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Volumn 53, Issue 3, 2003, Pages 151-164

Biochemistry of apoptotic cell death

Author keywords

Apoptosis; Apoptosis inducing factors (AIF); Bcl 2 family; Caspases; Heat shock proteins (Hsps); Inhibitors of apoptosis (IAP); Mitogen activated protein kinases (MAPKs)

Indexed keywords

APOPTOSIS INDUCING FACTOR; APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE; CASPASE 3; COMPLEMENT COMPONENT C1Q; CYTOCHROME C; DNA FRAGMENT; FAS ANTIGEN; FOCAL ADHESION KINASE; GELSOLIN; GRANZYME B; GUANINE NUCLEOTIDE BINDING PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; INHIBITOR OF APOPTOSIS PROTEIN; INTERCELLULAR ADHESION MOLECULE 3; MITOGEN ACTIVATED PROTEIN KINASE; MYOSIN LIGHT CHAIN KINASE; PROTEIN BAD; PROTEIN BCL 2; PROTEIN BCL W; PROTEIN BCL XL; PROTEIN BID; PROTEIN MCL 1; REACTIVE OXYGEN METABOLITE; RHO FACTOR; STRESS ACTIVATED PROTEIN KINASE; TUMOR NECROSIS FACTOR; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0142214549     PISSN: 13300075     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (34)

References (85)
  • 1
    • 0015408189 scopus 로고
    • Cytolysis induced by human lymphotoxin
    • S. W. Russell, W. Rosenau and J. C. Lee, Cytolysis induced by human lymphotoxin, Am. J. Pathol. 69 (1972) 103-118.
    • (1972) Am. J. Pathol. , vol.69 , pp. 103-118
    • Russell, S.W.1    Rosenau, W.2    Lee, J.C.3
  • 2
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J. F. Kerr, A. H. Wyllie and A. R. Currie, Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics, Br. J. Cancer 26 (1972) 239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0019731239 scopus 로고
    • Biophysical and morphological correlates of kinetic change and death in a starved human melanoma cell line
    • J. W. Sheridan, C. J. Bishop and R. J. Simmons, Biophysical and morphological correlates of kinetic change and death in a starved human melanoma cell line, J. Cell Sci. 49 (1981) 119-137.
    • (1981) J. Cell Sci. , vol.49 , pp. 119-137
    • Sheridan, J.W.1    Bishop, C.J.2    Simmons, R.J.3
  • 4
    • 0029063180 scopus 로고
    • Spontaneous apoptosis of dendritic cells is efficiently inhibited by TRAP (CD40-ligand) and TNF-, but strongly enhanced by interleukin-10
    • B. Ludewig, D. Graf, H. R. Gelderblom, Y. Becker, R. A. Kroczek and G. Pauli, Spontaneous apoptosis of dendritic cells is efficiently inhibited by TRAP (CD40-ligand) and TNF-, but strongly enhanced by interleukin-10, Eur. J. Immunol. 25 (1995) 1943-1950.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 1943-1950
    • Ludewig, B.1    Graf, D.2    Gelderblom, H.R.3    Becker, Y.4    Kroczek, R.A.5    Pauli, G.6
  • 5
    • 0033177892 scopus 로고    scopus 로고
    • Cytoplasmic vacuolation, adaptation and cell death: A view on new perspectives and features
    • T. Henics and D. N. Wheatley, Cytoplasmic vacuolation, adaptation and cell death: a view on new perspectives and features, Biol. Cell 91 (1999) 485-498.
    • (1999) Biol. Cell , vol.91 , pp. 485-498
    • Henics, T.1    Wheatley, D.N.2
  • 6
    • 0030712860 scopus 로고    scopus 로고
    • ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis
    • T. Kondo, K. Takeuchi, Y. Doi, S. Yonemura, S. Nagata and S. Tsukita, ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis, J. Cell Biol. 139 (1997) 749-758.
    • (1997) J. Cell Biol. , vol.139 , pp. 749-758
    • Kondo, T.1    Takeuchi, K.2    Doi, Y.3    Yonemura, S.4    Nagata, S.5    Tsukita, S.6
  • 7
    • 0032455357 scopus 로고    scopus 로고
    • An ultrastructural and immunohistochemical study of PC12 cells during apoptosis induced by serum deprivation with special reference to autophagy and lysosomal cathepsins
    • Y. Ohsawa, K. Isahara, S. Kanamori, M. Shibata, S. Kametaka, T. Gotow, T. Watanabe, E. Kominami and Y. Uchiyama, An ultrastructural and immunohistochemical study of PC12 cells during apoptosis induced by serum deprivation with special reference to autophagy and lysosomal cathepsins, Arch. Histol. Cytol. 61 (1998) 395-403.
    • (1998) Arch. Histol. Cytol. , vol.61 , pp. 395-403
    • Ohsawa, Y.1    Isahara, K.2    Kanamori, S.3    Shibata, M.4    Kametaka, S.5    Gotow, T.6    Watanabe, T.7    Kominami, E.8    Uchiyama, Y.9
  • 9
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • N. A. Thornberry and Y. Lazebnik, Caspases: enemies within, Science 281 (1998) 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 10
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • K. K. Wang, Calpain and caspase: can you tell the difference?, Trends Neurosci. 23 (2000) 20-26.
    • (2000) Trends Neurosci. , vol.23 , pp. 20-26
    • Wang, K.K.1
  • 12
    • 0035811511 scopus 로고    scopus 로고
    • Mitochondrial endonuclease G is important for apoptosis in C. elegans
    • J. Parrish, L. Li, K. Klotz, D. Ledwich, X. Wang and D. Xue, Mitochondrial endonuclease G is important for apoptosis in C. elegans, Nature 412 (2001) 90-94.
    • (2001) Nature , vol.412 , pp. 90-94
    • Parrish, J.1    Li, L.2    Klotz, K.3    Ledwich, D.4    Wang, X.5    Xue, D.6
  • 14
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • X. Liu, H. Zou, C. Slaughter and X. Wang, DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis, Cell 89 (1997) 175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 15
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • M. Enari, H. Sakahira, H. Yokoyama, K. Okawa, A. Iwamatsu and S. Nagata, A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD, Nature 391 (1998) 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 16
    • 0031889132 scopus 로고    scopus 로고
    • Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis
    • H. Sakahira, M. Enari and S. Nagata, Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis, Nature 391 (1998) 96-99.
    • (1998) Nature , vol.391 , pp. 96-99
    • Sakahira, H.1    Enari, M.2    Nagata, S.3
  • 17
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • L. Rao, D. Perez and E. White, Lamin proteolysis facilitates nuclear events during apoptosis, J. Cell Biol. 135 (1996) 1441-1455.
    • (1996) J. Cell Biol. , vol.135 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 18
    • 0033020265 scopus 로고    scopus 로고
    • Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis
    • B. Buendia, A. Santa-Maria and J. C. Courvalin, Caspase-dependent proteolysis of integral and peripheral proteins of nuclear membranes and nuclear pore complex proteins during apoptosis, J. Cell Sci. 112 (1999) 1743-1753.
    • (1999) J. Cell Sci. , vol.112 , pp. 1743-1753
    • Buendia, B.1    Santa-Maria, A.2    Courvalin, J.C.3
  • 19
    • 0032536543 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis
    • B. Levkau, B. Herren, H. Koyama, R. Ross and E. W. Raines, Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis, J. Exp. Med. 187 (1998) 579-586.
    • (1998) J. Exp. Med. , vol.187 , pp. 579-586
    • Levkau, B.1    Herren, B.2    Koyama, H.3    Ross, R.4    Raines, E.W.5
  • 20
    • 0032583203 scopus 로고    scopus 로고
    • SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis
    • J. Huot, F. Houle, S. Rousseau, R. G. Deschesnes, G. M. Shah and J. Landry, SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis, J. Cell Biol. 143 (1998) 1361-1373.
    • (1998) J. Cell Biol. , vol.143 , pp. 1361-1373
    • Huot, J.1    Houle, F.2    Rousseau, S.3    Deschesnes, R.G.4    Shah, G.M.5    Landry, J.6
  • 21
    • 0031443641 scopus 로고    scopus 로고
    • Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis
    • N. Lee, H. MacDonald, C. Reinhard, R. Halenbeck, A. Roulston, T. Shi and L. T. Williams, Activation of hPAK65 by caspase cleavage induces some of the morphological and biochemical changes of apoptosis, Proc. Natl. Acad. Sci. USA 94 (1997) 13642-13647.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13642-13647
    • Lee, N.1    MacDonald, H.2    Reinhard, C.3    Halenbeck, R.4    Roulston, A.5    Shi, T.6    Williams, L.T.7
  • 22
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • W. C. Earnshaw, L. M. Martins and S. H. Kaufmann, Mammalian caspases: structure, activation, substrates, and functions during apoptosis, Annu. Rev. Biochem. 68 (1999) 383-424.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 23
    • 0029125701 scopus 로고
    • Protease activation during apoptosis: Death by a thousand cuts?
    • S. J. Martin and D. R. Green, Protease activation during apoptosis: death by a thousand cuts? Cell 82 (1995) 349-352.
    • (1995) Cell , vol.82 , pp. 349-352
    • Martin, S.J.1    Green, D.R.2
  • 26
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • J. Rodriguez and Y. Lazebnik, Caspase-9 and APAF-1 form an active holoenzyme, Genes Dev. 13 (1999) 3179-3184.
    • (1999) Genes Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 27
    • 0032807406 scopus 로고    scopus 로고
    • The modular nature of apoptotic signaling proteins
    • K. Hofmann, The modular nature of apoptotic signaling proteins, Cell Mol. Life Sci. 55 (1999) 1113-1128.
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 1113-1128
    • Hofmann, K.1
  • 28
    • 0030465072 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain
    • B. Huang, M. Eberstadt, E. T. Olejniczak, R. P. Meadows and S. W. Fesik, NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain, Nature 384 (1996) 638-641.
    • (1996) Nature , vol.384 , pp. 638-641
    • Huang, B.1    Eberstadt, M.2    Olejniczak, E.T.3    Meadows, R.P.4    Fesik, S.W.5
  • 33
    • 0030822420 scopus 로고    scopus 로고
    • Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family
    • M. Aritomi, N. Kunishima, N. Inohara, Y. Ishibashi, S. Ohta and K. Morikawa, Crystal structure of rat Bcl-xL. Implications for the function of the Bcl-2 protein family, J. Biol. Chem. 272 (1997) 27886-27892.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27886-27892
    • Aritomi, M.1    Kunishima, N.2    Inohara, N.3    Ishibashi, Y.4    Ohta, S.5    Morikawa, K.6
  • 34
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • M. Suzuki, R. J. Youle and N. Tjandra, Structure of Bax: coregulation of dimer formation and intracellular localization, Cell 103 (2000) 645-654.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 35
    • 0033525749 scopus 로고    scopus 로고
    • Solution structure of the proapoptotic molecule BID: A structural basis for apoptotic agonists and antagonists
    • J. M. McDonnell, D. Fushman, C. L. Milliman, S. J. Korsmeyer and D. Cowburn, Solution structure of the proapoptotic molecule BID: a structural basis for apoptotic agonists and antagonists, Cell 96 (1999) 625-634.
    • (1999) Cell , vol.96 , pp. 625-634
    • McDonnell, J.M.1    Fushman, D.2    Milliman, C.L.3    Korsmeyer, S.J.4    Cowburn, D.5
  • 36
    • 0033525591 scopus 로고    scopus 로고
    • Solution structure of BID, an intracellular amplifier of apoptotic signalling
    • J. J. Chou, H. Li, G. S. Salvesen, J. Yuan and G. Wagner, Solution structure of BID, an intracellular amplifier of apoptotic signalling, Cell 96 (1999) 615-624.
    • (1999) Cell , vol.96 , pp. 615-624
    • Chou, J.J.1    Li, H.2    Salvesen, G.S.3    Yuan, J.4    Wagner, G.5
  • 37
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • R. M. Kluck, E. Bossy-Wetzel, D. R. Green and D. D. Newmeyer, The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis, Science 275 (1997) 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 41
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • M. Narita, S. Shimizu, T. Ito, T. Chittenden, R. J. Lutz, H. Matsuda and Y. Tsujimoto, Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria, Proc. Natl. Acad. Sci. USA 95 (1998) 14681-14686.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 43
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Q. L. Deveraux and J. C. Reed, IAP family proteins-suppressors of apoptosis, Genes Dev. 13 (1999) 239-252.
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 44
    • 0027537461 scopus 로고
    • An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif
    • N. E. Crook, R. J. Clem and L. K. Miller, An apoptosis-inhibiting baculovirus gene with a zinc finger-like motif, J. Virol. 67 (1993) 2168-2174.
    • (1993) J. Virol. , vol.67 , pp. 2168-2174
    • Crook, N.E.1    Clem, R.J.2    Miller, L.K.3
  • 45
    • 0031961994 scopus 로고    scopus 로고
    • Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c
    • S. Duckett, F. Li, Y. Wang, K. J. Tomaselli, C. B. Thompson and R. C. Armstrong, Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c, Mol. Cell. Biol. 18 (1998) 608-615.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 608-615
    • Duckett, S.1    Li, F.2    Wang, Y.3    Tomaselli, K.J.4    Thompson, C.B.5    Armstrong, R.C.6
  • 46
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • C. A. Joazeiro and A. M. Weissman, RING finger proteins: mediators of ubiquitin ligase activity, Cell 102 (2000) 549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 47
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli
    • Y. Yang, S. Fang, J. P. Jensen, A. M. Weissman and J. D. Ashwell, Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli, Science 288 (2000) 874-877.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 48
    • 0034282432 scopus 로고    scopus 로고
    • The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7
    • H. Huang, C. A. Joazeiro, E. Bonfoco, S. Kamada, J. D. Leverson and T. J. Hunter, The inhibitor of apoptosis, cIAP2, functions as a ubiquitin-protein ligase and promotes in vitro monoubiquitination of caspases 3 and 7, J. Biol. Chem. 275 (2000) 26661-26664.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26661-26664
    • Huang, H.1    Joazeiro, C.A.2    Bonfoco, E.3    Kamada, S.4    Leverson, J.D.5    Hunter, T.J.6
  • 49
    • 0035902601 scopus 로고    scopus 로고
    • Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
    • Y. Suzuki, Y. Nakabayashi and R. Takahashi, Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death, Proc. Natl. Acad. Sci. USA 98 (2001) 8662-8667.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 52
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control
    • Z. L. Chu, T. A. McKinsey, L. Liu, J. J. Gentry, M. H. Malim and D. W. Ballard, Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control, Proc. Natl. Acad. Sci. USA 94 (1997) 10057-10062.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 53
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • L. Hicke, Protein regulation by monoubiquitin, Nature Rev. Mol. Cell Biol. 2 (2001) 195-201.
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 54
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • C. Du, M. Fang, Y. Li, L. Li and X. Wang, Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition, Cell 102 (2000) 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 55
  • 56
    • 0034680876 scopus 로고    scopus 로고
    • Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
    • S. M. Srinivasula, P. Datta, X. J. Fan, T. Fernandes-Alnemri, Z. Huang and E. S. Alnemri, Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway, J. Biol. Chem. 275 (2000) 36152-36157.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36152-36157
    • Srinivasula, S.M.1    Datta, P.2    Fan, X.J.3    Fernandes-Alnemri, T.4    Huang, Z.5    Alnemri, E.S.6
  • 57
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis
    • D. Mosser, A. W. Caron, L. Bourget, C. Denis-Larose and B. Massie, Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis, Mol. Cell. Biol. 19 (1997) 5317-5327.
    • (1997) Mol. Cell. Biol. , vol.19 , pp. 5317-5327
    • Mosser, D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 58
    • 0030041936 scopus 로고    scopus 로고
    • Heat shock proteins increase resistance to apoptosis
    • Samali and T. G. Cotter, Heat shock proteins increase resistance to apoptosis, Exp. Cell Res. 223 (1996) 163-170.
    • (1996) Exp. Cell Res. , vol.223 , pp. 163-170
    • Samali1    Cotter, T.G.2
  • 60
    • 0036065788 scopus 로고    scopus 로고
    • Heat shock proteins and their clinical relevance
    • K. Barišić and J. Kopić, Heat shock proteins and their clinical relevance, Acta Pharm. 52 (2002) 71-82.
    • (2002) Acta Pharm. , vol.52 , pp. 71-82
    • Barisić, K.1    Kopić, J.2
  • 61
    • 0032476668 scopus 로고    scopus 로고
    • Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • M. Jaattela, D. Wissing, K. Kokholm, T. Kallunki and M. Egeblad, Hsp70 exerts its anti-apoptotic function downstream of caspase-3-like proteases, EMBO J. 17 (1998) 6124-6134.
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 62
    • 0038217763 scopus 로고    scopus 로고
    • Regulation of the heat shock conjugate Hsc70 in the mammalian cell: The characterization of the anti-apoptotic protein BAG-1 provides novel insights
    • J. Hohfeld, Regulation of the heat shock conjugate Hsc70 in the mammalian cell: the characterization of the anti-apoptotic protein BAG-1 provides novel insights, Biol. Chem. 379 (1998) 269-274.
    • (1998) Biol. Chem. , vol.379 , pp. 269-274
    • Hohfeld, J.1
  • 64
    • 0029933741 scopus 로고    scopus 로고
    • Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNF α-induced cell death
    • P. Mehlen, C. Kretz-Remy, X. Preville and A. P. Arrigo, Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNF α-induced cell death, EMBO J. 15 (1996) 2695-2706.
    • (1996) EMBO J. , vol.15 , pp. 2695-2706
    • Mehlen, P.1    Kretz-Remy, C.2    Preville, X.3    Arrigo, A.P.4
  • 65
    • 0030785821 scopus 로고    scopus 로고
    • HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs
    • C. Garrido, P. Ottavi, A. Fromentin, A. Hammann, A. P. Arrigo, B. Chauffert and P. Mehlen, HSP27 as a mediator of confluence-dependent resistance to cell death induced by anticancer drugs, Cancer Res. 57 (1997) 2661-2667.
    • (1997) Cancer Res. , vol.57 , pp. 2661-2667
    • Garrido, C.1    Ottavi, P.2    Fromentin, A.3    Hammann, A.4    Arrigo, A.P.5    Chauffert, B.6    Mehlen, P.7
  • 66
    • 0345410965 scopus 로고    scopus 로고
    • Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery
    • X. Preville, F. Salvemini, S. Ciraud, S. Chaufour, C. Paul, G. Stepien, M. V. Ursini and A. P. Arrigo, Mammalian small stress proteins protect against oxidative stress through their ability to increase glucose-6-phosphate dehydrogenase activity and by maintaining optimal cellular detoxifying machinery, Exp. Cell. Res. 247 (1999) 61-78.
    • (1999) Exp. Cell. Res. , vol.247 , pp. 61-78
    • Preville, X.1    Salvemini, F.2    Ciraud, S.3    Chaufour, S.4    Paul, C.5    Stepien, G.6    Ursini, M.V.7    Arrigo, A.P.8
  • 69
    • 0031849291 scopus 로고    scopus 로고
    • The role of phosphatidylserine in recognition of apoptotic cells by phagocytes
    • V. A. Fadok, D. L. Bratton, S. C. Frasch, M. L. Warner and P. M. Henson, The role of phosphatidylserine in recognition of apoptotic cells by phagocytes, Cell Death Differ. 5 (1998) 551-562.
    • (1998) Cell Death Differ. , vol.5 , pp. 551-562
    • Fadok, V.A.1    Bratton, D.L.2    Frasch, S.C.3    Warner, M.L.4    Henson, P.M.5
  • 70
    • 0032872280 scopus 로고    scopus 로고
    • Modulation of cell surface expression of liver carbohydrate receptors during in vivo induction of apoptosis with lead nitrate
    • M. Ruzittu, E. C. Carla, M. R. Montinari, G. Maietta and L. Dini, Modulation of cell surface expression of liver carbohydrate receptors during in vivo induction of apoptosis with lead nitrate, Cell Tissue Res. 298 (1999) 105-112.
    • (1999) Cell Tissue Res. , vol.298 , pp. 105-112
    • Ruzittu, M.1    Carla, E.C.2    Montinari, M.R.3    Maietta, G.4    Dini, L.5
  • 71
    • 0032473635 scopus 로고    scopus 로고
    • Apoptosis. Phagocytic docking without shocking
    • J. Savill, Apoptosis. Phagocytic docking without shocking, Nature 392 (1998) 442-443.
    • (1998) Nature , vol.392 , pp. 442-443
    • Savill, J.1
  • 73
    • 0032416392 scopus 로고    scopus 로고
    • Complement-dependent clearance of apoptotic cells by human macrophages
    • D. Mevorach, J. O. Mascarenhas, D. Gershov and K. B. Elkon, Complement-dependent clearance of apoptotic cells by human macrophages, J. Exp. Med. 188 (1998) 2313-2320.
    • (1998) J. Exp. Med. , vol.188 , pp. 2313-2320
    • Mevorach, D.1    Mascarenhas, J.O.2    Gershov, D.3    Elkon, K.B.4
  • 74
    • 0030666920 scopus 로고    scopus 로고
    • Immune clearance of phosphatidylserine-expressing cells by phagocytes. The role of β2-glycoprotein I in macrophage recognition
    • K. Balasubramanian, J. Chandra and A. J. Schroit, Immune clearance of phosphatidylserine-expressing cells by phagocytes. The role of β2-glycoprotein I in macrophage recognition, J. Biol. Chem. 272 (1997) 31113-31117.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31113-31117
    • Balasubramanian, K.1    Chandra, J.2    Schroit, A.J.3
  • 75
    • 0034641931 scopus 로고    scopus 로고
    • Corpse clearance defines the meaning of cell death
    • J. Savill and V. Fadok, Corpse clearance defines the meaning of cell death, Nature 407 (2000) 784-788.
    • (2000) Nature , vol.407 , pp. 784-788
    • Savill, J.1    Fadok, V.2
  • 76
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three acts
    • S. R. Datta, A. Brunet and M. E. Greenberg, Cellular survival: a play in three acts, Genes Dev. 13 (1999) 2905-2927.
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 77
    • 0032698075 scopus 로고    scopus 로고
    • Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms
    • A. Bonni, A. Brunet, A. E. West, S. R. Datta, M. A. Takasu and M. E. Greenberg, Cell survival promoted by the Ras-MAPK signaling pathway by transcription-dependent and -independent mechanisms, Science 286 (1999) 1358-1362.
    • (1999) Science , vol.286 , pp. 1358-1362
    • Bonni, A.1    Brunet, A.2    West, A.E.3    Datta, S.R.4    Takasu, M.A.5    Greenberg, M.E.6
  • 78
    • 0033198217 scopus 로고    scopus 로고
    • BAX translocation is a critical event in neuronal apoptosis: Regulation by neuroprotectants, BCL-2, and caspases
    • V. Putcha, M. Deshmukh and E. M. Johnson Jr., BAX translocation is a critical event in neuronal apoptosis: regulation by neuroprotectants, BCL-2, and caspases, J. Neurosci. 19 (1999) 7476-7485.
    • (1999) J. Neurosci. , vol.19 , pp. 7476-7485
    • Putcha, V.1    Deshmukh, M.2    Johnson E.M., Jr.3
  • 80
    • 0031982670 scopus 로고    scopus 로고
    • Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease
    • M. P. Mattson, Q. Guo, K. Furukawa and W. A. Pedersen, Presenilins, the endoplasmic reticulum, and neuronal apoptosis in Alzheimer's disease, J. Neurochem. 70 (1998) 1-14.
    • (1998) J. Neurochem. , vol.70 , pp. 1-14
    • Mattson, M.P.1    Guo, Q.2    Furukawa, K.3    Pedersen, W.A.4
  • 81
    • 0031047370 scopus 로고    scopus 로고
    • CD40 ligation counteracts Fas-induced apoptosis of human dendritic cells
    • P. Bjorck, J. Banchereau and L. Flores-Romo, CD40 ligation counteracts Fas-induced apoptosis of human dendritic cells, Int. Immunol. 9 (1997) 365-372.
    • (1997) Int. Immunol. , vol.9 , pp. 365-372
    • Bjorck, P.1    Banchereau, J.2    Flores-Romo, L.3
  • 82
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • J. M. Adams and S. Cory, The Bcl-2 protein family: arbiters of cell survival, Science 281 (1998) 1322-1326.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 83
    • 0032410818 scopus 로고    scopus 로고
    • The inhibitors of apoptosis (IAPs) and their emerging role in cancer
    • E. C. LaCasse, S. Baird, R. G. Korneluk and A. E. MacKenzie, The inhibitors of apoptosis (IAPs) and their emerging role in cancer, Oncogene 17 (1998) 3247-3259.
    • (1998) Oncogene , vol.17 , pp. 3247-3259
    • LaCasse, E.C.1    Baird, S.2    Korneluk, R.G.3    MacKenzie, A.E.4
  • 84
    • 0026703222 scopus 로고
    • Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity
    • M. Jaattela, D. Wissing, P. A. Bauer and G. C. Li, Major heat shock protein hsp70 protects tumor cells from tumor necrosis factor cytotoxicity, EMBO J. 11 (1992) 3507-3512.
    • (1992) EMBO J. , vol.11 , pp. 3507-3512
    • Jaattela, M.1    Wissing, D.2    Bauer, P.A.3    Li, G.C.4
  • 85
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • W. Nicholson, From bench to clinic with apoptosis-based therapeutic agents, Nature 407 (2000) 810-816.
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, W.1


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