메뉴 건너뛰기




Volumn 6, Issue 5, 2014, Pages 1034-1042

Fluorescence lifetime imaging of physiological free Cu(ii) levels in live cells with a Cu(ii)-selective carbonic anhydrase-based biosensor

Author keywords

[No Author keywords available]

Indexed keywords

CYTOLOGY; FLUORESCENCE; METAL IONS; ZINC; ZINC COMPOUNDS;

EID: 84899582519     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c3mt00305a     Document Type: Article
Times cited : (31)

References (59)
  • 2
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • T. V. O'Halloran Transition metals in control of gene expression Science 1993 261 715 725 (Pubitemid 23278386)
    • (1993) Science , vol.261 , Issue.5122 , pp. 715-725
    • O'Halloran, T.V.1
  • 3
    • 33747151612 scopus 로고    scopus 로고
    • Plasma copper, iron, ceruloplasmin and ferroxidase activity in schizophrenia
    • DOI 10.1016/j.schres.2006.05.027, PII S0920996406002532
    • T. L. Wolf J. Kotun J. H. Meador-Woodruff Plasma copper, iron, ceruloplasmin, and ferroxidase activity in schizophrenia Schizophr. Res. 2006 86 167 171 (Pubitemid 44234055)
    • (2006) Schizophrenia Research , vol.86 , Issue.1-3 , pp. 167-171
    • Wolf, T.L.1    Kotun, J.2    Meador-Woodruff, J.H.3
  • 5
    • 61549092140 scopus 로고    scopus 로고
    • New roles for copper metabolism in cell proliferation, signaling, and disease
    • M. L. Turski D. J. Thiele New roles for copper metabolism in cell proliferation, signaling, and disease J. Biol. Chem. 2009 284 2 717 721
    • (2009) J. Biol. Chem. , vol.284 , Issue.2 , pp. 717-721
    • Turski, M.L.1    Thiele, D.J.2
  • 7
    • 0035986679 scopus 로고    scopus 로고
    • Metallochaperones: Bind and deliver
    • DOI 10.1016/S1074-5521(02)00156-4, PII S1074552102001564
    • A. C. Rosenzweig Metallochaperones: Bind and deliver Chem. Biol. 2002 9 673 677 (Pubitemid 34653061)
    • (2002) Chemistry and Biology , vol.9 , Issue.6 , pp. 673-677
    • Rosenzweig, A.C.1
  • 8
    • 34447510930 scopus 로고    scopus 로고
    • Function and regulation of human copper-transporting ATPases
    • DOI 10.1152/physrev.00004.2006
    • S. Lutsenko N. Barnes M. Y. Bartee O. Y. Dmitriev Function and regulation of human copper-transporting ATPases Physiol. Rev. 2007 87 1011 1046 (Pubitemid 47084675)
    • (2007) Physiological Reviews , vol.87 , Issue.3 , pp. 1011-1046
    • Lutsenko, S.1    Barnes, N.L.2    Bartee, M.Y.3    Dmitriev, O.Y.4
  • 9
    • 77951571462 scopus 로고    scopus 로고
    • in, ed. R. D. Kornberg, C. R. H. Raetz, J. E. Rothman and J. W. Thorner, Annual Review of Biochemistry, Annual Reviews, Inc., Palo Alto, 537-562
    • N. J. Robinson and D. R. Winge, in Copper metallochaperones, ed., R. D. Kornberg, C. R. H. Raetz, J. E. Rothman, and, J. W. Thorner, Annual Review of Biochemistry, Annual Reviews, Inc., Palo Alto, 2010, pp. 537-562
    • (2010) Copper Metallochaperones
    • Robinson, N.J.1    Winge, D.R.2
  • 10
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • DOI 10.1126/science.284.5415.805
    • T. D. Rae P. J. Schmidt R. A. Pufahl V. C. Culotta T. V. O'Halloran Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase Science 1999 284 805 808 (Pubitemid 29291346)
    • (1999) Science , vol.284 , Issue.5415 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 11
    • 18544384019 scopus 로고
    • Oxidation of tartaric acid in the presence of iron
    • H. J. H. Fenton Oxidation of tartaric acid in the presence of iron J. Chem. Soc. 1894 65 899 910
    • (1894) J. Chem. Soc. , vol.65 , pp. 899-910
    • Fenton, H.J.H.1
  • 13
    • 0000750473 scopus 로고
    • Metal-binding properties of human erythrocyte carbonic anhydrases
    • S. Lindskog P. O. Nyman Metal-binding properties of human erythrocyte carbonic anhydrases Biochim. Biophys. Acta 1964 85 462 474
    • (1964) Biochim. Biophys. Acta , vol.85 , pp. 462-474
    • Lindskog, S.1    Nyman, P.O.2
  • 16
    • 70350627430 scopus 로고    scopus 로고
    • Structural Biology of Copper Trafficking
    • A. K. Boal A. C. Rosenzweig Structural Biology of Copper Trafficking Chem. Rev. 2009 109 10 4760 4779
    • (2009) Chem. Rev. , vol.109 , Issue.10 , pp. 4760-4779
    • Boal, A.K.1    Rosenzweig, A.C.2
  • 17
    • 34248662942 scopus 로고    scopus 로고
    • Copper entry into human cells: Progress and unanswered questions
    • DOI 10.1007/s10534-006-9066-3, Biometals: function and transport in bacteria, fungi, and humans
    • E. Maryon S. Molloy A. Zimnicka J. Kaplan Copper entry into human cells: progress and unanswered questions Biometals 2007 20 3-4 355 364 (Pubitemid 46776580)
    • (2007) BioMetals , vol.20 , Issue.3-4 , pp. 355-364
    • Maryon, E.B.1    Molloy, S.A.2    Zimnicka, A.M.3    Kaplan, J.H.4
  • 19
    • 80755187849 scopus 로고    scopus 로고
    • Copper: An essential metal in biology
    • R. A. Festa D. J. Thiele Copper: An essential metal in biology Curr. Biol. 2011 21 21 R877 R883
    • (2011) Curr. Biol. , vol.21 , Issue.21
    • Festa, R.A.1    Thiele, D.J.2
  • 20
    • 84864300450 scopus 로고    scopus 로고
    • Charting the travels of copper in eukaryotes from yeast to mammals
    • T. Nevitt H. Öhrvik D. J. Thiele Charting the travels of copper in eukaryotes from yeast to mammals Biochim. Biophys. Acta, Mol. Cell Res. 2012 1823 9 1580 1593
    • (2012) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1823 , Issue.9 , pp. 1580-1593
    • Nevitt, T.1    Öhrvik, H.2    Thiele, D.J.3
  • 21
    • 0034684215 scopus 로고    scopus 로고
    • + during Dioxygen Activation in a Copper Amine Oxidase from Yeast
    • + during Dioxygen Activation in a Copper Amine Oxidase from Yeast J. Am. Chem. Soc. 2000 122 41 9897 9904
    • (2000) J. Am. Chem. Soc. , vol.122 , Issue.41 , pp. 9897-9904
    • Mills, S.A.1    Klinman, J.P.2
  • 22
    • 1242341215 scopus 로고    scopus 로고
    • The multi-functional topa-quinone copper amine oxidases
    • DOI 10.1016/S1570-9639(03)00077-3
    • J. P. Klinman The multi-functional topa-quinone copper amine oxidases Biochim. Biophys. Acta, Proteins Proteomics 2003 1647 1-2 131 137 (Pubitemid 38234645)
    • (2003) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1647 , Issue.1-2 , pp. 131-137
    • Klinman, J.P.1
  • 24
    • 77950394708 scopus 로고    scopus 로고
    • Visualizing ascorbate-triggered release of labile copper within living cells using a ratiometric fluorescence sensor
    • D. W. Domaille L. Zeng C. J. Chang Visualizing ascorbate-triggered release of labile copper within living cells using a ratiometric fluorescence sensor J. Am. Chem. Soc. 2010 132 1194 1195
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1194-1195
    • Domaille, D.W.1    Zeng, L.2    Chang, C.J.3
  • 26
    • 84872777852 scopus 로고    scopus 로고
    • Et al. Fluorescent Ratiometric Indicators Based on Cu(ii)-Induced Changes in Poly(NIPAM) Microparticle Volume
    • J. Osambo W. Seitz D. Kennedy R. Planalp A. Jones R. Jackson et al. Fluorescent Ratiometric Indicators Based on Cu(ii)-Induced Changes in Poly(NIPAM) Microparticle Volume Sensors 2013 13 1 1341 1352
    • (2013) Sensors , vol.13 , Issue.1 , pp. 1341-1352
    • Osambo, J.1    Seitz, W.2    Kennedy, D.3    Planalp, R.4    Jones, A.5    Jackson, R.6
  • 27
    • 79960857894 scopus 로고    scopus 로고
    • Phosphorescent Sensor for Robust Quantification of Copper(ii) Ion
    • Y. You Y. Han Y.-M. Lee S. Y. Park W. Nam S. J. Lippard Phosphorescent Sensor for Robust Quantification of Copper(ii) Ion J. Am. Chem. Soc. 2011 133 30 11488 11491
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.30 , pp. 11488-11491
    • You, Y.1    Han, Y.2    Lee, Y.-M.3    Park, S.Y.4    Nam, W.5    Lippard, S.J.6
  • 28
    • 0346122959 scopus 로고    scopus 로고
    • Real-Time Determination of Picomolar Free Cu(II) in Seawater Using a Fluorescence-Based Fiber Optic Biosensor
    • DOI 10.1021/ac0345401
    • H. H. Zeng R. B. Thompson B. P. Maliwal G. R. Fones J. W. Moffett C. A. Fierke Real-time determination of picomolar free Cu(ii) in seawater using a fluorescence-based fiber optic biosensor Anal. Chem. 2003 75 24 6807 6812 (Pubitemid 37523578)
    • (2003) Analytical Chemistry , vol.75 , Issue.24 , pp. 6807-6812
    • Zeng, H.-H.1    Thompson, R.B.2    Maliwal, B.P.3    Fones, G.R.4    Moffett, J.W.5    Fierkel, C.A.6
  • 29
    • 58249091560 scopus 로고    scopus 로고
    • Et al. Determination of zinc using carbonic anhydrase-based fluorescence biosensors
    • in, ed. L. Brand and M. Johnson, Academic Press, San Diego, 287-309
    • R. Bozym, T. K. Hurst, N. Westerberg, A. Stoddard, C. A. Fierke and C. J. Frederickson, et al. Determination of zinc using carbonic anhydrase-based fluorescence biosensors, in Fluorescence Spectroscopy, ed., L. Brand, and, M. Johnson, Academic Press, San Diego, 2008, pp. 287-309
    • (2008) Fluorescence Spectroscopy
    • Bozym, R.1    Hurst, T.K.2    Westerberg, N.3    Stoddard, A.4    Fierke, C.A.5    Frederickson, C.J.6
  • 31
    • 0029930443 scopus 로고    scopus 로고
    • Fiber optic biosensor for Co(II) and Cu(II) based on fluorescence energy transfer with an enzyme transducer
    • DOI 10.1016/0956-5663(96)83291-X, Surface Characterization and Optical Sensing Methods in Biosensors
    • R. B. Thompson Z. Ge M. W. Patchan C.-c. Huang C. A. Fierke Fiber optic biosensor for Co(ii) and Cu(ii) based on fluorescence energy transfer with an enzyme transducer Biosens. Bioelectron. 1996 11 6 557 564 (Pubitemid 26153667)
    • (1996) Biosensors and Bioelectronics , vol.11 , Issue.6-7 , pp. 557-564
    • Thompson, R.B.1    Ge, Z.2    Patchan, M.3    Huang, C.-C.4    Fierke, C.A.5
  • 32
    • 0032533884 scopus 로고    scopus 로고
    • Determination of picomolar concentrations of metal ions using fluorescence anisotropy: Biosensing with a «reagentless» enzyme transducer
    • R. B. Thompson B. P. Maliwal V. L. Feliccia C. A. Fierke K. McCall Determination of picomolar concentrations of metal ions using fluorescence anisotropy: biosensing with a «reagentless» enzyme transducer Anal. Chem. 1998 70 22 4717 4723
    • (1998) Anal. Chem. , vol.70 , Issue.22 , pp. 4717-4723
    • Thompson, R.B.1    Maliwal, B.P.2    Feliccia, V.L.3    Fierke, C.A.4    McCall, K.5
  • 33
    • 34250916771 scopus 로고
    • Ein fluorometer, apparat zur messung von fluoreszenzabklingungszeiten [A fluorometer for measuring fluorescence lifetime]
    • Z. Gaviola Ein fluorometer, apparat zur messung von fluoreszenzabklingungszeiten [A fluorometer for measuring fluorescence lifetime] Z. Phys. 1926 42 853 861
    • (1926) Z. Phys. , vol.42 , pp. 853-861
    • Gaviola, Z.1
  • 34
    • 84981857769 scopus 로고
    • Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer
    • R. D. Spencer G. Weber Measurements of subnanosecond fluorescence lifetimes with a cross-correlation phase fluorometer Ann. N. Y. Acad. Sci. 1969 158 361 376
    • (1969) Ann. N. Y. Acad. Sci. , vol.158 , pp. 361-376
    • Spencer, R.D.1    Weber, G.2
  • 36
    • 0028673388 scopus 로고
    • Fluorescence lifetime imaging microscopy: Homodyne technique using high-speed gated image intensifier
    • in, ed. M. L. Johnson and L. Brand, Academic Press, New York, 723-748
    • H. Szmacinski, J. R. Lakowicz and M. L. Johnson, Fluorescence lifetime imaging microscopy: homodyne technique using high-speed gated image intensifier, in Numerical Computer Methods, ed., M. L. Johnson, and, L. Brand, Academic Press, New York, 1994, pp. 723-748
    • (1994) Numerical Computer Methods
    • Szmacinski, H.1    Lakowicz, J.R.2    Johnson, M.L.3
  • 37
    • 84882504258 scopus 로고    scopus 로고
    • Fluorescence lifetime biosensing: Entering the mainstream
    • in, ed. F. S. Ligler and C. R. Taitt, Elsevier, Amsterdam, 2nd edn, 287-315
    • R. B. Thompson, Fluorescence lifetime biosensing: Entering the mainstream, in Optical Biosensors: Today and Tomorrow, ed., F. S. Ligler, and, C. R. Taitt, Elsevier, Amsterdam, 2nd edn, 2008, pp. 287-315
    • (2008) Optical Biosensors: Today and Tomorrow
    • Thompson, R.B.1
  • 39
    • 29144446288 scopus 로고    scopus 로고
    • Polar plot representation for frequency-domain analysis of fluorescence lifetimes
    • DOI 10.1007/s10895-005-2990-8
    • G. I. Redford R. M. Clegg Polar plot representation for frequency-domain analysis of fluorescence lifetimes J. Fluoresc. 2005 15 5 805 815 (Pubitemid 41795606)
    • (2005) Journal of Fluorescence , vol.15 , Issue.5 , pp. 805-815
    • Redford, G.I.1    Clegg, R.M.2
  • 41
    • 0012795129 scopus 로고    scopus 로고
    • Serum-free media for neural cell cultures
    • in, ed. S. Federoff and A. Richardson, Humana Press, Totowa, NJ, Third edn, 255-264
    • P. J. Price and G. J. Brewer, Serum-free media for neural cell cultures, in Protocols for Neural Cell Culture, ed., S. Federoff, and, A. Richardson, Humana Press, Totowa, NJ, Third edn 2001, pp. 255-264
    • (2001) Protocols for Neural Cell Culture
    • Price, P.J.1    Brewer, G.J.2
  • 42
    • 33745029895 scopus 로고    scopus 로고
    • Measuring Picomolar Intracellular Exchangeable Zinc in PC-12 Cells Using a Ratiometric Fluorescence Biosensor
    • R. A. Bozym R. B. Thompson A. K. Stoddard C. A. Fierke Measuring Picomolar Intracellular Exchangeable Zinc in PC-12 Cells Using a Ratiometric Fluorescence Biosensor ACS Chem. Biol. 2006 1 2 103 111
    • (2006) ACS Chem. Biol. , vol.1 , Issue.2 , pp. 103-111
    • Bozym, R.A.1    Thompson, R.B.2    Stoddard, A.K.3    Fierke, C.A.4
  • 43
    • 0023990097 scopus 로고
    • Phase fluorimetric measurement for determination of standard lifetimes
    • R. B. Thompson E. Gratton Phase fluorimetric measurement for determination of standard lifetimes Anal. Chem. 1988 60 670 674
    • (1988) Anal. Chem. , vol.60 , pp. 670-674
    • Thompson, R.B.1    Gratton, E.2
  • 44
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • DOI 10.1126/science.285.5433.1569
    • S. R. Schwarze A. Ho A. Vocero-Akbani S. F. Dowdy In vivo protein transduction: Delivery of a biologically active protein into the mouse Science 1999 285 1569 1572 (Pubitemid 29420581)
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 45
    • 77449146289 scopus 로고    scopus 로고
    • Metal ionophores-An emerging class of anticancer drugs
    • W.-Q. Ding S. E. Lind Metal ionophores-An emerging class of anticancer drugs IUBMB Life 2009 61 11 1013 1018
    • (2009) IUBMB Life , vol.61 , Issue.11 , pp. 1013-1018
    • Ding, W.-Q.1    Lind, S.E.2
  • 46
    • 33751223540 scopus 로고    scopus 로고
    • Zinc-buffering capacity of a eukaryotic cell at physiological pZn
    • DOI 10.1007/s00775-006-0150-5
    • A. Krezel W. Maret Zinc-buffering capacity of a eukaryotic cell at physiological pZn JBIC, J. Biol. Inorg. Chem. 2006 11 1049 1062 (Pubitemid 44786393)
    • (2006) Journal of Biological Inorganic Chemistry , vol.11 , Issue.8 , pp. 1049-1062
    • Krezel, A.1    Maret, W.2
  • 47
    • 33947631807 scopus 로고    scopus 로고
    • Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(II) affinity in the picomolar to femtomolar range
    • DOI 10.1021/ja069105d
    • E. M. W. M. v. Dongen T. H. Evers L. M. Dekkers E. W. Meijer L. W. J. Klomp M. Merkx Variation of linker length in ratiometric fluorescent sensor proteins allows rational tuning of Zn(ii) affinity in the picomolar to femtomolar range J. Am. Chem. Soc. 2007 129 3494 3495 (Pubitemid 46502698)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.12 , pp. 3494-3495
    • Van Dongen, E.M.W.M.1    Evers, T.H.2    Dekkers, L.M.3    Meijer, E.W.4    Klomp, L.W.J.5    Merkx, M.6
  • 50
    • 56549089911 scopus 로고    scopus 로고
    • The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green
    • J. Zhao B. A. Bertoglio M. J. Devinney K. E. DInely A. R. Kay The interaction of biological and noxious transition metals with the zinc probes FluoZin-3 and Newport Green Anal. Biochem. 2009 384 34 41
    • (2009) Anal. Biochem. , vol.384 , pp. 34-41
    • Zhao, J.1    Bertoglio, B.A.2    Devinney, M.J.3    Dinely, K.E.4    Kay, A.R.5
  • 51
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • L. L. Kiefer S. A. Paterno C. A. Fierke Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency J. Am. Chem. Soc. 1995 117 6831 6837
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 52
    • 0035693721 scopus 로고    scopus 로고
    • Fluorescence-based biosensing of zinc using carbonic anhydrase
    • DOI 10.1023/A:1012980628412
    • C. A. Fierke R. B. Thompson Fluorescence-based biosensing of zinc using carbonic anhydrase Biometals 2001 14 3-4 205 222 (Pubitemid 34066630)
    • (2001) BioMetals , vol.14 , Issue.3-4 , pp. 205-222
    • Fierke, C.A.1    Thompson, R.B.2
  • 54
    • 1842591322 scopus 로고    scopus 로고
    • Probing Determinants of the Metal Ion Selectivity in Carbonic Anhydrase Using Mutagenesis
    • DOI 10.1021/bi0498914
    • K. A. McCall C. A. Fierke Probing determinants of the metal ion selectivity in carbonic anhydrase using mutagenesis Biochemistry 2004 43 3979 3986 (Pubitemid 38437064)
    • (2004) Biochemistry , vol.43 , Issue.13 , pp. 3979-3986
    • McCall, K.A.1    Fierke, C.A.2
  • 55
    • 0033081703 scopus 로고    scopus 로고
    • Selectivity and sensitivity of fluorescence lifetime-based metal ion biosensing using a carbonic anhydrase transducer
    • DOI 10.1006/abio.1998.2991
    • R. B. Thompson B. P. Maliwal C. A. Fierke Selectivity and sensitivity of fluorescence lifetime-based metal ion biosensing using a carbonic anhydrase transducer Anal. Biochem. 1999 267 185 195 (Pubitemid 29061821)
    • (1999) Analytical Biochemistry , vol.267 , Issue.1 , pp. 185-195
    • Thompson, R.B.1    Maliwal, B.P.2    Fierke, C.A.3
  • 56
    • 0005626480 scopus 로고    scopus 로고
    • Fluorescence-based sensing of transition metal ions by a carbonic anhydrase transducer with a tethered fluorophore
    • ed., SPIE, San Jose, CA, Bellingham, WA
    • Fluorescence-based sensing of transition metal ions by a carbonic anhydrase transducer with a tethered fluorophore, SPIE Conference on Advances in Fluorescence Sensing Technology IV, ed., R. B. Thompson, B. P. Maliwal, and, C. A. Fierke, SPIE, San Jose, CA, 1999, Bellingham, WA
    • (1999) SPIE Conference on Advances in Fluorescence Sensing Technology IV
    • Thompson, R.B.1    Maliwal, B.P.2    Fierke, C.A.3
  • 57
    • 0003831636 scopus 로고
    • U. S. Environmental protection Agency Environmental Research laboratory, Narragansett, Rhode Island
    • G. Thursby, Ambient water quality criteria: saltwater copper addendum, U. S. Environmental protection Agency Environmental Research laboratory, Narragansett, Rhode Island, 1995
    • (1995) Ambient Water Quality Criteria: Saltwater Copper Addendum
    • Thursby, G.1
  • 58
    • 0036765589 scopus 로고    scopus 로고
    • A reevaluation of neuronal zinc measurements: Artifacts associated with high intracellular dye concentration
    • DOI 10.1124/mol.62.3.618
    • K. E. Dinely L. M. Malaiyandi I. J. Reynolds A reevaluation of neuronal zinc measurements: artifacts associated with high intracellular dye concentration Mol. Pharmacol. 2002 62 3 618 627 (Pubitemid 36329380)
    • (2002) Molecular Pharmacology , vol.62 , Issue.3 , pp. 618-627
    • Dineley, K.E.1    Malaiyandi, L.M.2    Reynolds, I.J.3
  • 59
    • 85011235155 scopus 로고    scopus 로고
    • PEBBLE nanosensors for in vitro bioanalysis
    • in, ed. T. Vo-Dinh, CRC Press, Boca Raton, FL, 1-14
    • E. Monson, M. Brasuel, M. A. Philbert and R. Kopelman, PEBBLE nanosensors for in vitro bioanalysis, in Biomedical Photonics Handbook, ed., T. Vo-Dinh, CRC Press, Boca Raton, FL, 2003, pp. 1-14
    • (2003) Biomedical Photonics Handbook
    • Monson, E.1    Brasuel, M.2    Philbert, M.A.3    Kopelman, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.