopy and Chemometric Strategies for Forensic Analysis.
  A. Takamura, K. Watanabe, T. Akutsu and T. Ozawa.
  Sci. Rep., 8, 8459 (2018).
  
  
• Photo-activatable Akt probe - A new tool to study Akt-dependent
  physiopathology of cancer cells.
  S. Haga, T. Ozawa, N. Morita, M. Asano, S. Jin, Y. Min and M. Ozaki,
  Oncol. Res., in press.
  
  
• Establishing a split-luciferase-assay for PKG interaction studies.
  A. Schramm, P.Mueller -Thuemen, T. Littmann, M. Harloff, T. Ozawa, J.
  Schlossmann.
  Int. J. Med. Sci., 19, 1180 (2018).
  
  
• Detection of necroptosis in ligand-mediated and hypoxia-induced injury of hepatocytes using a novel optic probe detecting receptor-interacting protein (RIP)1/RIP3 binding.
  S. Haga, A. Kanno, T. Ozawa, N. Morita, M. Asano and M. Ozaki,
  Oncol. Res., 26, 503-513 (2018).
  
  
• Unique Roles of β-Arrestin in GPCR Trafficking Revealed by Photoinducible Dimerizers.
  O. Takenouchi, H. Yoshimura, T. Ozawa.
  Sci. Rep., 8, 677 (2018).
  
  
• Real-time fluorescence imaging of single-molecule endogenous non-coding
  RNA in living cells.
  H. Yoshimura and T. Ozawa,
  Methods Mol. Biol., 1649, 337-347 (2018)
  
  

 2017

• A genetic screen to discover SUMOylated proteins in living mammalian cells.
  M. Komiya, A. Ito, M. Endo, D. Hiruma, M. Hattori, H. Saitoh, M. Yoshida, and T. Ozawa,
  Sci. Rep., 7, 17443 (2017).
  
  
• In Search for NPY Y4R Antagonists: Incorporation of Carbamoylated
  Arginine, Aza-Amino Acids or D-Amino Acids into Oligopeptides Derived
  from the C-Termini of the Endogenous Agonists.
  K. Kuhn, T. Littmann, S. Dukorn, M. Tanaka, M. Keller, T. Ozawa, G. Bernhardt, and A. Buschauer,
  ACS Omega, 2, 3616-3631 (2017).
  
  
• Spectral Mining for Discriminating Blood Origins in the Presence of Substrate Interference via ATR FT-IR: Postmortem or Antemortem Blood?
  A.Takamura, K. Watanabe, T. Akutsu, H. Ikegaya and T. Ozawa,
  Anal. Chem., 89, 9797-9804 (2017).
  
  
• Dynamic Monitoring of p53 Translocation to Mitochondria for the Analysis
  of Specific Inhibitors Using Luciferase-fragment Complementation.
  N. Noda, R. Awais, R. Sutton, M. Awais and T. Ozawa,
  Biotechnol. Bioeng., 114, 2818-2827 (2017).
  
  
• Optogenetic interrogation reveals separable G-protein dependent and independent signalling linking G-protein coupled receptors to the circadian oscillator.
  H. J. Bailes, N. Milosavljevic, L.-Y. Zhuang, E. J. Gerrard, T. Nishiguchi, T. Ozawa and R. J. Lucas,
  BMC Biology, 15, 40 (2017).
  
  
• Luminescent sensors for single cell analysis.
  T. Ozawa,
  Progress Photon Sci., 115, 97-108 (2017).
  
  
• Single-shot phase-shifting incoherent digital holography.
  T. Tahara, T. Kanno, Y. Arai and T. Ozawa,
  J. Optics, 19, 065705 (2017).
  
  
• Liquid/Liquid Interfacial Synthesis of 'Click' Nanosheet.
  A. Rapakousiou, R. Sakamoto, R. Shiotsuki, R. Matsuoka, U. Nakajima, T. Pal, R. Shimada, M. A. Hossain, H. Masunaga, S. Horike, Y. Kitagawa, S. Sasaki, K. Kato, T. Ozawa, D. Astruc and H. Nishihara,
  Chem. Eur. J., 23, 8443-8449 (2017).
  
  
• Protein expression guided chemical profiling of living cells by the simultaneous observation of Raman scattering and anti-Stokes fluorescence emission.
  L.-D. Chiu, T. Ichimura, T. Sekiya, H. Machiyama, T. Watanabe, H. Fujita, T. Ozawa, and K. Fujita,
  Sci. Rep., 7, 43569 (2017).
  
  
• Split luciferase complementation assay for the analysis of G protein-coupled receptor ligand response in Saccharomyces cerevisiae.
  Y. Fukutani, J. Ishii, A. Kondo, T. Ozawa, H. Matsunami and M. Yohda,
  Biotech. Bioeng., 114, 1354-1361 (2017).
  
  
• Rapid in vivo lipid/carbohydrate quantification of single microalgal cell by Raman spectral imaging to reveal salinity-induced starch-to-lipid shift.
  L.-D. Chiu, S.-H. Ho, R. Shimada, N.-Q. Ren and T. Ozawa,
  Biotechnol. Biofuels, 10, 9 (2017)
  
  
• Strategies for development of optogenetic systems and their applications.
  M. Endo and T. Ozawa,
  J. Photochem. Photobiol. 30, 10-23 (2017).
  
  

2016

• Attenuation of Chemokine Receptor Function and Surface Expression as an Immunomodulatory Strategy Employed by HCMV is Linked to vGPCR US28.
  T. Frank, A. Reichel, O. Larsen, A.-C. Stilp, M. M. Rosenkilde, T. Stamminger, T. Ozawa and N. Tschammer,
  Cell Commun. Signal., 14, 31 (2016).
  
  
• Spatiotemporal analysis with a genetically encoded fluorescent RNA probe reveals TERRA function around telomeres.
  T. Yamada, H. Yoshimura, R. Shimada, M. Hattori, M. Eguchi, T. K. Fujiwara, A. Kusumi, T. Ozawa,
  Sci. Rep. 6, 38910 (2016).
  
  
• Strategies for development of optogenetic systems and their applications.
  M. Endo and T. Ozawa,
  J. Photochem. Photobiol. C, in press.
  
  
• Label-free versus conventional cellular assays: functional investigations on the human histamine H1 receptor.
  S. Lieb, T. Littmann, N. Plank, J. Felixberger, M. Tanaka, T. Schafer, S. Krief, S. Elz, K. Friedland, G. Bernhardt, J. Wegener, T. Ozawa and A. Buschauer,
  Pharmacol. Res., 114, 13-26 (2016).
  
  
• A Bioluminescent Indicator for Highly Sensitive Analysis of Estrogenic Activity in a Cell-based Format.
  O. Takenouchi, A. Kanno, H. Takakura, M. Hattori, T. Ozawa,
  Bioconjug. Chem., 27, 2689–2694 (2016).
  
  
• A genetically encoded bioluminescent indicator for illuminating proinflammatory cytokines.
  S.B. Kim, T. Ozawa, Y. Umezawa
  MethodsX, 7 (3), 483-489 (2016)
  
  
• Confocal bioluminescence imaging for living tissues with a caged substrate of luciferin.
  M. Hattori, G. Kawamura, R. Kojima, M. Kamiya, Y. Urano and T. Ozawa,
  Anal. Chem., 88 (12), 6231-6238 (2016).
  
  
• Live Cell Bioluminescence Imaging in Temporal Reaction of G Protein-Coupled Receptor for High-Throughput Screening and Analysis.
  M. Hattori and T. Ozawa,
  Methods Mol. Biol., 1461 , 195-202 (2016).
  
  
• In Situ Characterization of Bak Clusters Responsible for Cell Death Using Single Molecule Localization Microscopy.
  Y. Nasu, A. Benke, S. Arakawa, G. J. Yoshida, G. Kawamura, S. Manley, S. Shimizu, and T Ozawa,
  Sci. Rep.,6, 27505 (2016).
  
• Monitoring of RNA dynamics in living cells using PUM-HD and fluorescent protein reconstitution technique.
   H. Yoshimura and T. Ozawa,
  Methods in Enzymology, 572, 65-85 (2016).
  
  
• Optogenetic activation of axon guidance receptors controls direction of
  neurite outgrowth.
  M. Endo, M. Hattori, H. Toriyabe, H. Ohno, H. Kamiguchi, Y. Iino, T. Ozawa
  Sci. Rep., in press.
  
  
• 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 (1), 838-844 (2016).
  
  

  2015

• An optogenetic system for interrogating the temporal dynamics of Akt.
  Y. Katsura, H. Kubota, K. Kunida, A. Kanno, S. Kuroda, T. Ozawa,
  Sci. Rep., 5, 14589 (2015).
  

• CRY Drives Circadian CK2-mediated BMAL1 Phosphorylation to Control the
  Mammalian Clock.
  T. Tamaru, M. Hattori, K. Honda, G. T. J. Horst, Y.
  Nakahata, P. Sassone-Corsi, T. Ozawa and K. Takamatsu.,
  PLoS Biol., 13, e1002293 (2015).
  
  
• Recruitment of β-Arrestin 1 and 2 to the β2-Adrenoceptor: Analysis of 65
  Ligands.
  T. Littmann, M. Gottle, M.T. Reinartz, S. Kalble, I. W. Wainer, T. Ozawa, R. Seifert.
  J Pharmacol Exp Ther., 355, 183-190 (2015).
  
  
• Bioluminescent Tools for the Analysis of G-Protein-Coupled Receptor and
  Arrestin Interactions.
  M. Hattori and T. Ozawa,
  RSC Adv., 5, 12655-12663 (2015).
  
  
• 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).
  
  
• A new cell-based assay to evaluate myogenesis in mouse myoblast C2C12 cells.
  M. Kodaka, Z. Yang, K. Nakagawa, J. Maruyama, X. Xu, A. Sarkar, A. Ichimura, Y. Nasu, T. Ozawa, H. Iwasa, M. Ishigami-Yuasa, S. Ito, H. Kagechika, Y. Hata
  Exp. Cell. Res., 336, 171-181 (2015).
  
  
• High-throughput live cell imaging and analysis for temporal reaction of G protein-coupled receptor based on split luciferase fragment complementation.
  M. Hattori, T. Ozawa
  Anal. Sci., 31, 327-330 (2015).
  
  
• Multimodal imaging of living cells with multiplex coherent anti-Stokes Raman scattering (CARS), third-order sum frequency generation (TSFG) and Two-photon excitation fluorescence (TPEF) using a nanosecond white-light laser source
  H. Segawa, M. Okuno, P. Leproux, V. Couderc, T. Ozawa, H. Kano,
  Anal. Sci., 31, 299-305 (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).
  
  
• Cell-based assays and animal models for GPCR drug screening.
  H. Takakura, M Hattori, M. Tanaka, T Ozawa
  Methods. Mol. Biol., 1272, 257-270 (2015).
  
  
• Structure-bias relationships for fenoterol stereoisomers in six molecular and cellular assays at the β2-adrenoceptor.
  M.T. Reinartz, S. Kälble, T. Littmann, T. Ozawa, S. Dove, V. Kaever, I.W. Wainer, R. Seifrt,
  Naunyn Schmiedebergs Arch Pharmacol.,388, 51-65 (2015)
  
  
  

  2014

• Multimodal and multiplex spectral imaging of rat cornea ex vivo using a white-light laser source.
  H.Segawa, Y. Kaji, P. Leproux, V. Couderc, T. Ozawa, T. Oshika, and H. Kano,
  J. Biophotonics, 9999, 9999 (2014)
  
  
• Methods of split-reporter reconstitution for the analysis of biomolecules.
  H. Yoshimura and T. Ozawa,
  Chem. Rec., 14, 492-501 (2014).
  
  
• p62/SQSTM1 plays a protective role in oxidative injury of steatotic liver in a mouse hepatectomy model.
  S. Haga, T. Ozawa, Y. Yamada, N. Morita, I. Nagashima, H. Inoue, Y. Inaba, N. Noda, R. Abe, K. Umezawa, M. Ozaki,
  Antioxid. Redox Signal., 21, 2515-2530 (2014).
  
  
• Developing a potentially immunologically-inert tetracycline regulatable viral vector for gene therapy in the peripheral nerve.
  S. Hoyng, S. Gnavi, F. Winter, R. Eggers, T. Ozawa, A. Zaldumbide, R. Hoeben, M. Malessy, and J. Verhaagen,
  Gene Therapy, 21, 549-557 (2014).
  
  
• Electronically resonant third-order sum frequency generation
  spectroscopy using a nanosecond white-light supercontinuum.
  H. Segawa, N. Fukutake, P. Leproux, V. Couderc, T. Ozawa, and H. Kano,
  Opt. Express, 22, 10416-10429 (2014).
  
  
• Split Luciferase Complementation for Analysis of Intracellular Signaling.
  M. Hattori and T. Ozawa,
  Anal. Sci., 30, 539-543 (2014).
  
  
• Long noncoding RNA NEAT1-dependent SFPQ relocation between nuclear body paraspeckle and promoter mediates IL8 expression in response to immune stimuli.
  K. Imamura, N. Imamachi, G. Akizuki, M. Kumakura, A. Kawaguchi, K. Nagata, A. Kato, Y. Kawaguchi, H. Sato, M. Yoneda, C. Kai, T. Yada, Y. Suzuki, T. Yamada, T. Ozawa, K. Kaneki, T. Inoue, M. Kobayashi, T. Kodama, Y. Wada, K. Sekimizu, N. Akimitsu,
  Mol. Cell, 53, 393-406 (2014).
  
  
• Assay methods for SUMO-SIM interactions in vivo and in vitro using a split-luciferase complementation system.
  M. Hirohama, A.R. Voet, T. Ozawa, H. Saitoh, Y. Nakao, K.Y. Zhang, A. Ito and M. Yoshida,
  Anal. Biochem., 448, 92-94 (2014).
  
  

2013

• ROS stress resets circadian clocks to coordinate pro-survival signals.
  T. Tamaru, M. Hattori, Y. Ninomiya, G. Kawamura, G. Varès, K. Honda, D.
  P. Mishra, B. Wang, I. Benjamin, P. Sassone-Corsi, T. Ozawa and K.
  Takamatsu,
  PLoS ONE, 8, e82006 (2013).
  
  
• 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).
  
  
• Folding Coupled with Assembly in Split Green Fluorescent Proteins
  Studied by Structure-Based Molecular Simulations.
  M. Ito, T. Ozawa and S. Takada,
  J. Phys. Chem. B, 117, 13212-13218 (2013).
  
  
• Fabrication of Split-Luciferase Complementation Assays for Molecular Imaging.
  S.B. Kim and T. Ozawa,
  Curr. Mol. Imaging, 2, 148-157 (2013).
  
  
• Sustained Accurate Recording of Intracellular Acidification in Living
  Tissues with a Photo-controllable Bioluminescent Protein.
  M. Hattori, S. Haga, H. Takakura, M. Ozaki and T. Ozawa,
  Proc. Nat. Acad. Sci. USA, 110, 9332-9337 (2013).
  
  
• Spatiotemporal visualization of proHB-EGF ectodomain shedding in living cells.
  H. Inoue, T. Sakaue, T. Ozawa and S. Higashiyama,
  J. Biochem., 154, 67-76 (2013).
  
  
• Analysis of temporal patterns of GPCR–β-arrestin interactions using
  split luciferase-fragment complementation.
  M. Hattori, M. Tanaka, H. Takakura, K, Aoki, K. Miura, T. Anzai and T. Ozawa,
  Mol. Biosystems,9, 957-964 (2013).
  
  
• Longitudinal Bioluminescence Imaging of the Dynamics of Doxorubicin Induced Apoptosis.
  G. Niu, L. Zhu, D.N. Ho, F. Zhang, H. Gao, Q. Quan, N. Hida, T. Ozawa, G. Liu and X. Chen,
  Theranostics, 3, 190-200 (2013).
  
  
• Rational Design and Development of Near-infrared-emitting FireflyLuciferins Available in vivo.
  R. Kojima, H. Takakura, T. Ozawa, Y. Tada, T. Nagano and Y. Urano,
  Angew. Chem. Int. Ed., 52,1175-1179 (2013).
  
  
• Advances in fluorescence and bioluminescence imaging
  T. Ozawa, H. Yoshimura and S.B. Kim,
  Anal. Chem., 85, 590-609 (2013).

  2012

• Intelligent Design of Nano-Scale Molecular Imaging Agents.
  S.B. Kim, M. Hattori and T. Ozawa,
  Int. J. Mol. Sci., 13, 16986-17005 (2012).
  
  
• Measuring CREB activation using bioluminescent probes that detect KID-KIX interaction in living cells.
  T. Ishimoto, H. Mano, T. Ozawa and H. Mori
  Bioconjugate Chem., 23, 923-932 (2012).

• Development of 5 and 7 Substituent Luciferin Analogues as an Acidic-Tolerant Substrate of Firefly Luciferase.
  H. Takakura, R. Kojima, T. Ozawa, T. Nagano and Y. Urano
  ChemBioChem,13, 1424-1427 (2012).
  
  
• 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 and Quantitative Analysis of G Protein-Coupled Receptor β-Arrestin Interaction in Single Cells and Specific Organs of Living Mice Using Split Luciferase Complementation.
  H. Takakura, M. Hattori, M. Takeuchi and T. Ozawa
  ACS Chem. Biol.,7, 901-910 (2012).
  
  
• In vivo monitoring of liver damage using caspase-3 probe.
  M. Ozaki, S. Haga and T. Ozawa,
  Theranostics,2, 207-214 (2012).
  
  
  

   2011

• Synchronization of circadian Per2 rhythms and HSF1-BMAL1: CLOCK interaction in mouse fibroblasts after short-term heat shock pulse.
  T. Tamaru, M. Hattori, K. Honda, I. Benjamin, T. Ozawa and K. Takamatsu,
  PLoS ONE, 6, e24521 (2011).
  
  
• 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).
  
  
• Real-time monitoring of actin polymerization in living cells using split luciferase.
  T. Ishimoto, T. Ozawa and H. Mori,
  Bioconjugate Chem., 22, 1136-1144 (2011).
  
  
• Illuminating Intracellular Signaling and Molecules for Single Cell Analysis
  M. Awais and T. Ozawa
  Mol. Biosystems, 7, 1376-1387 (2011).
  
  
• Imaging of Endogenous RNA Using Genetically-encoded Probes,
  T. Ozawa and Y. Umezawa
  Current Protocols in Chemical Biology, 3, 27-37 (2011).
  
  
• Genetically-Encoded Fluorescent Probes for Imaging Endogenous mRNA in Living Cells,
  T. Ozawa and Y. Umezawa
  Methods in Molecular Biology,  714, 175-188 (2011).
  
  
• Dual-Color Bioluminescence Analysis for Quantitatively Monitoring G-Protein-Coupled Receptor and b-Arrestin Interactions.
  A.K.M. Kafi, M. Hattori, N. Misawa and T. Ozawa,
  Pharmaceuticals, 4, 457-469 (2011).
  
  
• Detection of Protein-Protein Interactions in Bacteria by GFP-fragment Reconstitution,
  A. Kanno, T. Ozawa and Y. Umezawa
  Methods in Molecular Biology, 705, 251-258 (2011).
  
  

   2010

• Ratiometric Bioluminescence Indicators for Monitoring Cyclic AMP in Live Cells Based on Luciferase-Fragment Complementation.
  Takeuchi M., Nagaoka Y., Yamada T., Takakura H. and Ozawa T.
  Anal. Chem., 82, 9306-9313 (2010).
  
  
• Luciferases for the Study of Protein-Protein Interactions in Live Cells and Animals.
  Kafi A.K.M., Hattori M., and Ozawa T.,
  Nano Life, 1, 45-62 (2010).
  
  
• p66(Shc) has a Pivotal Function in Impaired Liver Regeneration in Aged Mice by a Redox-Dependent Mechanism.
  Haga S., Morita N., Irani K., Fujiyoshi M., Ogino T., Ozawa T., and Ozaki M.,
  Lab Invest., 90, 1718-1726 (2010)
  
  
• Creating Bioluminescent Indicators to Visualize Biological Events in Living Cells and Animals.
  Kim S. B., and Ozawa T.,
  Supramol. Chem., 22, 439-448 (2010).
  
  
• Rapid and High-Sensitivity Cell Based Assays of Protein−Protein Interactions Using Split Click Beetle Luciferase Complimentation: An Approach to the Study of G-Protein Coupled Receptors
  Misawa N., Kafi A. K. M., Hattori M., Miura K., Masuda K., Ozawa T.,
  Anal. Chem. ,82, 2552-2560 (2010).
  
  

   2009

• Bioluminescenct Imaging of MAPK function with intein-mediated reporter gene assay,
  A. Kanno, T. Ozawa, and Y. Umezawa ,
  Methods Mol. Biol., 574, 185–192 (2009).
  

• Detection of Apoptosis Using Cyclic Luciferase in Living Mammals,
  A. Kanno, Y. Umezawa and T. Ozawa
  Bioluminescence, Methods in Molecular Biology , 574, 105–114 (2009).
  

• Protein Reconstitution Methods for Visualizing Biomolecular Function in Living Cells,
  T. Ozawa,
  YAKUGAKU ZASSHI, 129, 289–295 (2009).
  
  
• High-sensitivity real-time imaging of dual protein-protein interactions in living subjects using multicolor luciferases.
  Hida N, Awais M, Takeuchi M, Ueno N, Tashiro M, Takagi C, Singh T, Hayashi M, Ohmiya Y, Ozawa T,
  PLoS One, 4, e5868 (2009).

  2008

• Molecular Science for Analyzing Dynamics of Biomolecules in Living Cells,
  T. Ozawa,
  J. JSCAS., 10, 489–439 (2008).

   2007

• Cyclic Luciferase for Real-Time Sensing of Caspase-3 Activities in Living Mammals.
  A. Kanno, Y. Yamanaka, H. Hirano, Y. Umezawa and T. Ozawa,
  Angew. Chem. Int. Ed., 46, 7595–7599 (2007).
  
  
• Nongenomic Activity of Ligands in the Association of Androgen Receptor with Src.
  S.B. Kim, A. Kanno, T. Ozawa, H. Tao and Y. Umezawa,
  ACS Chem. Biol., 2, 484–492 (2007).
  
  
• Imaging Dynamics of Endogenous Mitochondrial RNA in Single Living Cells.
  T. Ozawa, Y. Natori, M. Sato and Y. Umezawa,
  Nature Methods, 4, 413–419 (2007).
  
  
• A Minimal Peptide Sequence That Targets Fluorescent and Functional Proteins into the Mitochondrial Intermembrane Space. 
  T. Ozawa, Y. Natori, Y. Sako, H. Kuroiwa, T. Kuroiwa and Y. Umezawa,
  ACS. Chem. Biol., 2, 176–186 (2007).
  
  
• A Proinflammatory Cytokine Sensor Cell for Assaying Inflammatory Activities of Nanoparticles. 
  S.B. Kim, T. Ozawa, H. Tao and Y. Umezawa,
  Anal. Biochem., 362,148–150 (2007).
  
  
• Methods for Imaging and Analyses of Intracellular Organelles Using Fluorescent and Luminescent Proteins. 
  M. Takeuchi and T. Ozawa,
  Anal. Sci., 23, 25–29 (2007).

• Genetic Nanomedicine and Tissue Engineering,
  C. Wei, M. Yamoto, W. Wei, Z. Zhao, K. Tsumoto, T. Yoshimura, T. Ozawa and Y. J. Chen,
  Med. Clin. North Am., 91, 889–898 (2007).

• Identification of Proteins Targeted into the Endoplasmic Reticulum by cDNA Library Screening,
  T. Ozawa and Y. Umezawa,
  Methods Mol. Biol., 390, 269–280 (2007).
  

• A Genetic Method to Identify Mitochondrial Proteins in Living Mammalian Cells,
  T. Ozawa and Y. Umezawa,
  Methods Mol. Biol., 390, 119–130, (2007).
  

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   2006

• A Genetically Encoded Optical Probe for Detecting Release of Proteins from Mitochondria toward Cytosol in Living Cells and Animals. 
  A. Kanno, T. Ozawa and Y. Umezawa,
  Anal. Chem., 78, 8076–8081 (2006).
  
  
• A. Method for Determining the Activities of Cytokines based on the Nuclear Transport of Nuclear Factor-κB.
  S.B. Kim, Y. Natori, T. Ozawa, H. Tao, Y. Umezawa,
  Anal. Biochem., 359, 147–149 (2006).
  
  
• Intein-Mediated Reporter Gene Assay for Detecting Protein–Protein Interactions in Living Mammalian Cells.
  A. Kanno, T. Ozawa, Y. Umezawa,
  Anal. Chem., 78, 556–560 (2006).
  
  
• Frontiers in Bioimaging,
  M. Takeuchi and T. Ozawa,
  ACS Chem. Biol., 1, 333–334 (2006).
  

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   2005

• Designing Split Reporter Proteins for Analytical Tools.
  T. Ozawa,
  Anal. Chim. Acta, 556, 58–68 (2006).
  
  
• Quantitative Determination of Protein Nuclear Transport Induced by Phosphorylation or by Proteolysis.
  S.B. Kim, R. Takao, T. Ozawa, Y. Umezawa,
  Anal. Chem., 77, 6928–6934 (2005).
  
  
• A Genetically Encoded Indicator for Assaying Bioactive Chemicals that Induce Nuclear Transport of Glucocorticoid Receptor.
  S.B. Kim, T. Ozawa, Y. Umezawa,
  Anal. Biochem., 347, 213–220 (2005).
  
  
• Genetically Encoded Stress Indicator for Noninvasively Imaging Endogenous Corticosterone in Living Mice.
  S.B. Kim, T. Ozawa, Y. Umezawa,
  Anal. Chem., 77, 6588–6593 (2005).
  
  
• A High-Throughput Screening of Genes that Encode Proteins Transported into the Endoplamsic Reticulum in Mammalian Cells,
  T. Ozawa, K. Nishitani, Y. Sako, Y. Umezawa,
  Nucleic. Acids Res., 33, e34 (2005).
  
  
• Methods of Analysis for Protein Dynamics in Living Cells Based on Protein Splicing.
  T. Ozawa,
  Bull Chem. Soc. Jpn., 78, 739–751 (2005).
  
  
• Methods of Analysis for Chemicals that Disrupt Cellular Signaling Pathways: Risk Assessment for Potential Endocrine Disruptors,
  Y. Umezawa, T. Ozawa, M. Sato, H. Inadera, S. Kaneko, M. Kunimoto, S. Hashimoto,
  Enviomental Sci., 12, 49–64 (2005).
  

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   2004

• High-Throughput Sensing and Noninvasive Imaging of Protein Nuclear Transport by Using Reconstitution of Split Renilla Luciferase. 
  S. B. Kim*, T. Ozawa*, S. Watanabe, Y. Umezawa,
  Proc. Natl. Acad. Sci. USA., 101, 11542–11547 (2004). (* Equal contribution to this work)
  

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   2003

• Locating a Protein–Protein Interaction in Living Cells via Split Renilla Luciferase Complementation. 
  A. Kaihara, Y. Kawai, M. Sato, T. Ozawa and Y. Umezawa,
  Anal. Chem., 75, 4176–4181 (2003).
  
  
• A Screening Method for Estrogens Using an Array-type DNA Glass Slide. 
  S. B. Kim, T. Ozawa, and Y. Umezawa,
  Anal. Sci., 19, 499–504 (2003).
  
  
• A Genetic Approach to Identifying Mitochondrial Proteins. 
  T. Ozawa, Y. Sako, M. Sato, T. Kitamura, and Y. Umezawa,
  Nature Biotechnol., 21, 287–293 (2003).
  
  
• A Genetic Approach to Identifying Organelle-Localized Proteins,
  T. Ozawa, Y. Sako, Y. Umezawa,
  Proceedings of the ISBC 2003, 276–279 (2003).
  

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   2002

• Peptide Assemblies in Living Cells. Methods for Detecting Protein–Protein Interactions,
  T. Ozawa and Y. Umezawa,
  Supramol. Chem., 14, 271–280 (2002).
  
  
• Probing Chemical Processes in Living Cells: Application for Assay and Screening of Chemicals that Disrupt Cellular Signaling Pathways,
  Y. Umezawa, T. Ozawa, M. Sato,
  Bull. Chem. Soc. Jpn., 75, 1423–1433 (2002).
  
  
• Fluorescent Indicators for Imaging Protein Phosphorylation in Single Living Cells. 
  M. Sato, T. Ozawa, K. Inukai, T. Asano, and Y. Umezawa,
  Nature Biotechnol., 20, 287–294 (2002).
  
  
• Peptide Assemblies in Living Cells.  Methods for Detecting Protein–Protein Interactions. 
  T. Ozawa and Y. Umezawa,
  Supramolecular Chemistry, 14, 271–280 (2002).
  

• Methods of Analysis for Chemicals that Promote/Disrupt Cellular Signaling. 
  Y. Umezawa, T. Ozawa and M. Sato,
  Anal. Sci., 18, 503–516 (2002).
  
  
• Probing Chemical Processes in Living Cells: Application for Assay and Screening of Chemicals that Disrupt Cellular Signaling Pathways.  
  Y. Umezawa, T. Ozawa and M. Sato,
  Bull. Chem. Soc. Jpn., 75, 1423–1433 (2002).
  
  
• Assay and Screening Methods for Chemicals that Disrupt Cellular Signaling Pathways.  Risk Assessment for Potential Endocrine Disruptors.
  Y. Umezawa, T. Ozawa and M. Sato,
  Environmental Sciences, 9, 23–35 (2002).
  
  

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   2001

• Protein Splicing-Based Reconstitution of Split Green Fluorescent Protein for Monitoring Protein–Protein Interactions in Bacteria: Improved Sensitivity and Reduced Screening Time. 
  T. Ozawa, M. Takeuchi, A. Kaihara, M. Sato and Y. Umezawa,
  Anal. Chem., 73, 5866–5874 (2001).
  
  
• A Screening Method for Antagonists that Inhibit the Binding of Calmodulin to a Target Peptide Using Surface Plasmon Resonance. 
  K. Sasaki, T. Ozawa and Y. Umezawa,
  Anal. Chim. Acta, 447, 63–74 (2001).
  
  
• Detection of Protein–Protein Interactions in vivo Based on Protein Splicing. 
  T. Ozawa and Y. Umezawa,
  Curr. Opin. Chem. Biol., 5, 578–583 (2001).
  
  
• Imaging of Conformational Changes of Proteins with a New Environment-Sensitive Fluorescent Probe Designed for Site-Specific Labeling of Recombinant Proteins in Live Cells. 
  J. Nakanishi, T. Nakajima, M, Sato, T, Ozawa, K. Tohda and Y. Umezawa,
  Anal. Chem., 73, 2920–2928 (2001).
  
  
• Split Luciferase as an Optical Probe for Detecting Protein–Protein Interactions in Mammalian Cells Based on Protein Splicing. 
  T. Ozawa, , A. Kaihara, M. Sato, K. Tachihara  and Y. Umezawa,
  Anal. Chem., 73, 2516–2521 (2001).
  
  
• Detection of Protein–Protein Interactions in vivo Based on Protein Splicing.
  T. Ozawa and Y. Umezawa,
  Curr. Opin. Chem. Biol., 5, 578–583 (2001).
  
  

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   Before 2000

• How Can Ca²⁺ Selectively Activate Recoverin in the Presence of Mg²⁺?  Surface Plasmon Resonance and FT-IR Spectroscopic Studies. 
  T. Ozawa, M. Fukuda, M. Nara, A. Nakamura, K. Kohama and Y. Umezawa,
  Biochemistry, 39, 14495–14503 (2000).
  
  
• Fluorescent Indicators for Cyclic GMP Based on Cyclic GMP-Dependent Protein Kinase Ia and Green Fluorescent Proteins. 
  M. Sato, N. Hida, T. Ozawa and Y. Umezawa,
  Anal. Chem., 72, 5918–5924 (2000).
  
  
• A Fluorescent Indicator for Detecting Protein–Protein Interactions in Vivo Based on Protein Splicing. 
  T. Ozawa, S. Nogami, M. Sato, Y. Ohya and Y. Umezawa,
  Anal. Chem., 72, No. 21, 5151–5157 (2000).
  
  
• A Screening Method for Substrates of Multidrug Resistance-Associated Protein (MRP). 
  Z. Quan, T. Ozawa, M. Sato and Y. Umezawa,
  Anal. Chim. Acta, 423, 197–203 (2000).
  
  
• An SPR-based Screening Method for Agonist Selectivity for Insulin Signaling Pathways Based on the Binding of Phosphotyrosine to its Specific Binding Protein. 
  T. Yoshida, M. Sato, T. Ozawa and Y. Umezawa,
  Anal. Chem.,　72, 6–11 (2000).
  
  
• Novel Interaction of the Voltage-Dependent Sodium Channel (VDSC) with Calmodulin: Does VDSC Acquire Calmodulin-Mediated Ca²⁺-Sensitivity?
  M. Mori, T. Konno, T. Ozawa, M. Murata, K. Imoto and K. Nagayama,
  Biochemistry, 39, 1316–1323 (2000).
  
  
• Metal Ion Selectivity for Formation of the Calmodulin-Metal-Target Peptide Ternary Complex Studied by Surface Plasmon Resonance Spectroscopy. 
  T. Ozawa, K. Sasaki and Y. Umezawa,
  Biochim. Biophys. Acta, 1434, 211–220 (1999).
  
  
• A Fluorescent Indicator for Tyrosine Phosphorylation-Based Insulin Signaling Pathways. 
  M. Sato, T. Ozawa, T. Yoshida and Y. Umezawa,
  Anal. Chem., 71, 3948–3954 (1999).
  
  
• An Assay Method for Evaluating Chemical Selectivity of Agonists for Insulin Signaling Pathways Based on Agonist-Induced Phosphorylation of a Target Peptide. 
  T. Ozawa, M. Sato, M. Sugawara and Y. Umezawa,
  Anal. Chem., 70, 2345–2352 (1998).
  
  
• An Optical Method for Evaluating Ion Selectivity for Calcium Signaling Pathways in the Cell.
  T. Ozawa, M. Kakuta, M. Sugawara, Y. Umezawa and M. Ikura,
  Anal. Chem., 69, 3081–3085 (1997).

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Reviews, Books

　2018

• Nano-Materials for Bioimaging.
  T. Ozawa,
  Anal. Sci., 34, 125-126 (2018).
  
  

　2005

• Inteins for Split-Protein Reconstitutions and Their Applications.
  T. Ozawa, Y. Umezawa, M. Belfort (ed.),
  Nucleic Acids and Molecular Biology, Vol.16, 307–323,
  Springer-Verlag/Berlin (2005).
  
  

　Before 2000

• Receptor Based Chemical Sensing.
  M. Sugawara, H. Sato, T. Ozawa, Y. Umezawa, F. W. Sheller, F. Schubert and J. Fedrowitz (eds.),
  Frontiers in Biosensorics, I, Fundamental Aspects,  121–131,  
  Birkhäuser Verlag Basel/Switzerland (1997).
  

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