메뉴 건너뛰기




Volumn 4, Issue , 2013, Pages

Visualization of caspase-3-like activity in cells using a genetically encoded fluorescent biosensor activated by protein cleavage

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 7; CISPLATIN; FLUOROURACIL;

EID: 84880382817     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms3157     Document Type: Article
Times cited : (106)

References (39)
  • 1
    • 0030814675 scopus 로고    scopus 로고
    • Caspases: Killer proteases
    • DOI 10.1016/S0968-0004(97)01085-2, PII S0968000497010852
    • Nicholson, D. W. & Thornberry, N. A. Caspases: killer proteases. Trends Biochem. Sci. 22, 299-306 (1997). (Pubitemid 27327087)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.8 , pp. 299-306
    • Nicholson, D.W.1    Thornberry, N.A.2
  • 2
    • 0033692510 scopus 로고    scopus 로고
    • Apoptosis: Mechanisms and clinical implications
    • Kam, P. C. & Ferch, N. I. Apoptosis: mechanisms and clinical implications. Anaesthesia 55, 1081-1093 (2000).
    • (2000) Anaesthesia , vol.55 , pp. 1081-1093
    • Kam, P.C.1    Ferch, N.I.2
  • 3
    • 70450205079 scopus 로고    scopus 로고
    • Apoptosis and human diseases: Mitochondrion damage and lethal role of released cytochrome C as proapoptotic protein
    • Caroppi, P., Sinibaldi, F., Fiorucci, L. & Santucci, R. Apoptosis and human diseases: mitochondrion damage and lethal role of released cytochrome C as proapoptotic protein. Curr. Med. Chem. 16, 4058-4065 (2009).
    • (2009) Curr. Med. Chem , vol.16 , pp. 4058-4065
    • Caroppi, P.1    Sinibaldi, F.2    Fiorucci, L.3    Santucci, R.4
  • 4
    • 0037455553 scopus 로고    scopus 로고
    • Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects
    • DOI 10.1083/jcb.200207111
    • Takemoto, K., Nagai, T., Miyawaki, A. & Miura, M. Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects. J. Cell Biol. 160, 235-243 (2003). (Pubitemid 36254957)
    • (2003) Journal of Cell Biology , vol.160 , Issue.2 , pp. 235-243
    • Takemoto, K.1    Nagai, T.2    Miyawaki, A.3    Miura, M.4
  • 5
    • 0034280126 scopus 로고    scopus 로고
    • Rapid caspase-3 activation during apoptosis revealed using fluorescence-resonance energy transfer
    • Tyas, L., Brophy, V. A., Pope, A., Rivett, A. J. & Tavare, J. M. Rapid caspase-3 activation during apoptosis revealed using fluorescence- resonance energy transfer. EMBO Rep. 1, 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
  • 6
    • 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
    • DOI 10.1074/jbc.M110789200
    • Rehm, M. et al. Single-cell fluorescence resonance energy transfer analysis demonstrates that caspase activation during apoptosis is a rapid process. Role of caspase-3. J. Biol. Chem. 277, 24506-24514 (2002). (Pubitemid 34951976)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24506-24514
    • Rehm, M.1    Dussmann, H.2    Janicke, R.U.3    Tavare, J.M.4    Kogel, D.5    Prehn, J.H.M.6
  • 7
    • 0037414451 scopus 로고    scopus 로고
    • Measuring dynamics of caspase-8 activation in a single living HeLa cell during TNFα-induced apoptosis
    • DOI 10.1016/S0006-291X(03)00559-X
    • Luo, K. Q., Yu, V. C., Pu, Y. & Chang, D. C. Measuring dynamics of caspase-8 activation in a single living HeLa cell during TNFalpha-induced apoptosis. Biochem. Biophys. Res. Commun. 304, 217-222 (2003). (Pubitemid 36444557)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.2 , pp. 217-222
    • Luo, K.Q.1    Yu, V.C.2    Pu, Y.3    Chang, D.C.4
  • 8
    • 79960110644 scopus 로고    scopus 로고
    • Mechanism of a genetically encoded dark-to-bright reporter for caspase activity
    • Nicholls, S. B., Chu, J., Abbruzzese, G., Tremblay, K. D. & Hardy, J. A. Mechanism of a genetically encoded dark-to-bright reporter for caspase activity. J. Biol. Chem. 286, 24977-24986 (2011).
    • (2011) J. Biol. Chem , vol.286 , pp. 24977-24986
    • Nicholls, S.B.1    Chu, J.2    Abbruzzese, G.3    Tremblay, K.D.4    Hardy, J.A.5
  • 9
    • 52949107580 scopus 로고    scopus 로고
    • A fluorescent reporter of caspase activity for live imaging
    • Bardet, P. L. et al. A fluorescent reporter of caspase activity for live imaging. Proc. Natl Acad. Sci. USA 105, 13901-13905 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 13901-13905
    • Bardet, P.L.1
  • 10
    • 84864560649 scopus 로고    scopus 로고
    • Molecular imaging with activatable reporter systems
    • Niu, G. & Chen, X. Molecular imaging with activatable reporter systems. Theranostics 2, 413-423 (2012).
    • (2012) Theranostics , vol.2 , pp. 413-423
    • Niu, G.1    Chen, X.2
  • 11
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • DOI 10.1038/nbt0102-87
    • 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). (Pubitemid 34044921)
    • (2002) Nature Biotechnology , vol.20 , Issue.1 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 12
    • 0037184962 scopus 로고    scopus 로고
    • Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity
    • DOI 10.1074/jbc.M209524200
    • Rekas, A., Alattia, J. R., Nagai, T., Miyawaki, A. & Ikura, M. Crystal structure of venus, a yellow fluorescent protein with improved maturation and reduced environmental sensitivity. J. Biol. Biochem. 277, 50573-50578 (2002). (Pubitemid 36042216)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.52 , pp. 50573-50578
    • Rekas, A.1    Alattia, J.-R.2    Nagai, T.3    Miyawaki, A.4    Ikura, M.5
  • 13
    • 53949107378 scopus 로고    scopus 로고
    • Fluorescence complementation: An emerging tool for biological research
    • Shyu, Y. J. & Hu, C. D. Fluorescence complementation: an emerging tool for biological research. Trends Biotechnol. 26, 622-630 (2008).
    • (2008) Trends Biotechnol , vol.26 , pp. 622-630
    • Shyu, Y.J.1    Hu, C.D.2
  • 14
    • 60749092724 scopus 로고    scopus 로고
    • The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction
    • Zettler, J., Schutz, V. & Mootz, H. D. The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction. FEBS Lett. 583, 909-914 (2009).
    • (2009) FEBS Lett , vol.583 , pp. 909-914
    • Zettler, J.1    Schutz, V.2    Mootz, H.D.3
  • 15
    • 33644912308 scopus 로고    scopus 로고
    • Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme
    • Iwai, H., Zuger, S., Jin, J. & Tam, P. H. Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme. FEBS Lett. 580, 1853-1858 (2006).
    • (2006) FEBS Lett , vol.580 , pp. 1853-1858
    • Iwai, H.1    Zuger, S.2    Jin, J.3    Tam, P.H.4
  • 16
    • 33644861986 scopus 로고    scopus 로고
    • Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions
    • DOI 10.2144/000112036
    • Shyu, Y. J., Liu, H., Deng, X. & Hu, C. D. Identification of new fluorescent protein fragments for bimolecular fluorescence complementation analysis under physiological conditions. BioTechniques 40, 61-66 (2006). (Pubitemid 46534939)
    • (2006) BioTechniques , vol.40 , Issue.1 , pp. 61-66
    • Shyu, Y.J.1    Liu, H.2    Deng, X.3    Hu, C.-D.4
  • 17
    • 84855846945 scopus 로고    scopus 로고
    • Targeting TRAIL towards the clinic
    • Mahalingam, D. et al. Targeting TRAIL towards the clinic. Curr. Drug Targets 12, 2079-2090 (2011).
    • (2011) Curr. Drug Targets , vol.12 , pp. 2079-2090
    • Mahalingam, D.1
  • 19
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • DOI 10.1074/jbc.273.16.9357
    • Janicke, R. U., Sprengart, M. L., Wati, M. R. & Porter, A. G. Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273, 9357-9360 (1998). (Pubitemid 28183012)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9357-9360
    • Janicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 20
    • 0035807288 scopus 로고    scopus 로고
    • Apoptosis in the absence of caspase 3
    • DOI 10.1038/sj.onc.1204815
    • Liang, Y., Yan, C. & Schor, N. F. Apoptosis in the absence of caspase 3. Oncogene 20, 6570-6578 (2001). (Pubitemid 32980283)
    • (2001) Oncogene , vol.20 , Issue.45 , pp. 6570-6578
    • Liang, Y.1    Yan, C.2    Schor, N.F.3
  • 22
    • 0033861172 scopus 로고    scopus 로고
    • Pathways through which a regimen of melatonin and retinoic acid induces apoptosis in MCF-7 human breast cancer cells
    • DOI 10.1023/A:1006442017658
    • Eck-Enriquez, K., Kiefer, T. L., Spriggs, L. L. & Hill, S. M. Pathways through which a regimen of melatonin and retinoic acid induces apoptosis in MCF-7 human breast cancer cells. Breast Cancer Res. Treat. 61, 229-239 (2000). (Pubitemid 30609556)
    • (2000) Breast Cancer Research and Treatment , vol.61 , Issue.3 , pp. 229-239
    • Eck-Enriquez, K.1    Kiefer2    Spriggs, L.L.3    Hill, S.M.4
  • 24
    • 33645237577 scopus 로고    scopus 로고
    • Caspase-7 is directly activated by the ∼700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 ∼200-kDa complex
    • DOI 10.1074/jbc.M507393200
    • Twiddy, D., Cohen, G. M., Macfarlane, M. & Cain, K. Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex. J. Biol. Chem. 281, 3876-3888 (2006). (Pubitemid 43847811)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 3876-3888
    • Twiddy, D.1    Cohen, G.M.2    MacFarlane, M.3    Cain, K.4
  • 25
    • 52049091499 scopus 로고    scopus 로고
    • Real time analysis of tumor necrosis factor-related apoptosis-inducing ligand/cycloheximide-induced caspase activities during apoptosis initiation
    • Hellwig, C. T. et al. Real time analysis of tumor necrosis factor-related apoptosis-inducing ligand/cycloheximide-induced caspase activities during apoptosis initiation. J. Biol. Chem. 283, 21676-21685 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 21676-21685
    • Hellwig, C.T.1
  • 27
    • 1842451620 scopus 로고    scopus 로고
    • Death without caspases, caspases without death
    • DOI 10.1016/j.tcb.2004.03.002, PII S0962892404000558
    • Abraham, M. C. & Shaham, S. Death without caspases, caspases without death. Trends Cell Biol. 14, 184-193 (2004). (Pubitemid 38447118)
    • (2004) Trends in Cell Biology , vol.14 , Issue.4 , pp. 184-193
    • Abraham, M.C.1    Shaham, S.2
  • 29
    • 84868698549 scopus 로고    scopus 로고
    • Caspase-3 protects stressed organs against cell death
    • Khalil, H. et al. Caspase-3 protects stressed organs against cell death. Mol. Cell Biol. 32, 4523-4533 (2012).
    • (2012) Mol. Cell Biol , vol.32 , pp. 4523-4533
    • Khalil, H.1
  • 30
    • 8644273229 scopus 로고    scopus 로고
    • Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions
    • Yang, J. Y. et al. Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions. Mol. Cell Biol. 24, 10425-10436 (2004).
    • (2004) Mol. Cell Biol , vol.24 , pp. 10425-10436
    • Yang, J.Y.1
  • 31
    • 0020918402 scopus 로고
    • The human tumor cloning assay in cancer drug development. A review
    • Agre, P. & Williams, T. E. The human tumor cloning assay in cancer drug development. A review. Invest. New Drug 1, 33-45 (1983). (Pubitemid 14117519)
    • (1983) Investigational New Drugs , vol.1 , Issue.1 , pp. 33-45
    • Agre, P.1    Williams, T.E.2
  • 32
    • 77952101348 scopus 로고    scopus 로고
    • Specific killing of Rb mutant cancer cells by inactivating TSC2
    • Li, B., Gordon, G. M., Du, C. H., Xu, J. & Du, W. Specific killing of Rb mutant cancer cells by inactivating TSC2. Cancer Cell 17, 469-480 (2010).
    • (2010) Cancer Cell , vol.17 , pp. 469-480
    • Li, B.1    Gordon, G.M.2    Du, C.H.3    Xu, J.4    Du, W.5
  • 34
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • DOI 10.1038/nbt1172, PII NBT1172
    • Pedelacq, J. D., Cabantous, S., Tran, T., Terwilliger, T. C. & Waldo, G. S. Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24, 79-88 (2006). (Pubitemid 43083170)
    • (2006) Nature Biotechnology , vol.24 , Issue.1 , pp. 79-88
    • Pedelacq, J.-D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 36
    • 38049115791 scopus 로고    scopus 로고
    • Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells
    • Fan, J. Y. et al. Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein-protein interactions in living cells. Biochem. Biophys. Res. Commun. 367, 47-53 (2008).
    • (2008) Biochem. Biophys. Res. Commun , vol.367 , pp. 47-53
    • Fan, J.Y.1
  • 37
    • 62149150302 scopus 로고    scopus 로고
    • Far-red fluorescent tags for protein imaging in living tissues
    • Shcherbo, D. et al. Far-red fluorescent tags for protein imaging in living tissues. Biochem. J. 418, 567-574 (2009).
    • (2009) Biochem. J , vol.418 , pp. 567-574
    • Shcherbo, D.1
  • 38
    • 68049137311 scopus 로고    scopus 로고
    • A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions
    • Chu, J. et al. A novel far-red bimolecular fluorescence complementation system that allows for efficient visualization of protein interactions under physiological conditions. Biosens. Bioelectron. 25, 234-239 (2009).
    • (2009) Biosens. Bioelectron , vol.25 , pp. 234-239
    • Chu, J.1
  • 39
    • 34447581119 scopus 로고    scopus 로고
    • Optimized production and concentration of lentiviral vectors containing large inserts
    • DOI 10.1002/jgm.1052
    • al Yacoub, N., Romanowska, M., Haritonova, N. & Foerster, J. Optimized production and concentration of lentiviral vectors containing large inserts. J. Gene Med. 9, 579-584 (2007). (Pubitemid 47073990)
    • (2007) Journal of Gene Medicine , vol.9 , Issue.7 , pp. 579-584
    • Al Yacoub, N.1    Romanowska, M.2    Haritonova, N.3    Foerster, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.