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Volumn 33, Issue 6, 2002, Pages 1284-1291

Marker for real-time analysis of caspase activity in intact cells

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYMES; FLUORESCENCE; REAL TIME SYSTEMS;

EID: 0036913248     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/02336rr02     Document Type: Article
Times cited : (8)

References (38)
  • 1
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair, A., D. Finley, and A. Varshavsky. 1986. In vivo half-life of a protein is a function of its amino-terminal residue. Science 234:179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair, A.1    Finley, D.2    Varshavsky, A.3
  • 2
    • 0034682502 scopus 로고    scopus 로고
    • Inhibition of proteasomal degradation by the gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal
    • Dantuma, N.P., S. Heessen, K. Lindsten, M. Jellne, and M.G. Masucci. 2000. Inhibition of proteasomal degradation by the gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal. Proc. Natl. Acad. Sci. USA 97:8381-8385.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8381-8385
    • Dantuma, N.P.1    Heessen, S.2    Lindsten, K.3    Jellne, M.4    Masucci, M.G.5
  • 3
    • 0034023407 scopus 로고    scopus 로고
    • Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
    • Dantuma, N.P., K. Lindsten, R. Glas, M. Jellne, and M.G. Masucci. 2000. Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells. Nat. Biotechnol. 18:538-543.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 538-543
    • Dantuma, N.P.1    Lindsten, K.2    Glas, R.3    Jellne, M.4    Masucci, M.G.5
  • 5
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du, C., M. Fang, Y. Li, L. Li, and X. Wang. 2000. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102:33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 6
    • 0037166054 scopus 로고    scopus 로고
    • The endoplasmic reticulum is the main site for caspase-3 activation following aluminum-induced neurotoxicity in rabbit hippocampus
    • Ghribi, O., M.M. Herman, and J. Savory. 2002. The endoplasmic reticulum is the main site for caspase-3 activation following aluminum-induced neurotoxicity in rabbit hippocampus. Neurosci. Lett. 324:217-221.
    • (2002) Neurosci. Lett. , vol.324 , pp. 217-221
    • Ghribi, O.1    Herman, M.M.2    Savory, J.3
  • 7
    • 0034905394 scopus 로고    scopus 로고
    • XIAP: Apoptotic brake and promising therapeutic target
    • Holcik, M., H. Gibson, and R.G. Korneluk. 2001. XIAP: Apoptotic brake and promising therapeutic target. Apoptosis 6:253-261.
    • (2001) Apoptosis , vol.6 , pp. 253-261
    • Holcik, M.1    Gibson, H.2    Korneluk, R.G.3
  • 9
    • 0033555642 scopus 로고    scopus 로고
    • Analysis of a conditional degradation signal in yeast and mammalian cells
    • Levy, F., J.A. Johnston, and A. Varshavsky. 1999. Analysis of a conditional degradation signal in yeast and mammalian cells. Eur. J. Biochem. 259:244-252.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 244-252
    • Levy, F.1    Johnston, J.A.2    Varshavsky, A.3
  • 10
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane, M., W. Merrison, S.B. Bratton, and G.M. Cohen. 2002. Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J. Biol. Chem. 277:36611-36616.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 11
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal
    • Martin, D.A., R.M. Siegel, L. Zheng, and M.J. Lenardo. 1998. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J. Biol. Chem. 273:4345-4349.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 12
    • 0031664635 scopus 로고    scopus 로고
    • Signaling by proteolysis: Death receptors induce apoptosis
    • Muzio, M. 1998. Signaling by proteolysis: Death receptors induce apoptosis. Int. J. Clin. Lab. Res. 28:141-147.
    • (1998) Int. J. Clin. Lab. Res. , vol.28 , pp. 141-147
    • Muzio, M.1
  • 13
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
    • Muzio, M., G.S. Salvesen, and V.M. Dixit. 1997. FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem. 272:2952-2956.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 15
    • 0018795188 scopus 로고
    • A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • Noel, D., K. Nikaido, and G.F. Ames. 1979. A single amino acid substitution in a histidine-transport protein drastically alters its mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Biochemistry 18:4159-4165.
    • (1979) Biochemistry , vol.18 , pp. 4159-4165
    • Noel, D.1    Nikaido, K.2    Ames, G.F.3
  • 16
    • 0035896592 scopus 로고    scopus 로고
    • Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation
    • Qin, Z.H., Y. Wang, K.K. Kikly, E. Sapp, K.B. Kegel, N. Aronin, and M. DiFiglia. 2001. Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation. J. Biol. Chem. 276:8079-8086.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8079-8086
    • Qin, Z.H.1    Wang, Y.2    Kikly, K.K.3    Sapp, E.4    Kegel, K.B.5    Aronin, N.6    DiFiglia, M.7
  • 17
    • 0032511880 scopus 로고    scopus 로고
    • Cell suicide for beginners
    • Raff, M. 1998. Cell suicide for beginners. Nature 396:119-122.
    • (1998) Nature , vol.396 , pp. 119-122
    • Raff, M.1
  • 19
    • 0034129406 scopus 로고    scopus 로고
    • Nuclear localization of procaspase-9 and processing by a caspase-3-like activity in mammary epithelial cells
    • Ritter, P.M., A. Marti, C. Blanc, A. Baltzer, S. Krajewski, J.C. Reed, and R. Jaggi. 2000. Nuclear localization of procaspase-9 and processing by a caspase-3-like activity in mammary epithelial cells. Eur. J. Cell Biol. 79:358-364.
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 358-364
    • Ritter, P.M.1    Marti, A.2    Blanc, C.3    Baltzer, A.4    Krajewski, S.5    Reed, J.C.6    Jaggi, R.7
  • 20
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • Salvesen, G.S. and V.M. Dixit. 1997. Caspases: Intracellular signaling by proteolysis. Cell 91:443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 21
    • 0032541132 scopus 로고    scopus 로고
    • Detection of pro-caspase-3 in cytosol and mitochondria of various tissues
    • Samali, A., B. Zhivotovsky, D.P. Jones, and S. Orrenius. 1998. Detection of pro-caspase-3 in cytosol and mitochondria of various tissues. FEBS Lett. 431:167-169.
    • (1998) FEBS Lett. , vol.431 , pp. 167-169
    • Samali, A.1    Zhivotovsky, B.2    Jones, D.P.3    Orrenius, S.4
  • 23
    • 0034796446 scopus 로고    scopus 로고
    • Effect of pH, ionic charge, and osmolality on cytochrome c-mediated caspase-3 activity
    • Segal, M.S. and E. Beem. 2001. Effect of pH, ionic charge, and osmolality on cytochrome c-mediated caspase-3 activity. Am. J. Physiol. Cell Physiol. 281:C1196-C1204.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Segal, M.S.1    Beem, E.2
  • 27
    • 0034615555 scopus 로고    scopus 로고
    • Caspases - Controlling intracellular signals by protease zymogen activation
    • Stennicke, H.R. and G.S. Salvesen. 2000. Caspases - Controlling intracellular signals by protease zymogen activation. Biochim. Biophys. Acta 1477:299-306.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 299-306
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 29
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry, N.A. and Y. Lazebnik. 1998. Caspases: Enemies within. Science 281:1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 30
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry, N.A., T.A. Rano, E.P. Peterson, D.M. Rasper, T. Timkey, M. Garcia-Calvo, V.M. Houtzager, P.A. Nordstrom, et al. 1997. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272:17907-17911.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3    Rasper, D.M.4    Timkey, T.5    Garcia-Calvo, M.6    Houtzager, V.M.7    Nordstrom, P.A.8
  • 31
    • 3342989359 scopus 로고    scopus 로고
    • Diversity of caspase involvement in neuronal cell death
    • M.P. Mattson, S. Estus, and V.M. Rangnekar (Eds.), Elsevier, Baltimore, MD
    • Troy, C.M. 2001. Diversity of caspase involvement in neuronal cell death, p. 67-91. In M.P. Mattson, S. Estus, and V.M. Rangnekar (Eds.), Programmed Cell Death Volume 1 -Cellular and Molecular Mechanisms. Elsevier, Baltimore, MD.
    • (2001) Programmed Cell Death-Cellular and Molecular Mechanisms , vol.1 , pp. 67-91
    • Troy, C.M.1
  • 32
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: Functions, mysteries, uses
    • Varshavsky, A. 1996. The N-end rule: Functions, mysteries, uses. Proc. Natl. Acad. Sci. USA 93:12142-12149.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 34
    • 0034921727 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
    • 2:REVIEWS
    • Verhagen, A.M., E.J. Coulson, and D.L. Vaux. 2001. Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs. Genome Biol 2:REVIEWS3009.
    • (2001) Genome Biol. , vol.3009
    • Verhagen, A.M.1    Coulson, E.J.2    Vaux, D.L.3
  • 35
    • 0036204018 scopus 로고    scopus 로고
    • Cell death regulation by the mammalian IAP antagonist Diablo/Smac
    • Verhagen, A.M. and D.L. Vaux. 2002. Cell death regulation by the mammalian IAP antagonist Diablo/Smac. Apoptosis 7:163-166.
    • (2002) Apoptosis , vol.7 , pp. 163-166
    • Verhagen, A.M.1    Vaux, D.L.2
  • 37
    • 12244294034 scopus 로고    scopus 로고
    • Detection of caspase activity associated with apoptosis using fluorimetric and colorimetric methods
    • L. Zhu and J. Chun (Eds.). Eaton Publishing, Westborough, MA
    • Zhang, G., V. Gurtu, C. Spencer, J.-T. Ma, and S.R. Kain. 1998. Detection of caspase activity associated with apoptosis using fluorimetric and colorimetric methods, p. 7-14. In L. Zhu and J. Chun (Eds.), Apoptosis Detection and Assay Methods. Eaton Publishing, Westborough, MA.
    • (1998) Apoptosis Detection and Assay Methods , pp. 7-14
    • Zhang, G.1    Gurtu, V.2    Spencer, C.3    Ma, J.-T.4    Kain, S.R.5
  • 38
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • Zhivotovsky, B., A. Samali, A. Gahm, and S. Orrenius. 1999. Caspases: Their intracellular localization and translocation during apoptosis. Cell Death Differ. 6:644-651.
    • (1999) Cell Death Differ. , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.