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2013年10月9日 (水) 13:55時点におけるTfuruya (トーク | 投稿記録)による版

表1.
分類 対象 プローブ名 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][5]
サイクリックAMP (cAMP) Epac 2000,2004 2, 3-1 [6][7]
イノシトール3リン酸 (IP3) LIBRA, Fretino, FIRE 2004, 2005, 2006 3-1 [8][9][10]
一酸化窒素 (NO) NOA-1, Piccell 2005, 2006 3-1 [11][12]
アデノシン3リン酸 (ATP) A Team 1.03-nD/nA 2012 3-1 [13]
エストロゲン SCCoR 2004 3-3 [14]
アンドロゲン Ficaro 2006 3-3 [15]
グルココルチコイド受容体リガンド GLUCOCOR 2007 3-3 [16][17]
神経成長因子 ECaus 2008 3-3 [18]
核内受容体 conpro 2007 3-2 [19]
O-N-アセチルグルコサミン (O-GlcNAc) 2006 3-3 [20]
ビタミンA (レチノイン酸) GEPRAS 2013 3-1 [21]
モリブデン酸 MolyProbe 2013 3-1 [22]
グルタミン酸 FLIPE 2005 3-1 [23]
Zn2+ eCALWY-1 2009 2 [24]
Cl- Clomeleon 2000 other [25]
水素イオン濃度 (pH) GFpH, YFpH 2001 other [26]
グルコース FLIPglu 2003 3-1 [27]
マルトース FLIPmal 2002 3-1 [28]
リボース FLIPrib 2003 3-1 [29]
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 [30][31][32][33]
Src Srcus 2005, 2005, 2007 3-3 [34][35][36]
プロテインキナーゼC (PKC) CKAR, CY-PKCdelta 2003, 2005 3-3, 3-1 [37][38]
プロテインキナーゼD (PKD) DKAR 2007 3-3 [39]
プロテインキナーゼA (PKA) ART, AKAR 2000, 2001 3-3 [40][41]
Abl Picchu 2001 3-3 [34]
Bcr-Abl Bcr-Abl activity sensor 2010 3-3 [42]
c-Raf Prin-cRaf 2005 3-1 [43]
PAK1 Pakabi 2009 3-1 [44]
B-raf Prin-Braf 2006 3-1 [45]
ZAP-70 ROZA 2008 3-3 [46]
Akt Aktus, BKAR, Akind 2003, 2005, 2007 3-3 [47][48][49]
ERK Miu2, Erkus, EKAR 2006, 2007, 2008 3-1,3-3,3-3 [50][51][52]
インシュリン受容体 Phocus 2002 3-3 [53]
上皮成長因子受容体 (EGFR) 2001 3-3 [34]
Ataxia telangiectasia mutated (ATM) 2007 3-3 [54]
オーロラBキナーゼ 2008 3-3 [55]
Cyclin B1-CDK1 2010 3-3 [56]
ミオシン軽鎖キナーゼ MLCK-FIP 2002 3-1 [57]
JNK JNKAR1, JUNKAR1EV 2010, 2011 3-3 [58][59]
RSK Eevee-RSK 2011 3-3 [59]
S6K Eevee-S6K 2011 3-3 [59]
Focal Adhesion Kinase (FAK) CYFAK413, FERM-sensor 2008, 2009 2, 3-1 [60][61]
PLK1 2008 3-3 [62]
SAP3K 2009 3-3 [63]
DAPK1 DAPK1(334)-F40 2011 3-1 [33]
ホスファターゼ カルシニューリン CaNAR1 2008, 2013 3-1 [32][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 [67][69]
Ral Raichu-Ral 2004 3-3 [71]
TC10 Raichu-TC10 2006 3-2 [72]
シグナル伝達 RCC1(GEF of Ran) CFP-RCC1-YFP 2008 3-1 [73]
CrkII phosphorylation Picchu 2001 3-1 [74]
N-WASP Stinger 2004 3-1 [75][76]
アドレナリン受容体 α2AAR-cam 2003 3-1 [77]
Parathyroid hormone receptor PTHR-cam 2003 3-1 [77]
細胞膜カルシウムポンプ BFP-PMCA-GFP 2007 3-1 [78]
アセチル化 ヒストンアセチル化 Histac 2004, 2009 3-3 [79][80]
脂質 Phosphatidylinositol (3,4,5)-trisphosphate (PIP3) Fllip, FLIMPA 2003 3-4 [81]
Phosphatidylinositol (4,5)-bisphosphate (PIP2) Pippi-PI(4,5)P2 2008 3-4 [82]
Phosphatidylinositol (3,4)-bisphosphate (PI(3,4)P2) Pippi-PI(3,4)P2 2008 3-4 [82]
Phosphatidylinositol 4-phosphate (PI4P) Pippi-PI(4)P 2008 3-4 [82]
ホスファチジン酸 Pii 2010 3-4 [83]
ジアシルグリセロール (DAG) Daglas, DIGDA 2006, 2008 3-4 [82][84]
タンパク質相互作用 アクチン 2004, 2008 2 [85][86]
PDK1-Akt interaction 2007 2 [49]
Protein tyrosine phosphatase 1B-receptor tyrosine kinases (PTP 1B-RTKs) interaction 2002 2 [87]
Breast cancer resistance protein/ATP-binding cassette sub-family G member) BCRP/ABCG 2010 2 [88]
Cofiin-actin interaction 2008 2 [89]
PTEN-Myosin V interaction 2009 2 [90]
プロテアーゼ カスパーゼ-3 EGFP-DEVD-EBFP 1998 1 [91]
カスパーゼ-8 CFP-c3-YFP-c6-mRFP 2002 1 [92]
カスパーゼ-9 SCAT9 2011 1 [93]
カスパーゼ-7 VDEVDc 2006 1 [94]
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 [95][96]
プロテアーゼ活性 (Factor Xa) 1996 1 [97]
カルパイン活性 pYSCS 2000 1 [98]
プレセニリン GFP-PSI-RFP 2009 3-1 [99]
その他 Strain sensor stFRET 2008 3-1 [100]
膜電位 VSFP, Mermaid, ArcLight, VSFP-Butterfly 2001, 2008, 2012 3-1 [101][102][103][104]
ミオシン II GSldCB 1998, 2006 3-1 [105][106]
ヒト免疫不全ウイルスRevタンパク質 YRGnC-11ad 2005 3-1 [107]
レドックス Redoxfluor, Gaskins 2010, 2011 3-1 [108][109]

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.

  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. 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]
  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. Thunemann, M., Wen, L., Hillenbrand, M., Vachaviolos, A., Feil, S., Ott, T., ..., & Feil, R. (2013).
    Transgenic mice for cGMP imaging. Circulation research, 113(4), 365-71. [PubMed:23801067] [PMC] [WorldCat] [DOI]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. Nishi, M., Tanaka, M., Matsuda, K., Sunaguchi, M., & Kawata, M. (2004).
    Visualization of glucocorticoid receptor and mineralocorticoid receptor interactions in living cells with GFP-based fluorescence resonance energy transfer. The Journal of neuroscience : the official journal of the Society for Neuroscience, 24(21), 4918-27. [PubMed:15163683] [PMC] [WorldCat] [DOI]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. 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]
  27. 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]
  28. 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]
  29. 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]
  30. 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]
  31. 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]
  32. 32.0 32.1 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]
  33. 33.0 33.1 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]
  34. 34.0 34.1 34.2 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]
  35. 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]
  36. 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]
  37. 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]
  38. 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]
  39. 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]
  40. 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]
  41. 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]
  42. 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]
  43. 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]
  44. 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]
  45. 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]
  46. 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]
  47. 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]
  48. 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]
  49. 49.0 49.1 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]
  50. 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]
  51. 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]
  52. 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]
  53. 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]
  54. 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]
  55. 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]
  56. 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]
  57. 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]
  58. 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]
  59. 59.0 59.1 59.2 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]
  60. 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]
  61. 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]
  62. Macůrek, L., Lindqvist, A., Lim, D., Lampson, M.A., Klompmaker, R., Freire, R., ..., & Medema, R.H. (2008).
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