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Volumn 33, Issue 8, 2008, Pages 352-355

Necrotic cell death and 'necrostatins': now we can control cellular explosion

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DEATH RECEPTOR; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INDOLE DERIVATIVE; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; NECROSTATIN DERIVATIVE; RECEPTOR INTERACTING PROTEIN 1 KINASE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR AP 1; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED DEATH DOMAIN PROTEIN; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 48149086045     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.05.007     Document Type: Short Survey
Times cited : (32)

References (25)
  • 1
    • 0032971161 scopus 로고    scopus 로고
    • Caspase-independent programmed cell death with necrotic morphology
    • Kitanaka C., and Kuchino Y. Caspase-independent programmed cell death with necrotic morphology. Cell Death Differ. 6 (1999) 508-515
    • (1999) Cell Death Differ. , vol.6 , pp. 508-515
    • Kitanaka, C.1    Kuchino, Y.2
  • 2
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • Schweichel J.U., and Merker H.J. The morphology of various types of cell death in prenatal tissues. Teratology 7 (1973) 253-266
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 3
    • 33749178260 scopus 로고    scopus 로고
    • Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response
    • Festjens N., et al. Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response. Biochim. Biophys. Acta 1757 (2006) 1371-1387
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1
  • 4
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • Golstein P., and Kroemer G. Cell death by necrosis: towards a molecular definition. Trends Biochem. Sci. 32 (2007) 37-43
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 5
    • 29944438881 scopus 로고    scopus 로고
    • Necrotic death as a cell fate
    • Zong W.X., and Thompson C.B. Necrotic death as a cell fate. Genes Dev. 20 (2006) 1-15
    • (2006) Genes Dev. , vol.20 , pp. 1-15
    • Zong, W.X.1    Thompson, C.B.2
  • 6
    • 0032494143 scopus 로고    scopus 로고
    • Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways
    • Vercammen D., et al. Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J. Exp. Med. 188 (1998) 919-930
    • (1998) J. Exp. Med. , vol.188 , pp. 919-930
    • Vercammen, D.1
  • 7
    • 33644840693 scopus 로고    scopus 로고
    • Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury
    • Degterev A., et al. Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury. Nat. Chem. Biol. 1 (2005) 112-119
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 112-119
    • Degterev, A.1
  • 8
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N., et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1 (2000) 489-495
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1
  • 9
    • 42249102086 scopus 로고    scopus 로고
    • Identification of RIP1 kinase as a specific cellular target of necrostatins
    • Degterev A., et al. Identification of RIP1 kinase as a specific cellular target of necrostatins. Nat. Chem. Biol. 4 (2008) 313-321
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 313-321
    • Degterev, A.1
  • 10
    • 36849056027 scopus 로고    scopus 로고
    • The cardioprotective effect of necrostatin requires the cyclophilin-D component of the mitochondrial permeability transition pore
    • Lim S.Y., et al. The cardioprotective effect of necrostatin requires the cyclophilin-D component of the mitochondrial permeability transition pore. Cardiovasc. Drugs Ther. 21 (2007) 467-469
    • (2007) Cardiovasc. Drugs Ther. , vol.21 , pp. 467-469
    • Lim, S.Y.1
  • 11
    • 34548564715 scopus 로고    scopus 로고
    • Necrostatin: a potentially novel cardioprotective agent?
    • Smith C.C., et al. Necrostatin: a potentially novel cardioprotective agent?. Cardiovasc. Drugs Ther. 21 (2007) 227-233
    • (2007) Cardiovasc. Drugs Ther. , vol.21 , pp. 227-233
    • Smith, C.C.1
  • 12
    • 14744299357 scopus 로고    scopus 로고
    • The RIP kinases: crucial integrators of cellular stress
    • Meylan E., and Tschopp J. The RIP kinases: crucial integrators of cellular stress. Trends Biochem. Sci. 30 (2005) 151-159
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 151-159
    • Meylan, E.1    Tschopp, J.2
  • 13
    • 0242663910 scopus 로고    scopus 로고
    • The death domain kinase RIP1 is essential for tumor necrosis factor α signaling to p38 mitogen-activated protein kinase
    • Lee T.H., et al. The death domain kinase RIP1 is essential for tumor necrosis factor α signaling to p38 mitogen-activated protein kinase. Mol. Cell. Biol. 23 (2003) 8377-8385
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8377-8385
    • Lee, T.H.1
  • 14
    • 0008206988 scopus 로고    scopus 로고
    • TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival
    • Lee S.Y., et al. TRAF2 is essential for JNK but not NF-κB activation and regulates lymphocyte proliferation and survival. Immunity 7 (1997) 703-713
    • (1997) Immunity , vol.7 , pp. 703-713
    • Lee, S.Y.1
  • 15
    • 0042090891 scopus 로고    scopus 로고
    • The role of the death-domain kinase RIP in tumour-necrosis-factor-induced activation of mitogen-activated protein kinases
    • Devin A., et al. The role of the death-domain kinase RIP in tumour-necrosis-factor-induced activation of mitogen-activated protein kinases. EMBO Rep. 4 (2003) 623-627
    • (2003) EMBO Rep. , vol.4 , pp. 623-627
    • Devin, A.1
  • 16
    • 4043136609 scopus 로고    scopus 로고
    • The kinase activity of Rip1 is not required for tumor necrosis factor-α-induced IκB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2
    • Lee T.H., et al. The kinase activity of Rip1 is not required for tumor necrosis factor-α-induced IκB kinase or p38 MAP kinase activation or for the ubiquitination of Rip1 by Traf2. J. Biol. Chem. 279 (2004) 33185-33191
    • (2004) J. Biol. Chem. , vol.279 , pp. 33185-33191
    • Lee, T.H.1
  • 17
    • 33847051539 scopus 로고    scopus 로고
    • RIP1, a kinase on the crossroads of a cell's decision to live or die
    • Festjens N., et al. RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ. 14 (2007) 400-410
    • (2007) Cell Death Differ. , vol.14 , pp. 400-410
    • Festjens, N.1
  • 18
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-κB signal
    • Kelliher M.A., et al. The death domain kinase RIP mediates the TNF-induced NF-κB signal. Immunity 8 (1998) 297-303
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.A.1
  • 19
    • 0033214236 scopus 로고    scopus 로고
    • Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis
    • Lin Y., et al. Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. Genes Dev. 13 (1999) 2514-2526
    • (1999) Genes Dev. , vol.13 , pp. 2514-2526
    • Lin, Y.1
  • 20
    • 34249820757 scopus 로고    scopus 로고
    • TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death
    • Kim Y.S., et al. TNF-induced activation of the Nox1 NADPH oxidase and its role in the induction of necrotic cell death. Mol. Cell 26 (2007) 675-687
    • (2007) Mol. Cell , vol.26 , pp. 675-687
    • Kim, Y.S.1
  • 21
    • 34247264421 scopus 로고    scopus 로고
    • Structure-activity relationship study of tricyclic necroptosis inhibitors
    • Jagtap P.G., et al. Structure-activity relationship study of tricyclic necroptosis inhibitors. J. Med. Chem. 50 (2007) 1886-1895
    • (2007) J. Med. Chem. , vol.50 , pp. 1886-1895
    • Jagtap, P.G.1
  • 22
    • 33846913723 scopus 로고    scopus 로고
    • Structure-activity relationship analysis of a novel necroptosis inhibitor, Necrostatin-5
    • Wang K., et al. Structure-activity relationship analysis of a novel necroptosis inhibitor, Necrostatin-5. Bioorg. Med. Chem. Lett. 17 (2007) 1455-1465
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 1455-1465
    • Wang, K.1
  • 23
    • 34547154729 scopus 로고    scopus 로고
    • Activation segment exchange: a common mechanism of kinase autophosphorylation?
    • Oliver A.W., et al. Activation segment exchange: a common mechanism of kinase autophosphorylation?. Trends Biochem. Sci. 32 (2007) 351-356
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 351-356
    • Oliver, A.W.1
  • 24
    • 0034675919 scopus 로고    scopus 로고
    • Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601
    • Zhang B.H., and Guan K.L. Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601. EMBO J. 19 (2000) 5429-5439
    • (2000) EMBO J. , vol.19 , pp. 5429-5439
    • Zhang, B.H.1    Guan, K.L.2
  • 25
    • 4444341939 scopus 로고    scopus 로고
    • Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles
    • Schneider-Brachert W., et al. Compartmentalization of TNF receptor 1 signaling: internalized TNF receptosomes as death signaling vesicles. Immunity 21 (2004) 415-428
    • (2004) Immunity , vol.21 , pp. 415-428
    • Schneider-Brachert, W.1


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