Test

2013年10月4日 (金) 09:30時点におけるWikiSysop (トーク | 投稿記録)による版

}
  1. Miyawaki, A., Llopis, J., Heim, R., McCaffery, J.M., Adams, J.A., Ikura, M., & Tsien, R.Y. (1997).
    Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature, 388(6645), 882-7. [PubMed:9278050] [WorldCat] [DOI]
  2. Resource not found in PubMed.
  3. Honda, A., Adams, S.R., Sawyer, C.L., Lev-Ram, V., Tsien, R.Y., & Dostmann, W.R. (2001).
    Spatiotemporal dynamics of guanosine 3',5'-cyclic monophosphate revealed by a genetically encoded, fluorescent indicator. Proceedings of the National Academy of Sciences of the United States of America, 98(5), 2437-42. [PubMed:11226257] [PMC] [WorldCat] [DOI]
  4. Nikolaev, V.O., Gambaryan, S., & Lohse, M.J. (2006).
    Fluorescent sensors for rapid monitoring of intracellular cGMP. Nature methods, 3(1), 23-5. [PubMed:16369548] [WorldCat] [DOI]
  5. Zaccolo, M., & Pozzan, T. (2002).
    Discrete microdomains with high concentration of cAMP in stimulated rat neonatal cardiac myocytes. Science (New York, N.Y.), 295(5560), 1711-5. [PubMed:11872839] [WorldCat] [DOI]
  6. Nikolaev, V.O., Bünemann, M., Hein, L., Hannawacker, A., & Lohse, M.J. (2004).
    Novel single chain cAMP sensors for receptor-induced signal propagation. The Journal of biological chemistry, 279(36), 37215-8. [PubMed:15231839] [WorldCat] [DOI]
  7. Tanimura, A., Nezu, A., Morita, T., Turner, R.J., & Tojyo, Y. (2004).
    Fluorescent biosensor for quantitative real-time measurements of inositol 1,4,5-trisphosphate in single living cells. The Journal of biological chemistry, 279(37), 38095-8. [PubMed:15272011] [WorldCat] [DOI]
  8. Sato, M., Ueda, Y., Shibuya, M., & Umezawa, Y. (2005).
    Locating inositol 1,4,5-trisphosphate in the nucleus and neuronal dendrites with genetically encoded fluorescent indicators. Analytical chemistry, 77(15), 4751-8. [PubMed:16053285] [WorldCat] [DOI]
  9. Matsu-ura, T., Michikawa, T., Inoue, T., Miyawaki, A., Yoshida, M., & Mikoshiba, K. (2006).
    Cytosolic inositol 1,4,5-trisphosphate dynamics during intracellular calcium oscillations in living cells. The Journal of cell biology, 173(5), 755-65. [PubMed:16754959] [PMC] [WorldCat] [DOI]
  10. Sato, M., Hida, N., & Umezawa, Y. (2005).
    Imaging the nanomolar range of nitric oxide with an amplifier-coupled fluorescent indicator in living cells. Proceedings of the National Academy of Sciences of the United States of America, 102(41), 14515-20. [PubMed:16176986] [PMC] [WorldCat] [DOI]
  11. Sato, M., Nakajima, T., Goto, M., & Umezawa, Y. (2006).
    Cell-based indicator to visualize picomolar dynamics of nitric oxide release from living cells. Analytical chemistry, 78(24), 8175-82. [PubMed:17165805] [WorldCat] [DOI]
  12. Imamura, H., Nhat, K.P., Togawa, H., Saito, K., Iino, R., Kato-Yamada, Y., ..., & Noji, H. (2009).
    Visualization of ATP levels inside single living cells with fluorescence resonance energy transfer-based genetically encoded indicators. Proceedings of the National Academy of Sciences of the United States of America, 106(37), 15651-6. [PubMed:19720993] [PMC] [WorldCat] [DOI]
  13. Awais, M., Sato, M., Sasaki, K., & Umezawa, Y. (2004).
    A genetically encoded fluorescent indicator capable of discriminating estrogen agonists from antagonists in living cells. Analytical chemistry, 76(8), 2181-6. [PubMed:15080726] [WorldCat] [DOI]
  14. Awais, M., Sato, M., Lee, X., & Umezawa, Y. (2006).
    A fluorescent indicator to visualize activities of the androgen receptor ligands in single living cells. Angewandte Chemie (International ed. in English), 45(17), 2707-12. [PubMed:16555356] [WorldCat] [DOI]
  15. Awais, M., Sato, M., & Umezawa, Y. (2007).
    Optical probes to identify the glucocorticoid receptor ligands in living cells. Steroids, 72(14), 949-54. [PubMed:17897691] [WorldCat] [DOI]
  16. Nakajima, T., Sato, M., Akaza, N., & Umezawa, Y. (2008).
    Cell-based fluorescent indicator to visualize brain-derived neurotrophic factor secreted from living neurons. ACS chemical biology, 3(6), 352-8. [PubMed:18510313] [WorldCat] [DOI]
  17. Awais, M., Sato, M., & Umezawa, Y. (2007).
    Imaging of selective nuclear receptor modulator-induced conformational changes in the nuclear receptor to allow interaction with coactivator and corepressor proteins in living cells. Chembiochem : a European journal of chemical biology, 8(7), 737-43. [PubMed:17387660] [WorldCat] [DOI]
  18. Carrillo, L.D., Krishnamoorthy, L., & Mahal, L.K. (2006).
    A cellular FRET-based sensor for beta-O-GlcNAc, a dynamic carbohydrate modification involved in signaling. Journal of the American Chemical Society, 128(46), 14768-9. [PubMed:17105262] [WorldCat] [DOI]
  19. Shimozono, S., Iimura, T., Kitaguchi, T., Higashijima, S., & Miyawaki, A. (2013).
    Visualization of an endogenous retinoic acid gradient across embryonic development. Nature, 496(7445), 363-6. [PubMed:23563268] [WorldCat] [DOI]
  20. Nakanishi, Y., Iida, S., Ueoka-Nakanishi, H., Niimi, T., Tomioka, R., & Maeshima, M. (2013).
    Exploring dynamics of molybdate in living animal cells by a genetically encoded FRET nanosensor. PloS one, 8(3), e58175. [PubMed:23472155] [PMC] [WorldCat] [DOI]
  21. Okumoto, S., Looger, L.L., Micheva, K.D., Reimer, R.J., Smith, S.J., & Frommer, W.B. (2005).
    Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors. Proceedings of the National Academy of Sciences of the United States of America, 102(24), 8740-5. [PubMed:15939876] [PMC] [WorldCat] [DOI]
  22. Vinkenborg, J.L., Nicolson, T.J., Bellomo, E.A., Koay, M.S., Rutter, G.A., & Merkx, M. (2009).
    Genetically encoded FRET sensors to monitor intracellular Zn2+ homeostasis. Nature methods, 6(10), 737-40. [PubMed:19718032] [PMC] [WorldCat] [DOI]
  23. Kuner, T., & Augustine, G.J. (2000).
    A genetically encoded ratiometric indicator for chloride: capturing chloride transients in cultured hippocampal neurons. Neuron, 27(3), 447-59. [PubMed:11055428] [WorldCat] [DOI]
  24. Awaji, T., Hirasawa, A., Shirakawa, H., Tsujimoto, G., & Miyazaki, S. (2001).
    Novel green fluorescent protein-based ratiometric indicators for monitoring pH in defined intracellular microdomains. Biochemical and biophysical research communications, 289(2), 457-62. [PubMed:11716495] [WorldCat] [DOI]
  25. Fehr, M., Lalonde, S., Lager, I., Wolff, M.W., & Frommer, W.B. (2003).
    In vivo imaging of the dynamics of glucose uptake in the cytosol of COS-7 cells by fluorescent nanosensors. The Journal of biological chemistry, 278(21), 19127-33. [PubMed:12649277] [WorldCat] [DOI]
  26. Fehr, M., Frommer, W.B., & Lalonde, S. (2002).
    Visualization of maltose uptake in living yeast cells by fluorescent nanosensors. Proceedings of the National Academy of Sciences of the United States of America, 99(15), 9846-51. [PubMed:12097642] [PMC] [WorldCat] [DOI]
  27. Lager, I., Fehr, M., Frommer, W.B., & Lalonde, S. (2003).
    Development of a fluorescent nanosensor for ribose. FEBS letters, 553(1-2), 85-9. [PubMed:14550551] [WorldCat] [DOI]
  28. Takao, K., Okamoto, K., Nakagawa, T., Neve, R.L., Nagai, T., Miyawaki, A., ..., & Hayashi, Y. (2005).
    Visualization of synaptic Ca2+ /calmodulin-dependent protein kinase II activity in living neurons. The Journal of neuroscience : the official journal of the Society for Neuroscience, 25(12), 3107-12. [PubMed:15788767] [PMC] [WorldCat] [DOI]
  29. Lee, S.J., Escobedo-Lozoya, Y., Szatmari, E.M., & Yasuda, R. (2009).
    Activation of CaMKII in single dendritic spines during long-term potentiation. Nature, 458(7236), 299-304. [PubMed:19295602] [PMC] [WorldCat] [DOI]
  30. Fujii, H., Inoue, M., Okuno, H., Sano, Y., Takemoto-Kimura, S., Kitamura, K., ..., & Bito, H. (2013).
    Nonlinear decoding and asymmetric representation of neuronal input information by CaMKIIα and calcineurin. Cell reports, 3(4), 978-87. [PubMed:23602566] [WorldCat] [DOI]
  31. Piljić, A., de Diego, I., Wilmanns, M., & Schultz, C. (2011).
    Rapid development of genetically encoded FRET reporters. ACS chemical biology, 6(7), 685-91. [PubMed:21506563] [WorldCat] [DOI]
  32. Ting, A.Y., Kain, K.H., Klemke, R.L., & Tsien, R.Y. (2001).
    Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proceedings of the National Academy of Sciences of the United States of America, 98(26), 15003-8. [PubMed:11752449] [PMC] [WorldCat] [DOI]
  33. Wang, Y., Botvinick, E.L., Zhao, Y., Berns, M.W., Usami, S., Tsien, R.Y., & Chien, S. (2005).
    Visualizing the mechanical activation of Src. Nature, 434(7036), 1040-5. [PubMed:15846350] [WorldCat] [DOI]
  34. Hitosugi, T., Sasaki, K., Sato, M., Suzuki, Y., & Umezawa, Y. (2007).
    Epidermal growth factor directs sex-specific steroid signaling through Src activation. The Journal of biological chemistry, 282(14), 10697-706. [PubMed:17284441] [WorldCat] [DOI]
  35. Violin, J.D., Zhang, J., Tsien, R.Y., & Newton, A.C. (2003).
    A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. The Journal of cell biology, 161(5), 899-909. [PubMed:12782683] [PMC] [WorldCat] [DOI]
  36. Braun, D.C., Garfield, S.H., & Blumberg, P.M. (2005).
    Analysis by fluorescence resonance energy transfer of the interaction between ligands and protein kinase Cdelta in the intact cell. The Journal of biological chemistry, 280(9), 8164-71. [PubMed:15611119] [WorldCat] [DOI]
  37. Kunkel, M.T., Toker, A., Tsien, R.Y., & Newton, A.C. (2007).
    Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter. The Journal of biological chemistry, 282(9), 6733-42. [PubMed:17189263] [PMC] [WorldCat] [DOI]
  38. Nagai, Y., Miyazaki, M., Aoki, R., Zama, T., Inouye, S., Hirose, K., ..., & Hagiwara, M. (2000).
    A fluorescent indicator for visualizing cAMP-induced phosphorylation in vivo. Nature biotechnology, 18(3), 313-6. [PubMed:10700148] [WorldCat] [DOI]

    Zhang, J., Ma, Y., Taylor, S.S., & Tsien, R.Y. (2001).
    Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proceedings of the National Academy of Sciences of the United States of America, 98(26), 14997-5002. [PubMed:11752448] [PMC] [WorldCat] [DOI]
  39. Ting, A.Y., Kain, K.H., Klemke, R.L., & Tsien, R.Y. (2001).
    Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proceedings of the National Academy of Sciences of the United States of America, 98(26), 15003-8. [PubMed:11752449] [PMC] [WorldCat] [DOI]
  40. Tunceroglu, A., Matsuda, M., & Birge, R.B. (2010).
    Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia. Molecular cancer therapeutics, 9(11), 3065-73. [PubMed:20817824] [PMC] [WorldCat] [DOI]
  41. Terai, K., & Matsuda, M. (2005).
    Ras binding opens c-Raf to expose the docking site for mitogen-activated protein kinase kinase. EMBO reports, 6(3), 251-5. [PubMed:15711535] [PMC] [WorldCat] [DOI]
  42. Parrini, M.C., Camonis, J., Matsuda, M., & de Gunzburg, J. (2009).
    Dissecting activation of the PAK1 kinase at protrusions in living cells. The Journal of biological chemistry, 284(36), 24133-43. [PubMed:19574218] [PMC] [WorldCat] [DOI]
  43. Terai, K., & Matsuda, M. (2006).
    The amino-terminal B-Raf-specific region mediates calcium-dependent homo- and hetero-dimerization of Raf. The EMBO journal, 25(15), 3556-64. [PubMed:16858395] [PMC] [WorldCat] [DOI]
  44. Randriamampita, C., Mouchacca, P., Malissen, B., Marguet, D., Trautmann, A., & Lellouch, A.C. (2008).
    A novel ZAP-70 dependent FRET based biosensor reveals kinase activity at both the immunological synapse and the antisynapse. PloS one, 3(1), e1521. [PubMed:18231606] [PMC] [WorldCat] [DOI]
  45. Sasaki, K., Sato, M., & Umezawa, Y. (2003).
    Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells. The Journal of biological chemistry, 278(33), 30945-51. [PubMed:12773546] [WorldCat] [DOI]
  46. Kunkel, M.T., Ni, Q., Tsien, R.Y., Zhang, J., & Newton, A.C. (2005).
    Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter. The Journal of biological chemistry, 280(7), 5581-7. [PubMed:15583002] [PMC] [WorldCat] [DOI]
  47. Calleja, V., Alcor, D., Laguerre, M., Park, J., Vojnovic, B., Hemmings, B.A., ..., & Larijani, B. (2007).
    Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo. PLoS biology, 5(4), e95. [PubMed:17407381] [PMC] [WorldCat] [DOI]
  48. Fujioka, A., Terai, K., Itoh, R.E., Aoki, K., Nakamura, T., Kuroda, S., ..., & Matsuda, M. (2006).
    Dynamics of the Ras/ERK MAPK cascade as monitored by fluorescent probes. The Journal of biological chemistry, 281(13), 8917-26. [PubMed:16418172] [WorldCat] [DOI]
  49. Sato, M., Kawai, Y., & Umezawa, Y. (2007).
    Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells. Analytical chemistry, 79(6), 2570-5. [PubMed:17261026] [WorldCat] [DOI]
  50. Harvey, C.D., Ehrhardt, A.G., Cellurale, C., Zhong, H., Yasuda, R., Davis, R.J., & Svoboda, K. (2008).
    A genetically encoded fluorescent sensor of ERK activity. Proceedings of the National Academy of Sciences of the United States of America, 105(49), 19264-9. [PubMed:19033456] [PMC] [WorldCat] [DOI]
  51. Sato, M., Ozawa, T., Inukai, K., Asano, T., & Umezawa, Y. (2002).
    Fluorescent indicators for imaging protein phosphorylation in single living cells. Nature biotechnology, 20(3), 287-94. [PubMed:11875431] [WorldCat] [DOI]
  52. Ting, A.Y., Kain, K.H., Klemke, R.L., & Tsien, R.Y. (2001).
    Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proceedings of the National Academy of Sciences of the United States of America, 98(26), 15003-8. [PubMed:11752449] [PMC] [WorldCat] [DOI]
  53. Johnson, S.A., You, Z., & Hunter, T. (2007).
    Monitoring ATM kinase activity in living cells. DNA repair, 6(9), 1277-84. [PubMed:17428747] [WorldCat] [DOI]
  54. Fuller, B.G., Lampson, M.A., Foley, E.A., Rosasco-Nitcher, S., Le, K.V., Tobelmann, P., ..., & Kapoor, T.M. (2008).
    Midzone activation of aurora B in anaphase produces an intracellular phosphorylation gradient. Nature, 453(7198), 1132-6. [PubMed:18463638] [PMC] [WorldCat] [DOI]
  55. Gavet, O., & Pines, J. (2010).
    Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis. Developmental cell, 18(4), 533-43. [PubMed:20412769] [PMC] [WorldCat] [DOI]
  56. Chew, T.L., Wolf, W.A., Gallagher, P.J., Matsumura, F., & Chisholm, R.L. (2002).
    A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows. The Journal of cell biology, 156(3), 543-53. [PubMed:11815633] [PMC] [WorldCat] [DOI]
  57. Fosbrink, M., Aye-Han, N.N., Cheong, R., Levchenko, A., & Zhang, J. (2010).
    Visualization of JNK activity dynamics with a genetically encoded fluorescent biosensor. Proceedings of the National Academy of Sciences of the United States of America, 107(12), 5459-64. [PubMed:20212108] [PMC] [WorldCat] [DOI]
  58. Komatsu, N., Aoki, K., Yamada, M., Yukinaga, H., Fujita, Y., Kamioka, Y., & Matsuda, M. (2011).
    Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular biology of the cell, 22(23), 4647-56. [PubMed:21976697] [PMC] [WorldCat] [DOI]
  59. Komatsu, N., Aoki, K., Yamada, M., Yukinaga, H., Fujita, Y., Kamioka, Y., & Matsuda, M. (2011).
    Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular biology of the cell, 22(23), 4647-56. [PubMed:21976697] [PMC] [WorldCat] [DOI]
  60. Komatsu, N., Aoki, K., Yamada, M., Yukinaga, H., Fujita, Y., Kamioka, Y., & Matsuda, M. (2011).
    Development of an optimized backbone of FRET biosensors for kinases and GTPases. Molecular biology of the cell, 22(23), 4647-56. [PubMed:21976697] [PMC] [WorldCat] [DOI]
  61. Cai, X., Lietha, D., Ceccarelli, D.F., Karginov, A.V., Rajfur, Z., Jacobson, K., ..., & Schaller, M.D. (2008).
    Spatial and temporal regulation of focal adhesion kinase activity in living cells. Molecular and cellular biology, 28(1), 201-14. [PubMed:17967873] [PMC] [WorldCat] [DOI]
  62. Papusheva, E., Mello de Queiroz, F., Dalous, J., Han, Y., Esposito, A., Jares-Erijmanxa, E.A., ..., & Bunt, G. (2009).
    Dynamic conformational changes in the FERM domain of FAK are involved in focal-adhesion behavior during cell spreading and motility. Journal of cell science, 122(Pt 5), 656-66. [PubMed:19208768] [WorldCat] [DOI]
  63. Macůrek, L., Lindqvist, A., Lim, D., Lampson, M.A., Klompmaker, R., Freire, R., ..., & Medema, R.H. (2008).
    Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery. Nature, 455(7209), 119-23. [PubMed:18615013] [WorldCat] [DOI]
  64. Tomida, T., Takekawa, M., O'Grady, P., & Saito, H. (2009).
    Stimulus-specific distinctions in spatial and temporal dynamics of stress-activated protein kinase kinase kinases revealed by a fluorescence resonance energy transfer biosensor. Molecular and cellular biology, 29(22), 6117-27. [PubMed:19737916] [PMC] [WorldCat] [DOI]
  65. Piljić, A., de Diego, I., Wilmanns, M., & Schultz, C. (2011).
    Rapid development of genetically encoded FRET reporters. ACS chemical biology, 6(7), 685-91. [PubMed:21506563] [WorldCat] [DOI]
  66. Fujii, H., Inoue, M., Okuno, H., Sano, Y., Takemoto-Kimura, S., Kitamura, K., ..., & Bito, H. (2013).
    Nonlinear decoding and asymmetric representation of neuronal input information by CaMKIIα and calcineurin. Cell reports, 3(4), 978-87. [PubMed:23602566] [WorldCat] [DOI]
  67. Newman, R.H., & Zhang, J. (2008).
    Visualization of phosphatase activity in living cells with a FRET-based calcineurin activity sensor. Molecular bioSystems, 4(6), 496-501. [PubMed:18493642] [WorldCat] [DOI]
  68. Yasuda, R., Harvey, C.D., Zhong, H., Sobczyk, A., van Aelst, L., & Svoboda, K. (2006).
    Supersensitive Ras activation in dendrites and spines revealed by two-photon fluorescence lifetime imaging. Nature neuroscience, 9(2), 283-91. [PubMed:16429133] [WorldCat] [DOI]
  69. Mochizuki, N., Yamashita, S., Kurokawa, K., Ohba, Y., Nagai, T., Miyawaki, A., & Matsuda, M. (2001).
    Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature, 411(6841), 1065-8. [PubMed:11429608] [WorldCat] [DOI]
  70. Mochizuki, N., Yamashita, S., Kurokawa, K., Ohba, Y., Nagai, T., Miyawaki, A., & Matsuda, M. (2001).
    Spatio-temporal images of growth-factor-induced activation of Ras and Rap1. Nature, 411(6841), 1065-8. [PubMed:11429608] [WorldCat] [DOI]
  71. Aoki, K., Nakamura, T., & Matsuda, M. (2004).
    Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells. The Journal of biological chemistry, 279(1), 713-9. [PubMed:14570905] [WorldCat] [DOI]
  72. Kitano, M., Nakaya, M., Nakamura, T., Nagata, S., & Matsuda, M. (2008).
    Imaging of Rab5 activity identifies essential regulators for phagosome maturation. Nature, 453(7192), 241-5. [PubMed:18385674] [WorldCat] [DOI]
  73. Murakoshi, H., Wang, H., & Yasuda, R. (2011).
    Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature, 472(7341), 100-4. [PubMed:21423166] [PMC] [WorldCat] [DOI]
  74. Yoshizaki, H., Ohba, Y., Kurokawa, K., Itoh, R.E., Nakamura, T., Mochizuki, N., ..., & Matsuda, M. (2003).
    Activity of Rho-family GTPases during cell division as visualized with FRET-based probes. The Journal of cell biology, 162(2), 223-32. [PubMed:12860967] [PMC] [WorldCat] [DOI]
  75. Aoki, K., Nakamura, T., & Matsuda, M. (2004).
    Spatio-temporal regulation of Rac1 and Cdc42 activity during nerve growth factor-induced neurite outgrowth in PC12 cells. The Journal of biological chemistry, 279(1), 713-9. [PubMed:14570905] [WorldCat] [DOI]
  76. Murakoshi, H., Wang, H., & Yasuda, R. (2011).
    Local, persistent activation of Rho GTPases during plasticity of single dendritic spines. Nature, 472(7341), 100-4. [PubMed:21423166] [PMC] [WorldCat] [DOI]
  77. Takaya, A., Ohba, Y., Kurokawa, K., & Matsuda, M. (2004).
    RalA activation at nascent lamellipodia of epidermal growth factor-stimulated Cos7 cells and migrating Madin-Darby canine kidney cells. Molecular biology of the cell, 15(6), 2549-57. [PubMed:15034142] [PMC] [WorldCat] [DOI]
  78. Kawase, K., Nakamura, T., Takaya, A., Aoki, K., Namikawa, K., Kiyama, H., ..., & Matsuda, M. (2006).
    GTP hydrolysis by the Rho family GTPase TC10 promotes exocytic vesicle fusion. Developmental cell, 11(3), 411-21. [PubMed:16950130] [WorldCat] [DOI]
  79. Hao, Y., & Macara, I.G. (2008).
    Regulation of chromatin binding by a conformational switch in the tail of the Ran exchange factor RCC1. The Journal of cell biology, 182(5), 827-36. [PubMed:18762580] [PMC] [WorldCat] [DOI]
  80. Kurokawa, K., Mochizuki, N., Ohba, Y., Mizuno, H., Miyawaki, A., & Matsuda, M. (2001).
    A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo. The Journal of biological chemistry, 276(33), 31305-10. [PubMed:11406630] [WorldCat] [DOI]
  81. Lorenz, M., Yamaguchi, H., Wang, Y., Singer, R.H., & Condeelis, J. (2004).
    Imaging sites of N-wasp activity in lamellipodia and invadopodia of carcinoma cells. Current biology : CB, 14(8), 697-703. [PubMed:15084285] [WorldCat] [DOI]
  82. Ward, M.E., Wu, J.Y., & Rao, Y. (2004).
    Visualization of spatially and temporally regulated N-WASP activity during cytoskeletal reorganization in living cells. Proceedings of the National Academy of Sciences of the United States of America, 101(4), 970-4. [PubMed:14732696] [PMC] [WorldCat] [DOI]
  83. Vilardaga, J.P., Bünemann, M., Krasel, C., Castro, M., & Lohse, M.J. (2003).
    Measurement of the millisecond activation switch of G protein-coupled receptors in living cells. Nature biotechnology, 21(7), 807-12. [PubMed:12808462] [WorldCat] [DOI]
  84. Vilardaga, J.P., Bünemann, M., Krasel, C., Castro, M., & Lohse, M.J. (2003).
    Measurement of the millisecond activation switch of G protein-coupled receptors in living cells. Nature biotechnology, 21(7), 807-12. [PubMed:12808462] [WorldCat] [DOI]
  85. Corradi, G.R., & Adamo, H.P. (2007).
    Intramolecular fluorescence resonance energy transfer between fused autofluorescent proteins reveals rearrangements of the N- and C-terminal segments of the plasma membrane Ca2+ pump involved in the activation. The Journal of biological chemistry, 282(49), 35440-8. [PubMed:17901055] [WorldCat] [DOI]
  86. Lin, C.W., Jao, C.Y., & Ting, A.Y. (2004).
    Genetically encoded fluorescent reporters of histone methylation in living cells. Journal of the American Chemical Society, 126(19), 5982-3. [PubMed:15137760] [WorldCat] [DOI]
  87. Sasaki, K., Ito, T., Nishino, N., Khochbin, S., & Yoshida, M. (2009).
    Real-time imaging of histone H4 hyperacetylation in living cells. Proceedings of the National Academy of Sciences of the United States of America, 106(38), 16257-62. [PubMed:19805290] [PMC] [WorldCat] [DOI]
  88. Sato, M., Ueda, Y., Takagi, T., & Umezawa, Y. (2003).
    Production of PtdInsP3 at endomembranes is triggered by receptor endocytosis. Nature cell biology, 5(11), 1016-22. [PubMed:14528311] [WorldCat] [DOI]
  89. Nishioka, T., Aoki, K., Hikake, K., Yoshizaki, H., Kiyokawa, E., & Matsuda, M. (2008).
    Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Molecular biology of the cell, 19(10), 4213-23. [PubMed:18685081] [PMC] [WorldCat] [DOI]
  90. Nishioka, T., Aoki, K., Hikake, K., Yoshizaki, H., Kiyokawa, E., & Matsuda, M. (2008).
    Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Molecular biology of the cell, 19(10), 4213-23. [PubMed:18685081] [PMC] [WorldCat] [DOI]
  91. Nishioka, T., Aoki, K., Hikake, K., Yoshizaki, H., Kiyokawa, E., & Matsuda, M. (2008).
    Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Molecular biology of the cell, 19(10), 4213-23. [PubMed:18685081] [PMC] [WorldCat] [DOI]
  92. Nishioka, T., Frohman, M.A., Matsuda, M., & Kiyokawa, E. (2010).
    Heterogeneity of phosphatidic acid levels and distribution at the plasma membrane in living cells as visualized by a Föster resonance energy transfer (FRET) biosensor. The Journal of biological chemistry, 285(46), 35979-87. [PubMed:20826779] [PMC] [WorldCat] [DOI]
  93. Nishioka, T., Aoki, K., Hikake, K., Yoshizaki, H., Kiyokawa, E., & Matsuda, M. (2008).
    Rapid turnover rate of phosphoinositides at the front of migrating MDCK cells. Molecular biology of the cell, 19(10), 4213-23. [PubMed:18685081] [PMC] [WorldCat] [DOI]
  94. Sato, M., Ueda, Y., & Umezawa, Y. (2006).
    Imaging diacylglycerol dynamics at organelle membranes. Nature methods, 3(10), 797-9. [PubMed:16990811] [WorldCat] [DOI]
  95. Okamoto, K., Nagai, T., Miyawaki, A., & Hayashi, Y. (2004).
    Rapid and persistent modulation of actin dynamics regulates postsynaptic reorganization underlying bidirectional plasticity. Nature neuroscience, 7(10), 1104-12. [PubMed:15361876] [WorldCat] [DOI]
  96. Murakoshi, H., Lee, S.J., & Yasuda, R. (2008).
    Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain cell biology, 36(1-4), 31-42. [PubMed:18512154] [PMC] [WorldCat] [DOI]
  97. Calleja, V., Alcor, D., Laguerre, M., Park, J., Vojnovic, B., Hemmings, B.A., ..., & Larijani, B. (2007).
    Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo. PLoS biology, 5(4), e95. [PubMed:17407381] [PMC] [WorldCat] [DOI]
  98. Haj, F.G., Verveer, P.J., Squire, A., Neel, B.G., & Bastiaens, P.I. (2002).
    Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science (New York, N.Y.), 295(5560), 1708-11. [PubMed:11872838] [WorldCat] [DOI]
  99. Ni, Z., Mark, M.E., Cai, X., & Mao, Q. (2010).
    Fluorescence resonance energy transfer (FRET) analysis demonstrates dimer/oligomer formation of the human breast cancer resistance protein (BCRP/ABCG2) in intact cells. International journal of biochemistry and molecular biology, 1(1), 1-11. [PubMed:20622991] [PMC] [WorldCat]
  100. Homma, K., Niino, Y., Hotta, K., & Oka, K. (2008).
    Ca(2+) influx through P2X receptors induces actin cytoskeleton reorganization by the formation of cofilin rods in neurites. Molecular and cellular neurosciences, 37(2), 261-70. [PubMed:17993279] [WorldCat] [DOI]
  101. van Diepen, M.T., Parsons, M., Downes, C.P., Leslie, N.R., Hindges, R., & Eickholt, B.J. (2009).
    MyosinV controls PTEN function and neuronal cell size. Nature cell biology, 11(10), 1191-6. [PubMed:19767745] [PMC] [WorldCat] [DOI]
  102. Xu, X., Gerard, A.L., Huang, B.C., Anderson, D.C., Payan, D.G., & Luo, Y. (1998).
    Detection of programmed cell death using fluorescence energy transfer. Nucleic acids research, 26(8), 2034-5. [PubMed:9518501] [PMC] [WorldCat] [DOI]
  103. Onuki, R., Nagasaki, A., Kawasaki, H., Baba, T., Uyeda, T.Q., & Taira, K. (2002).
    Confirmation by FRET in individual living cells of the absence of significant amyloid beta -mediated caspase 8 activation. Proceedings of the National Academy of Sciences of the United States of America, 99(23), 14716-21. [PubMed:12409609] [PMC] [WorldCat] [DOI]
  104. Joseph, J., Seervi, M., Sobhan, P.K., & Retnabai, S.T. (2011).
    High throughput ratio imaging to profile caspase activity: potential application in multiparameter high content apoptosis analysis and drug screening. PloS one, 6(5), e20114. [PubMed:21637712] [PMC] [WorldCat] [DOI]
  105. Li, I.T., Chiang, J.J., & Truong, K. (2006).
    FRET evidence that an isoform of caspase-7 binds but does not cleave its substrate. Conference proceedings : ... Annual International Conference of the IEEE Engineering in Medicine and Biology Society. IEEE Engineering in Medicine and Biology Society. Annual Conference, 1, 531-4. [PubMed:17946841] [WorldCat] [DOI]
  106. Yang, J., Zhang, Z., Lin, J., Lu, J., Liu, B.F., Zeng, S., & Luo, Q. (2007).
    Detection of MMP activity in living cells by a genetically encoded surface-displayed FRET sensor. Biochimica et biophysica acta, 1773(3), 400-7. [PubMed:17187878] [WorldCat] [DOI]
  107. Ouyang, M., Lu, S., Li, X.Y., Xu, J., Seong, J., Giepmans, B.N., ..., & Wang, Y. (2008).
    Visualization of polarized membrane type 1 matrix metalloproteinase activity in live cells by fluorescence resonance energy transfer imaging. The Journal of biological chemistry, 283(25), 17740-8. [PubMed:18441011] [PMC] [WorldCat] [DOI]
  108. Mitra, R.D., Silva, C.M., & Youvan, D.C. (1996).
    Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene, 173(1 Spec No), 13-7. [PubMed:8707050] [WorldCat] [DOI]
  109. Vanderklish, P.W., Krushel, L.A., Holst, B.H., Gally, J.A., Crossin, K.L., & Edelman, G.M. (2000).
    Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proceedings of the National Academy of Sciences of the United States of America, 97(5), 2253-8. [PubMed:10688895] [PMC] [WorldCat] [DOI]
  110. Uemura, K., Lill, C.M., Li, X., Peters, J.A., Ivanov, A., Fan, Z., ..., & Berezovska, O. (2009).
    Allosteric modulation of PS1/gamma-secretase conformation correlates with amyloid beta(42/40) ratio. PloS one, 4(11), e7893. [PubMed:19924286] [PMC] [WorldCat] [DOI]
  111. Meng, F., Suchyna, T.M., & Sachs, F. (2008).
    A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ. The FEBS journal, 275(12), 3072-87. [PubMed:18479457] [PMC] [WorldCat] [DOI]
  112. Sakai, R., Repunte-Canonigo, V., Raj, C.D., & Knöpfel, T. (2001).
    Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein. The European journal of neuroscience, 13(12), 2314-8. [PubMed:11454036] [WorldCat] [DOI]
  113. Tsutsui, H., Karasawa, S., Okamura, Y., & Miyawaki, A. (2008).
    Improving membrane voltage measurements using FRET with new fluorescent proteins. Nature methods, 5(8), 683-5. [PubMed:18622396] [WorldCat] [DOI]
  114. Jin, L., Han, Z., Platisa, J., Wooltorton, J.R., Cohen, L.B., & Pieribone, V.A. (2012).
    Single action potentials and subthreshold electrical events imaged in neurons with a fluorescent protein voltage probe. Neuron, 75(5), 779-85. [PubMed:22958819] [PMC] [WorldCat] [DOI]
  115. Suzuki, Y., Yasunaga, T., Ohkura, R., Wakabayashi, T., & Sutoh, K. (1998).
    Swing of the lever arm of a myosin motor at the isomerization and phosphate-release steps. Nature, 396(6709), 380-3. [PubMed:9845076] [WorldCat] [DOI]
  116. Zeng, W., Seward, H.E., Málnási-Csizmadia, A., Wakelin, S., Woolley, R.J., Cheema, G.S., ..., & Bagshaw, C.R. (2006).
    Resonance energy transfer between green fluorescent protein variants: complexities revealed with myosin fusion proteins. Biochemistry, 45(35), 10482-91. [PubMed:16939200] [WorldCat] [DOI]
  117. Endoh, T., Funabashi, H., Mie, M., & Kobatake, E. (2005).
    Method for detection of specific nucleic acids by recombinant protein with fluorescent resonance energy transfer. Analytical chemistry, 77(14), 4308-14. [PubMed:16013840] [WorldCat] [DOI]
  118. Yano, T., Oku, M., Akeyama, N., Itoyama, A., Yurimoto, H., Kuge, S., ..., & Sakai, Y. (2010).
    A novel fluorescent sensor protein for visualization of redox states in the cytoplasm and in peroxisomes. Molecular and cellular biology, 30(15), 3758-66. [PubMed:20498274] [PMC] [WorldCat] [DOI]
  119. Kolossov, V.L., Spring, B.Q., Clegg, R.M., Henry, J.J., Sokolowski, A., Kenis, P.J., & Gaskins, H.R. (2011).
    Development of a high-dynamic range, GFP-based FRET probe sensitive to oxidative microenvironments. Experimental biology and medicine (Maywood, N.J.), 236(6), 681-91. [PubMed:21606117] [PMC] [WorldCat] [DOI]
表1.
Classification Target Year Probe design References
Small molecule Calcium 1997 3-2 [1]
Small molecule Cyclic guanosine monophosphate (cGMP) 2000, 2001, 2006 3-1 [2][3][4]
Small molecule Cyclic adenosine monophosphate (cAMP) 2000,2004 2, 3-1 [5][6]
Small molecule Inositol trisphosphate (IP3) 2004, 2005, 2006 3-1 [7][8][9]
Small molecule Nitric oxide (NO) 2005, 2006 3-1 [10][11]
Small molecule Adenosine triphosphate (ATP) 2012 3-1 [12]
Small molecule Estrogen 2004 3-3 [13]
Small molecule Androgen 2006 3-3 [14]
Small molecule Glucocorticoid receptor ligands 2007 3-3 [15]
Small molecule Neurotrophic factor 2008 3-3 [16]
Small molecule Nuclear receptor 2007 3-2 [17]
Small molecule O-N-acetylglucosamine (O-GlcNAc) 2006 3-3 [18]
Small molecule Vitamin A (Retinoic acid) 2013 3-1 [19]
Small molecule Molybdate 2013 3-1 [20]
Small molecule Glutamate 2005 3-1 [21]
Small molecule Zn2+ 2009 2 [22]
Small molecule Cl- 2000 other [23]
Small molecule pH 2001 other [24]
Small molecule Glucose 2003 3-1 [25]
Small molecule Maltose 2002 3-1 [26]
Small molecule Ribose 2003 3-1 [27]
Kinase Calcium/Calmodulin-dependent protein kinase II (CaMKII) 2005, 2009, 2011, 2013 3-1 [28][29][30][31]
Kinase Src 2005, 2005, 2007 3-3 [32][33][34]
Kinase Protein kinase C (PKC) 2003, 2005 3-3, 3-1 [35][36]
Kinase Protein kinase D (PKD) 2007 3-3 [37]
Kinase Protein kinase A (PKA) 2000, 2001 3-3 [38]
Kinase Abl 2001 3-3 [39]
Kinase Bcr-Abl 2010 3-3 [40]
Kinase c-Raf 2005 3-1 [41]
Kinase PAK1 2009 3-1 [42]
Kinase B-raf 2006 3-1 [43]
Kinase ZAP-70 2008 3-3 [44]
Kinase Akt 2003, 2005, 2007 3-3 [45][46][47]
Kinase ERK 2006, 2007, 2008 3-1,3-3,3-3 [48][49][50]
Kinase Insulin receptor 2002 3-3 [51]
Kinase Epidermal Growth factor receptor (EGFR) 2001 3-3 [52]
Kinase Ataxia telangiectasia mutated (ATM) 2007 3-3 [53]
Kinase Aurora B kinase 2008 3-3 [54]
Kinase Cyclin B1-CDK1 2010 3-3 [55]
Kinase Myosine light chain kinase 2002 3-1 [56]
Kinase JNK 2010, 2011 3-3 [57][58]
Kinase RSK 2011 3-3 [59]
Kinase S6K 2011 3-3 [60]
Kinase Focal Adhesion Kinase (FAK) 2008, 2009 2, 3-1 [61][62]
Kinase PLK1 2008 3-3 [63]
Kinase SAP3K 2009 3-3 [64]
Kinase DAPK1 2011 3-1 [65]
Phosphatase Calcineurin 2008, 2013 3-1 [66][67]
Small GTPase Ras 2001, 2006 3-2,2 [68][69]
Small GTPase Rap 2001 3-2 [70]
Small GTPase Rac 2004 3-2 [71]
Small GTPase Rab5 2008 3-2 [72]
Small GTPase Rho 2003, 2011 3-2, 2 [73][74]
Small GTPase Cdc42 2004, 2011 3-2, 2 [75][76]
Small GTPase Ral 2004 3-3 [77]
Small GTPase TC10 2006 3-2 [78]
Signal transduction RCC1(GEF of Ran) 2008 3-1 [79]
Signal transduction CrkII phosphorylation 2001 3-1 [80]
Signal transduction N-WASP 2004 3-1 [81][82]
Signal transduction Adrenergic receptor 2003 3-1 [83]
Signal transduction Parathyroid hormone receptor 2003 3-1 [84]
Signal transduction Plasma membrane Calcium pump 2007 3-1 [85]
Acetylation Histone acetylation 2004, 2009 3-3 [86][87]
Lipid Phosphatidylinositol (3,4,5)-trisphosphate (PIP3) 2003 3-4 [88]
Lipid Phosphatidylinositol (4,5)-bisphosphate (PIP2) 2008 3-4 [89]
Lipid Phosphatidylinositol (3,4)-bisphosphate (PI(3,4)P2) 2008 3-4 [90]
Lipid Phosphatidylinositol 4-phosphate (PI4P) 2008 3-4 [91]
Lipid Phosphatidic acid 2010 3-4 [92]
Lipid Diacylglycerol (DAG) 2006, 2008 3-4 [93][94]
Protein interaction Actin 2004, 2008 2 [95][96]
Protein interaction PDK1-Akt interaction 2007 2 [97]
Protein interaction Protein tyrosine phosphatase 1B-receptor tyrosine kinases (PTP 1B-RTKs) interaction 2002 2 [98]
Protein interaction Breast cancer resistance protein/ATP-binding cassette sub-family G member) BCRP/ABCG 2010 2 [99]
Protein interaction Cofiin-actin interaction 2008 2 [100]
Protein interaction PTEN-Myosin V interaction 2009 2 [101]
Protease Caspase-3 1998 1 [102]
Protease Caspase-8 2002 1 [103]
Protease Caspase-9 2011 1 [104]
Protease Caspase-7 2006 1 [105]
Protease Matrix Metalloproteinase (MMP) 2007, 2008 1 [106][107]
Protease Protease activity (Factor Xa) 1996 1 [108]
Protease Calpain activity 2000 1 [109]
Protease Presenilin 2009 3-1 [110]
Other Strain sensor 2008 3-1 [111]
Other Membrane potential 2001, 2008, 2012 3-1 [112][113][114]
Other Myosin II 1998, 2006 3-1 [115][116]
Other HIV Rev protein 2005 3-1 [117]
Other Redox 2010, 2011 3-1 [118][119]