메뉴 건너뛰기




Volumn 256, Issue 3, 2014, Pages 166-176

Effect of fixation procedures on the fluorescence lifetimes of Aequorea victoria derived fluorescent proteins

Author keywords

Fixation; FLIM; Fluorescence lifetime unmixing; FRET; GFP; Mounting

Indexed keywords

ANTIBODIES; CELLS; CYTOLOGY; ENERGY TRANSFER; FLUORESCENCE IMAGING; MOUNTINGS;

EID: 84911462210     PISSN: 00222720     EISSN: 13652818     Source Type: Journal    
DOI: 10.1111/jmi.12168     Document Type: Article
Times cited : (32)

References (24)
  • 1
    • 84863876597 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging-techniques and applications
    • Becker, W. (2012) Fluorescence lifetime imaging-techniques and applications. J. Microsc. 247, 119-136.
    • (2012) J. Microsc. , vol.247 , pp. 119-136
    • Becker, W.1
  • 2
    • 18644377743 scopus 로고    scopus 로고
    • Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins
    • Borst, J.W., Hink, M.A., van Hoek, A. & Visser, A.J. (2005) Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins. J. fluoresce. 15, 153-160.
    • (2005) J. fluoresce. , vol.15 , pp. 153-160
    • Borst, J.W.1    Hink, M.A.2    van Hoek, A.3    Visser, A.J.4
  • 3
    • 84873401872 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt
    • Broussard, J.A., Rappaz, B., Webb, D.J. & Brown, C.M. (2013) Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt. Nat. Protocols 8, 265-281.
    • (2013) Nat. Protocols , vol.8 , pp. 265-281
    • Broussard, J.A.1    Rappaz, B.2    Webb, D.J.3    Brown, C.M.4
  • 4
    • 77955640606 scopus 로고    scopus 로고
    • Fluorescent proteins and their applications in imaging living cells and tissues
    • Chudakov, D.M., Matz, M.V., Lukyanov, S. & Lukyanov, K.A. (2010) Fluorescent proteins and their applications in imaging living cells and tissues. Physiol. Rev. 90, 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
  • 5
    • 84874055690 scopus 로고    scopus 로고
    • Fluorescent proteins: shine on, you crazy diamond
    • Dedecker, P., De Schryver, F.C. & Hofkens, J. (2013) Fluorescent proteins: shine on, you crazy diamond. J. Am. Chem. Soc. 135, 2387-2402.
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 2387-2402
    • Dedecker, P.1    De Schryver, F.C.2    Hofkens, J.3
  • 6
    • 79651470396 scopus 로고    scopus 로고
    • Fixation alters fluorescence lifetime and anisotropy of cells expressing EYFP-tagged serotonin1A receptor
    • Ganguly, S., Clayton, A.H. & Chattopadhyay, A. (2011) Fixation alters fluorescence lifetime and anisotropy of cells expressing EYFP-tagged serotonin1A receptor. Biochem. Biophys. Res. Commun. 405, 234-237.
    • (2011) Biochem. Biophys. Res. Commun. , vol.405 , pp. 234-237
    • Ganguly, S.1    Clayton, A.H.2    Chattopadhyay, A.3
  • 7
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B.N., Adams, S.R., Ellisman, M.H. & Tsien, R.Y. (2006) The fluorescent toolbox for assessing protein location and function. Science 312, 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
  • 8
    • 22144452926 scopus 로고    scopus 로고
    • Analysis of oligonucleotide annealing by electrophoresis in agarose gels using sodium borate conductive medium
    • Goedhart, J. & Gadella, T.W., Jr. (2005) Analysis of oligonucleotide annealing by electrophoresis in agarose gels using sodium borate conductive medium. Anal. Biochem. 343, 186-187.
    • (2005) Anal. Biochem , vol.343 , pp. 186-187
    • Goedhart, J.1    Gadella Jr., T.W.2
  • 9
    • 81255195819 scopus 로고    scopus 로고
    • Quantitative co-expression of proteins at the single cell level-application to a multimeric FRET sensor
    • Goedhart, J., van Weeren, L., Adjobo-Hermans, M.J., Elzenaar, I., Hink, M.A. & Gadella, T.W., Jr. (2011) Quantitative co-expression of proteins at the single cell level-application to a multimeric FRET sensor. PloS one 6, e27321.
    • (2011) PloS one , vol.6 , pp. e27321
    • Goedhart, J.1    van Weeren, L.2    Adjobo-Hermans, M.J.3    Elzenaar, I.4    Hink, M.A.5    Gadella Jr., T.W.6
  • 11
    • 84859173050 scopus 로고    scopus 로고
    • Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%
    • Goedhart, J., von Stetten, D., Noirclerc-Savoye, M. et al. (2012) Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nat. Commun. 3, 751.
    • (2012) Nat. Commun. , vol.3 , pp. 751
    • Goedhart, J.1    von Stetten, D.2    Noirclerc-Savoye, M.3
  • 12
    • 0031725221 scopus 로고    scopus 로고
    • Differential extraction of proteins from paraformaldehyde-fixed cells: lessons from synaptophysin and other membrane proteins
    • Hannah, M.J., Weiss, U. & Huttner, W.B. (1998) Differential extraction of proteins from paraformaldehyde-fixed cells: lessons from synaptophysin and other membrane proteins. Methods 16, 170-181.
    • (1998) Methods , vol.16 , pp. 170-181
    • Hannah, M.J.1    Weiss, U.2    Huttner, W.B.3
  • 13
  • 14
    • 33744779420 scopus 로고    scopus 로고
    • Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Forster radius
    • Kremers, G.J., Goedhart, J., van Munster, E.B. & Gadella, T.W., Jr. (2006) Cyan and yellow super fluorescent proteins with improved brightness, protein folding, and FRET Forster radius. Biochemistry 45, 6570-6580.
    • (2006) Biochemistry , vol.45 , pp. 6570-6580
    • Kremers, G.J.1    Goedhart, J.2    van Munster, E.B.3    Gadella Jr., T.W.4
  • 15
    • 46749125072 scopus 로고    scopus 로고
    • Quantitative lifetime unmixing of multiexponentially decaying fluorophores using single-frequency fluorescence lifetime imaging microscopy
    • Kremers, G.J., van Munster, E.B., Goedhart, J. & Gadella, T.W., Jr. (2008) Quantitative lifetime unmixing of multiexponentially decaying fluorophores using single-frequency fluorescence lifetime imaging microscopy. Biophys. J. 95, 378-389.
    • (2008) Biophys. J. , vol.95 , pp. 378-389
    • Kremers, G.J.1    van Munster, E.B.2    Goedhart, J.3    Gadella Jr., T.W.4
  • 16
    • 0021943625 scopus 로고
    • Structural organization of interphase 3T3 fibroblasts studied by total internal reflection fluorescence microscopy
    • Lanni, F., Waggoner, A.S. & Taylor, D.L. (1985) Structural organization of interphase 3T3 fibroblasts studied by total internal reflection fluorescence microscopy. J. Cell Biol. 100, 1091-1102.
    • (1985) J. Cell Biol. , vol.100 , pp. 1091-1102
    • Lanni, F.1    Waggoner, A.S.2    Taylor, D.L.3
  • 17
    • 58149265015 scopus 로고    scopus 로고
    • Putting super-resolution fluorescence microscopy to work
    • Lippincott-Schwartz, J. & Manley, S. (2009) Putting super-resolution fluorescence microscopy to work. Nat. Methods 6, 21-23.
    • (2009) Nat. Methods , vol.6 , pp. 21-23
    • Lippincott-Schwartz, J.1    Manley, S.2
  • 18
    • 0026529270 scopus 로고
    • Redistribution and differential extraction of soluble proteins in permeabilized cultured cells. Implications for immunofluorescence microscopy
    • Melan, M.A. & Sluder, G. (1992) Redistribution and differential extraction of soluble proteins in permeabilized cultured cells. Implications for immunofluorescence microscopy. J. Cell Sci. 101(Pt 4), 731-743.
    • (1992) J. Cell Sci. , vol.101 , Issue.PART. 4 , pp. 731-743
    • Melan, M.A.1    Sluder, G.2
  • 19
    • 0033545695 scopus 로고    scopus 로고
    • Simultaneous detection of multiple green fluorescent proteins in live cells by fluorescence lifetime imaging microscopy
    • Pepperkok, R., Squire, A., Geley, S. & Bastiaens, P.I. (1999) Simultaneous detection of multiple green fluorescent proteins in live cells by fluorescence lifetime imaging microscopy. Curr. Biol.: CB. 9, 269-272.
    • (1999) Curr. Biol.: CB , vol.9 , pp. 269-272
    • Pepperkok, R.1    Squire, A.2    Geley, S.3    Bastiaens, P.I.4
  • 20
    • 78651230932 scopus 로고    scopus 로고
    • FRET microscopy: from principle to routine technology in cell biology
    • Pietraszewska-Bogiel, A. & Gadella, T.W. (2011) FRET microscopy: from principle to routine technology in cell biology. J. Microsc. 241, 111-118.
    • (2011) J. Microsc. , vol.241 , pp. 111-118
    • Pietraszewska-Bogiel, A.1    Gadella, T.W.2
  • 21
    • 84856427183 scopus 로고    scopus 로고
    • Immunolabeling artifacts and the need for live-cell imaging
    • Schnell, U., Dijk, F., Sjollema, K.A. & Giepmans, B.N. (2012) Immunolabeling artifacts and the need for live-cell imaging. Nat. Methods 9, 152-158.
    • (2012) Nat. Methods , vol.9 , pp. 152-158
    • Schnell, U.1    Dijk, F.2    Sjollema, K.A.3    Giepmans, B.N.4
  • 23
    • 80052399465 scopus 로고    scopus 로고
    • Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy
    • Sun, Y., Day, R.N. & Periasamy, A. (2011) Investigating protein-protein interactions in living cells using fluorescence lifetime imaging microscopy. Nat. Protocols 6, 1324-1340.
    • (2011) Nat. Protocols , vol.6 , pp. 1324-1340
    • Sun, Y.1    Day, R.N.2    Periasamy, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.