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Volumn 5, Issue 1, 2006, Pages 41-45

Computational modeling of a new fluorescent biosensor for caspase proteolytic activity improves dynamic range

Author keywords

Biosensor; Fluorescence resonance energy transfer (FRET); Imaging; Protein engineering

Indexed keywords

FLUORESCENCE RESONANCE ENERGY TRANSFER (FRET); PROTEASE; PROTEIN COMPLEXES; PROTEIN ENGINEERING;

EID: 33644989490     PISSN: 15361241     EISSN: None     Source Type: Journal    
DOI: 10.1109/TNB.2005.864020     Document Type: Article
Times cited : (8)

References (19)
  • 1
    • 0035442412 scopus 로고    scopus 로고
    • The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo
    • K. Truong and M. Ikura, "The use of FRET imaging microscopy to detect protein-protein interactions and protein conformational changes in vivo," Curr: Opin. Struct. Biol., vol. 11, pp. 573-578, 2001.
    • (2001) Curr: Opin. Struct. Biol. , vol.11 , pp. 573-578
    • Truong, K.1    Ikura, M.2
  • 3
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • A. Miyawaki, J. Llopis, R. Heim, J. M. McCaffery, J. A. Adams, M. Ikura, and R. Y. Tsien, "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin," Nature, vol. 388, pp. 882-887, 1997.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6    Tsien, R.Y.7
  • 5
    • 2442681401 scopus 로고    scopus 로고
    • A high-throughput method for development of FRET-based indicators for proteolysis
    • T. Nagai and A. Miyawaki, "A high-throughput method for development of FRET-based indicators for proteolysis," Biochem. Biophys. Res. Commun., vol. 319, pp. 72-77, 2004.
    • (2004) Biochem. Biophys. Res. Commun. , vol.319 , pp. 72-77
    • Nagai, T.1    Miyawaki, A.2
  • 6
    • 3242706582 scopus 로고    scopus 로고
    • Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins
    • T. Nagai, S. Yamada, T. Tominaga, M. Ichikawa, and A. Miyawaki, "Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins," Proc. Nat, Acad. Sci. USA, vol. 101, pp. 10554-1059, 2004.
    • (2004) Proc. Nat, Acad. Sci. USA , vol.101 , pp. 10554-11059
    • Nagai, T.1    Yamada, S.2    Tominaga, T.3    Ichikawa, M.4    Miyawaki, A.5
  • 9
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • L. Tyas, V. A. Brophy, A. Pope, A. J. Rivett, and J. M. Tavare, "Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer," EMBO Rep., vol. 1, pp. 266-270, 2000.
    • (2000) EMBO Rep. , vol.1 , pp. 266-270
    • Tyas, L.1    Brophy, V.A.2    Pope, A.3    Rivett, A.J.4    Tavare, J.M.5
  • 10
    • 0034801529 scopus 로고    scopus 로고
    • Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during uv-induced apoptosis in living hela cells
    • K. Q. Luo, V. C. Yu, Y. Pu, and D. C. Chang, "Application of the fluorescence resonance energy transfer method for studying the dynamics of caspase-3 activation during uv-induced apoptosis in living hela cells," Biochem. Biophys. Res. Commun., vol. 283, pp. 1054-1060, 2001.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 1054-1060
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 11
    • 0037025346 scopus 로고    scopus 로고
    • Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3
    • M. Rehm, H. Dussmann, R. U. Janicke, J. M. Tavare, D. Kogel, and J. H. Prehn, "Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3," J. Biol. Chem., vol. 277, pp. 24506-24514, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavare, J.M.4    Kogel, D.5    Prehn, J.H.6
  • 12
    • 0037455553 scopus 로고    scopus 로고
    • Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects
    • K. Takemoto, T. Nagai, A. Miyawaki, and M. Miura, "Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects," J. Cell Biol., vol. 160, pp. 235-243, 2003.
    • (2003) J. Cell Biol. , vol.160 , pp. 235-243
    • Takemoto, K.1    Nagai, T.2    Miyawaki, A.3    Miura, M.4
  • 13
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • A. Fiser and A. Sali, "Modeller: Generation and refinement of homology-based protein structure models," Methods. Enzymol., vol. 374, pp. 461-491, 2003.
    • (2003) Methods. Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 14
    • 0037184962 scopus 로고    scopus 로고
    • Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity
    • A. Rekas, J. R. Alattia, T. Nagai, A. Miyawaki, and M. Ikura, "Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity," J. Biol. Chem., vol. 277, pp. 50573-50578, 2002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50573-50578
    • Rekas, A.1    Alattia, J.R.2    Nagai, T.3    Miyawaki, A.4    Ikura, M.5
  • 16
    • 3042515169 scopus 로고    scopus 로고
    • A fluorescent cassette-based strategy for engineering multiple domain fusion proteins
    • K. Truong, A. Khorchid, and M. Ikura, "A fluorescent cassette-based strategy for engineering multiple domain fusion proteins," BMC Biotechnol., vol. 3. pp. 1-8, 2003.
    • (2003) BMC Biotechnol. , vol.3 , pp. 1-8
    • Truong, K.1    Khorchid, A.2    Ikura, M.3
  • 17
    • 0032536519 scopus 로고    scopus 로고
    • Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis
    • H. Hirata, A. Takahashi, S. Kobayashi, S. Yonehara, H. Sawai, T. Okazaki, K. Yamamoto, and M. Sasada, "Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis," J. Exp. Med., vol. 187, pp. 587-600, 1998.
    • (1998) J. Exp. Med. , vol.187 , pp. 587-600
    • Hirata, H.1    Takahashi, A.2    Kobayashi, S.3    Yonehara, S.4    Sawai, H.5    Okazaki, T.6    Yamamoto, K.7    Sasada, M.8
  • 18
    • 0032522223 scopus 로고    scopus 로고
    • Detection of programmed cell death using fluorescence energy transfer
    • X. Xu, A. L. Gerard, B. C. Huang, D. C. Anderson, D. G. Payan, and Y. Luo, "Detection of programmed cell death using fluorescence energy transfer," Nucleic Acids Res., vol. 26, pp. 2034-2035, 1998.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2034-2035
    • Xu, X.1    Gerard, A.L.2    Huang, B.C.3    Anderson, D.C.4    Payan, D.G.5    Luo, Y.6
  • 19
    • 0242609099 scopus 로고    scopus 로고
    • Cathepsin D mediates cytochrome e release and caspase activation in human fibroblast apoptosis induced by staurosporine
    • A. C. Johansson, H. Steen, K. Ollinger, and K. Roberg, "Cathepsin D mediates cytochrome e release and caspase activation in human fibroblast apoptosis induced by staurosporine," Cell Death Differ., vol. 10, pp. 1253-1259, 2003.
    • (2003) Cell Death Differ. , vol.10 , pp. 1253-1259
    • Johansson, A.C.1    Steen, H.2    Ollinger, K.3    Roberg, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.