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Volumn 17, Issue 1, 2012, Pages

ExiFRET: Flexible tool for understanding FRET in complex geometries

Author keywords

Fluorescence; Microscopy; Simulations; Spectroscopy

Indexed keywords

FLUORESCENT DYE; LIPID; PROTEIN;

EID: 84861443604     PISSN: 10833668     EISSN: 15602281     Source Type: Journal    
DOI: 10.1117/1.JBO.17.1.011005     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 84981779372 scopus 로고
    • Zwischenmolekulare Energiewanderung und Fluoreszenz
    • T. Forster, "Zwischenmolekulare Energiewanderung und Fluoreszenz," Annalen der Physik 2(1-2), 55-75 (1948).
    • (1948) Annalen der Physik , vol.2 , Issue.1-2 , pp. 55-75
    • Forster, T.1
  • 2
    • 0036669824 scopus 로고    scopus 로고
    • Measuring protein conformational changes by FRET/LRET
    • DOI 10.1016/S0958-1669(02)00332-4
    • T. Heyduk, "Measuring protein conformational changes by FRET/ LRET," Curr. Opin. Biotechnol. 13(4), 292-296 (2002). (Pubitemid 35254084)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 292-296
    • Heyduk, T.1
  • 4
    • 13844297577 scopus 로고    scopus 로고
    • Imaging protein molecules using FRET and FLIM microscopy
    • DOI 10.1016/j.copbio.2004.12.002, PII S0958166904001673
    • H. Wallrabe and A. Periasamy, "Imaging protein molecules using FRET and FLIM microscopy," Curr. Opin. Biotechnol. 16(1), 19-27 (2005). (Pubitemid 40249755)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.1 SPEC. ISS. , pp. 19-27
    • Wallrabe, H.1    Periasamy, A.2
  • 5
    • 58149201036 scopus 로고    scopus 로고
    • FRET analysis of domain formation and properties in complex membrane systems
    • Sp. Iss. SI)
    • L. Loura, et al., "FRET analysis of domain formation and properties in complex membrane systems," Biochim. Biophys. Acta-Biomembr. 1788(1, Sp. Iss. SI), 209-224 (2009).
    • (2009) Biochim. Biophys. Acta-Biomembr , vol.1788 , Issue.1 , pp. 209-224
    • Loura, L.1
  • 6
    • 33645275730 scopus 로고    scopus 로고
    • Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes
    • J. Silvius and I. Nabi, "Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes," Mol. Membr. Biol. 23(1), 5-16 (2006).
    • (2006) Mol. Membr. Biol , vol.23 , Issue.1 , pp. 5-16
    • Silvius, J.1    Nabi, I.2
  • 7
    • 0036710588 scopus 로고    scopus 로고
    • Peering inside lipid rafts and caveolae
    • DOI 10.1016/S0968-0004(02)02178-3, PII S0968000402021783
    • A. Kenworthy, "Peering inside lipid rafts and caveolae," Trends Biochem. Sci. 27(9), 435-438 (2002). (Pubitemid 35246247)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.9 , pp. 435-438
    • Kenworthy, A.1
  • 8
    • 0037974186 scopus 로고    scopus 로고
    • Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes
    • H. Wallrabe, et al., "Confocal FRET microscopy to measure clustering of ligand-receptor complexes in endocytic membranes," Biophys. J. 85(1), 559-571.
    • Biophys. J , vol.85 , Issue.1 , pp. 559-571
    • Wallrabe, H.1
  • 9
    • 49149120029 scopus 로고    scopus 로고
    • Resonance energy transfer in polymer nanodomains
    • J. Farinha and J. Martinho, "Resonance energy transfer in polymer nanodomains," J. Phys. Chem. C 112(29), 10591-10601 (2008).
    • (2008) J. Phys. Chem. C , vol.112 , Issue.29 , pp. 10591-10601
    • Farinha, J.1    Martinho, J.2
  • 10
    • 14644428986 scopus 로고    scopus 로고
    • Energy transfer study of symmetric polyisoprene-poly(methyl methacrylate) diblock copolymers bearing dyes at the junctions: Dye orientation
    • DOI 10.1021/ma049245c
    • J. Yang, et al., "Energy transfer study of symmetric polyisoprenepoly( methyl methacrylate) diblock copolymers bearing dyes at the junctions: dye orientation," Macromolecules 38(4), 1256-1263 (2005). (Pubitemid 40308184)
    • (2005) Macromolecules , vol.38 , Issue.4 , pp. 1256-1263
    • Yang, J.1    Roller, R.S.2    Winnik, M.A.3    Zhang, Y.4    Pakula, T.5
  • 11
    • 33646715369 scopus 로고    scopus 로고
    • Non-uniform membrane probe distribution in resonance energy transfer: Application to protein-lipid selectivity
    • DOI 10.1007/s10895-005-0036-x
    • R. Capeta, J. Poveda, and L. Loura, "Non-uniform membrane probe distribution in resonance energy transfer: application to protein-lipid selectivity," J. Fluoresc. 16(2), 161-172 (2006). (Pubitemid 43742217)
    • (2006) Journal of Fluorescence , vol.16 , Issue.2 , pp. 161-172
    • Capeta, R.C.1    Poveda, J.A.2    Loura, L.M.S.3
  • 12
    • 32344453443 scopus 로고    scopus 로고
    • Two-dimensional Förster resonance energy transfer (2-D FRET) and the membrane raft hypothesis
    • DOI 10.1016/j.cplett.2005.11.104, PII S000926140501849X
    • M. Acasandrei, et al., "Two-dimensional Forster resonance energy transfer (2-DFRET) and the membrane raft hypothesis," Chem. Phys. Lett. 419(4-6), 469-473 (2006). (Pubitemid 43220514)
    • (2006) Chemical Physics Letters , vol.419 , Issue.4-6 , pp. 469-473
    • Acasandrei, M.A.1    Dale, R.E.2    VandeVen, M.3    Ameloot, M.4
  • 13
    • 34447313944 scopus 로고    scopus 로고
    • Effect of membrane microheterogeneity and domain size on fluorescence resonance energy transfer
    • DOI 10.1529/biophysj.106.090274
    • K. Towles, et al., "Effect of membrane microheterogeneity and domain size on fluorescence resonance energy transfer," Biophys. J. 93(2), 655-667 (2007). (Pubitemid 47057830)
    • (2007) Biophysical Journal , vol.93 , Issue.2 , pp. 655-667
    • Towles, K.B.1    Brown, A.C.2    Wrenn, S.P.3    Dan, N.4
  • 14
    • 43049094118 scopus 로고    scopus 로고
    • Resonance energy transfer study of lysozyme-lipid interactions
    • G. Gorbenko, et al., "Resonance energy transfer study of lysozyme-lipid interactions," Biochim. Biophys. Acta-Biomembr. 1778(5), 1213-1221 (2008).
    • (2008) Biochim. Biophys. Acta-Biomembr , vol.1778 , Issue.5 , pp. 1213-1221
    • Gorbenko, G.1
  • 15
    • 48849099899 scopus 로고    scopus 로고
    • Resonance energy transfer in cells: A new look at fixation effect and receptor aggregation on cell membrane
    • M. Anikovsky, et al., "Resonance energy transfer in cells: a new look at fixation effect and receptor aggregation on cell membrane," Biophys. J. 95(3), 1349-1359 (2008).
    • (2008) Biophys. J , vol.95 , Issue.3 , pp. 1349-1359
    • Anikovsky, M.1
  • 16
    • 77952757509 scopus 로고    scopus 로고
    • Oligomeric size of the M-2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer
    • L. Pisterzi, et al., "Oligomeric size of the M-2 muscarinic receptor in live cells as determined by quantitative fluorescence resonance energy transfer," J. Biol. Chem. 285(22), 16723-16738 (2010).
    • (2010) J. Biol. Chem , vol.285 , Issue.22 , pp. 16723-16738
    • Pisterzi, L.1
  • 17
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • V. Raicu, et al., "Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer," Biochem. J. 385(1), 265-277 (2005).
    • (2005) Biochem. J , vol.385 , Issue.1 , pp. 265-277
    • Raicu, V.1
  • 18
    • 34247599842 scopus 로고    scopus 로고
    • Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: Theory and application
    • DOI 10.1529/biophysj.106.099424
    • E. Yeow and A. Clayton, "Enumeration of oligomerization states of membrane proteins in living cells by homo-FRET spectroscopy and microscopy: theory and application," Biophys. J. 92(9), 3098-3104 (2007). (Pubitemid 46684571)
    • (2007) Biophysical Journal , vol.92 , Issue.9 , pp. 3098-3104
    • Yeow, E.K.L.1    Clayton, A.H.A.2
  • 19
    • 0032988826 scopus 로고    scopus 로고
    • A fluorescence energy transfer method for analyzing protein oligomeric structure: Application to phospholamban
    • M. Li, et al., "A fluorescence energy transfer method for analyzing protein oligomeric structure: application to phospholamban," Biophys. J. 76(5), 2587-2599 (1999). (Pubitemid 29264618)
    • (1999) Biophysical Journal , vol.76 , Issue.5 , pp. 2587-2599
    • Li, M.1    Reddy, L.G.2    Bennett, R.3    Silva Jr., N.D.4    Jones, L.R.5    Thomas, D.D.6
  • 20
    • 0018650688 scopus 로고
    • An analytic solution to the Forster energy transfer problem in two dimensions
    • P. Wolber and B. Hundson, "Analytical solution to the Forster energy transfer problem in 2 dimensions," Biophys. J. 28(2), 197-210 (1979). (Pubitemid 10196482)
    • (1979) Biophysical Journal , vol.28 , Issue.2 , pp. 197-210
    • Wolber, P.K.1    Hudson, B.S.2
  • 21
    • 77952766497 scopus 로고    scopus 로고
    • Comparison between whole distribution- and average-based approaches to the determination of fluorescence resonance energy transfer efficiency in ensembles of proteins in living cells
    • D. Singh and V. Raicu, "Comparison between whole distribution- and average-based approaches to the determination of fluorescence resonance energy transfer efficiency in ensembles of proteins in living cells," Biophys. J. 98(10), 2127-2135 (2010).
    • (2010) Biophys. J , vol.98 , Issue.10 , pp. 2127-2135
    • Singh, D.1    Raicu, V.2
  • 22
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • C. Berney and G. Danuser, "FRET or no FRET: a quantitative comparison," Biophys. J. 84(6), 3992-4010 (2003). (Pubitemid 36637892)
    • (2003) Biophysical Journal , vol.84 , Issue.6 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 23
    • 0037019478 scopus 로고    scopus 로고
    • Dynamic Monte Carlo simulations to model FRET and photobleaching in systems with multiple donor-acceptor interactions
    • DOI 10.1021/jp014549b
    • P. Frederix, et al., "Dynamic Monte Carlo simulations to model FRET and photobleaching in systems with multiple donor-acceptor interactions," J. Phys. Chem. B 106(26), 6793-6801 (2002). (Pubitemid 35281763)
    • (2002) Journal of Physical Chemistry B , vol.106 , Issue.26 , pp. 6793-6801
    • Frederix, P.L.T.M.1    De Beer, E.L.2    Hamelink, W.3    Gerritsen, H.C.4
  • 24
    • 34047195768 scopus 로고    scopus 로고
    • Investigation of domain formation in sphingomyelin/cholesterol/POPC mixtures by fluorescence resonance energy transfer and Monte Carlo simulations
    • DOI 10.1529/biophysj.106.100107
    • M. Frazier, et al., "Investigation of domain formation in sphingomyelin/ cholesterol/POPC mixtures by fluorescence resonance energy transfer and Monte Carlo simulations," Biophys. J. 92(7), 2422-2433 (2007). (Pubitemid 46536424)
    • (2007) Biophysical Journal , vol.92 , Issue.7 , pp. 2422-2433
    • Frazier, M.L.1    Wright, J.R.2    Pokorny, A.3    Almeida, P.F.F.4
  • 25
    • 0028903255 scopus 로고
    • Calculation of resonance energy transfer in crowded biological membranes
    • D. Zimet, et al., "Calculation of resonance energy transfer in crowded biological membranes," Biophys. J. 68(4), 1592-1603 (1995).
    • (1995) Biophys. J , vol.68 , Issue.4 , pp. 1592-1603
    • Zimet, D.1
  • 26
    • 0020212826 scopus 로고
    • Fluorescence energy transfer in 2 dimensions - A numerical solution for random and non-random distributions
    • B. Snyder and E. Freire, "Fluorescence energy transfer in 2 dimensions - a numerical solution for random and non-random distributions," Biophys. J. 40(2), 137-148 (1982).
    • (1982) Biophys. J , vol.40 , Issue.2 , pp. 137-148
    • Snyder, B.1    Freire, E.2
  • 27
    • 34247648685 scopus 로고    scopus 로고
    • In silico characterization of resonance energy transfer for disk-shaped membrane domains
    • DOI 10.1529/biophysj.106.093245
    • M. Kiskowski and A. Kenworthy, "In silico characterization of resonance energy transfer for disk-shaped membrane domains," Biophys. J. 92(9), 3040-3051 (2007). (Pubitemid 46684565)
    • (2007) Biophysical Journal , vol.92 , Issue.9 , pp. 3040-3051
    • Kiskowski, M.A.1    Kenworthy, A.K.2
  • 28
    • 28444437454 scopus 로고    scopus 로고
    • A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries
    • DOI 10.1529/biophysj.105.069351
    • B. Corry, D. Jayatilaka, and P. Rigby, "A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries," Biophys. J. 89(6), 3822-3836 (2005). (Pubitemid 41725604)
    • (2005) Biophysical Journal , vol.89 , Issue.6 , pp. 3822-3836
    • Corry, B.1    Jayatilaka, D.2    Rigby, P.3
  • 29
    • 71049156731 scopus 로고    scopus 로고
    • Anomalous surplus energy transfer observed with multiple FRET acceptors
    • S. Koushik, P. Blank, and S. Vogel, "Anomalous surplus energy transfer observed with multiple FRET acceptors," PLoS ONE 4(11) (2009).
    • (2009) PLoS ONE , vol.4 , Issue.11
    • Koushik, S.1    Blank, P.2    Vogel, S.3
  • 31
    • 0030991352 scopus 로고    scopus 로고
    • Intrinsic fluorescence of hemoglobins and myoglobins
    • DOI 10.1016/S0076-6879(97)78030-3
    • Z. Gryczynski, J. Lubkowski, and E. Bucci, Intrinsic fluorescence of hemoglobins and myoglobins," in Fluorescence Spectroscopy," Volume 278 of Methods in Enzymology, pp. 538-569 (1997). (Pubitemid 27229939)
    • (1997) Methods in Enzymology , vol.278 , pp. 538-569
    • Gryczynski, Z.1    Lubkowski, J.2    Bucci, E.3
  • 32
    • 28444478453 scopus 로고    scopus 로고
    • Conformational changes involved in MscL channel gating measured using FRET spectroscopy
    • DOI 10.1529/biophysj.105.072009
    • B. Corry, et al., "Conformational changes involved in MscL channel gating measured using FRET spectroscopy," Biophys. J. 89(6), L49-L51 (2005). (Pubitemid 41725584)
    • (2005) Biophysical Journal , vol.89 , Issue.6
    • Corry, B.1    Rigby, P.2    Liu, Z.-W.3    Martinac, B.4
  • 33
    • 77957833040 scopus 로고    scopus 로고
    • An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation
    • B. Corry, et al., "An improved open-channel structure of MscL determined from FRET confocal microscopy and simulation," J. Gen. Physiol. 136(4), 483-494 (2010).
    • (2010) J. Gen. Physiol , vol.136 , Issue.4 , pp. 483-494
    • Corry, B.1
  • 34
    • 0028359878 scopus 로고
    • Glycophorin A helical transmembrane domains dimerize in phospholipid bilayers: A resonance energy transfer study
    • DOI 10.1021/bi00184a024
    • B. Adair and D. Engelman, "Glcyophorin-A helical transmembrane domains dimerize in phospholipids-bilayers a resonance energy transfer study," Biochemistry 33(18), 5539-5544 (1994). (Pubitemid 24162990)
    • (1994) Biochemistry , vol.33 , Issue.18 , pp. 5539-5544
    • Adair, B.D.1    Engelman, D.M.2
  • 35
    • 40149099722 scopus 로고    scopus 로고
    • Efficiency of resonance energy transfer in homo-oligomeric complexes of proteins
    • DOI 10.1007/s10867-007-9046-z
    • V. Raicu, "Efficiency of resonance energy transfer in homo-oligomeric complexes of proteins," J. Biol. Phys. 33(2), 109-127 (2007). (Pubitemid 351326293)
    • (2007) Journal of Biological Physics , vol.33 , Issue.2 , pp. 109-127
    • Raicu, V.1
  • 36
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • DOI 10.1038/29563
    • R. Varma and S. Mayor, "GPI-anchored proteins are organized in submicron domains at the cell surface," Nature 394(6695), 798-801 (1998). (Pubitemid 28391646)
    • (1998) Nature , vol.394 , Issue.6695 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 37
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of <100 Ä using imaging fluorescence resonance energy transfer
    • DOI 10.1083/jcb.142.1.69
    • A. Kenworthy and M. Edidin, "Distribution of a glycosylphosphatidylinositol- anchored protein at the apical surface of MDCK cells examined at a resolution of < 100 angstrom using imaging fluorescence resonance energy transfer," J. Cell Biol. 142(1), 69-84 1998). (Pubitemid 28341141)
    • (1998) Journal of Cell Biology , vol.142 , Issue.1 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 38
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • DOI 10.1016/S0092-8674(04)00167-9
    • P. Sharma, et al., "Nanoscale organization of multiple GPI-anchored proteins in living cell membranes," Cell 116(4), 577-589 (2004). (Pubitemid 38264434)
    • (2004) Cell , vol.116 , Issue.4 , pp. 577-589
    • Sharma, P.1
  • 39
    • 0034075971 scopus 로고    scopus 로고
    • High-resolution FRET microscopy of cholera toxin B-subunit and GPI- anchored proteins in cell plasma membranes
    • A. Kenworthy, N. Petranova, and M. Edidin, "High-resolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes," Mol. Biol. Cell 11(5), 1645-1655 (2000). (Pubitemid 30307902)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.5 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 40
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • DOI 10.1126/science.1068539
    • D. Zacharias, et al., "Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells," Science 296(5569), 913-916 (2002). (Pubitemid 34464897)
    • (2002) Science , vol.296 , Issue.5569 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 41
    • 67849103980 scopus 로고    scopus 로고
    • Nucleic base analog FRET pair facilitating detailed structural measurements in nucleic acid containing systems
    • K. Börjesson, et al., "Nucleic base analog FRET pair facilitating detailed structural measurements in nucleic acid containing systems," J. Am. Chem. Soc. 131, 4288-4293 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4288-4293
    • Börjesson, K.1


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