東京大学大学院総合文化研究科 佐藤守俊研究室

生命現象の光操作　ゲノム編集　バイオメージング

■募集■

大学院生

ポスドク

Original Papers

1. 1.Y. Kuwasaki, K. Suzuki, G. Yu, S. Yamamoto, T. Otabe, Y. Kakihara, M. Nishiwaki, K. Miyake, K. Fushimi, R. Bekdash, Y. Shimizu, R. Narikawa, T. Nakajima, M. Yazawa and M. Sato, “A red-light-responsive photoswitch for deep tissue optogenetics” Nature Biotechnology, published online. DOI: 10.1038/s41587-022-01351-w.
   

2. 2.Y. Koganezawa, M. Umetani, M. Sato and Y. Wakamoto, “History-dependent physiological adaptation to lethal genetic modification under antibiotic exposure” eLife, 11, e74486 (2022). DOI: 10.7554/eLife.74486.
   

3. 3.K. Kishi, H. Koyama, S. Oka, A. Kato, M. Sato and T. Fujimori, “Repetitive short-pulsed illumination efficiently activates photoactivatable-Cre as continuous illumination in embryonic stem cells and pre-implantation embryos of transgenic mouse” Genesis, 59, e23457 (2021). DOI: 10.1002/dvg.23457.
   

4. 4.S. R. Tachibana, L. Tang, L. Zhu, Y. Takeda, K. Fushimi, Y. Ueda, T. Nakajima, Y. Kuwasaki, M. Sato, R. Narikawa and C. Fang, “An engineered biliverdin-compatible cyanobacteriochrome enables a unique ultrafast reversible photoswitching pathway” Int. J. Mol. Sci., 22, 5252 (2021). DOI: 10.3390/ijms22105252.
   

5. 5.S. R. Tachibana, L. Tang, C. Chen, L. Zhu, Y. Takeda, K. Fushimi, T. K. Seevers, R. Narikawa, M. Sato and C. Fang, “Transient electronic and vibrational signatures during reversible photoswitching of a cyanobacteriochrome photoreceptor” Spectrochim. Acta A, 250, 119379 (2021). DOI: 10.1016/j.saa.2020.119379.
   

6. 6.K. Yoshimi, Y. Yamauchi, T. Tanaka, T. Shimada, M. Sato and T. Mashimo, “Photoactivatable Cre knock-in mice for spatiotemporal control of genetic engineering in vivo” Lab. Invest., 101, 125-135 (2021). DOI: 10.1038/s41374-020-00482-5.
   

7. 7.T. Takao, M. Sato and T. Maruyama, “Optogenetic regulation of embryo implantation in mice using photoactivatable CRISPR–Cas9” Proc. Natl. Acad. Sci. USA, 117, 28579-28581 (2020). DOI: 10.1073/pnas.2016850117.
   

8. 8.K. Fushimi, H. Hoshino, N. Shinozaki-Narikawa, Y. Kuwasaki, K. Miyake, T. Nakajima, M. Sato, F. Kano and R. Narikawa, “The cruciality of single amino acid replacement for the spectral tuning of biliverdin-binding cyanobacteriochromes” Int. J. Mol. Sci., 21, 6278 (2020). DOI: 10.3390/ijms21176278.
   

9. 9.K. Morikawa, K. Furuhashi, C. de Sena-Tomas, A. L. Garcia-Garcia, R. Bekdash, A. D. Klein, N. Gallerani, H. E. Yamamoto, S.-H. E. Park, G. S. Collins, F. Kawano, M. Sato, C.-S. Lin, K. L. Targoff, E. Au, M. Salling and M. Yazawa, “Photoactivatable Cre recombinase 3.0 for in vivo mouse applications” Nature Communications, 11, 2141 (2020). DOI: 10.1038/s41467-020-16030-0.
   

10. 10.T. Takao, Y. Hiraoka, K. Kawabe, D. Yamada, L. Ming, K. Tanaka, M. Sato and T. Takarada, “Establishment of a tTA-dependent photoactivatable Cre recombinase knock-in mouse model for optogenetic genome engineering” Biochem. Biophys. Res. Commun., 526, 213-217 (2020). DOI: 10.1016/j.bbrc.2020.03.015.
    

11. 11.H. -J. Kim, S. Ogura, T. Otabe, R. Kamegawa, M. Sato, K. Kataoka and K. Miyata, “Fine-tuning of hydrophobicity in amphiphilic polyaspartamide derivatives for rapid and transient expression of messenger RNA directed toward genome engineering in brain” ACS Cent. Sci., 5, 1866-1875 (2019). DOI: 10.1021/acscentsci.9b00843.
    

12. 12.Y. Sasaki, M. Oshikawa, P. Bharmoria, H. Kouno, A. Hayashi-Takagi, M. Sato, I. Ajioka, N. Yanai and N. Kimizuka, “Near-infrared optogenetic genome engineering by photon upconversion hydrogels” Angew. Chem. Int. Ed., 58, 17827-17833 (2019). DOI: 10.1002/anie.201911025.
    

13. 13.Y. Nihongaki, T. Otabe, Y. Ueda and M. Sato, “A split CRISPR–Cpf1 platform for inducible genome editing and gene activation” Nature Chemical Biology, 15, 882-888 (2019). DOI: 10.1038/s41589-019-0338-y.
    

14. 14.N. Nomura, R. Nishihara, T. Nakajima, S. B. Kim, N. Iwasawa, Y. Hiruta, S. Nishiyama, M. Sato, D. Citterio and K. Suzuki, “Biothiol-activatable bioluminescent coelenterazine derivative for molecular imaging in vitro and in vivo” Anal. Chem., 91, 9546-9553 (2019). DOI: 10.1021/acs.analchem.9b00694.
    

15. 15.M. Abe, R. Nishihara, Y. Ikeda, T. Nakajima, M. Sato, N. Iwasawa, S. Nishiyama, R. Paulmurugan, D. Citterio, S. B. Kim and K. Suzuki, “Near infrared bioluminescence imaging with through-bond energy transfer cassette” ChemBioChem, 20, 1919-1923 (2019). DOI: 10.1002/cbic.201900149.
    

16. 16.Y. Kuwasaki, K. Miyake, K. Fushimi, Y. Takeda, Y. Ueda, T. Nakajima, M. Ikeuchi, M. Sato and R. Narikawa, “Protein engineering of dual-Cys cyanobacteriochrome AM1_1186g2 for biliverdin incorporation and far-red/blue reversible photoconversion” Int. J. Mol. Sci., 20, 2935 (2019). DOI: 10.3390/ijms20122935.
    

17. 17.M. Tahara, Y. Takishima, S. Miyamoto, Y. Nakatsu, K. Someya, M. Sato, K. Tani and M. Takeda, “Photocontrollable mononegaviruses” Proc. Natl. Acad. Sci. USA, 116, 11587-11589 (2019). DOI: 10.1073/pnas.1906531116.
    

18. 18.R. Nishihara, R. Paulmurugan, T. Nakajima, E. Yamamoto, A. Natarajan, R. Afjei, Y. Hiruta, N. Iwasawa, S. Nishiyama, D. Citterio, M. Sato, S. B. Kim and K. Suzuki, “Highly bright and stable NIR-BRET with blue-shifted coelenterazine derivatives for deep-tissue imaging of molecular events in vivo” Theranostics, 9, 2646-2661 (2019). DOI: 10.7150/thno.32219.
    

19. 19.K. Fushimi, T. Miyazaki, Y. Kuwasaki, T. Nakajima, T. Yamamoto, K. Suzuki, Y. Ueda, K. Miyake, Y. Takeda, J.-H. Choi, H. Kawagishi, E. Y. Park, M. Ikeuchi, M. Sato and R. Narikawa, “Rational conversion of chromophore selectivity of cyanobacteriochromes to accept mammalian intrinsic biliverdin” Proc. Natl. Acad. Sci. USA, 116, 8301-8309 (2019). DOI: 10.1073/pnas.1818836116.
    

20. 20.S. Yamamoto, Y. Iwamaru, Y. Shimizu, Y. Ueda, M. Sato, K. Yamaguchi and J. Nakanishi, “Epidermal growth factor-nanoparticle conjugates change the activity from anti-apoptotic to pro-apoptotic at membrane rafts” Acta Biomater., 88, 383-391 (2019). DOI: 10.1016/j.actbio.2019.02.026.
    

21. 21.Y. Ueda, T. Ii, Y. Aono, N. Sugimoto, S. Shinji, H. Yoshida and M. Sato, “Membrane dynamics induced by a phosphatidylinositol 3,4,5-trisphosphate optogenetic tool” Anal. Sci., 35, 57-63 (2019). DOI: 10.2116/analsci.18SDP06.
    

22. 22.R. Nishihara, E. Hoshino, Y. Kakudate, S. Kishigami, N. Iwasawa, S. Sasaki, T. Nakajima, M. Sato, S. Nishiyama, D. Citterio, K. Suzuki and S. B. Kim, “Azide- and dye-conjugated coelenterazine analogues for a multiplex molecular imaging platform” Bioconjugate Chem., 29, 1922-1931 (2018). DOI: 10.1021/acs.bioconjchem.8b00188.
    

23. 23.Y. Ueda, T. Ishiwata, S. Shinji, T. Arai, Y. Matsuda, J. Aida, N. Sugimoto, T. Okazaki, J. Kikuta, M. Ishii and M. Sato, “In vivo imaging of T cell lymphoma infiltration process at the colon” Sci. Rep., 8, 3978 (2018). DOI: 10.1038/s41598-018-22399-2.
    

24. 24.M. Hemmi, Y. Ikeda, Y. Shindo, T. Nakajima, S. Nishiyama, K. Oka, M. Sato, Y. Hiruta, D. Citterio and K. Suzuki, “Highly sensitive bioluminescent probe for thiol detection in living cells” Chem. Asian J., 13, 648-655 (2018). DOI: 10.1002/asia.201701774.
    

25. 25.Y. Ikeda, T. Saitoh, K. Niwa, T. Nakajima, N. Kitada, S. A. Maki, M. Sato, D. Citterio, S. Nishiyama and K. Suzuki, “An allylated firefly luciferin analogue with luciferase specific response in living cells” Chem. Commun., 54, 1774-1777 (2018). DOI: 10.1039/c7cc09720d.
    

26. 26.M. Hasegawa, K. Fushimi, K. Miyake, T. Nakajima, Y. Oikawa, G. Enomoto, M. Sato, M. Ikeuchi and R. Narikawa, “Molecular characterization of DXCF cyanobacteriochromes from the cyanobacterium Acaryochloris marina identifies a blue-light power sensor” J. Biol. Chem., 293, 1713-1727 (2018). DOI: 10.1074/jbc.M117.816553.
    

27. 27.Y. Furuhata, Y. Nihongaki, M. Sato and K. Yoshimoto, “Control of adipogenic differentiation in mesenchymal stem cells via endogenous gene activation using CRISPR-Cas9” ACS Synth. Biol., 6, 2191-2197 (2017). DOI: 10.1021/acssynbio.7b00246.
    

28. 28.Y. Nihongaki, Y. Furuhata, T. Otabe, S. Hasegawa, K. Yoshimoto and M. Sato, “CRISPR-Cas9-based Photoactivatable Transcription Systems to Induce Neuronal Differentiation” Nature Methods, published online.  DOI: 10.1038/nmeth.4430.
    

29. 29.A. Furuya, F. Kawano, T. Nakajima, Y. Ueda and M. Sato, “Assembly Domain-Based Optogenetic System for the Efficient Control of Cellular Signaling” ACS Synth. Biol., 6, 1086-1095 (2017). DOI: 10.1021/acssynbio.7b00022.
    

30. 30.G. Yu, H. Onodera, Y. Aono, F. Kawano, Y. Ueda, A. Furuya, H. Suzuki and M. Sato, “Optical Manipulation of the Alpha Subunits of Heterotrimeric G Proteins Using Photoswitchable Dimerization Systems” Sci. Rep., 6, 35777 (2016). DOI: 10.1038/srep35777.
    

31. 31.F. Kawano, R. Okazaki, M. Yazawa and M. Sato, “A Photoactivatable Cre–loxP Recombination System for Optogenetic Genome Engineering” Nature Chemical Biology, 12, 1059-1064 (2016). DOI: 10.1038/nchembio2205.
    

32. 32.K. Fushimi, T. Nakajima, Y. Aono, T. Yamamoto, Ni-Ni Win, M. Ikeuchi, M. Sato and R. Narikawa, “Photoconversion and Fluorescence Properties of a Red/Green-Type Cyanobacteriochrome AM1_C0023g2 That Binds Not Only Phycocyanobilin But Also Biliverdin” Front. Microbiol., 7, 588 (2016). DOI: 10.3389/fmicb.2016.00588.
    

33. 33.Y. Ueda, H. Ogiso, M. Sato, Y. Umezawa, T. Okazaki and T. Kobayashi, “Asymmetrical Diacylglycerol Dynamics on the Cytosolic and Luminal Sides of a Single Endomembrane in Living Cells” Sci. Rep., 5, 12960 (2015). DOI: 10.1038/srep12960.
    

34. 34.Y. Nihongaki, F. Kawano, T. Nakajima and M. Sato, “Photoactivatable CRISPR-Cas9 for Optogenetic Genome Editing” Nature Biotechnology, 33, 755-760 (2015).  DOI: 10.1038/nbt.3245.
    

35. 35.F. Kawano, H. Suzuki, A. Furuya and M. Sato, “Engineered Pairs of Distinct Photoswitches for Optogenetic Control of Cellular Proteins” Nature Communications, 6, 6256 (2015). DOI: 10.1038/ncomms7256.
    

36. 36.Y. Nihongaki, S. Yamamoto, F. Kawano, H. Suzuki and M. Sato, “CRISPR-Cas9-Based Photoactivatable Transcription System” Chem. Biol., 22, 169-174 (2015). DOI: 10.1016/j.chembiol.2014.12.011.
    

37. 37.R. Narikawa, T. Nakajima, Y. Aono, K. Fushimi, G. Enomoto, W. Ni Ni, S. Itoh, M. Sato and M. Ikeuchi, “A Biliverdin-Binding Cyanobacteriochrome from the Chlorophyll d-Bearing Cyanobacterium Acaryochloris marina” Sci. Rep., 5, 7950 (2015). DOI: 10.1038/srep07950.
    

38. 38.R. Nishihara, H. Suzuki, E. Hoshino, S. Suganuma, M. Sato, T. Saitoh, S. Nishiyama, N. Iwasawa, D. Citterio and K. Suzuki, “Bioluminescent Coelenterazine Derivatives with Imidazopyrazinone C-6 Extended Substitution” Chem. Commun., 51, 391-394 (2015).
    

39. 39.Y. Nihongaki, H. Suzuki, F. Kawano and M. Sato, “Genetically Engineered Photoinducible Homodimerization System with Improved Dimer-Forming Efficiency” ACS Chem. Biol., 9, 617-621 (2014).
    

40. 40.F. Kawano, H. Suzuki, Y. Aono and M. Sato, “Fluorescence Imaging-Based High-Throughput Screening of Fast- and Slow-Cycling LOV proteins” PLOS ONE, 8(12), e82693 (2013).
    

41. 41.Y. C.  Lin, Y. Nihongaki, T. Y. Lin, S. Razavi, M. Sato, and T. Inoue, “Rapidly Reversible Manipulation of Molecular Activities Using Dual Chemical Dimerizers” Angew. Chem. Int. Ed., 53, 6450-6454 (2013).
    

42. 42.S. B. Kim, H. Suzuki, M. Sato and H. Tao, “Superluminescent Variants of Marine Luciferases for Bioassays” Anal. Chem., 83, 8732-8740 (2011).
    

43. 43.M. Oya, H. Suzuki, Y. Watanabe, M. Sato and T. Tsuboi, “Amino acid taste receptor regulates insulin secretion in pancreatic β-cell line MIN6 cells” Genes Cells, 16, 608-616 (2011).
    

44. 44.F. Kano, T. Arai, M. Matsuto, H. Hayashi, M. Sato and M. Murata, “Hydrogen peroxide depletes phosphatidylinosidol-3-phosphatefrom endosomes in a p38 MAPK-dependent manner and perturbs endocytosis” Biochim. Biophys. Acta-Mol. Cell Res., 1813, 784-801 (2011).
    

45. 45.K. Jang, K. Sato, Y. Tanaka, X. Yan, M. Sato, T. Nakajima, K. Mawatari, T. Konno, K. Ishihara and T. Kitamori, “An Efficient Surface Modification Using 2-Methacryloyloxyethyl Phosphorylcholine to Control Cell Attachment via Photochemical Reaction in a Microchannel” Lab Chip, 10, 1937-1945 (2010).
    

46. 46.H. Suzuki and M. Sato, “Genetically encoded fluorescent indicators to visualize protein phosphorylation by c-Jun NH2-terminal kinase (JNK) in living cells” Supramol. Chem., 22, 434-439 (2010).
    

47. 47.S. B. Kim, M. Sato and H. Tao, “Molecular Tension-Indexed Bioluminescent Probes for Determining Protein—Protein interactions” Bioconjugate Chem., 20, 2324-2330 (2009).
    

48. 48.S. B. Kim, M. Sato and H. Tao, “Genetically Encoded Bioluminescent Indicators for Stress Hormones” Anal. Chem., 81, 3760-3768 (2009).
    

49. 49.S. B. Kim, M. Sato and H. Tao, “A Split Gaussia Luciferase-Based Bioluminescence Template for Tracing Protein Dynamics in Living Cells” Anal. Chem., 81, 67-74 (2009).
    

50. 50.S. B. Kim, M. Sato and H. Tao, “Circularly Permutated Bioluminescent Probes for Illuminating Ligand-Activated Protein Dynamics” Bioconjugate Chem., 19, 2480-2486 (2008).
    

51. 51.H. Suzuki, M. Sato and Y. Umezawa, “Accurate Targeting of Activated Macrophages Based on Synergistic Activation of Functional Molecules Uptake by Scavenger Receptor and Matrix Metalloproteinase” ACS Chem. Biol. 3, 471-479 (2008).
    

52. 52.T. Nakajima, M. Sato, N. Akaza and Y. Umezawa, “Cell-Based Fluorescent Indicator To Visualize Brain-Derived Neurotrophic Factor Secreted from Living Neurons” ACS Chem. Biol., 3, 352-358 (2008).
    

53. 53.M. Awais, M. Sato, and Y. Umezawa, “Optical probes to identify the glucocorticoid         receptor ligands in living cells” Steroids, 72, 949-954 (2007).
    

54. 54.T. Hitosugi, M. Sato, K. Sasaki and Y. Umezawa, “Lipid Raft-Specific Knockdown of Src Family Kinase Activity Inhibits Cell Adhesion and Cell Cycle Progression of Breast Cancer Cells” Cancer Res., 67, 8139-8148 (2007).
    

55. 55.T. Ozawa, Y. Natori, M. Sato and Y. Umezawa, “Imaging Dynamics of Endogenous Mitochondrial RNA in Single Living Cells” Nature Methods, 4, 413-419 (2007).
    

56. 56.M. Awais, M. Sato and Y. Umezawa, “Imaging of Selective Nuclear Receptor Modulator-Induced Conformational Change in the Nuclear Receptor to Interact with Coactivator and Corepressor Proteins in Living Cells” ChemBioChem, 8, 737-743 (2007).
    

57. 57.T. Hitosugi, K. Sasaki, M. Sato, Y. Suzuki and Y. Umezawa, “EGF Directs Sex-Specific Steroid Signaling through Src Activation” J. Biol. Chem., 282, 10694-10706 (2007).
    

58. 58.M. Awais, M. Sato, and Y. Umezawa, “A Fluorescent Indicator to Visualize Ligand-Induced Receptor/Coactivator Interactions for Screening of Peroxisome Proliferator-Activated Receptorγ Ligands in Living Cells” Biosens. Bioelectron., 22, 2564-2569 (2007).
    

59. 59.M. Sato, Y. Kawai and Y. Umezawa, “Genetically Encoded Fluorescent Indicators to Visualize Protein Phosphorylation by Extracellular Signal-Regulated Kinase (ERK) in Single Living Cells” Anal. Chem., 79, 2570-2575 (2007).
    

60. 60.S. B. Kim, M. Awais, M. Sato, Y. Umezawa and H. Tao, “Integrated Molecule-Format Bioluminescent Probe for Visualizing Androgenicity of Ligands Based on the Intramolecular Association of Androgen Receptor with Its Recognition Peptide” Anal. Chem., 79, 1874-1880 (2007).
    

61. 61.M. Sato, T. Nakajima, M. Goto and Y. Umezawa, “Cell-Based Indicator to Visualize Picomolar Dynamics of Nitric Oxide Release from Living Cells” Anal. Chem., 78, 8175-8182 (2006).
    

62. 62.T. Furukawa, C.-X. Bai, A. Kaihara, E. Ozaki, T. Kawano, Y. Nakaya, M. Awais, M. Sato, Y. Umezawa and J. Kurokawa, “Ginsenoside Re, a Main Phytosterol of Panax Ginseng, Activates Cardiac Potassium Channels via a Non-Genomic Pathway of Sex Hormones” Mol. Pharmacol., 70, 1916-1924 (2006).
    

63. 63.M. Sato, Y. Ueda and Y. Umezawa, “Imaging Diacylglycerol Dynamics at Organelle Membranes” Nature Methods, 3, 797-799 (2006).
    

64. 64.H. Shirakawa, M. Ito, M. Sato, Y. Umezawa and S. Miyazaki, “Measurement of Intracellular IP3 during Ca2+ Oscillations in Mouse Eggs with GFP-Based FRET Probe” Biochem. Biophys. Res. Commun., 345, 781-788 (2006).
    

65. 65.M. Awais, M. Sato, X. Lee and Y. Umezawa, “A Fluorescent Indicator to Visualize Activities of the Androgen Receptor Ligands in Single Living Cells” Angew. Chem. Int. Ed., 45, 2707-2712 (2006).
    

66. 66.M. Sato, N. Hida, M. and Y. Umezawa, “Imaging the Nanomolar Range of Nitric Oxide with an Amplifier-Coupled Fluorescent Indicator in Living Cells” Proc. Natl. Acad. Sci. USA, 102, 14515-14520 (2005).
    

67. 67.M. Sato, Y. Ueda, M. Shibuya and Y. Umezawa, “Locating Inositol 1,4,5-trisphosphate in the Nucleus and Neuronal Dendrites with Genetically Encoded Fluorescent Indicators” Anal. Chem., 77, 4751-4758 (2005).
    

68. 68.Y. Kawai, M. Sato and Y. Umezawa, “Single Color Fluorescent Indicators of Protein Phosphorylaion for Multicolor Imaging of Intracellular Signal Flow Dynamics” Anal. Chem., 76, 6144-6149 (2004).
    

69. 69.M. Awais, M. Sato, K. Sasaki and Y. Umezawa, “A Genetically Encoded Fluorescent Indicator Capable of Discriminating Estrogen Agonists from Antagonists in Living Cells” Anal. Chem., 76, 2181-2186 (2004).
    

70. 70.M. Sato, Y. Ueda, T. Takagi and Y. Umezawa, “Production of PtdInsP3 at Endomembranes is Triggered by Receptor Endocytosis” Nature Cell Biology, 5, 1016-1022 (2003).
    

71. 71.K. Sasaki, M. Sato and Y. Umezawa, “Fluorescent Indicators for Akt/Protein Kinase B and Dynamics of Akt Activity Visualized in Living Cells” J. Biol. Chem., 278, 30945-30951 (2003).
    

72. 72.T. Ozawa, Y. Sako, M. Sato, T. Kitamura and Y. Umezawa, “A Genetic Approach to Identifying Mitochondrial Proteins” Nature Biotechnology, 21, 287-293 (2003).
    

73. 73.A. Kaihara, Y. Kawai, M. Sato, T. Ozawa and Y. Umezawa, “Locating a Protein-Protein Interaction in Living Cells via Split Renilla Luciferase Complementation” Anal. Chem., 75, 4176-4181 (2003).
    

74. 74.Y. Umezawa, K. Umezawa, P. Buhlmann, N. Hamada, H. Aoki, J. Nakanishi, M. Sato, K.P. Xiao, and Y. Nishimura, “Potentiometric selectivity coefficients of ion-selective electrodes part II. Inorganic anions” Pure Appl. Chem., 74, 923-994 (2002).
    

75. 75.M. Sato, T. Ozawa, K. Inukai, T. Asano and Y. Umezawa, “Fluorescent Indicators for Imaging Protein Phosphorylation in Single Living Cells” Nature Biotechnology, 20, 287-294 (2002).
    

76. 76.T. Ozawa, M. Takeuchi, A. Kaihara, M. Sato and Y. Umezawa, “Protein Splicing-Based Reconsition of Split Green Fluorescent Protein for Monitoring Protein-Protein Interactions in Bacteria: Improved Sensitivity and Reduced Screening Time” Anal. Chem., 73, 5866-5874 (2001).
    

77. 77.J. Nakanishi, T. Nakajima, M, Sato, T, Ozawa, K. Tohda and Y. Umezawa, “Imaging of Conformational Changes of Proteins with a New Environment-Sensitive Fluorescent Probe Designed for Site-Specific Labeling of Recombinant Proteins in Live Cells” Anal. Chem., 73, 2920-2928 (2001).
    

78. 78.T. Ozawa, A. Kaihara, M. Sato, K. Tachihara and Y. Umezawa, “Split Luciferase as an Optical Probe for Detecting Protein-Protein Interactions in Mammalian Cells Based on Protein Splicing” Anal. Chem., 73, 2516-2521 (2001).
    

79. 79.M. Sato, N. Hida, T. Ozawa and Y. Umezawa, “Fluorescent Indicators for Cyclic GMP Based on Cyclic GMP-Dependent Protein Kinase Iα and Green Fluorescent Proteins” Anal. Chem., 72, 5918-5924 (2000).
    

80. 80.T. Ozawa, S. Nogami, M. Sato, Y. Ohya and Y. Umezawa, “A New Fluorescent Indicator for Detecting Protein-Protein Interactions in vivo Based on Protein Splicing” Anal. Chem., 72, 5151-5157 (2000).
    

81. 81.Z. Quan, T. Ozawa, M. Sato and Y. Umezawa, “A Screening Method for Substrates of Multidrug Resistance-Associated Protein (MRP)” Anal. Chim. Acta, 423, 197-203 (2000).
    

82. 82.T. Yoshida, M. Sato, T. Ozawa and Y. Umezawa, “An SPR-Based Screening Method for Agonist Selectivity for Insulin Signaling Pathways Based on the Binding of Phosphotyrosine to its Specific Binding Protein” Anal. Chem., 72, 6-11 (2000).
    

83. 83.M. Sato, T. Ozawa, T. Yoshida and Y. Umezawa, “A Fluorescent Indicator for Tyrosine Phosphorylation-Based Insulin Signaling Pathways” Anal. Chem., 71, 3948-3954 (1999).
    

84. 84.T. Ozawa, M. Sato, M. Sugawara and Y. Umezawa, “An Assay Method for Evaluating Chemical Selectivity of Agonists for Insulin Signaling Pathways Based on Agonist-Induced Phosphorylation of a Target Peptide” Anal. Chem., 70, 2345-2352 (1998).
    

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