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Volumn 22, Issue 4, 2004, Pages 445-449

An improved cyan fluorescent protein variant useful for FRET

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOSENSORS; CELLS; ENERGY TRANSFER; MUTAGENESIS; RESONANCE; SIGNAL TO NOISE RATIO;

EID: 1842424983     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt945     Document Type: Article
Times cited : (931)

References (20)
  • 1
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R. & Tsien, R.Y. Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182 (1996).
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 2
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea victoria green fluorescent protein
    • Ormo, M. et al. Crystal structure of the Aequorea victoria green fluorescent protein. Science 273, 1392-1395 (1996).
    • (1996) Science , vol.273 , pp. 1392-1395
    • Ormo, M.1
  • 3
    • 0034633010 scopus 로고    scopus 로고
    • Forster distances between green fluorescent protein pairs
    • Patterson, G.H, Piston, D.W. & Barisas, B.G. Forster distances between green fluorescent protein pairs. Anal. Biochem. 284, 438-440 (2000).
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 5
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki, A. et al. Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388, 882-887 (1997).
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 6
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting, A.Y., Kain, K.H., Klemke, R.L. & Tsien, R.Y. Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. USA 98, 15003-15008 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 7
    • 0035910074 scopus 로고    scopus 로고
    • Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering
    • Zhang, J., Ma, Y., Taylor, S.S. & Tsien, R.Y. Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering. Proc. Natl. Acad. Sci. USA 98, 14997-15002 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14997-15002
    • Zhang, J.1    Ma, Y.2    Taylor, S.S.3    Tsien, R.Y.4
  • 8
    • 0037072825 scopus 로고    scopus 로고
    • A functional link between glucokinase binding to insulin granules and conformational alterations in response to glucose and insulin
    • Rizzo, M.A., Magnuson, M.A., Drain, P.F. & Piston, D.W. A functional link between glucokinase binding to insulin granules and conformational alterations in response to glucose and insulin. J. Biol. Chem. 277, 34168-34175 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34168-34175
    • Rizzo, M.A.1    Magnuson, M.A.2    Drain, P.F.3    Piston, D.W.4
  • 9
    • 0034094370 scopus 로고    scopus 로고
    • Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer
    • Vanderklish, P.W. et al. Marking synaptic activity in dendritic spines with a calpain substrate exhibiting fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 97, 2253-2258 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2253-2258
    • Vanderklish, P.W.1
  • 10
    • 0035179080 scopus 로고    scopus 로고
    • 2+ imaging by a new calmodulin-GFP fusion molecule
    • 2+ imaging by a new calmodulin-GFP fusion molecule. Nat. Struct. Biol. 8, 1069-1073 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1069-1073
    • Truong, K.1
  • 11
    • 0037133239 scopus 로고    scopus 로고
    • Measuring tubulin content in Toxoplasmagondii: A comparison of laser-scanning confocal and wide-field fluorescence microscopy
    • Swedlow, J.R., Hu, K., Andrews, P.D., Roos, D.S. & Murray, J.M. Measuring tubulin content in Toxoplasmagondii: a comparison of laser-scanning confocal and wide-field fluorescence microscopy. Proc. Natl. Acad. Sci. USA 99, 2014-2019 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2014-2019
    • Swedlow, J.R.1    Hu, K.2    Andrews, P.D.3    Roos, D.S.4    Murray, J.M.5
  • 12
    • 0035800773 scopus 로고    scopus 로고
    • Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications
    • Griesbeck, O., Baird, G.S., Campbell, R.E., Zacharias, D.A. & Tsien, R.Y. Reducing the environmental sensitivity of yellow fluorescent protein. Mechanism and applications. J. Biol. Chem. 276, 29188-29194 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29188-29194
    • Griesbeck, O.1    Baird, G.S.2    Campbell, R.E.3    Zacharias, D.A.4    Tsien, R.Y.5
  • 13
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T. et al. A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90 (2002).
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1
  • 15
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • Zacharias, D.A., Violin, J.D., Newton, A.C. & Tsien, R.Y. Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells. Science 296, 913-916 (2002).
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 16
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P.I. & Squire, A. Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol. 9, 48-45 (1999).
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-45
    • Bastiaens, P.I.1    Squire, A.2
  • 17
    • 0036932415 scopus 로고    scopus 로고
    • Picosecond-hetero-FRET microscopy to probe protein-protein interactions in live cells
    • Tramier, M. et al. Picosecond-hetero-FRET microscopy to probe protein-protein interactions in live cells. Biophys. J. 83, 3570-3577 (2002).
    • (2002) Biophys. J. , vol.83 , pp. 3570-3577
    • Tramier, M.1
  • 18
    • 0037449124 scopus 로고    scopus 로고
    • Expansion of the genetic code enables design of a novel "gold" class of green fluorescent proteins
    • Hyun Bae, J. et al. Expansion of the genetic code enables design of a novel "gold" class of green fluorescent proteins. J. Mol. Biol. 328, 1071-1081 (2003).
    • (2003) J. Mol. Biol. , vol.328 , pp. 1071-1081
    • Hyun Bae, J.1
  • 19
    • 0032607587 scopus 로고    scopus 로고
    • Understanding structure-function relationships in the Aequorea victoria green fluorescent protein
    • Cubitt, A.B., Woollenweber, L.A. & Heim, R. Understanding structure-function relationships in the Aequorea victoria green fluorescent protein. Methods Cell Biol. 58, 19-30 (1999).
    • (1999) Methods Cell Biol. , vol.58 , pp. 19-30
    • Cubitt, A.B.1    Woollenweber, L.A.2    Heim, R.3
  • 20
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson, G.H., Knobel, S.M., Sharif, W.D., Kain, S.R. & Piston, D.W. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73, 2782-2790 (1997).
    • (1997) Biophys. J. , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.