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Volumn 6, Issue 5, 2000, Pages 564-567

Apoptosis induced in normal human hepatocytes by tumor necrosis factor- related apoptosis-inducing ligand

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DNA FRAGMENT; LIGAND; TUMOR NECROSIS FACTOR;

EID: 0034022160     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/75045     Document Type: Article
Times cited : (775)

References (24)
  • 1
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti, R.M. et al. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J. Biol. Chem. 271, 12687-12690 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 12687-12690
    • Pitti, R.M.1
  • 2
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley, S.R. et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 3, 673-682 (1995).
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1
  • 3
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak, H. et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nature Med. 5, 157-163 (1999).
    • (1999) Nature Med. , vol.5 , pp. 157-163
    • Walczak, H.1
  • 4
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activity of recombinant soluble Apo2 ligand
    • Ashkenazi, A. et al. Safety and antitumor activity of recombinant soluble Apo2 ligand. J. Clin. Invest. 104, 155-162 (1999).
    • (1999) J. Clin. Invest. , vol.104 , pp. 155-162
    • Ashkenazi, A.1
  • 5
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li, P. et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91, 479-489 (1997).
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1
  • 6
    • 0033214624 scopus 로고    scopus 로고
    • Cleavage of automodified Poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7
    • Germain, M. et al. Cleavage of automodified Poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. J. Biol. Chem. 274, 28379-28384 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28379-28384
    • Germain, M.1
  • 7
    • 0031832488 scopus 로고    scopus 로고
    • Proteolysis of poly(ADP-ribose) polymerase by caspase 3: Kinetics of cleavage of mono(ADP-ribosyl)ated and DNA-bound substrates
    • D'Amours, D., Germain, M., Orth, K., Dixit, V.M. & Poirier, G.G. Proteolysis of poly(ADP-ribose) polymerase by caspase 3: kinetics of cleavage of mono(ADP-ribosyl)ated and DNA-bound substrates. Radiat. Res. 150, 3-10 (1998).
    • (1998) Radiat. Res. , vol.150 , pp. 3-10
    • D'Amours, D.1    Germain, M.2    Orth, K.3    Dixit, V.M.4    Poirier, G.G.5
  • 8
    • 0032582539 scopus 로고    scopus 로고
    • Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis
    • Tang, D. & Kidd, V.J. Cleavage of DFF-45/ICAD by multiple caspases is essential for its function during apoptosis. J. Biol. Chem. 273, 28549-28552 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 28549-28552
    • Tang, D.1    Kidd, V.J.2
  • 9
    • 0030996297 scopus 로고    scopus 로고
    • The receptor for the cytotoxic ligand TRAIL
    • Pan, G. et al. The receptor for the cytotoxic ligand TRAIL. Science 276, 111-3 (1997).
    • (1997) Science , vol.276 , pp. 111-113
    • Pan, G.1
  • 10
    • 0030880548 scopus 로고    scopus 로고
    • TRAIL-R2: A novel apoptosis-mediating receptor for TRAIL
    • Walczak, H. et al. TRAIL-R2: a novel apoptosis-mediating receptor for TRAIL. Embo. J. 16, 5386-5397 (1997).
    • (1997) Embo. J. , vol.16 , pp. 5386-5397
    • Walczak, H.1
  • 11
    • 0030762815 scopus 로고    scopus 로고
    • An antagonist decoy receptor and a death domain-containing receptor for TRAIL
    • Pan, G. et al. An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 277, 815-818 (1997).
    • (1997) Science , vol.277 , pp. 815-818
    • Pan, G.1
  • 12
    • 0030792712 scopus 로고    scopus 로고
    • Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors
    • Sheridan, J.P. et al. Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science 277, 818-821 (1997).
    • (1997) Science , vol.277 , pp. 818-821
    • Sheridan, J.P.1
  • 13
    • 0030869432 scopus 로고    scopus 로고
    • Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family
    • Degli-Esposti, M.A. et al. Cloning and characterization of TRAIL-R3, a novel member of the emerging TRAIL receptor family. J. Exp. Med. 186, 1165-1170 (1997).
    • (1997) J. Exp. Med. , vol.186 , pp. 1165-1170
    • Degli-Esposti, M.A.1
  • 14
    • 0032489353 scopus 로고    scopus 로고
    • TRUNDD, a new member of the TRAIl receptor family that antagonizes TRAIL signalling
    • Pan, G., Ni, J., Yu, G., Wei, Y.F. & Dixit, V.M. TRUNDD, a new member of the TRAIL receptor family that antagonizes TRAIL signalling. FEBS Lett. 424, 41-55 (1998).
    • (1998) Febs Lett. , vol.424 , pp. 41-55
    • Pan, G.1    Ni, J.2    Yu, G.3    Wei, Y.F.4    Dixit, V.M.5
  • 15
    • 0025884625 scopus 로고
    • Tumor necrosis factor. Characterization at the molecular, cellular and in vivo level
    • Fiers, W. Tumor necrosis factor. Characterization at the molecular, cellular and in vivo level. FEBS Lett. 285, 199-212 (1991).
    • (1991) FEBS Lett. , vol.285 , pp. 199-212
    • Fiers, W.1
  • 16
    • 0023940875 scopus 로고
    • The antitumor function of tumor necrosis factor (TNF), I. Therapeutic action of TNF against an established murine sarcoma is indirect, immunologically dependent, and limited by severe toxicity
    • Havell, E.A., Fiers, W. & North, R.J. The antitumor function of tumor necrosis factor (TNF), I. Therapeutic action of TNF against an established murine sarcoma is indirect, immunologically dependent, and limited by severe toxicity. J. Exp. Med. 167, 1067-1085 (1988).
    • (1988) J. Exp. Med. , vol.167 , pp. 1067-1085
    • Havell, E.A.1    Fiers, W.2    North, R.J.3
  • 17
    • 0031092634 scopus 로고    scopus 로고
    • Lethal effect of recombinant human fas ligand in mice pretreated with propionibacterium acnes
    • Tanaka, M., Suda, T., Yatomi, T., Nakamura, N. & Nagata, S. Lethal effect of recombinant human Fas ligand in mice pretreated with Propionibacterium acnes. J. Immunol. 158, 2303-2309 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 2303-2309
    • Tanaka, M.1    Suda, T.2    Yatomi, T.3    Nakamura, N.4    Nagata, S.5
  • 18
    • 0027291205 scopus 로고
    • Lethal effect of the anti-Fas antibody in mice
    • erratum 365(6446):568 (1993)
    • Ogasawara, J. et al. Lethal effect of the anti-Fas antibody in mice. Nature 364, 806-809 (1993); erratum 365(6446):568 (1993).
    • (1993) Nature , vol.364 , pp. 806-809
    • Ogasawara, J.1
  • 19
    • 0029737488 scopus 로고    scopus 로고
    • Use of human hepatocytes to study P450 gene induction
    • Strom, S.C. et al. Use of human hepatocytes to study P450 gene induction. Meth. Enzymol. 272, 388-401 (1996).
    • (1996) Meth. Enzymol. , vol.272 , pp. 388-401
    • Strom, S.C.1
  • 21
    • 0032958953 scopus 로고    scopus 로고
    • Isolation and characterization of a human hepatic epithelial-like cell line (AKN-1) from a normal liver
    • Nussler, A.K. et al. Isolation and characterization of a human hepatic epithelial-like cell line (AKN-1) from a normal liver. In Vitro Cell Dev. Biol. Anim. 35, 190-197 (1999).
    • (1999) Vitro Cell Dev. Biol. Anim. , vol.35 , pp. 190-197
    • Nussler, A.K.1
  • 22
    • 0033593201 scopus 로고    scopus 로고
    • A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis
    • Seol, D.W. & Billiar, T.R. A caspase-9 variant missing the catalytic site is an endogenous inhibitor of apoptosis. J. Biol. Chem. 274, 2072-2076 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2072-2076
    • Seol, D.W.1    Billiar, T.R.2
  • 23
    • 0029822925 scopus 로고    scopus 로고
    • DNA fragmentation in mouse organs during endotoxic shock
    • Bohlinger, I. et al. DNA fragmentation in mouse organs during endotoxic shock. Am. J. Pathol. 149, 1381-1393 (1996).
    • (1996) Am. J. Pathol. , vol.149 , pp. 1381-1393
    • Bohlinger, I.1
  • 24
    • 0032582673 scopus 로고    scopus 로고
    • Interleukin-1 protects transformed keratinocytes from tumor necrosis factor-related apoptosis-inducing ligand
    • Kothny-Wilkes, G. et al. Interleukin-1 protects transformed keratinocytes from tumor necrosis factor-related apoptosis-inducing ligand. J. Biol. Chem. 273, 29247-53 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 29247-29253
    • Kothny-Wilkes, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.