메뉴 건너뛰기




Volumn 44, Issue 3, 2012, Pages 489-495

X-linked Inhibitor of Apoptosis Protein promotes the degradation of its antagonist, the pro-apoptotic ARTS protein

Author keywords

Apoptosis; ARTS; Mitochondria; Ubiquitination; XIAP

Indexed keywords

PROTEASOME; PROTEIN; PROTEIN ARTS; UNCLASSIFIED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 84857211665     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2011.12.005     Document Type: Article
Times cited : (15)

References (69)
  • 1
    • 0035803568 scopus 로고    scopus 로고
    • Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2
    • C. Adrain, E.M. Creagh, and S.J. Martin Apoptosis-associated release of Smac/DIABLO from mitochondria requires active caspases and is blocked by Bcl-2 EMBO J 20 2001 6627 6636
    • (2001) EMBO J , vol.20 , pp. 6627-6636
    • Adrain, C.1    Creagh, E.M.2    Martin, S.J.3
  • 3
    • 0032440288 scopus 로고    scopus 로고
    • Mechanisms and control of programmed cell death in invertebrates
    • A. Bergmann, J. Agapite, and H. Steller Mechanisms and control of programmed cell death in invertebrates Oncogene 17 1998 3215 3223
    • (1998) Oncogene , vol.17 , pp. 3215-3223
    • Bergmann, A.1    Agapite, J.2    Steller, H.3
  • 4
    • 80052437295 scopus 로고    scopus 로고
    • ARTS binds to a distinct domain in XIAP-BIR3 and promotes apoptosis by a mechanism that is different from other IAP-antagonists
    • B. Bornstein, Y. Gottfried, N. Edison, A. Shekhtman, T. Lev, and F. Glaser ARTS binds to a distinct domain in XIAP-BIR3 and promotes apoptosis by a mechanism that is different from other IAP-antagonists Apoptosis 2011
    • (2011) Apoptosis
    • Bornstein, B.1    Gottfried, Y.2    Edison, N.3    Shekhtman, A.4    Lev, T.5    Glaser, F.6
  • 5
    • 1642474148 scopus 로고    scopus 로고
    • Caspases: An ancient cellular sword of Damocles
    • M. Boyce, A. Degterev, and J. Yuan Caspases: an ancient cellular sword of Damocles Cell Death Differ 11 2004 29 37
    • (2004) Cell Death Differ , vol.11 , pp. 29-37
    • Boyce, M.1    Degterev, A.2    Yuan, J.3
  • 6
    • 19644372162 scopus 로고    scopus 로고
    • Mature DIABLO/Smac is produced by the IMP protease complex on the mitochondrial inner membrane
    • L. Burri, Y. Strahm, C.J. Hawkins, I.E. Gentle, M.A. Puryer, and A. Verhagen Mature DIABLO/Smac is produced by the IMP protease complex on the mitochondrial inner membrane Mol Biol Cell 16 2005 2926 2933
    • (2005) Mol Biol Cell , vol.16 , pp. 2926-2933
    • Burri, L.1    Strahm, Y.2    Hawkins, C.J.3    Gentle, I.E.4    Puryer, M.A.5    Verhagen, A.6
  • 8
    • 0037184954 scopus 로고    scopus 로고
    • Early mitochondrial activation and cytochrome C up-regulation during apoptosis
    • D. Chandra, J.W. Liu, and D.G. Tang Early mitochondrial activation and cytochrome C up-regulation during apoptosis J Biol Chem 277 2002 50842 50854
    • (2002) J Biol Chem , vol.277 , pp. 50842-50854
    • Chandra, D.1    Liu, J.W.2    Tang, D.G.3
  • 9
    • 0018992813 scopus 로고
    • ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • A. Ciechanover, H. Heller, S. Elias, A.L. Haas, and A. Hershko ATP-dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation Proc Natl Acad Sci USA 77 1980 1365 1368
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 10
    • 0033643742 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mode of action and clinical implications
    • A. Ciechanover, A. Orian, and A.L. Schwartz The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications J Cell Biochem Suppl 34 2000 40 51
    • (2000) J Cell Biochem Suppl , vol.34 , pp. 40-51
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 11
    • 0032539909 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death
    • A. Ciechanover, and A.L. Schwartz The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death Proc Natl Acad Sci USA 95 1998 2727 2730
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2727-2730
    • Ciechanover, A.1    Schwartz, A.L.2
  • 12
    • 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
  • 13
    • 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
  • 14
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Q.L. Deveraux, R. Takahashi, G.S. Salvesen, and J.C. Reed X-linked IAP is a direct inhibitor of cell-death proteases Nature 388 1997 300 304
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 15
    • 0037936841 scopus 로고    scopus 로고
    • Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis
    • M. Ditzel, R. Wilson, T. Tenev, A. Zachariou, A. Paul, and E. Deas Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis Nat Cell Biol 5 2003 467 473
    • (2003) Nat Cell Biol , vol.5 , pp. 467-473
    • Ditzel, M.1    Wilson, R.2    Tenev, T.3    Zachariou, A.4    Paul, A.5    Deas, E.6
  • 16
    • 57049153979 scopus 로고    scopus 로고
    • X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility
    • T. Dogan, G.S. Harms, M. Hekman, C. Karreman, T.K. Oberoi, and E.S. Alnemri X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility Nat Cell Biol 10 2008 1447 1455
    • (2008) Nat Cell Biol , vol.10 , pp. 1447-1455
    • Dogan, T.1    Harms, G.S.2    Hekman, M.3    Karreman, C.4    Oberoi, T.K.5    Alnemri, E.S.6
  • 17
    • 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
  • 19
    • 3843059163 scopus 로고    scopus 로고
    • Mitochondrial pro-apoptotic ARTS protein is lost in the majority of acute lymphoblastic leukemia patients
    • R. Elhasid, D. Sahar, A. Merling, Y. Zivony, A. Rotem, and M. Ben-Arush Mitochondrial pro-apoptotic ARTS protein is lost in the majority of acute lymphoblastic leukemia patients Oncogene 23 2004 5468 5475
    • (2004) Oncogene , vol.23 , pp. 5468-5475
    • Elhasid, R.1    Sahar, D.2    Merling, A.3    Zivony, Y.4    Rotem, A.5    Ben-Arush, M.6
  • 21
    • 77449136104 scopus 로고    scopus 로고
    • XIAP as a ubiquitin ligase in cellular signaling
    • S. Galban, and C.S. Duckett XIAP as a ubiquitin ligase in cellular signaling Cell Death Differ 17 2010 54 60
    • (2010) Cell Death Differ , vol.17 , pp. 54-60
    • Galban, S.1    Duckett, C.S.2
  • 24
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol Rev 82 2002 373 428
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 25
    • 2342561882 scopus 로고    scopus 로고
    • The mitochondrial ARTS protein promotes apoptosis through targeting XIAP
    • Y. Gottfried, A. Rotem, R. Lotan, H. Steller, and S. Larisch The mitochondrial ARTS protein promotes apoptosis through targeting XIAP EMBO J 23 2004 1627 1635
    • (2004) EMBO J , vol.23 , pp. 1627-1635
    • Gottfried, Y.1    Rotem, A.2    Lotan, R.3    Steller, H.4    Larisch, S.5
  • 26
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • D.R. Green, and G. Kroemer The pathophysiology of mitochondrial cell death Science 305 2004 626 629
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 27
    • 55549140475 scopus 로고    scopus 로고
    • IAPs contain an evolutionarily conserved ubiquitin-binding domain that regulates NF-kappaB as well as cell survival and oncogenesis
    • M. Gyrd-Hansen, M. Darding, M. Miasari, M.M. Santoro, L. Zender, and W. Xue IAPs contain an evolutionarily conserved ubiquitin-binding domain that regulates NF-kappaB as well as cell survival and oncogenesis Nat Cell Biol 10 2008 1309 1317
    • (2008) Nat Cell Biol , vol.10 , pp. 1309-1317
    • Gyrd-Hansen, M.1    Darding, M.2    Miasari, M.3    Santoro, M.M.4    Zender, L.5    Xue, W.6
  • 28
    • 4444329609 scopus 로고    scopus 로고
    • Apollon ubiquitinates SMAC and caspase-9, and has an essential cytoprotection function
    • Y. Hao, K. Sekine, A. Kawabata, H. Nakamura, T. Ishioka, and H. Ohata Apollon ubiquitinates SMAC and caspase-9, and has an essential cytoprotection function Nat Cell Biol 6 2004 849 860
    • (2004) Nat Cell Biol , vol.6 , pp. 849-860
    • Hao, Y.1    Sekine, K.2    Kawabata, A.3    Nakamura, H.4    Ishioka, T.5    Ohata, H.6
  • 29
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • R. Hegde, S.M. Srinivasula, Z. Zhang, R. Wassell, R. Mukattash, and L. Cilenti Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction J Biol Chem 277 2002 432 438
    • (2002) J Biol Chem , vol.277 , pp. 432-438
    • Hegde, R.1    Srinivasula, S.M.2    Zhang, Z.3    Wassell, R.4    Mukattash, R.5    Cilenti, L.6
  • 30
    • 0018772190 scopus 로고
    • Resolution of the ATP-dependent proteolytic system from reticulocytes: A component that interacts with ATP
    • A. Hershko, A. Ciechanover, and I.A. Rose Resolution of the ATP-dependent proteolytic system from reticulocytes: a component that interacts with ATP Proc Natl Acad Sci USA 76 1979 3107 3110
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 3107-3110
    • Hershko, A.1    Ciechanover, A.2    Rose, I.A.3
  • 31
    • 0036303143 scopus 로고    scopus 로고
    • Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition
    • C.L. Holley, M.R. Olson, D.A. Colon-Ramos, and S. Kornbluth Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition Nat Cell Biol 4 2002 439 444
    • (2002) Nat Cell Biol , vol.4 , pp. 439-444
    • Holley, C.L.1    Olson, M.R.2    Colon-Ramos, D.A.3    Kornbluth, S.4
  • 32
    • 0037855783 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO
    • S. Hu, and X. Yang Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO J Biol Chem 278 2003 10055 10060
    • (2003) J Biol Chem , vol.278 , pp. 10055-10060
    • Hu, S.1    Yang, X.2
  • 33
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Y. Huang, Y.C. Park, R.L. Rich, D. Segal, D.G. Myszka, and H. Wu Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain Cell 104 2001 781 790
    • (2001) Cell , vol.104 , pp. 781-790
    • Huang, Y.1    Park, Y.C.2    Rich, R.L.3    Segal, D.4    Myszka, D.G.5    Wu, H.6
  • 34
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series
    • F. Ikeda, and I. Dikic Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' review series EMBO Rep 9 2008 536 542
    • (2008) EMBO Rep , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 36
    • 0033974321 scopus 로고    scopus 로고
    • Selective loss of the transforming growth factor-beta apoptotic signaling pathway in mutant NRP-154 rat prostatic epithelial cells
    • S. Larisch-Bloch, D. Danielpour, N.S. Roche, R. Lotan, A.Y. Hsing, and H. Kerner Selective loss of the transforming growth factor-beta apoptotic signaling pathway in mutant NRP-154 rat prostatic epithelial cells Cell Growth Differ 11 2000 1 10
    • (2000) Cell Growth Differ , vol.11 , pp. 1-10
    • Larisch-Bloch, S.1    Danielpour, D.2    Roche, N.S.3    Lotan, R.4    Hsing, A.Y.5    Kerner, H.6
  • 37
    • 13944265973 scopus 로고    scopus 로고
    • The ARTS connection: Role of ARTS in apoptosis and cancer
    • S. Larisch The ARTS connection: role of ARTS in apoptosis and cancer Cell Cycle 3 2004 1021 1023
    • (2004) Cell Cycle , vol.3 , pp. 1021-1023
    • Larisch, S.1
  • 38
    • 0033671655 scopus 로고    scopus 로고
    • A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif
    • S. Larisch, Y. Yi, R. Lotan, H. Kerner, S. Eimerl, and W. Tony Parks A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif Nat Cell Biol 2 2000 915 921
    • (2000) Nat Cell Biol , vol.2 , pp. 915-921
    • Larisch, S.1    Yi, Y.2    Lotan, R.3    Kerner, H.4    Eimerl, S.5    Tony Parks, W.6
  • 39
    • 0346880501 scopus 로고    scopus 로고
    • The inhibitors of apoptosis: There is more to life than Bcl2
    • P. Liston, W.G. Fong, and R.G. Korneluk The inhibitors of apoptosis: there is more to life than Bcl2 Oncogene 22 2003 8568 8580
    • (2003) Oncogene , vol.22 , pp. 8568-8580
    • Liston, P.1    Fong, W.G.2    Korneluk, R.G.3
  • 40
    • 21844444804 scopus 로고    scopus 로고
    • Regulation of the proapoptotic ARTS protein by ubiquitin-mediated degradation
    • R. Lotan, A. Rotem, H. Gonen, J.P. Finberg, S. Kemeny, and H. Steller Regulation of the proapoptotic ARTS protein by ubiquitin-mediated degradation J Biol Chem 280 2005 25802 25810
    • (2005) J Biol Chem , vol.280 , pp. 25802-25810
    • Lotan, R.1    Rotem, A.2    Gonen, H.3    Finberg, J.P.4    Kemeny, S.5    Steller, H.6
  • 41
    • 33750982397 scopus 로고    scopus 로고
    • Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway
    • L. Ma, Y. Huang, Z. Song, S. Feng, X. Tian, and W. Du Livin promotes Smac/DIABLO degradation by ubiquitin-proteasome pathway Cell Death Differ 13 2006 2079 2088
    • (2006) Cell Death Differ , vol.13 , pp. 2079-2088
    • Ma, L.1    Huang, Y.2    Song, Z.3    Feng, S.4    Tian, X.5    Du, W.6
  • 42
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • M. MacFarlane, W. Merrison, S.B. Bratton, and G.M. Cohen Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro J Biol Chem 277 2002 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
  • 43
    • 0037016707 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif
    • L.M. Martins, I. Iaccarino, T. Tenev, S. Gschmeissner, N.F. Totty, and N.R. Lemoine The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif J Biol Chem 277 2002 439 444
    • (2002) J Biol Chem , vol.277 , pp. 439-444
    • Martins, L.M.1    Iaccarino, I.2    Tenev, T.3    Gschmeissner, S.4    Totty, N.F.5    Lemoine, N.R.6
  • 44
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • P. Meier, A. Finch, and G. Evan Apoptosis in development Nature 407 2000 796 801
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 45
    • 17044368875 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO
    • Y. Morizane, R. Honda, K. Fukami, and H. Yasuda X-linked inhibitor of apoptosis functions as ubiquitin ligase toward mature caspase-9 and cytosolic Smac/DIABLO J Biochem 137 2005 125 132
    • (2005) J Biochem , vol.137 , pp. 125-132
    • Morizane, Y.1    Honda, R.2    Fukami, K.3    Yasuda, H.4
  • 46
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • D.W. Nicholson Caspase structure, proteolytic substrates, and function during apoptotic cell death Cell Death Differ 6 1999 1028 1042
    • (1999) Cell Death Differ , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 47
    • 0035295778 scopus 로고    scopus 로고
    • Mitochondria in apoptosis and human disease
    • M. Olson, and S. Kornbluth Mitochondria in apoptosis and human disease Curr Mol Med 1 2001 91 122
    • (2001) Curr Mol Med , vol.1 , pp. 91-122
    • Olson, M.1    Kornbluth, S.2
  • 49
    • 74049154785 scopus 로고    scopus 로고
    • Role for X-linked Inhibitor of apoptosis protein upstream of mitochondrial permeabilization
    • T.W. Owens, F.M. Foster, A. Valentijn, A.P. Gilmore, and C.H. Streuli Role for X-linked Inhibitor of apoptosis protein upstream of mitochondrial permeabilization J Biol Chem 285 2010 1081 1088
    • (2010) J Biol Chem , vol.285 , pp. 1081-1088
    • Owens, T.W.1    Foster, F.M.2    Valentijn, A.3    Gilmore, A.P.4    Streuli, C.H.5
  • 50
    • 58249091522 scopus 로고    scopus 로고
    • Inhibitors of apoptosis catch ubiquitin
    • K. Rajalingam, and I. Dikic Inhibitors of apoptosis catch ubiquitin Biochem J 417 2009 e1 e3
    • (2009) Biochem J , vol.417
    • Rajalingam, K.1    Dikic, I.2
  • 51
    • 80052944668 scopus 로고    scopus 로고
    • Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP
    • T.H. Reingewertz, D.E. Shalev, S. Sukenik, O. Blatt, S. Rotem-Bamberger, and M. Lebendiker Mechanism of the interaction between the intrinsically disordered C-terminus of the pro-apoptotic ARTS protein and the Bir3 domain of XIAP PLoS One 6 2011 e24655
    • (2011) PLoS One , vol.6 , pp. 24655
    • Reingewertz, T.H.1    Shalev, D.E.2    Sukenik, S.3    Blatt, O.4    Rotem-Bamberger, S.5    Lebendiker, M.6
  • 52
    • 0036300083 scopus 로고    scopus 로고
    • Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1
    • H.D. Ryoo, A. Bergmann, H. Gonen, A. Ciechanover, and H. Steller Regulation of Drosophila IAP1 degradation and apoptosis by reaper and ubcD1 Nat Cell Biol 4 2002 432 438
    • (2002) Nat Cell Biol , vol.4 , pp. 432-438
    • Ryoo, H.D.1    Bergmann, A.2    Gonen, H.3    Ciechanover, A.4    Steller, H.5
  • 53
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: Blocking the road to death's door
    • G.S. Salvesen, and C.S. Duckett IAP proteins: blocking the road to death's door Nat Rev Mol Cell Biol 3 2002 401 410
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 54
    • 77957195300 scopus 로고    scopus 로고
    • Drosophila IAP antagonists form multimeric complexes to promote cell death
    • C. Sandu, H.D. Ryoo, and H. Steller Drosophila IAP antagonists form multimeric complexes to promote cell death J Cell Biol 190 2010 1039 1052
    • (2010) J Cell Biol , vol.190 , pp. 1039-1052
    • Sandu, C.1    Ryoo, H.D.2    Steller, H.3
  • 55
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • A.J. Schile, M. Garcia-Fernandez, and H. Steller Regulation of apoptosis by XIAP ubiquitin-ligase activity Genes Dev 22 2008 2256 2266
    • (2008) Genes Dev , vol.22 , pp. 2256-2266
    • Schile, A.J.1    Garcia-Fernandez, M.2    Steller, H.3
  • 56
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • Y. Shi Mechanisms of caspase activation and inhibition during apoptosis Mol Cell 9 2002 459 470
    • (2002) Mol Cell , vol.9 , pp. 459-470
    • Shi, Y.1
  • 58
    • 45449093594 scopus 로고    scopus 로고
    • Regulation of apoptosis in Drosophila
    • H. Steller Regulation of apoptosis in Drosophila Cell Death Differ 15 2008 1132 1138
    • (2008) Cell Death Differ , vol.15 , pp. 1132-1138
    • Steller, H.1
  • 59
    • 0034721940 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP
    • C. Sun, M. Cai, R.P. Meadows, N. Xu, A.H. Gunasekera, and J. Herrmann NMR structure and mutagenesis of the third Bir domain of the inhibitor of apoptosis protein XIAP J Biol Chem 275 2000 33777 33781
    • (2000) J Biol Chem , vol.275 , pp. 33777-33781
    • Sun, C.1    Cai, M.2    Meadows, R.P.3    Xu, N.4    Gunasekera, A.H.5    Herrmann, J.6
  • 60
    • 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
  • 61
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • C.B. Thompson Apoptosis in the pathogenesis and treatment of disease Science 267 1995 1456 1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 62
    • 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
  • 63
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • A.M. Verhagen, P.G. Ekert, M. Pakusch, J. Silke, L.M. Connolly, and G.E. Reid Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins Cell 102 2000 43 53
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3    Silke, J.4    Connolly, L.M.5    Reid, G.E.6
  • 64
    • 33846251849 scopus 로고    scopus 로고
    • Identification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs
    • A.M. Verhagen, T.K. Kratina, C.J. Hawkins, J. Silke, P.G. Ekert, and D.L. Vaux Identification of mammalian mitochondrial proteins that interact with IAPs via N-terminal IAP binding motifs Cell Death Differ 14 2007 348 357
    • (2007) Cell Death Differ , vol.14 , pp. 348-357
    • Verhagen, A.M.1    Kratina, T.K.2    Hawkins, C.J.3    Silke, J.4    Ekert, P.G.5    Vaux, D.L.6
  • 65
    • 10944247878 scopus 로고    scopus 로고
    • Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs) A caspase-independent mechanism for apoptotic inhibition
    • J.C. Wilkinson, A.S. Wilkinson, F.L. Scott, R.A. Csomos, G.S. Salvesen, and C.S. Duckett Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs) A caspase-independent mechanism for apoptotic inhibition J Biol Chem 279 2004 51082 51090
    • (2004) J Biol Chem , vol.279 , pp. 51082-51090
    • Wilkinson, J.C.1    Wilkinson, A.S.2    Scott, F.L.3    Csomos, R.A.4    Salvesen, G.S.5    Duckett, C.S.6
  • 66
    • 0036300214 scopus 로고    scopus 로고
    • The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis
    • R. Wilson, L. Goyal, M. Ditzel, A. Zachariou, D.A. Baker, and J. Agapite The DIAP1 RING finger mediates ubiquitination of Dronc and is indispensable for regulating apoptosis Nat Cell Biol 4 2002 445 450
    • (2002) Nat Cell Biol , vol.4 , pp. 445-450
    • Wilson, R.1    Goyal, L.2    Ditzel, M.3    Zachariou, A.4    Baker, D.A.5    Agapite, J.6
  • 67
    • 0029880987 scopus 로고    scopus 로고
    • The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease
    • D. Xue, S. Shaham, and H.R. Horvitz The Caenorhabditis elegans cell-death protein CED-3 is a cysteine protease with substrate specificities similar to those of the human CPP32 protease Genes Dev 10 1996 1073 1083
    • (1996) Genes Dev , vol.10 , pp. 1073-1083
    • Xue, D.1    Shaham, S.2    Horvitz, H.R.3
  • 68
    • 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
  • 69
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme
    • J. Yuan, S. Shaham, S. Ledoux, H.M. Ellis, and H.R. Horvitz The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme Cell 75 1993 641 652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.