메뉴 건너뛰기




Volumn 19, Issue 6, 1997, Pages 501-507

Death substrates come alive

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0031170966     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950190609     Document Type: Review
Times cited : (166)

References (60)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr, J.F.R., Wyllie, A.H. and Currie, A.R. (1972). Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0029670265 scopus 로고    scopus 로고
    • ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis
    • Nicholson, D.W. (1996). ICE/CED3-like proteases as therapeutic targets for the control of inappropriate apoptosis. Nature Biotech. 14, 297-301.
    • (1996) Nature Biotech. , vol.14 , pp. 297-301
    • Nicholson, D.W.1
  • 3
    • 0029959882 scopus 로고    scopus 로고
    • Apoptosis: Molecular regulation of cell death
    • Hale, A.J. et al. (1996). Apoptosis: molecular regulation of cell death. Eur. J. Biochem. 236, 1-26.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 1-26
    • Hale, A.J.1
  • 4
    • 0009530192 scopus 로고    scopus 로고
    • Human ICE/CED-3 protease nomenclature
    • Alnemri, E.S. et al. (1996). Human ICE/CED-3 protease nomenclature. Cell 87, 171.
    • (1996) Cell , vol.87 , pp. 171
    • Alnemri, E.S.1
  • 5
    • 0029894529 scopus 로고    scopus 로고
    • ICE/CED-3 proteases in apoptosis
    • Whyte, M. (1996). ICE/CED-3 proteases in apoptosis. Trends Cell Biol. 6, 245-248.
    • (1996) Trends Cell Biol. , vol.6 , pp. 245-248
    • Whyte, M.1
  • 6
    • 0029794385 scopus 로고    scopus 로고
    • The ICE family of cysteine proteases as effectors of cell death
    • Kumar, S. and Lavin, M.F. (1996). The ICE family of cysteine proteases as effectors of cell death. Cell Death Diff. 3, 255-267.
    • (1996) Cell Death Diff. , vol.3 , pp. 255-267
    • Kumar, S.1    Lavin, M.F.2
  • 7
    • 0029657717 scopus 로고    scopus 로고
    • Cell death in vertebrates: Lessons from the worm
    • Osborne, B.A. (1996). Cell death in vertebrates: lessons from the worm. Trends Genet. 12, 489-491.
    • (1996) Trends Genet. , vol.12 , pp. 489-491
    • Osborne, B.A.1
  • 8
    • 0028102478 scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE
    • Lazebnik, Y.A., Kaufmann, S.H., Desnoyers, S., Poirier, G.G. and Earnshaw, W.C. (1994). Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature 371, 346-347.
    • (1994) Nature , vol.371 , pp. 346-347
    • Lazebnik, Y.A.1    Kaufmann, S.H.2    Desnoyers, S.3    Poirier, G.G.4    Earnshaw, W.C.5
  • 9
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida, K. et al. (1996). Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384, 368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1
  • 10
    • 0031023782 scopus 로고    scopus 로고
    • DCP-1, a Drosophila cell death protease essential for development
    • Song, Z., McCall, K. and Steller, H. (1997). DCP-1, a Drosophila cell death protease essential for development. Science 275, 536-540.
    • (1997) Science , vol.275 , pp. 536-540
    • Song, Z.1    McCall, K.2    Steller, H.3
  • 12
    • 0030044324 scopus 로고    scopus 로고
    • ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein, Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis
    • Duan H., Chinnaiyan A.M., Hudson, P.L., Wing, J.P., He, W.-W. and Dixit, V.M. (1996). ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein, Ced-3 is activated during Fas-and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 271, 1621-1625.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1621-1625
    • Duan, H.1    Chinnaiyan, A.M.2    Hudson, P.L.3    Wing, J.P.4    He, W.-W.5    Dixit, V.M.6
  • 13
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during fas-mediated apoptosis
    • Enari, M., Talanian, R.V., Wong, W.W. and Nagata, S. (1996). Sequential activation of ICE-like and CPP32-like proteases during fas-mediated apoptosis. Nature 380, 723-726.
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 14
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains
    • Fernandez-Alnemri, T. et al. (1996). In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proc. Natl Acad. Sci. USA 93, 7464-7469.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7464-7469
    • Fernandez-Alnemri, T.1
  • 15
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of mammalian CED-3/ICE-like proteases
    • Orth, K., O'Rourke, K., Salvesen, G.S. and Dixit, V.M. (1996). Molecular ordering of mammalian CED-3/ICE-like proteases. J. Biol. Chem. 271, 20977-20980.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20977-20980
    • Orth, K.1    O'Rourke, K.2    Salvesen, G.S.3    Dixit, V.M.4
  • 16
    • 16044372676 scopus 로고    scopus 로고
    • Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B
    • Shi, L. et al. (1996). Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B. Proc. Natl Acad. Sci. USA 93, 11002-11007.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11002-11007
    • Shi, L.1
  • 17
    • 0030008812 scopus 로고    scopus 로고
    • ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B
    • Duan, H. et al. (1996). ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. J. Biol. Chem. 271, 16720-16724.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16720-16724
    • Duan, H.1
  • 19
    • 9344261615 scopus 로고    scopus 로고
    • The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease CPP32, via a novel two-step mechanism
    • Martin, S.J. et al. (1996). The cytotoxic cell protease granzyme B initiates apoptosis in a cell-free system by proteolytic processing and activation of the ICE/CED-3 family protease CPP32, via a novel two-step mechanism. EMBO J. 15, 2407-2416.
    • (1996) EMBO J. , vol.15 , pp. 2407-2416
    • Martin, S.J.1
  • 20
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex
    • Muzio, M. et al. (1996). FLICE, a novel FADD homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/Apo-1) death-inducing signaling complex. Cell 85, 817-827.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1
  • 21
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in fas/APO-1 and TNF receptor-induced cell death
    • Boldin, M., Goncharov, T.M., Goltsev, Y.V. and Wallach, D. (1996). Involvement of MACH, a novel MORT1/FADD-interacting protease, in fas/APO-1 and TNF receptor-induced cell death. Cell 85, 805-815.
    • (1996) Cell , vol.85 , pp. 805-815
    • Boldin, M.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 22
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme
    • Kuida, K. et al. (1995). Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267, 2000-2002.
    • (1995) Science , vol.267 , pp. 2000-2002
    • Kuida, K.1
  • 23
    • 15644369352 scopus 로고    scopus 로고
    • Activation of interferon-γ inducing factor mediated by interleukin-1β converting enzyme
    • Gu, Y. et al. (1996). Activation of interferon-γ inducing factor mediated by interleukin-1β converting enzyme. Science 275, 206-209.
    • (1996) Science , vol.275 , pp. 206-209
    • Gu, Y.1
  • 24
    • 0029788702 scopus 로고    scopus 로고
    • Functional role of interleukin 1β (1L-1β) in IL-1β-converting enzyme-mediated apoptosis
    • Friedlander, R.M., Gagliardini, V., Rotello, R.J. and Yuan, J. (1996). Functional role of interleukin 1β (1L-1β) in IL-1β-converting enzyme-mediated apoptosis. J. Exp. Med 184, 717-724.
    • (1996) J. Exp. Med , vol.184 , pp. 717-724
    • Friedlander, R.M.1    Gagliardini, V.2    Rotello, R.J.3    Yuan, J.4
  • 25
    • 13344259987 scopus 로고
    • Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells
    • Emoto, Y. et al. (1995). Proteolytic activation of protein kinase Cδ by an ICE-like protease in apoptotic cells. EMBO J. 14, 6148-6156.
    • (1995) EMBO J. , vol.14 , pp. 6148-6156
    • Emoto, Y.1
  • 26
    • 12644268232 scopus 로고    scopus 로고
    • Proteolytic activation of protein kinase Cδ by an ICE/CED 3-like protease induces characteristics of apoptosis
    • Ghayur, T. et al. (1996). Proteolytic activation of protein kinase Cδ by an ICE/CED 3-like protease induces characteristics of apoptosis. J. Exp. Med. 184, 2399-2404.
    • (1996) J. Exp. Med. , vol.184 , pp. 2399-2404
    • Ghayur, T.1
  • 27
    • 0029895343 scopus 로고    scopus 로고
    • Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins
    • Pai, J.-T., Brown, M.S. and Goldstein, J.L. (1996). Purification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteins. Proc. Natl Acad. Sci. USA 93, 5437-5442.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 5437-5442
    • Pai, J.-T.1    Brown, M.S.2    Goldstein, J.L.3
  • 28
    • 0029046470 scopus 로고
    • Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution
    • Lazebnik, Y. et al. (1995). Studies of the lamin proteinase reveal multiple parallel biochemical pathways during apoptotic execution. Proc. Natl Acad. Sci. USA 92, 9042-9046.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9042-9046
    • Lazebnik, Y.1
  • 29
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth, K., Chinnaiyan, A.M., Garg, M., Froelich, C.J. and Dixit, V.M. (1996). The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271, 16443-16446.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 30
    • 0029758833 scopus 로고    scopus 로고
    • Cleavage of lamin A by Mch2α but not CPP32: Multiple interleukin 1β-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis
    • Takahashi, A. et al. (1996). Cleavage of lamin A by Mch2α but not CPP32: multiple interleukin 1β-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosis. Proc. Natl Acad. Sci. USA 93, 8395-8400.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 8395-8400
    • Takahashi, A.1
  • 31
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • Rao, L., Perez, D. and White, E. (1996). Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135, 1441-1455.
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 32
    • 0028788309 scopus 로고
    • Microfilament reorganization during apoptosis: The role of Gas2, a possible substrate for ICE-like proteases
    • Brancolini, C., Benedetti, M. and Schneider, C. (1995). Microfilament reorganization during apoptosis: the role of Gas2, a possible substrate for ICE-like proteases. EMBO J. 14, 5179-5190.
    • (1995) EMBO J. , vol.14 , pp. 5179-5190
    • Brancolini, C.1    Benedetti, M.2    Schneider, C.3
  • 33
    • 0029959632 scopus 로고    scopus 로고
    • Specific cleavage of α-fodrin during fas- and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1β-converting enzyme/ced3 protease distinct from the poly(ADP-ribose) polymerase protease
    • Cryns, V.L., Bergeron, L., Zhu, H., Li, H. and Yuan, J. (1996). Specific cleavage of α-fodrin during fas-and tumor necrosis factor-induced apoptosis is mediated by an interleukin-1β-converting enzyme/ced3 protease distinct from the poly(ADP-ribose) polymerase protease. J. Biol. Chem. 271, 31277-31282.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31277-31282
    • Cryns, V.L.1    Bergeron, L.2    Zhu, H.3    Li, H.4    Yuan, J.5
  • 34
    • 0029876247 scopus 로고    scopus 로고
    • Cleavage of actin by interleukin 1β-converting enzyme to reverse DNase I inhibition
    • Kayalar, C., Ord, T., Pia Testa, M., Zhong, L.-T. and Bredesen, D.E. (1996). Cleavage of actin by interleukin 1β-converting enzyme to reverse DNase I inhibition. Proc. Natl Acad. Sci. USA 93, 2234-2238.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2234-2238
    • Kayalar, C.1    Ord, T.2    Pia Testa, M.3    Zhong, L.-T.4    Bredesen, D.E.5
  • 36
    • 0028922462 scopus 로고
    • Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease
    • Wang, Z-Q. et al. (1995). Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes Dev. 9, 509-520.
    • (1995) Genes Dev. , vol.9 , pp. 509-520
    • Wang, Z.-Q.1
  • 37
    • 0029166984 scopus 로고
    • Cleavage of poly(ADP-ribose)polymerase by interleukin-1β converting enzyme and its homologs TX and Nedd-2
    • Gu, Y., Sarnecki, C., Aldape, R.A., Livingston, D.J. and Su, M.S.-S. (1995). Cleavage of poly(ADP-ribose)polymerase by interleukin-1β converting enzyme and its homologs TX and Nedd-2. J. Biol. Chem. 270, 18715-18718.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18715-18718
    • Gu, Y.1    Sarnecki, C.2    Aldape, R.A.3    Livingston, D.J.4    Su, M.S.-S.5
  • 38
    • 0030044012 scopus 로고    scopus 로고
    • Identification and characterization of CPP32/Mch2 Homology 1, a novel cysteine protease similar to CPP32
    • Lippke, J.A., Gu, Y., Sarnecki, C., Caron, P.R. and Su, M.S.-S. (1996). Identification and characterization of CPP32/Mch2 Homology 1, a novel cysteine protease similar to CPP32. J Biol. Chem. 271, 1825-1828.
    • (1996) J Biol. Chem. , vol.271 , pp. 1825-1828
    • Lippke, J.A.1    Gu, Y.2    Sarnecki, C.3    Caron, P.R.4    Su, M.S.-S.5
  • 39
    • 0029670910 scopus 로고    scopus 로고
    • CPP32/apopain is a key interleukin 1β-converting enzyme-like protease involved in fas-mediated apoptosis
    • Schlegel, J. et al. (1996). CPP32/apopain is a key interleukin 1β-converting enzyme-like protease involved in fas-mediated apoptosis. J. Biol. Chem. 271, 1841-1844.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1841-1844
    • Schlegel, J.1
  • 40
    • 8944241298 scopus 로고    scopus 로고
    • DNA-dependent protein kinase catalytic subunit: A target for an ICE-like protease in apoptosis
    • Song, Q. et al. (1996). DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis. EMBO J. 15, 3238-3246.
    • (1996) EMBO J. , vol.15 , pp. 3238-3246
    • Song, Q.1
  • 41
    • 0029890823 scopus 로고    scopus 로고
    • Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death
    • Casciola-Rosen, L. et al. (1996). Apopain/CPP32 cleaves proteins that are essential for cellular repair: a fundamental principle of apoptotic death. J. Exp. Med. 183, 1957-1964.
    • (1996) J. Exp. Med. , vol.183 , pp. 1957-1964
    • Casciola-Rosen, L.1
  • 42
    • 0027999537 scopus 로고
    • Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death
    • Casciola-Rosen, L.A., Miller, D.K., Anhalt, G.J. and Rosen, A. (1994). Specific cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein is a characteristic biochemical feature of apoptotic cell death. J. Biol. Chem. 269, 30757-30760.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30757-30760
    • Casciola-Rosen, L.A.1    Miller, D.K.2    Anhalt, G.J.3    Rosen, A.4
  • 43
    • 0029102383 scopus 로고
    • CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas- and tumor necrosis factor-induced apoptosis
    • Tewari, M., Beidler, D. and Dixit, V.M. (1995). CrmA-inhibitable cleavage of the 70-kDa protein component of the U1 small nuclear ribonucleoprotein during Fas-and tumor necrosis factor-induced apoptosis. J. Biol. Chem. 270, 18738-18741.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18738-18741
    • Tewari, M.1    Beidler, D.2    Dixit, V.M.3
  • 44
    • 0029789073 scopus 로고    scopus 로고
    • Selective cleavage of nuclear autoantigens during CD95 (Fas/APO-1)-mediated T cell apoptosis
    • Casiano, C.A., Martin, S.J., Green, D.R. and Tan, E.M. (1996). Selective cleavage of nuclear autoantigens during CD95 (Fas/APO-1)-mediated T cell apoptosis. J. Exp. Med. 184, 765-770.
    • (1996) J. Exp. Med. , vol.184 , pp. 765-770
    • Casiano, C.A.1    Martin, S.J.2    Green, D.R.3    Tan, E.M.4
  • 46
    • 0028791435 scopus 로고
    • Functions of pRb and p53: What's the connection?
    • Kouzarides, T. (1995). Functions of pRb and p53: what's the connection? Trends Cell Biol. 5, 448-450.
    • (1995) Trends Cell Biol. , vol.5 , pp. 448-450
    • Kouzarides, T.1
  • 47
    • 0030462563 scopus 로고    scopus 로고
    • Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
    • Jänicke, R.U., Walker, P.A., Lin, X.Y. and Porter, A.G. (1996) Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. 15, 6969-6978.
    • (1996) EMBO J. , vol.15 , pp. 6969-6978
    • Jänicke, R.U.1    Walker, P.A.2    Lin, X.Y.3    Porter, A.G.4
  • 48
    • 0030023846 scopus 로고    scopus 로고
    • Cleavage of the retinoblastoma protein during apoptosis: An interleukin 1β-converting enzyme-like protease as candidate
    • An, B. and Ping Dou, Q. (1996). Cleavage of the retinoblastoma protein during apoptosis: an interleukin 1β-converting enzyme-like protease as candidate. Cancer Res. 56, 438-442.
    • (1996) Cancer Res. , vol.56 , pp. 438-442
    • An, B.1    Ping Dou, Q.2
  • 49
    • 0029985647 scopus 로고    scopus 로고
    • Cell type-specific inhibition of p53-mediated apoptosis by mdm2
    • Haupt, Y., Barak, Y. and Oren, M. (1996). Cell type-specific inhibition of p53-mediated apoptosis by mdm2. EMBO J. 15, 1596-1606.
    • (1996) EMBO J. , vol.15 , pp. 1596-1606
    • Haupt, Y.1    Barak, Y.2    Oren, M.3
  • 50
    • 0141630973 scopus 로고    scopus 로고
    • Cyclin D3 sensitizes tumor cells to tumor necrosis factor-induced, c-Myc-dependent apoptosis
    • Jänicke, R.U., Lin, X.Y., Lee, F.H.H. and Porter, A.G. (1996). Cyclin D3 sensitizes tumor cells to tumor necrosis factor-induced, c-Myc-dependent apoptosis. Mol. Cell. Biol. 16, 5245-5253.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5245-5253
    • Jänicke, R.U.1    Lin, X.Y.2    Lee, F.H.H.3    Porter, A.G.4
  • 51
    • 9344227302 scopus 로고    scopus 로고
    • Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract
    • Goldberg, Y.P. et al. (1996). Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nature Genetics 13, 442-449.
    • (1996) Nature Genetics , vol.13 , pp. 442-449
    • Goldberg, Y.P.1
  • 52
    • 0028268215 scopus 로고
    • Programmed cell death and Bcl-2 protection in the absence of a nucleus
    • Jacobson, M.D., Burne, J.F. and Raff, M.C. (1994). Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J. 13, 1899-1910.
    • (1994) EMBO J. , vol.13 , pp. 1899-1910
    • Jacobson, M.D.1    Burne, J.F.2    Raff, M.C.3
  • 53
    • 0027437541 scopus 로고
    • Nuclear events of apoptosis in vitro in cell-free mitotic extracts: A model system for analysis of the active phase of apoptosis
    • Lazebnik, J.A., Cole, S., Cooke, C.A., Nelson, W.G. and Earnshaw, W.C. (1993). Nuclear events of apoptosis in vitro in cell-free mitotic extracts: a model system for analysis of the active phase of apoptosis. J. Cell. Biol. 123, 7-22.
    • (1993) J. Cell. Biol. , vol.123 , pp. 7-22
    • Lazebnik, J.A.1    Cole, S.2    Cooke, C.A.3    Nelson, W.G.4    Earnshaw, W.C.5
  • 54
    • 0027994239 scopus 로고
    • Cell nucleus and DNA fragmentation are not required for apoptosis
    • Schulze-Osthoff, K., Walczak, H., Dröge, W. and Krammer, P.H. (1994). Cell nucleus and DNA fragmentation are not required for apoptosis. J. Cell Biol. 127, 15-20.
    • (1994) J. Cell Biol. , vol.127 , pp. 15-20
    • Schulze-Osthoff, K.1    Walczak, H.2    Dröge, W.3    Krammer, P.H.4
  • 55
    • 0029959819 scopus 로고    scopus 로고
    • Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents
    • Lotem, J. and Sachs, L. (1996). Differential suppression by protease inhibitors and cytokines of apoptosis induced by wild-type p53 and cytotoxic agents. Proc. Natl Acad. Sci. USA 93, 12507-12512.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12507-12512
    • Lotem, J.1    Sachs, L.2
  • 56
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/APO-1 and TNF-α
    • Deiss, L.P., Galinka, H., Berissi, H., Cohen, O. and Kimchi, A. (1996). Cathepsin D protease mediates programmed cell death induced by interferon-γ, Fas/APO-1 and TNF-α. EMBO J. 15, 3861-3870.
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 58
    • 0029951250 scopus 로고    scopus 로고
    • Defective Rho GTPase regulation by IL-1β-converting enzyme-mediated cleavage of D4 GDP dissociation inhibitor
    • Danley, D.E., Chuang, T.-H. and Bokoch, G.M. (1996). Defective Rho GTPase regulation by IL-1β-converting enzyme-mediated cleavage of D4 GDP dissociation inhibitor. J. Immunol. 157, 500-503.
    • (1996) J. Immunol. , vol.157 , pp. 500-503
    • Danley, D.E.1    Chuang, T.-H.2    Bokoch, G.M.3
  • 59
    • 15844409177 scopus 로고    scopus 로고
    • D4-GDI, a substrate of CPP32, is proteolysed during fas-induced apoptosis
    • Na, S. et al. (1996). D4-GDI, a substrate of CPP32, is proteolysed during fas-induced apoptosis. J. Biol. Chem. 271, 11209-11213.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11209-11213
    • Na, S.1
  • 60
    • 10544220838 scopus 로고    scopus 로고
    • Heteronuclear ribonucleoproteins C1 and C2, components of the spliceosome, are specific targets of interleukin 1β-converting enzyme-like proteases in apoptosis
    • Waterhouse, N. et al. (1996). Heteronuclear ribonucleoproteins C1 and C2, components of the spliceosome, are specific targets of interleukin 1β-converting enzyme-like proteases in apoptosis. J. Biol. Chem. 271, 29335-29341.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29335-29341
    • Waterhouse, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.