分類 | 対象 | プローブ名 | 年 | プローブデザイン | 参考文献 |
生体内小分子 | カルシウム | Cameleon | 1997 | 3-2 | [1] |
サイクリックGMP (cGMP) | CGY, Cygnet, pGES-DE2, cGi | 2000, 2001, 2006 | 3-1 | [2][3][4] | |
サイクリックAMP (cAMP) | Epac | 2000,2004 | 2, 3-1 | [5][6] | |
イノシトール3リン酸 (IP3) | LIBRA, Fretino, FIRE | 2004, 2005, 2006 | 3-1 | [7][8][9] | |
一酸化窒素 (NO) | NOA-1, Piccell | 2005, 2006 | 3-1 | [10][11] | |
アデノシン3リン酸 (ATP) | A Team 1.03-nD/nA | 2012 | 3-1 | [12] | |
エストロゲン | SCCoR | 2004 | 3-3 | [13] | |
アンドロゲン | Ficaro | 2006 | 3-3 | [14] | |
グルココルチコイド受容体リガンド | GLUCOCOR | 2007 | 3-3 | [15] | |
神経成長因子 | ECaus | 2008 | 3-3 | [16] | |
核内受容体 | conpro | 2007 | 3-2 | [17] | |
O-N-アセチルグルコサミン (O-GlcNAc) | 2006 | 3-3 | [18] | ||
ビタミンA (レチノイン酸) | GEPRAS | 2013 | 3-1 | [19] | |
モリブデン酸 | MolyProbe | 2013 | 3-1 | [20] | |
グルタミン酸 | FLIPE | 2005 | 3-1 | [21] | |
Zn2+ | eCALWY-1 | 2009 | 2 | [22] | |
Cl- | Clomeleon | 2000 | other | [23] | |
水素イオン濃度 (pH) | GFpH, YFpH | 2001 | other | [24] | |
グルコース | FLIPglu | 2003 | 3-1 | [25] | |
マルトース | FLIPmal | 2002 | 3-1 | [26] | |
リボース | FLIPrib | 2003 | 3-1 | [27] | |
キナーゼ | カルシウム/カルモジュリン依存製タンパク質キナーゼII (CaMKII) | Camui α, green-Camui α, Camk2a reporter | 2005, 2009, 2011, 2013 | 3-1 | [28][29][30][31] |
Src | Srcus | 2005, 2005, 2007 | 3-3 | [32][33][34] | |
プロテインキナーゼC (PKC) | CKAR, CY-PKCdelta | 2003, 2005 | 3-3, 3-1 | [35][36] | |
プロテインキナーゼD (PKD) | DKAR | 2007 | 3-3 | [37] | |
プロテインキナーゼA (PKA) | ART, AKAR | 2000, 2001 | 3-3 | [38][39] | |
Abl | Picchu | 2001 | 3-3 | [40] | |
Bcr-Abl | Bcr-Abl activity sensor | 2010 | 3-3 | [41] | |
c-Raf | Prin-cRaf | 2005 | 3-1 | [42] | |
PAK1 | Pakabi | 2009 | 3-1 | [43] | |
B-raf | Prin-Braf | 2006 | 3-1 | [44] | |
ZAP-70 | ROZA | 2008 | 3-3 | [45] | |
Akt | Aktus, BKAR, Akind | 2003, 2005, 2007 | 3-3 | [46][47][48] | |
ERK | Miu2, Erkus, EKAR | 2006, 2007, 2008 | 3-1,3-3,3-3 | [49][50][51] | |
インシュリン受容体 | Phocus | 2002 | 3-3 | [52] | |
上皮成長因子受容体 (EGFR) | 2001 | 3-3 | [40] | ||
Ataxia telangiectasia mutated (ATM) | 2007 | 3-3 | [53] | ||
オーロラBキナーゼ | 2008 | 3-3 | [54] | ||
Cyclin B1-CDK1 | 2010 | 3-3 | [55] | ||
ミオシン軽鎖キナーゼ | MLCK-FIP | 2002 | 3-1 | [56] | |
JNK | JNKAR1, JUNKAR1EV | 2010, 2011 | 3-3 | [57][58] | |
RSK | Eevee-RSK | 2011 | 3-3 | [58] | |
S6K | Eevee-S6K | 2011 | 3-3 | [58] | |
Focal Adhesion Kinase (FAK) | CYFAK413, FERM-sensor | 2008, 2009 | 2, 3-1 | [59][60] | |
PLK1 | 2008 | 3-3 | [61] | ||
SAP3K | 2009 | 3-3 | [62] | ||
DAPK1 | DAPK1(334)-F40 | 2011 | 3-1 | [63] | |
ホスファターゼ | カルシニューリン | CaNAR1 | 2008, 2013 | 3-1 | [30][64] |
低分子量GTPアーゼ | Ras | Raichu-Ras, Fras | 2001, 2006 | 3-2,2 | [65][66] |
Rap | Raichu-Rap | 2001 | 3-2 | [66] | |
Rac | Raichu-Rac1 | 2004 | 3-2 | [67] | |
Rab5 | Raichu-Rab5 | 2008 | 3-2 | [68] | |
Rho | Raichu-RhoA | 2003, 2011 | 3-2, 2 | [69][70] | |
Cdc42 | Raichu-cdc42 | 2004, 2011 | 3-2, 2 | [71][72] | |
Ral | Raichu-Ral | 2004 | 3-3 | [73] | |
TC10 | Raichu-TC10 | 2006 | 3-2 | [74] | |
シグナル伝達 | RCC1(GEF of Ran) | CFP-RCC1-YFP | 2008 | 3-1 | [75] |
CrkII phosphorylation | Picchu | 2001 | 3-1 | [76] | |
N-WASP | Stinger | 2004 | 3-1 | [77][78] | |
アドレナリン受容体 | α2AAR-cam | 2003 | 3-1 | [79] | |
Parathyroid hormone receptor | PTHR-cam | 2003 | 3-1 | [79] | |
細胞膜カルシウムポンプ | BFP-PMCA-GFP | 2007 | 3-1 | [80] | |
アセチル化 | ヒストンアセチル化 | Histac | 2004, 2009 | 3-3 | [81][82] |
脂質 | Phosphatidylinositol (3,4,5)-trisphosphate (PIP3) | Fllip, FLIMPA | 2003 | 3-4 | [83] |
Phosphatidylinositol (4,5)-bisphosphate (PIP2) | Pippi-PI(4,5)P2 | 2008 | 3-4 | [84] | |
Phosphatidylinositol (3,4)-bisphosphate (PI(3,4)P2) | Pippi-PI(3,4)P2 | 2008 | 3-4 | [84] | |
Phosphatidylinositol 4-phosphate (PI4P) | Pippi-PI(4)P | 2008 | 3-4 | [84] | |
ホスファチジン酸 | Pii | 2010 | 3-4 | [85] | |
ジアシルグリセロール (DAG) | Daglas, DIGDA | 2006, 2008 | 3-4 | [84][86] | |
タンパク質相互作用 | アクチン | 2004, 2008 | 2 | [87][88] | |
PDK1-Akt interaction | 2007 | 2 | [89] | ||
Protein tyrosine phosphatase 1B-receptor tyrosine kinases (PTP 1B-RTKs) interaction | 2002 | 2 | [90] | ||
Breast cancer resistance protein/ATP-binding cassette sub-family G member) BCRP/ABCG | 2010 | 2 | [91] | ||
Cofiin-actin interaction | 2008 | 2 | [92] | ||
PTEN-Myosin V interaction | 2009 | 2 | [93] | ||
プロテアーゼ | カスパーゼ-3 | EGFP-DEVD-EBFP | 1998 | 1 | [94] |
カスパーゼ-8 | CFP-c3-YFP-c6-mRFP | 2002 | 1 | [95] | |
カスパーゼ-9 | SCAT9 | 2011 | 1 | [96] | |
カスパーゼ-7 | VDEVDc | 2006 | 1 | [97] | |
マトリックスメタロプロテアーゼ (MMP) | YFP-MSS-CFPdisplay, MTI-MMP-FRET biosensor | 2007, 2008 | 1 | [98][99] | |
プロテアーゼ活性 (Factor Xa) | 1996 | 1 | [100] | ||
カルパイン活性 | pYSCS | 2000 | 1 | [101] | |
プレセニリン | GFP-PSI-RFP | 2009 | 3-1 | [102] | |
その他 | Strain sensor | stFRET | 2008 | 3-1 | [103] |
膜電位 | VSFP, Mermaid, ArcLight, VSFP-Butterfly | 2001, 2008, 2012 | 3-1 | [104][105][106] | |
ミオシン II | GSldCB | 1998, 2006 | 3-1 | [107][108] | |
ヒト免疫不全ウイルスRevタンパク質 | YRGnC-11ad | 2005 | 3-1 | [109] | |
レドックス | Redoxfluor, Gaskins | 2010, 2011 | 3-1 | [110][111] |
The numbers in the Probe Design column correspond to the section number in the “Strategies of probe design” chapter of the main text. See the webpage by Dr. Michiyuki Matsuda http://www.lif.kyoto-u.ac.jp/labs/fret/e-phogemon/unifret.htm for updated information.
- ↑
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] - ↑
Sato, M., Hida, N., Ozawa, T., & Umezawa, Y. (2000).
Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Ialpha and green fluorescent proteins. Analytical chemistry, 72(24), 5918-24. [PubMed:11140757] [WorldCat] [DOI] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 30.0 30.1
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 40.0 40.1 引用エラー: 無効な
<ref>
タグです。「ref11752449
」という名前の注釈に対するテキストが指定されていません - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 58.0 58.1 58.2
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 引用エラー: 無効な
<ref>
タグです。「ref21506563
」という名前の注釈に対するテキストが指定されていません - ↑
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] - ↑
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] - ↑ 66.0 66.1
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 引用エラー: 無効な
<ref>
タグです。「ref14570905
」という名前の注釈に対するテキストが指定されていません - ↑ 引用エラー: 無効な
<ref>
タグです。「ref21423166
」という名前の注釈に対するテキストが指定されていません - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 79.0 79.1
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑ 84.0 84.1 84.2 84.3
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] - ↑
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] - ↑
Sato, M., Ueda, Y., & Umezawa, Y. (2006).
Imaging diacylglycerol dynamics at organelle membranes. Nature methods, 3(10), 797-9. [PubMed:16990811] [WorldCat] [DOI] - ↑
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] - ↑
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] - ↑ 引用エラー: 無効な
<ref>
タグです。「ref17407381
」という名前の注釈に対するテキストが指定されていません - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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] - ↑
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]