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Volumn 113, Issue , 2013, Pages 217-274

Fluorescent sensors of protein Kinases: From basics to biomedical applications

Author keywords

Biosensor; Diagnostics; Drug discovery; Fluorescence; Live cell imaging; Molecular imaging; Protein kinase

Indexed keywords


EID: 84871061446     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-386932-6.00006-5     Document Type: Chapter
Times cited : (33)

References (179)
  • 1
    • 20444370016 scopus 로고
    • The cleavage products of vitellin
    • P.A. Levene, and C.L. Alsberg The cleavage products of vitellin J Biol Chem 2 1906 127 133
    • (1906) J Biol Chem , vol.2 , pp. 127-133
    • Levene, P.A.1    Alsberg, C.L.2
  • 2
    • 0000685288 scopus 로고
    • Serinephosphoric acid obtained on hydrolysis of vitellinic acid
    • F.A. Lipmann, and P.A. Levene Serinephosphoric acid obtained on hydrolysis of vitellinic acid J Biol Chem 98 1932 109 114
    • (1932) J Biol Chem , vol.98 , pp. 109-114
    • Lipmann, F.A.1    Levene, P.A.2
  • 3
    • 0001010573 scopus 로고
    • The enzymatic phosphorylation of proteins
    • G. Burnett, and E.P. Kennedy The enzymatic phosphorylation of proteins J Biol Chem 211 1954 969 980
    • (1954) J Biol Chem , vol.211 , pp. 969-980
    • Burnett, G.1    Kennedy, E.P.2
  • 5
    • 0018337894 scopus 로고
    • Phosphorylation-dephosphorylation of enzymes
    • E.G. Krebs, and J.A. Beavo Phosphorylation-dephosphorylation of enzymes Annu Rev Biochem 48 1979 923 959
    • (1979) Annu Rev Biochem , vol.48 , pp. 923-959
    • Krebs, E.G.1    Beavo, J.A.2
  • 6
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • T. Hunter Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling Cell 80 1995 225 236
    • (1995) Cell , vol.80 , pp. 225-236
    • Hunter, T.1
  • 7
    • 0036097364 scopus 로고    scopus 로고
    • The origins of protein phosphorylation
    • P. Cohen The origins of protein phosphorylation Nat Cell Biol 4 2002 E127 E130
    • (2002) Nat Cell Biol , vol.4
    • Cohen, P.1
  • 8
    • 0026336662 scopus 로고
    • Protein kinase classification
    • T. Hunter Protein kinase classification Methods Enzymol 200 1991 3 37
    • (1991) Methods Enzymol , vol.200 , pp. 3-37
    • Hunter, T.1
  • 9
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • G. Manning, D.B. Whyte, R. Martinez, T. Hunter, and S. Sudarsanam The protein kinase complement of the human genome Science 298 2002 1912 1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 10
    • 0023651349 scopus 로고
    • A thousand and one protein kinases
    • T. Hunter A thousand and one protein kinases Cell 50 1987 823 829
    • (1987) Cell , vol.50 , pp. 823-829
    • Hunter, T.1
  • 11
    • 0027772445 scopus 로고
    • On the importance of protein phosphorylation in cell cycle control
    • J.L. Maller On the importance of protein phosphorylation in cell cycle control Mol Cell Biochem 127-128 1993 267 281 (Pubitemid 24032672)
    • (1993) Molecular and Cellular Biochemistry , vol.127-128 , pp. 267-281
    • Maller, J.L.1
  • 13
    • 0028773477 scopus 로고
    • Three protein kinase structures define a common motif
    • S.S. Taylor, and E. Radzio-Andzelm Three protein kinase structures define a common motif Structure 2 1994 345 355
    • (1994) Structure , vol.2 , pp. 345-355
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 14
    • 0028476615 scopus 로고
    • Protein kinases share a common structural motif outside the conserved catalytic domain
    • M. Véron, E. Radzio-Andzelm, I. Tsigelny, and S.S. Taylor Protein kinases share a common structural motif outside the conserved catalytic domain Cell Mol Biol 40 1994 587 596
    • (1994) Cell Mol Biol , vol.40 , pp. 587-596
    • Véron, M.1    Radzio-Andzelm, E.2    Tsigelny, I.3    Taylor, S.S.4
  • 15
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • DOI 10.1016/S0092-8674(00)81092-2
    • L.N. Johnson, M.E. Noble, and D.J. Owen Active and inactive protein kinases: structural basis for regulation Cell 85 1996 149 158 (Pubitemid 26118158)
    • (1996) Cell , vol.85 , Issue.2 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 16
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282 (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 17
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • DOI 10.1038/nrm2203, PII NRM2203
    • J.A. Ubersax, and J.E. Ferrell Jr. Mechanisms of specificity in protein phosphorylation Nat Rev Mol Cell Biol 8 2007 530 541 (Pubitemid 46985383)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 530-541
    • Ubersax, J.A.1    Ferrell Jr., J.E.2
  • 18
    • 40849119616 scopus 로고    scopus 로고
    • Understanding and exploiting substrate recognition by protein kinases
    • B.E. Turk Understanding and exploiting substrate recognition by protein kinases Curr Opin Chem Biol 12 2008 4 10
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 4-10
    • Turk, B.E.1
  • 19
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • DOI 10.1016/j.molcel.2004.08.024, PII S1097276504004800
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases: controlling activity through activation segment conformation Mol Cell 15 2004 661 675 (Pubitemid 39194898)
    • (2004) Molecular Cell , vol.15 , Issue.5 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 20
    • 79551632876 scopus 로고    scopus 로고
    • Protein kinase signaling networks in cancer
    • J. Brognard, and T. Hunter Protein kinase signaling networks in cancer Curr Opin Genet Dev 21 2011 4 11
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 4-11
    • Brognard, J.1    Hunter, T.2
  • 22
    • 27144444110 scopus 로고    scopus 로고
    • Targeting kinases in asthma
    • DOI 10.1517/13543784.14.10.1213
    • K. Blease Targeting kinases in asthma Expert Opin Investig Drugs 14 2005 1213 1220 (Pubitemid 41488870)
    • (2005) Expert Opinion on Investigational Drugs , vol.14 , Issue.10 , pp. 1213-1220
    • Blease, K.1
  • 23
    • 0035176191 scopus 로고    scopus 로고
    • Biological activity of tyrosine kinase inhibitors: Novel agents for psoriasis therapy
    • H. Ben-Bassat Biological activity of tyrosine kinase inhibitors: novel agents for psoriasis therapy Curr Opin Investig Drugs 2 2001 1539 1545 (Pubitemid 33081072)
    • (2001) Current Opinion in Investigational Drugs , vol.2 , Issue.11 , pp. 1539-1545
    • Ben-Bassat, H.1
  • 24
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • P. Cohen Protein kinases - the major drug targets of the twenty-first century? Nat Rev Drug Discov 1 2002 309 315 (Pubitemid 37361447)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 25
    • 66149125644 scopus 로고    scopus 로고
    • Challenges and opportunities in defining the essential cancer kinome
    • B.D. Manning Challenges and opportunities in defining the essential cancer kinome Sci Signal 2 2009 pe15
    • (2009) Sci Signal , vol.2 , pp. 15
    • Manning, B.D.1
  • 26
    • 33847058474 scopus 로고    scopus 로고
    • Protein kinases and their therapeutic exploitation
    • L. Johnson Protein kinases and their therapeutic exploitation Biochem Soc Trans 35 2007 7 11
    • (2007) Biochem Soc Trans , vol.35 , pp. 7-11
    • Johnson, L.1
  • 27
    • 67650073265 scopus 로고    scopus 로고
    • Cell cycle kinases as therapeutic targets for cancer
    • S. Lapenna, and A. Giordano Cell cycle kinases as therapeutic targets for cancer Nat Rev Drug Discov 8 2009 547 566
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 547-566
    • Lapenna, S.1    Giordano, A.2
  • 28
    • 0029947186 scopus 로고    scopus 로고
    • Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
    • B.J. Druker, S. Tamura, E. Buchdunger, S. Ohno, G.M. Segal, and S. Fanning Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells Nat Med 2 1996 561 566
    • (1996) Nat Med , vol.2 , pp. 561-566
    • Druker, B.J.1    Tamura, S.2    Buchdunger, E.3    Ohno, S.4    Segal, G.M.5    Fanning, S.6
  • 29
    • 0034664960 scopus 로고    scopus 로고
    • A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element- binding protein
    • H.H. Versteeg, E. Nijhuis, G.R. van den Brink, M. Evertzen, G.N. Pynaert, and S.J. van Deventer A new phosphospecific cell-based ELISA for p42/p44 mitogen-activated protein kinase (MAPK), p38 MAPK, protein kinase B and cAMP-response-element-binding protein Biochem J 350 Pt 3 2000 717 722
    • (2000) Biochem J , vol.350 , Issue.PART 3 , pp. 717-722
    • Versteeg, H.H.1    Nijhuis, E.2    Van Den Brink, G.R.3    Evertzen, M.4    Pynaert, G.N.5    Van Deventer, S.J.6
  • 30
    • 0037620455 scopus 로고    scopus 로고
    • A homogeneous, nonradioactive high-throughput fluorogenic protein kinase assay
    • DOI 10.1016/S0003-2697(03)00094-0
    • K. Kupcho, R. Somberg, B. Bulleit, and S.A. Goueli A homogeneous, nonradioactive high-throughput fluorogenic protein kinase assay Anal Biochem 317 2003 210 217 (Pubitemid 36577630)
    • (2003) Analytical Biochemistry , vol.317 , Issue.2 , pp. 210-217
    • Kupcho, K.1    Somberg, R.2    Bulleit, B.3    Goueli, S.A.4
  • 31
    • 79960527513 scopus 로고    scopus 로고
    • Principles for designing fluorescent sensors and reporters
    • E.A. Lemke, and C. Schultz Principles for designing fluorescent sensors and reporters Nat Chem Biol 7 2011 480 483
    • (2011) Nat Chem Biol , vol.7 , pp. 480-483
    • Lemke, E.A.1    Schultz, C.2
  • 32
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • DOI 10.1146/annurev.biochem.67.1.509
    • R.Y. Tsien The green fluorescent protein Annu Rev Biochem 67 1998 509 544 (Pubitemid 28411137)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 34
    • 75149112222 scopus 로고    scopus 로고
    • Designs and applications of fluorescent protein-based biosensors
    • A. Ibraheem, and R.E. Campbell Designs and applications of fluorescent protein-based biosensors Curr Opin Chem Biol 14 2010 30 36
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 30-36
    • Ibraheem, A.1    Campbell, R.E.2
  • 35
    • 71049131212 scopus 로고    scopus 로고
    • Recent progress in strategies for the creation of protein-based fluorescent biosensors
    • H. Wang, E. Nakata, and I. Hamachi Recent progress in strategies for the creation of protein-based fluorescent biosensors Chembiochem 10 2009 2560 2577
    • (2009) Chembiochem , vol.10 , pp. 2560-2577
    • Wang, H.1    Nakata, E.2    Hamachi, I.3
  • 36
    • 77951211821 scopus 로고    scopus 로고
    • Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes
    • M.C. Morris Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes Cell Biochem Biophys 56 2010 19 37
    • (2010) Cell Biochem Biophys , vol.56 , pp. 19-37
    • Morris, M.C.1
  • 37
    • 84856854097 scopus 로고    scopus 로고
    • Probing the kinome in real time with fluorescent peptides
    • J.A. González-Vera Probing the kinome in real time with fluorescent peptides Chem Soc Rev 41 2012 1652 1664
    • (2012) Chem Soc Rev , vol.41 , pp. 1652-1664
    • González-Vera, J.A.1
  • 39
    • 0037418882 scopus 로고    scopus 로고
    • Development and use of fluorescent protein markers in living cells
    • DOI 10.1126/science.1082520
    • J. Lippincott-Schwartz, and G.H. Patterson Development and use of fluorescent protein markers in living cells Science 300 2003 87 91 (Pubitemid 36423032)
    • (2003) Science , vol.300 , Issue.5616 , pp. 87-91
    • Lippincott-Schwartz, J.1    Patterson, G.H.2
  • 40
    • 30944467113 scopus 로고    scopus 로고
    • A guide to choosing fluorescent proteins
    • DOI 10.1038/nmeth819, PII N819
    • N.C. Shaner, P.A. Steinbach, and R.Y. Tsien A guide to choosing fluorescent proteins Nat Methods 2 2005 905 909 (Pubitemid 43108726)
    • (2005) Nature Methods , vol.2 , Issue.12 , pp. 905-909
    • Shaner, N.C.1    Steinbach, P.A.2    Tsien, R.Y.3
  • 41
    • 14544286521 scopus 로고    scopus 로고
    • Building and breeding molecules to spy on cells and tumors
    • DOI 10.1016/j.febslet.2004.11.025
    • R.Y. Tsien Breeding and building molecules to spy on cells and tumors FEBS Lett 579 2005 927 932 (Pubitemid 40361867)
    • (2005) FEBS Letters , vol.579 , Issue.4 SPEC. ISS. , pp. 927-932
    • Tsien, R.Y.1
  • 42
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • B.N. Giepmans, S.R. Adams, M.H. Ellisman, and R.Y. Tsien The fluorescent toolbox for assessing protein location and function Science 312 2006 217 224
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 43
    • 79957843777 scopus 로고    scopus 로고
    • Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics
    • B. Wu, K.D. Piatkevich, T. Lionnet, R.H. Singer, and V.V. Verkhusha Modern fluorescent proteins and imaging technologies to study gene expression, nuclear localization, and dynamics Curr Opin Cell Biol 23 2011 310 317
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 310-317
    • Wu, B.1    Piatkevich, K.D.2    Lionnet, T.3    Singer, R.H.4    Verkhusha, V.V.5
  • 44
    • 4244082343 scopus 로고    scopus 로고
    • Shedding light on cell signaling: Interpretation of FRET biosensors
    • F. Gaits, and K. Hahn Shedding light on cell signaling: interpretation of FRET biosensors Sci STKE 165 2003 PE3
    • (2003) Sci STKE , vol.165 , pp. 3
    • Gaits, F.1    Hahn, K.2
  • 45
    • 70349124959 scopus 로고    scopus 로고
    • Fluorescent biosensors for real-time tracking of post-translational modification dynamics
    • N.-N. Aye-Han, N. Qiang, and J. Zhang Fluorescent biosensors for real-time tracking of post-translational modification dynamics Curr Opin Chem Biol 13 2009 392 397
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 392-397
    • Aye-Han, N.-N.1    Qiang, N.2    Zhang, J.3
  • 47
    • 0035903217 scopus 로고    scopus 로고
    • A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the crkii adaptor protein in vivo
    • DOI 10.1074/jbc.M104341200
    • K. Kurokawa, N. Mochizuki, Y. Ohba, H. Mizuno, A. Miyawakiand, and M. Matsuda A pair of fluorescent resonance energy transfer-based probes for tyrosine phosphorylation of the CrkII adaptor protein in vivo J Biol Chem 276 2001 31305 31310 (Pubitemid 37385001)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.33 , pp. 31305-31310
    • Kurokawa, K.1    Mochizuki, N.2    Ohba, Y.3    Mizuno, H.4    Miyawaki, A.5    Matsuda, M.6
  • 48
    • 77955099778 scopus 로고    scopus 로고
    • A novel FRET-based biosensor for the measurement of BCR-ABL activity and its response to drugs in living cells
    • T. Mizutani, T. Kondo, S. Darmanin, M. Tsuda, S. Tanaka, and M. Tobiume A novel FRET-based biosensor for the measurement of BCR-ABL activity and its response to drugs in living cells Clin Cancer Res 16 2010 3964 3975
    • (2010) Clin Cancer Res , vol.16 , pp. 3964-3975
    • Mizutani, T.1    Kondo, T.2    Darmanin, S.3    Tsuda, M.4    Tanaka, S.5    Tobiume, M.6
  • 50
    • 57349145336 scopus 로고    scopus 로고
    • Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains
    • X. Gao, and J. Zhang Spatiotemporal analysis of differential Akt regulation in plasma membrane microdomains Mol Biol Cell 19 2008 4366 4373
    • (2008) Mol Biol Cell , vol.19 , pp. 4366-4373
    • Gao, X.1    Zhang, J.2
  • 51
    • 0042733215 scopus 로고    scopus 로고
    • Fluorescent indicators for Akt/protein kinase B and dynamics of Akt activity visualized in living cells
    • DOI 10.1074/jbc.M212167200
    • 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 2003 30945 30951 (Pubitemid 36994606)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.33 , pp. 30945-30951
    • Sasaki, K.1    Sato, M.2    Umezawa, Y.3
  • 52
    • 14044266297 scopus 로고    scopus 로고
    • Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter
    • DOI 10.1074/jbc.M411534200
    • M.T. Kunkel, Q. Ni, R.Y. Tsien, J. Zhang, and A.C. Newton Spatio-temporal dynamics of protein kinase B/Akt signaling revealed by a genetically encoded fluorescent reporter J Biol Chem 280 2005 5581 5587 (Pubitemid 40280036)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.7 , pp. 5581-5587
    • Kunkel, M.T.1    Ni, Q.2    Tsien, R.Y.3    Zhang, J.4    Newton, A.C.5
  • 53
    • 79953732149 scopus 로고    scopus 로고
    • A fluorescent reporter of AMPK activity and cellular energy stress
    • P. Tsou, B. Zheng, C.-H. Hsu, A.T. Sasaki, and L.C. Cantley A fluorescent reporter of AMPK activity and cellular energy stress Cell Metab 13 2011 476 486
    • (2011) Cell Metab , vol.13 , pp. 476-486
    • Tsou, P.1    Zheng, B.2    Hsu, C.-H.3    Sasaki, A.T.4    Cantley, L.C.5
  • 54
    • 34547824221 scopus 로고    scopus 로고
    • Monitoring ATM kinase activity in living cells
    • DOI 10.1016/j.dnarep.2007.02.025, PII S1568786407000742
    • S.A. Johnson, Y. Zhongsheng, and T. Hunter Monitoring ATM kinase activity in living cells DNA Repair (Amst) 6 2007 1277 1284 (Pubitemid 47238681)
    • (2007) DNA Repair , vol.6 , Issue.9 , pp. 1277-1284
    • Johnson, S.A.1    You, Z.2    Hunter, T.3
  • 55
    • 80052962709 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer-based sensor Camui provides new insight into mechanisms of calcium/calmodulin-dependent protein kinase II activation in intact cardiomyocytes
    • J.R. Erickson, R. Patel, A. Ferguson, J. Bossuyt, and D.M. Bers Fluorescence resonance energy transfer-based sensor Camui provides new insight into mechanisms of calcium/calmodulin-dependent protein kinase II activation in intact cardiomyocytes Circ Res 109 2011 729 738
    • (2011) Circ Res , vol.109 , pp. 729-738
    • Erickson, J.R.1    Patel, R.2    Ferguson, A.3    Bossuyt, J.4    Bers, D.M.5
  • 56
    • 77951184302 scopus 로고    scopus 로고
    • Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis
    • O. Gavet, and J. Pines Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis Dev Cell 18 2010 533 543
    • (2010) Dev Cell , vol.18 , pp. 533-543
    • Gavet, O.1    Pines, J.2
  • 58
    • 33947361161 scopus 로고    scopus 로고
    • Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells
    • DOI 10.1021/ac062171d
    • M. Sato, Y. Kawai, and Y. Umezawa Genetically encoded fluorescent indicators to visualize protein phosphorylation by extracellular signal-regulated kinase in single living cells Anal Chem 79 2007 2570 2575 (Pubitemid 46449042)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2570-2575
    • Sato, M.1    Kawai, Y.2    Umezawa, Y.3
  • 59
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • DOI 10.1038/nbt0302-287
    • M. Sato, T. Ozawa, K. Inukai, T. Asano, and Y. Umezawa Fluorescent indicators for imaging protein phosphorylation in single living cells Nat Biotechnol 20 2002 287 294 (Pubitemid 34205423)
    • (2002) Nature Biotechnology , vol.20 , Issue.3 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 60
    • 77950434011 scopus 로고    scopus 로고
    • Visualization of JNK activity dynamics with a genetically-encoded fluorescent biosensor
    • M. Fosbrink, N.N. Aye-Han, R. Cheong, A. Levchenko, and J. Zhang Visualization of JNK activity dynamics with a genetically-encoded fluorescent biosensor Proc Natl Acad Sci USA 107 2010 5459 5464
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5459-5464
    • Fosbrink, M.1    Aye-Han, N.N.2    Cheong, R.3    Levchenko, A.4    Zhang, J.5
  • 61
    • 79960903742 scopus 로고    scopus 로고
    • Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer
    • J. Seong, M. Ouyang, T. Kim, J. Sun, P.C. Wen, and S. Lu Detection of focal adhesion kinase activation at membrane microdomains by fluorescence resonance energy transfer Nat Commun 2 2011 406
    • (2011) Nat Commun , vol.2 , pp. 406
    • Seong, J.1    Ouyang, M.2    Kim, T.3    Sun, J.4    Wen, P.C.5    Lu, S.6
  • 62
    • 4544361391 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter of histone phosphorylation in living cells
    • DOI 10.1002/anie.200353375
    • C.W. Lin, and A.Y. Ting A genetically encoded fluorescent reporter of histone phosphorylation in living cells Angew Chem Int Ed Engl 43 2004 2940 2943 (Pubitemid 39257650)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.22 , pp. 2940-2943
    • Lin, C.-W.1    Ting, A.Y.2
  • 63
    • 0037017397 scopus 로고    scopus 로고
    • A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows
    • DOI 10.1083/jcb.200110161
    • T.L. Chew, W.A. Wolf, P.J. Gallagher, F. Matsumura, and R.L. Chisholm A fluorescent resonant energy transfer-based biosensor reveals transient and regional myosin light chain kinase activation in lamella and cleavage furrows J Cell Biol 156 2002 543 553 (Pubitemid 34839901)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 543-553
    • Chew, T.-L.1    Wolf, W.A.2    Gallagher, P.J.3    Matsumura, F.4    Chisholm, R.L.5
  • 66
    • 25644446102 scopus 로고    scopus 로고
    • Insulin disrupts β-adrenergic signalling to protein kinase A in adipocytes
    • DOI 10.1038/nature04140, PII N04140
    • J. Zhang Insulin disrupts beta-adrenergic signalling to protein kinase A in adipocytes Nature 437 2005 569 573 (Pubitemid 41613556)
    • (2005) Nature , vol.437 , Issue.7058 , pp. 569-573
    • Zhang, J.1    Hupfeld, C.J.2    Taylor, S.S.3    Olefsky, J.M.4    Tsien, R.Y.5
  • 67
    • 33746907024 scopus 로고    scopus 로고
    • Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters
    • DOI 10.1016/j.bbrc.2006.07.136, PII S0006291X06016925
    • M.D. Allen, and J. Zhang Subcellular dynamics of protein kinase A activity visualized by FRET-based reporters Biochem Biophys Res Commun 348 2006 716 721 (Pubitemid 44188622)
    • (2006) Biochemical and Biophysical Research Communications , vol.348 , Issue.2 , pp. 716-721
    • Allen, M.D.1    Zhang, J.2
  • 68
    • 78651369353 scopus 로고    scopus 로고
    • FRET-based direct detection of dynamic protein kinase A activity on the sarcoplasmic reticulum in cardiomyocytes
    • S. Liu, J. Zhang, and Y.K. Xiang FRET-based direct detection of dynamic protein kinase A activity on the sarcoplasmic reticulum in cardiomyocytes Biochem Biophys Res Commun 404 2011 581 586
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 581-586
    • Liu, S.1    Zhang, J.2    Xiang, Y.K.3
  • 69
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • DOI 10.1083/jcb.200302125
    • J.D. Violin, J. Zhang, R.Y. Tsien, and A.C. Newton A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C J Cell Biol 161 2003 899 909 (Pubitemid 36718423)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 70
    • 78650635555 scopus 로고    scopus 로고
    • Protein kinase C (delta)-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases
    • T. Kajimoto, S. Sawamura, Y. Tohyama, Y. Mori, and A.C. Newton Protein kinase C (delta)-specific activity reporter reveals agonist-evoked nuclear activity controlled by Src family of kinases J Biol Chem 285 2010 41896 41910
    • (2010) J Biol Chem , vol.285 , pp. 41896-41910
    • Kajimoto, T.1    Sawamura, S.2    Tohyama, Y.3    Mori, Y.4    Newton, A.C.5
  • 73
    • 34250338923 scopus 로고    scopus 로고
    • Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter
    • DOI 10.1074/jbc.M608086200
    • M.T. Kunkel, A. Toker, R.Y. Tsien, and A.C. Newton Calcium-dependent regulation of protein kinase D revealed by a genetically encoded kinase activity reporter J Biol Chem 282 2007 6733 6742 (Pubitemid 47100892)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6733-6742
    • Kunkel, M.T.1    Toker, A.2    Tsien, R.Y.3    Newton, A.C.4
  • 74
    • 51349144633 scopus 로고    scopus 로고
    • Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery
    • L. Macůrek, A. Lindqvist, D. Lim, M.A. Lampson, R. Klompmaker, and R. Freire Polo-like kinase-1 is activated by aurora A to promote checkpoint recovery Nature 455 2008 119 124
    • (2008) Nature , vol.455 , pp. 119-124
    • MacŮrek, L.1    Lindqvist, A.2    Lim, D.3    Lampson, M.A.4    Klompmaker, R.5    Freire, R.6
  • 75
    • 71949090473 scopus 로고    scopus 로고
    • Stimulus-specific distinctions in spatial and temporal dynamics of stress-activated protein kinase kinase kinases revealed by a fluorescence resonance energy transfer biosensor
    • T. Tomida, M. Takekawa, P. O'Grady, and H. Saito Stimulus-specific distinctions in spatial and temporal dynamics of stress-activated protein kinase kinase kinases revealed by a fluorescence resonance energy transfer biosensor Mol Cell Biol 29 2009 6117 6127
    • (2009) Mol Cell Biol , vol.29 , pp. 6117-6127
    • Tomida, T.1    Takekawa, M.2    O'Grady, P.3    Saito, H.4
  • 77
    • 34249306702 scopus 로고    scopus 로고
    • Epidermal growth factor directs sex-specific steroid signaling through Src activation
    • DOI 10.1074/jbc.M610444200
    • T. Hitosugi, K. Sasaki, M. Sato, Y. Suzuki, and Y. Umezawa Epidermal growth factor directs sex-specific steroid signaling through Src activation J Biol Chem 282 2007 10697 10706 (Pubitemid 47093460)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.14 , pp. 10697-10706
    • Hitosugi, T.1    Sasaki, K.2    Sato, M.3    Suzuki, Y.4    Umezawa, Y.5
  • 78
    • 84863023763 scopus 로고    scopus 로고
    • A FRET-based biosensor for imaging Syk activities in living cells
    • X. Xiang, J. Sun, J. Wu, H.T. He, Y. Wang, and C. Zhu A FRET-based biosensor for imaging Syk activities in living cells Cell Mol Bioeng 4 2011 670 677
    • (2011) Cell Mol Bioeng , vol.4 , pp. 670-677
    • Xiang, X.1    Sun, J.2    Wu, J.3    He, H.T.4    Wang, Y.5    Zhu, C.6
  • 79
    • 45249124996 scopus 로고    scopus 로고
    • Dependent FRET based biosensor reveals kinase activity at both the immunological synapse and the antisynapse
    • C. Randriamampita, P. Mouchacca, B. Malissen, D. Marguet, A. Trautmann, and A.C. Lellouch Dependent FRET based biosensor reveals kinase activity at both the immunological synapse and the antisynapse PLoS One 3 2008 e1521
    • (2008) PLoS One , vol.3 , pp. 1521
    • Randriamampita, C.1    Mouchacca, P.2    Malissen, B.3    Marguet, D.4    Trautmann, A.5    Lellouch, A.C.6
  • 80
    • 0033613857 scopus 로고    scopus 로고
    • Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo
    • DOI 10.1074/jbc.274.5.2893
    • J.A. Smith Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo J Biol Chem 274 1999 2893 2898 (Pubitemid 29075375)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 2893-2898
    • Smith, J.A.1    Poteet-Smith, C.E.2    Malarkey, K.3    Sturgill, T.W.4
  • 81
    • 0033529034 scopus 로고    scopus 로고
    • Protein modification: Docking sites for kinases
    • P.M. Holland, and J.A. Cooper Protein modification: docking sites for kinases Curr Biol 9 1999 R329 R331
    • (1999) Curr Biol , vol.9
    • Holland, P.M.1    Cooper, J.A.2
  • 82
    • 35948997760 scopus 로고    scopus 로고
    • Use of docking peptides to design modular substrates with high efficiency for mitogen-activated protein kinase extracellular signal-regulated kinase
    • DOI 10.1021/cb700158q
    • N. Fernandes Use of docking peptides to design modular substrates with high efficiency for mitogen-activated protein kinase extracellular signal-regulated kinase ACS Chem Biol 2 2007 665 673 (Pubitemid 350066015)
    • (2007) ACS Chemical Biology , vol.2 , Issue.10 , pp. 665-673
    • Fernandes, N.1    Bailey, D.E.2    Van Vranken, D.L.3    Allbritton, N.L.4
  • 83
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • DOI 10.1016/S0955-0674(00)00189-7
    • M.B. Yaffe, and A.E. Elia Phosphoserine/threonine-binding domains Curr Opin Cell Biol 13 2001 131 138 (Pubitemid 32209212)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.2 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.H.2
  • 84
    • 0036518996 scopus 로고    scopus 로고
    • Phosphotyrosine-binding domains in signal transduction
    • M.B. Yaffe Phosphotyrosine-binding domains in signal transduction Nat Rev Mol Cell Biol 3 2002 177 186
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 177-186
    • Yaffe, M.B.1
  • 86
    • 63749127483 scopus 로고    scopus 로고
    • Kinome signaling through regulated protein-protein interactions in normal and cancer cells
    • T. Pawson, and M. Kofler Kinome signaling through regulated protein-protein interactions in normal and cancer cells Curr Opin Cell Biol 21 2009 147 153
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 147-153
    • Pawson, T.1    Kofler, M.2
  • 87
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • D. Durocher The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms Mol Cell 6 2000 1169 1182
    • (2000) Mol Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1
  • 88
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine- or phosphothreonine-binding modules
    • P.J. Lu Function of WW domains as phosphoserine- or phosphothreonine- binding modules Science 283 1999 1325 1328
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.J.1
  • 89
    • 3843100686 scopus 로고    scopus 로고
    • The Polo-box domain: A molecular integrator of mitotic kinase cascades and Polo-like kinase function
    • D.M. Lowery, D.H. Mohammad, A.E. Elia, and M.B. Yaffe The Polo-box domain: a molecular integrator of mitotic kinase cascades and Polo-like kinase function Cell Cycle 3 2004 128 131 (Pubitemid 40268680)
    • (2004) Cell Cycle , vol.3 , Issue.2 , pp. 128-131
    • Lowery, D.M.1    Mohammed, D.H.2    Elia, A.E.H.3    Yaffe, M.B.4
  • 90
    • 81055138866 scopus 로고    scopus 로고
    • A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors
    • A. Ibraheem A bacteria colony-based screen for optimal linker combinations in genetically encoded biosensors BMC Biotechnol 11 2011 105
    • (2011) BMC Biotechnol , vol.11 , pp. 105
    • Ibraheem, A.1
  • 91
    • 79960490475 scopus 로고    scopus 로고
    • Rapid development of genetically encoded FRET reporters
    • A. Piljic Rapid development of genetically encoded FRET reporters ACS Chem Biol 6 2011 685 691
    • (2011) ACS Chem Biol , vol.6 , pp. 685-691
    • Piljic, A.1
  • 92
    • 82655181489 scopus 로고    scopus 로고
    • Development of an optimized backbone of FRET biosensors for kinases and GTPases
    • N. Komatsu, K. Aoki, M. Yamada, H. Yukinaga, Y. Fujita, and Y. Kamioka Development of an optimized backbone of FRET biosensors for kinases and GTPases Mol Biol Cell 22 2011 4647 4656
    • (2011) Mol Biol Cell , vol.22 , pp. 4647-4656
    • Komatsu, N.1    Aoki, K.2    Yamada, M.3    Yukinaga, H.4    Fujita, Y.5    Kamioka, Y.6
  • 93
    • 21444436724 scopus 로고    scopus 로고
    • Evolutionary optimization of fluorescent proteins for intracellular FRET
    • DOI 10.1038/nbt1066
    • A.W. Nguyen, and P.S. Daugherty Evolutionary optimization of fluorescent proteins for intracellular FRET Nat Biotechnol 23 2005 355 360 (Pubitemid 41094425)
    • (2005) Nature Biotechnology , vol.23 , Issue.3 , pp. 355-360
    • Nguyen, A.W.1    Daugherty, P.S.2
  • 94
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • D.M. Chudakov, M.V. Matz, S. Lukyanov, and K.A. Lukyanov Fluorescent proteins and their applications in imaging living cells and tissues Physiol Rev 90 2010 1103 1163
    • (2010) Physiol Rev , vol.90 , pp. 1103-1163
    • Chudakov, D.M.1    Matz, M.V.2    Lukyanov, S.3    Lukyanov, K.A.4
  • 95
    • 77955119704 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer biosensors for cancer detection and evaluation of drug efficacy
    • S. Lu, and Y. Wang Fluorescence resonance energy transfer biosensors for cancer detection and evaluation of drug efficacy Clin Cancer Res 16 2010 3822 3824
    • (2010) Clin Cancer Res , vol.16 , pp. 3822-3824
    • Lu, S.1    Wang, Y.2
  • 96
    • 78649650268 scopus 로고    scopus 로고
    • Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia
    • A. Tunceroglu, M. Matsuda, and R.B. Birge Real-time fluorescent resonance energy transfer analysis to monitor drug resistance in chronic myelogenous leukemia Mol Cancer Ther 9 2010 3065 3073
    • (2010) Mol Cancer Ther , vol.9 , pp. 3065-3073
    • Tunceroglu, A.1    Matsuda, M.2    Birge, R.B.3
  • 97
    • 7944231535 scopus 로고    scopus 로고
    • The road to Src
    • DOI 10.1038/sj.onc.1208077
    • G.S. Martin The road to Src Oncogene 23 2004 7910 7917 (Pubitemid 39468850)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7910-7917
    • Martin, G.S.1
  • 98
    • 33746671852 scopus 로고    scopus 로고
    • The Syk tyrosine kinase: A new negative regulator in tumor growth and progression
    • DOI 10.1016/j.canlet.2005.11.004, PII S0304383505009869
    • P.J. Coopman, and S.C. Mueller The Syk tyrosine kinase: a new negative regulator in tumor growth and progression Cancer Lett 241 2006 159 173 (Pubitemid 44163045)
    • (2006) Cancer Letters , vol.241 , Issue.2 , pp. 159-173
    • Coopman, P.J.1    Mueller, S.C.2
  • 100
    • 80054729071 scopus 로고    scopus 로고
    • Using FRET-based reporters to visualize subcellular dynamics of protein kinase A activity
    • C. Depry, and J. Zhang Using FRET-based reporters to visualize subcellular dynamics of protein kinase A activity Methods Mol Biol 756 2011 285 294
    • (2011) Methods Mol Biol , vol.756 , pp. 285-294
    • Depry, C.1    Zhang, J.2
  • 101
    • 0034194092 scopus 로고    scopus 로고
    • Identification of PKC-isoform-specific biological actions using pharmacological approaches
    • DOI 10.1016/S0165-6147(00)01468-1, PII S0165614700014681
    • K.J. Way, E. Chou, and G.L. King Identification of PKC-isoform specific biological actions using pharmacological approaches Trends Pharmacol Sci 21 2000 181 187 (Pubitemid 30243200)
    • (2000) Trends in Pharmacological Sciences , vol.21 , Issue.5 , pp. 181-187
    • Way, K.J.1    Chou, E.2    King, G.L.3
  • 102
    • 34250788809 scopus 로고    scopus 로고
    • AKT/PKB signalling: Navigating downstream
    • B.D. Manning, and L.C. Cantley AKT/PKB signalling: navigating downstream Cell 129 2007 1261 1274
    • (2007) Cell , vol.129 , pp. 1261-1274
    • Manning, B.D.1    Cantley, L.C.2
  • 103
    • 33645287685 scopus 로고    scopus 로고
    • Akt/PKB signalling in cancer: A function in cell motility and invasion
    • M. Yoeli-Lerner, and A. Toker Akt/PKB signalling in cancer: a function in cell motility and invasion Cell Cycle 5 2006 603 605
    • (2006) Cell Cycle , vol.5 , pp. 603-605
    • Yoeli-Lerner, M.1    Toker, A.2
  • 104
    • 2942530310 scopus 로고    scopus 로고
    • ERK and p38 MAPK-activated protein kinases: A family of protein kinases with diverse biological functions
    • DOI 10.1128/MMBR.68.2.320-344.2004
    • P.P. Roux, and J. Blenis ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions Microbiol Mol Biol Rev 68 2004 320 344 (Pubitemid 38756868)
    • (2004) Microbiology and Molecular Biology Reviews , vol.68 , Issue.2 , pp. 320-344
    • Roux, P.P.1    Blenis, J.2
  • 105
    • 74049147038 scopus 로고    scopus 로고
    • Monitoring protein interactions and dynamics with solvatochromic fluorophores
    • G.S. Loving, M. Sainlos, and B. Imperiali Monitoring protein interactions and dynamics with solvatochromic fluorophores Trends Biotechnol 28 2010 73 83
    • (2010) Trends Biotechnol , vol.28 , pp. 73-83
    • Loving, G.S.1    Sainlos, M.2    Imperiali, B.3
  • 106
    • 42449100481 scopus 로고    scopus 로고
    • Bright ideas for chemical biology
    • L.D. Lavis, and R.T. Raines Bright ideas for chemical biology ACS Chem Biol 3 2008 142 155
    • (2008) ACS Chem Biol , vol.3 , pp. 142-155
    • Lavis, L.D.1    Raines, R.T.2
  • 107
    • 42049095153 scopus 로고    scopus 로고
    • Cell-penetrating peptides: From molecular mechanisms to therapeutics
    • DOI 10.1042/BC20070116
    • M.C. Morris, S. Deshayes, F. Heitz, and G. Divita Cell-penetrating peptides: from molecular mechanisms to therapeutics Biol Cell 100 2008 201 217 (Pubitemid 351517084)
    • (2008) Biology of the Cell , vol.100 , Issue.4 , pp. 201-217
    • Morris, M.C.1    Deshayes, S.2    Heitz, F.3    Divita, G.4
  • 108
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: From molecular mechanisms to therapeutics
    • F. Heitz, M.C. Morris, and G. Divita Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics Br J Pharmacol 157 2009 195 206
    • (2009) Br J Pharmacol , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 111
    • 19744378995 scopus 로고    scopus 로고
    • Phosphorylation-driven protein-protein interactions: A protein kinase sensing system
    • DOI 10.1021/ja050789j
    • Q. Wang, and D.S. Lawrence Phosphorylation-driven protein-protein interactions: a protein kinase sensing system J Am Chem Soc 127 2005 7684 7685 (Pubitemid 40745950)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.21 , pp. 7684-7685
    • Wang, Q.1    Lawrence, D.S.2
  • 112
    • 79959379424 scopus 로고    scopus 로고
    • A biosensor generated via high-throughput screening quantifies cell edge Src dynamics
    • A. Gulyani, E. Vitriol, R. Allen, J. Wu, D. Gremyachinskiy, and S. Lewis A biosensor generated via high-throughput screening quantifies cell edge Src dynamics Nat Chem Biol 7 2011 437 444
    • (2011) Nat Chem Biol , vol.7 , pp. 437-444
    • Gulyani, A.1    Vitriol, E.2    Allen, R.3    Wu, J.4    Gremyachinskiy, D.5    Lewis, S.6
  • 113
    • 80054767002 scopus 로고    scopus 로고
    • Fluorescent peptide biosensor for probing the relative abundance of cyclin-dependent kinases in living cells
    • L. Kurzawa, M. Pellerano, J.B. Coppolani, and M.C. Morris Fluorescent peptide biosensor for probing the relative abundance of cyclin-dependent kinases in living cells PLoS One 6 2011 e26555
    • (2011) PLoS One , vol.6 , pp. 26555
    • Kurzawa, L.1    Pellerano, M.2    Coppolani, J.B.3    Morris, M.C.4
  • 115
    • 0037123172 scopus 로고    scopus 로고
    • Design and synthesis of a fluorescent reporter of protein kinase activity
    • DOI 10.1021/ja017530v
    • C.A. Chen, R.H. Yeh, and D.S. Lawrence Design and synthesis of a fluorescent reporter of protein kinase activity J Am Chem Soc 124 2002 3840 3841 (Pubitemid 34310893)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.15 , pp. 3840-3841
    • Chen, C.-A.1    Yeh, R.-H.2    Lawrence, D.S.3
  • 117
    • 0344443386 scopus 로고    scopus 로고
    • Versatile fluorescence probes of protein kinase activity
    • DOI 10.1021/ja0380502
    • M.D. Shults, and B. Imperiali Versatile fluorescence probes of protein kinase activity J Am Chem Soc 125 2003 14248 14249 (Pubitemid 37452343)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.47 , pp. 14248-14249
    • Shults, M.D.1    Imperiali, B.2
  • 118
    • 33646164175 scopus 로고    scopus 로고
    • Optimal Sox-based fluorescent chemosensor design for serine/threonine protein kinases
    • M.D. Shults, D. Carrico-Moniz, and B. Imperiali Optimal Sox-based fluorescent chemosensor design for serine/threonine protein kinases Anal Biochem 352 2006 198 207
    • (2006) Anal Biochem , vol.352 , pp. 198-207
    • Shults, M.D.1    Carrico-Moniz, D.2    Imperiali, B.3
  • 119
    • 18744408814 scopus 로고    scopus 로고
    • A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates
    • DOI 10.1038/nmeth747
    • M.D. Shults, K.A. Janes, D.A. Lauffenburger, and B. Imperiali A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates Nat Methods 2 2005 277 283 (Pubitemid 41131009)
    • (2005) Nature Methods , vol.2 , Issue.4 , pp. 277-283
    • Shults, M.D.1    Janes, K.A.2    Lauffenburger, D.A.3    Imperiali, B.4
  • 120
    • 52449096942 scopus 로고    scopus 로고
    • Recognition-domain focused chemosensors: Versatile and efficient reporters of protein kinase activity
    • E. Luković, J.A. González-Vera, and B. Imperiali Recognition-domain focused chemosensors: versatile and efficient reporters of protein kinase activity J Am Chem Soc 130 2008 12821 12827
    • (2008) J Am Chem Soc , vol.130 , pp. 12821-12827
    • Luković, E.1    González-Vera, J.A.2    Imperiali, B.3
  • 121
    • 59649083677 scopus 로고    scopus 로고
    • A rapid method for generation of selective sox-based chemosensors of Ser/Thr kinases using combinatorial peptide libraries
    • J.A. González-Vera, E. Luković, and B. Imperiali A rapid method for generation of selective sox-based chemosensors of Ser/Thr kinases using combinatorial peptide libraries Bioorg Med Chem Lett 19 2010 1258 1260
    • (2010) Bioorg Med Chem Lett , vol.19 , pp. 1258-1260
    • González-Vera, J.A.1    Luković, E.2    Imperiali, B.3
  • 122
    • 69649085747 scopus 로고    scopus 로고
    • Monitoring protein kinases in cellular media with highly selective chimeric reporters
    • E. Lukovic, E. Vogel Taylor, and B. Imperiali Monitoring protein kinases in cellular media with highly selective chimeric reporters Angew Chem Int Ed Engl 48 2009 6828 6831
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 6828-6831
    • Lukovic, E.1    Vogel Taylor, E.2    Imperiali, B.3
  • 123
    • 79251482450 scopus 로고    scopus 로고
    • A p38α-selective chemosensor for use in unfractionated cell lysates
    • C.I. Stains, E. Luković, and B. Imperiali A p38α-selective chemosensor for use in unfractionated cell lysates ACS Chem Biol 6 2011 101 105
    • (2011) ACS Chem Biol , vol.6 , pp. 101-105
    • Stains, C.I.1    Luković, E.2    Imperiali, B.3
  • 124
    • 34249053810 scopus 로고    scopus 로고
    • Design of a hybrid biosensor for enhanced phosphopeptide recognition based on a phosphoprotein binding domain coupled with a fluorescent chemosensor
    • T. Anai, E. Nakata, Y. Koshi, A. Ojida, and I. Hamachi Design of a hybrid biosensor for enhanced phosphopeptide recognition based on a phosphoprotein binding domain coupled with a fluorescent chemosensor J Am Chem Soc 129 2007 6232 6239
    • (2007) J Am Chem Soc , vol.129 , pp. 6232-6239
    • Anai, T.1    Nakata, E.2    Koshi, Y.3    Ojida, A.4    Hamachi, I.5
  • 125
    • 38349097411 scopus 로고    scopus 로고
    • A luminescent sensor for tyrosine phosphorylation
    • M.S. Tremblay, M. Lee, and D. Sames A luminescent sensor for tyrosine phosphorylation Org Lett 10 2008 5 8
    • (2008) Org Lett , vol.10 , pp. 5-8
    • Tremblay, M.S.1    Lee, M.2    Sames, D.3
  • 129
    • 33947266913 scopus 로고    scopus 로고
    • Deep quench: An expanded dynamic range for protein kinase sensors
    • DOI 10.1021/ja068280r
    • V. Sharma, R.S. Agnes, and D.S. Lawrence Deep quench: an expanded dynamic range for protein kinase sensors J Am Chem Soc 129 2007 2742 2743 (Pubitemid 46417936)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.10 , pp. 2742-2743
    • Sharma, V.1    Agnes, R.S.2    Lawrence, D.S.3
  • 130
    • 77951682590 scopus 로고    scopus 로고
    • Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity
    • R.S. Agnes, F. Jernigan, J.R. Shell, V. Sharma, and D.S. Lawrence Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity J Am Chem Soc 132 2010 6075 6080
    • (2010) J Am Chem Soc , vol.132 , pp. 6075-6080
    • Agnes, R.S.1    Jernigan, F.2    Shell, J.R.3    Sharma, V.4    Lawrence, D.S.5
  • 132
    • 67649458218 scopus 로고    scopus 로고
    • Anion sensor-based ratiometric peptide probe for protein kinase activity
    • K. Kikuchi, S. Hashimoto, S. Mizukami, and T. Nagano Anion sensor-based ratiometric peptide probe for protein kinase activity Org Lett 11 2009 2732 2735
    • (2009) Org Lett , vol.11 , pp. 2732-2735
    • Kikuchi, K.1    Hashimoto, S.2    Mizukami, S.3    Nagano, T.4
  • 133
    • 36048958871 scopus 로고    scopus 로고
    • Visual snapshots of intracellular kinase activity at the onset of mitosis
    • DOI 10.1016/j.chembiol.2007.10.007, PII S1074552107003572
    • Z. Dai, N.G. Dulyaninova, S. Kumar, A.R. Bresnick, and D.S. Lawrence Visual snapshots of intracellular kinase activity at the onset of mitosis Chem Biol 14 2007 1254 1260 (Pubitemid 350102241)
    • (2007) Chemistry and Biology , vol.14 , Issue.11 , pp. 1254-1260
    • Dai, Z.1    Dulyaninova, N.G.2    Kumar, S.3    Bresnick, A.R.4    Lawrence, D.S.5
  • 135
    • 34247851104 scopus 로고    scopus 로고
    • Seeing is believing: Peptide-based fluorescent sensors of protein tyrosine kinase activity
    • DOI 10.1002/cbic.200600473
    • D.S. Lawrence, and Q. Wang Seeing is believing: peptide-based fluorescent sensors of protein tyrosine kinase activity Chembiochem 8 2007 373 378 (Pubitemid 47183654)
    • (2007) ChemBioChem , vol.8 , Issue.4 , pp. 373-378
    • Lawrence, D.S.1    Wang, Q.2
  • 136
    • 38149036581 scopus 로고    scopus 로고
    • Peptide-based fluorescent sensors of protein kinase activity: Design and applications
    • V. Sharma, Q. Wang, and D.S. Lawrence Peptide-based fluorescent sensors of protein kinase activity: design and applications Biochim Biophys Acta 1784 2008 94 99
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 94-99
    • Sharma, V.1    Wang, Q.2    Lawrence, D.S.3
  • 137
    • 70350648894 scopus 로고    scopus 로고
    • Application of metal coordination chemistry to explore and manipulate cell biology
    • K.L. Haas, and K.J. Franz Application of metal coordination chemistry to explore and manipulate cell biology Chem Rev 109 2009 4921 4960
    • (2009) Chem Rev , vol.109 , pp. 4921-4960
    • Haas, K.L.1    Franz, K.J.2
  • 138
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • A. Minta, J.P.Y. Kao, and R.Y. Tsien Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores J Biol Chem 264 1989 8171 8178 (Pubitemid 19137304)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.14 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.Y.2    Tsien, R.Y.3
  • 139
    • 58049202245 scopus 로고    scopus 로고
    • Molecular recognition, fluorescence sensing, and biological assay of phosphate anion derivatives using artificial Zn(II)-Dpa complexes
    • T. Sakamoto, A. Ojida, and I. Hamachi Molecular recognition, fluorescence sensing, and biological assay of phosphate anion derivatives using artificial Zn(II)-Dpa complexes Chem Commun 2 2009 141 152
    • (2009) Chem Commun , vol.2 , pp. 141-152
    • Sakamoto, T.1    Ojida, A.2    Hamachi, I.3
  • 140
    • 77949910887 scopus 로고    scopus 로고
    • Lanthanide-tagged proteins - An illuminating partnership
    • K.N. Allen, and B. Imperiali Lanthanide-tagged proteins - an illuminating partnership Curr Opin Chem Biol 14 2010 247 254
    • (2010) Curr Opin Chem Biol , vol.14 , pp. 247-254
    • Allen, K.N.1    Imperiali, B.2
  • 141
    • 0344494656 scopus 로고    scopus 로고
    • Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan
    • DOI 10.1021/bc0341324
    • N. Marme, J.P. Knemeyer, M. Sauer, and J. Wolfrum Inter- and intramolecular fluorescence quenching of organic dyes by tryptophan Bioconjug Chem 14 2003 1133 1139 (Pubitemid 37449040)
    • (2003) Bioconjugate Chemistry , vol.14 , Issue.6 , pp. 1133-1139
    • Marme, N.1    Knemeyer, J.-P.2    Sauer, M.3    Wolfrum, J.4
  • 142
    • 67650787319 scopus 로고    scopus 로고
    • H-type dimer formation of fluorophores: A mechanism for activatable, in vivo optical molecular imaging
    • M. Ogawa, N. Kosaka, P.L. Choyke, and H. Kobayashi H-type dimer formation of fluorophores: a mechanism for activatable, in vivo optical molecular imaging ACS Chem Biol 4 2009 535 546
    • (2009) ACS Chem Biol , vol.4 , pp. 535-546
    • Ogawa, M.1    Kosaka, N.2    Choyke, P.L.3    Kobayashi, H.4
  • 143
    • 67649243556 scopus 로고    scopus 로고
    • Illuminating the chemistry of life: Design, synthesis, and applications of "caged" and related photoresponsive compounds
    • H.M. Lee, D.R. Larson, and D.S. Lawrence Illuminating the chemistry of life: design, synthesis, and applications of "caged" and related photoresponsive compounds ACS Chem Biol 4 2009 409 427
    • (2009) ACS Chem Biol , vol.4 , pp. 409-427
    • Lee, H.M.1    Larson, D.R.2    Lawrence, D.S.3
  • 144
    • 79960088065 scopus 로고    scopus 로고
    • Physiological relevance of cell cycle kinases
    • M. Malumbres Physiological relevance of cell cycle kinases Physiol Rev 91 2011 973 1007
    • (2011) Physiol Rev , vol.91 , pp. 973-1007
    • Malumbres, M.1
  • 145
    • 33846212350 scopus 로고    scopus 로고
    • Cell cycle kinases in cancer
    • DOI 10.1016/j.gde.2006.12.008, PII S0959437X06002425, Genetic and Cellular mechanisms of oncogenesis
    • M. Malumbres, and M. Barbacid Cell cycle kinases in cancer Curr Opin Genet Dev 17 2007 60 65 (Pubitemid 46109297)
    • (2007) Current Opinion in Genetics and Development , vol.17 , Issue.1 , pp. 60-65
    • Malumbres, M.1    Barbacid, M.2
  • 146
    • 77952154960 scopus 로고    scopus 로고
    • Cell-cycle markers and biosensors
    • L. Kurzawa, and M. Morris Cell-cycle markers and biosensors Chembiochem 11 2010 1037 1047
    • (2010) Chembiochem , vol.11 , pp. 1037-1047
    • Kurzawa, L.1    Morris, M.2
  • 147
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • DOI 10.1146/annurev.cellbio.13.1.261
    • D.O. Morgan Cyclin-dependent kinases: engines, clocks, and microprocessors Annu Rev Cell Dev Biol 13 1997 261 291 (Pubitemid 28034527)
    • (1997) Annual Review of Cell and Developmental Biology , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 148
    • 0036163745 scopus 로고    scopus 로고
    • Regulation of cyclin-Cdk activity in mammalian cells
    • DOI 10.1007/s00018-002-8410-1
    • A.J. Obaya, and J.M. Sedivy Regulation of cyclin-Cdk activity in mammalian cells Cell Mol Life Sci 59 2002 126 142 (Pubitemid 34117361)
    • (2002) Cellular and Molecular Life Sciences , vol.59 , Issue.1 , pp. 126-142
    • Obaya, A.J.1    Sedivy, J.M.2
  • 149
    • 69249230769 scopus 로고    scopus 로고
    • Mammalian cell-cycle regulation: Several Cdks, numerous cyclins and diverse compensatory mechanisms
    • A. Satyanarayana, and P. Kaldis Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms Oncogene 28 2009 2925 2939
    • (2009) Oncogene , vol.28 , pp. 2925-2939
    • Satyanarayana, A.1    Kaldis, P.2
  • 150
    • 33750345725 scopus 로고    scopus 로고
    • Analyzing protein kinase dynamics in living cells with FRET reporters
    • DOI 10.1016/j.ymeth.2006.06.013, PII S1046202306001046
    • Q. Ni, D.V. Titov, and J. Zhang Analyzing protein kinase dynamics in living cells with FRET reporters Methods 40 2006 279 286 (Pubitemid 44635295)
    • (2006) Methods , vol.40 , Issue.3 , pp. 279-286
    • Ni, Q.1    Titov, D.V.2    Zhang, J.3
  • 151
    • 35348887075 scopus 로고    scopus 로고
    • FRET-based biosensors for protein kinases: Illuminating the kinome
    • DOI 10.1039/b706628g
    • J. Zhang, and M.D. Allen FRET-based biosensors for protein kinases: illuminating the kinome Mol Biosyst 3 2007 759 765 (Pubitemid 47587185)
    • (2007) Molecular BioSystems , vol.3 , Issue.11 , pp. 759-765
    • Zhang, J.1    Allen, M.D.2
  • 152
    • 84871063660 scopus 로고    scopus 로고
    • Fluorescent biosensors for cancer cell imaging and diagnostics
    • Science Publishers Victor Preedy Ed
    • M.C. Morris Fluorescent biosensors for cancer cell imaging and diagnostics Biosensor and Cancer 2012 Science Publishers Victor Preedy Ed
    • (2012) Biosensor and Cancer
    • Morris, M.C.1
  • 153
    • 20444432725 scopus 로고    scopus 로고
    • High-throughput screening for kinase inhibitors
    • DOI 10.1002/cbic.200400211
    • O. Von Ahsen, and U. Bomer High throughput screening for kinase inhibitors Chembiochem 6 2005 481 490 (Pubitemid 40868135)
    • (2005) ChemBioChem , vol.6 , Issue.3 , pp. 481-490
    • Von Ahsen, O.1    Bomer, U.2
  • 154
    • 33947147539 scopus 로고    scopus 로고
    • Reading dynamic kinase activity in living cells for high-throughput screening
    • M.D. Allen, L.M. DiPilato, M. Rahdar, Y.R. Ren, C. Chong, and J.O. Liu Reading dynamic kinase activity in living cells for high-throughput screening ACS Chem Biol 1 2006 371 376
    • (2006) ACS Chem Biol , vol.1 , pp. 371-376
    • Allen, M.D.1    Dipilato, L.M.2    Rahdar, M.3    Ren, Y.R.4    Chong, C.5    Liu, J.O.6
  • 155
    • 0032031530 scopus 로고    scopus 로고
    • Fluorescent-protein biosensors: New tools for drug discovery
    • DOI 10.1016/S0167-7799(97)01166-9, PII S0167779997011669
    • K.A. Giuliano, and D.L. Taylor Fluorescent-protein biosensors: new tools for drug discovery Trends Biotechnol 16 1998 135 140 (Pubitemid 28123107)
    • (1998) Trends in Biotechnology , vol.16 , Issue.3 , pp. 135-140
    • Giuliano, K.A.1    Taylor, D.L.2
  • 156
    • 33751219560 scopus 로고    scopus 로고
    • Novel fluorescent proteins for high-content screening
    • DOI 10.1016/j.drudis.2006.09.005, PII S1359644606003667
    • M. Wolff, J. Wiedenmann, G.U. Nienhaus, M. Valler, and R. Heilker Novel fluorescent proteins for high-content screening Drug Discov Today 11 2006 1054 1060 (Pubitemid 44792472)
    • (2006) Drug Discovery Today , vol.11 , Issue.23-24 , pp. 1054-1060
    • Wolff, M.1    Wiedenmann, J.2    Nienhaus, G.U.3    Valler, M.4    Heilker, R.5
  • 160
    • 65449153321 scopus 로고    scopus 로고
    • Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging
    • H.J. Carlson, and R.E. Campbell Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging Curr Opin Biotechnol 20 2009 19 27
    • (2009) Curr Opin Biotechnol , vol.20 , pp. 19-27
    • Carlson, H.J.1    Campbell, R.E.2
  • 161
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • A. Piljic, and C. Schultz Simultaneous recording of multiple cellular events by FRET ACS Chem Biol 3 2008 156 160
    • (2008) ACS Chem Biol , vol.3 , pp. 156-160
    • Piljic, A.1    Schultz, C.2
  • 162
    • 42949146948 scopus 로고    scopus 로고
    • Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors
    • DOI 10.1038/nmeth.1207, PII NMETH.1207
    • H.W. Ai, K.L. Hazelwood, M.W. Davidson, and R.E. Campbell Fluorescent protein FRET pairs for ratiometric imaging of dual biosensors Nat Methods 5 2008 401 403 (Pubitemid 351619097)
    • (2008) Nature Methods , vol.5 , Issue.5 , pp. 401-403
    • Ai, H.-W.1    Hazelwood, K.L.2    Davidson, M.W.3    Campbell, R.E.4
  • 163
    • 67650302266 scopus 로고    scopus 로고
    • Simultaneous live cell imaging using dual FRET sensors with a single excitation light
    • Y. Niino, K. Hotta, and K. Oka Simultaneous live cell imaging using dual FRET sensors with a single excitation light PLoS One 4 2009 e6036
    • (2009) PLoS One , vol.4 , pp. 6036
    • Niino, Y.1    Hotta, K.2    Oka, K.3
  • 164
    • 33846926304 scopus 로고    scopus 로고
    • Fluorescence imaging in vivo: Recent advances
    • DOI 10.1016/j.copbio.2007.01.003, PII S0958166907000043
    • J. Rao, A. Dragulescu-Andrasi, and H. Yao Fluorescence imaging in vivo: recent advances Curr Opin Biotechnol 18 2007 17 25 (Pubitemid 46237739)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.1 , pp. 17-25
    • Rao, J.1    Dragulescu-Andrasi, A.2    Yao, H.3
  • 165
    • 79959420942 scopus 로고    scopus 로고
    • Strategies for in vivo imaging of enzyme activity: An overview and recent advances
    • A. Razgulin, N. Ma, and J. Rao Strategies for in vivo imaging of enzyme activity: an overview and recent advances Chem Soc Rev 40 2011 4186 4216
    • (2011) Chem Soc Rev , vol.40 , pp. 4186-4216
    • Razgulin, A.1    Ma, N.2    Rao, J.3
  • 166
    • 28844463521 scopus 로고    scopus 로고
    • Development of water-soluble far-red fluorogenic dyes for enzyme sensing
    • DOI 10.1016/j.tet.2005.10.020, PII S0040402005018375
    • N. Ho, R. Weissleder, and C.H. Tung Development of water-soluble far-red fluorogenic dyes for enzyme sensing Tetrahedron 62 2006 578 585 (Pubitemid 41779376)
    • (2006) Tetrahedron , vol.62 , Issue.4 , pp. 578-585
    • Ho, N.-H.1    Weissleder, R.2    Tung, C.-H.3
  • 168
    • 41649110649 scopus 로고    scopus 로고
    • Imaging in the era of molecular oncology
    • DOI 10.1038/nature06917, PII NATURE06917
    • R. Weissleder, and M.J. Pittet Imaging in the era of molecular oncology Nature 452 2008 580 589 (Pubitemid 351483372)
    • (2008) Nature , vol.452 , Issue.7187 , pp. 580-589
    • Weissleder, R.1    Pittet, M.J.2
  • 170
    • 33645460264 scopus 로고    scopus 로고
    • Whole-body fluorescence lifetime imaging of a tumor-targeted near-infrared molecular probe in mice
    • S. Bloch, F. Lesage, L. McIntosh, A. Gandjbakhche, K. Liang, and S. Achilefu Whole-body fluorescence lifetime imaging of a tumor-targeted near-infrared molecular probe in mice J Biomed Opt 10 2005 054003
    • (2005) J Biomed Opt , vol.10 , pp. 054003
    • Bloch, S.1    Lesage, F.2    McIntosh, L.3    Gandjbakhche, A.4    Liang, K.5    Achilefu, S.6
  • 171
    • 84871093195 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of kinase signaling visualized by targeted reporters
    • M.T. Kunkel, and A.C. Newton Spatiotemporal dynamics of kinase signaling visualized by targeted reporters Curr Protoc Chem Biol 1 2009 17 18
    • (2009) Curr Protoc Chem Biol , vol.1 , pp. 17-18
    • Kunkel, M.T.1    Newton, A.C.2
  • 172
    • 58149357048 scopus 로고    scopus 로고
    • Selective molecular imaging of viable cancer cells with pH-activatable fluorescence probes
    • Y. Urano, D. Asanuma, Y. Hama, Y. Koyama, T. Barrett, and M. Kamiya Selective molecular imaging of viable cancer cells with pH-activatable fluorescence probes Nat Med 15 2009 104 109
    • (2009) Nat Med , vol.15 , pp. 104-109
    • Urano, Y.1    Asanuma, D.2    Hama, Y.3    Koyama, Y.4    Barrett, T.5    Kamiya, M.6
  • 174
    • 84859005332 scopus 로고    scopus 로고
    • Stable expression of FRET biosensors: A new light in cancer research
    • K. Aoki, N. Komatsu, E. Hirata, Y. Kamioka, and M. Matsuda Stable expression of FRET biosensors: a new light in cancer research Cancer Sci 103 2012 614 619
    • (2012) Cancer Sci , vol.103 , pp. 614-619
    • Aoki, K.1    Komatsu, N.2    Hirata, E.3    Kamioka, Y.4    Matsuda, M.5
  • 175
    • 84862304850 scopus 로고    scopus 로고
    • Live imaging of protein kinase activities in transgenic mice expressing FRET biosensors
    • Y. Kamioka, K. Sumiyama, R. Mizuno, Y. Sakai, E. Hirata, and E. Kiyokawa Live imaging of protein kinase activities in transgenic mice expressing FRET biosensors Cell Struct Funct 37 2012 65 73
    • (2012) Cell Struct Funct , vol.37 , pp. 65-73
    • Kamioka, Y.1    Sumiyama, K.2    Mizuno, R.3    Sakai, Y.4    Hirata, E.5    Kiyokawa, E.6
  • 177
    • 81855205302 scopus 로고    scopus 로고
    • Rapid cancer detection by topically spraying a γ- glutamyltranspeptidase-activated fluorescent probe
    • Y. Urano, M. Sakabe, N. Kosaka, M. Ogawa, M. Mitsunaga, and D. Asanuma Rapid cancer detection by topically spraying a γ-glutamyltranspeptidase- activated fluorescent probe Sci Transl Med 3 2011 110ra119
    • (2011) Sci Transl Med , vol.3
    • Urano, Y.1    Sakabe, M.2    Kosaka, N.3    Ogawa, M.4    Mitsunaga, M.5    Asanuma, D.6
  • 178
    • 67649359994 scopus 로고    scopus 로고
    • RGD-human serum albumin conjugates as efficient tumor targeting probes
    • K. Chen, J. Xie, and X. Chen RGD-human serum albumin conjugates as efficient tumor targeting probes Mol Imaging 8 2009 65 73
    • (2009) Mol Imaging , vol.8 , pp. 65-73
    • Chen, K.1    Xie, J.2    Chen, X.3
  • 179
    • 56949097880 scopus 로고    scopus 로고
    • Characterization and performance of a near-infrared 2-deoxyglucose optical imaging agent for mouse cancer models
    • J.L. Kovar, W. Volcheck, E. Sevick-Muraca, M.A. Simpson, and D.M. Olive Characterization and performance of a near-infrared 2-deoxyglucose optical imaging agent for mouse cancer models Anal Biochem 384 2009 254 262
    • (2009) Anal Biochem , vol.384 , pp. 254-262
    • Kovar, J.L.1    Volcheck, W.2    Sevick-Muraca, E.3    Simpson, M.A.4    Olive, D.M.5


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