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Volumn 2, Issue , 2009, Pages 1297-1302

Caspases: Cell Signaling by Proteolysis

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EID: 84862870531     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374145-5.00162-5     Document Type: Chapter
Times cited : (3)

References (53)
  • 1
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1-beta converting enzyme
    • K Kuida, JA Lippke, G Ku, MW Harding, DJ Livingston, MSS Su and RA Flavell (1995) Altered cytokine export and apoptosis in mice deficient in interleukin-1-beta converting enzyme. Science 267 2000-2003.
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.S.6    Flavell, R.A.7
  • 2
    • 0032548919 scopus 로고    scopus 로고
    • Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE
    • S Wang, M Miura, Y-K Jung, H Zhu and J Yuan (1998) Murine caspase-11, an ICE-interacting protease, is essential for the activation of ICE. Cell 92 501-509.
    • (1998) Cell , vol.92 , pp. 501-509
    • Wang, S.1    Miura, M.2    Jung, Y.-K.3    Zhu, H.4    Yuan, J.5
  • 7
    • 0030702084 scopus 로고    scopus 로고
    • Caspases: Intracellular signaling by proteolysis
    • GS Salvesen and VM Dixit (1997) Caspases: intracellular signaling by proteolysis. Cell 91 443-446.
    • (1997) Cell , vol.91 , pp. 443-446
    • Salvesen, G.S.1    Dixit, V.M.2
  • 8
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • GM Cohen (1997) Caspases: the executioners of apoptosis. Biochem J 326 1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 9
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • NA Thornberry and Y Lazebnik (1998) Caspases: enemies within. Science 281 1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 11
    • 0025971396 scopus 로고
    • Human and murine cytotoxic T lymphocyte serine proteases: Subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins
    • S Odake, CM Kam, L Narasimhan, M Poe, JT Blake, O Krahenbuhl, J Tschopp and JC Powers (1991) Human and murine cytotoxic T lymphocyte serine proteases: subsite mapping with peptide thioester substrates and inhibition of enzyme activity and cytolysis by isocoumarins. Biochem USA 30 2217-2227.
    • (1991) Biochem USA , vol.30 , pp. 2217-2227
    • Odake, S.1    Kam, C.M.2    Narasimhan, L.3    Poe, M.4    Blake, J.T.5    Krahenbuhl, O.6    Tschopp, J.7    Powers, J.C.8
  • 12
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • JL Harris, BJ Backes, F Leonetti, S Mahrus, JA Ellman and CS Craik (2000) Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci USA 97 7754-7759.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3    Mahrus, S.4    Ellman, J.A.5    Craik, C.S.6
  • 13
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • DW Nicholson (1999) Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ 6 1028-1042.
    • (1999) Cell Death Differ , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 15
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • J Yuan, S Shaham, S Ledoux, HM Ellis and HM Horvitz (1993) The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 75 641-652.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.M.5
  • 17
    • 42949148784 scopus 로고    scopus 로고
    • Surprising complexity of the ancestral apoptosis network
    • CM Zmasek, Q Zhang, Y Ye and A Godzik (2007) Surprising complexity of the ancestral apoptosis network. Genome Biol 8 R226.
    • (2007) Genome Biol , vol.8 , pp. R226
    • Zmasek, C.M.1    Zhang, Q.2    Ye, Y.3    Godzik, A.4
  • 19
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • MP Boldin, TM Goncharov, YV Goltsev and D Wallach (1996) Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 85 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 21
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • H Zou, WJ Henzel, X Liu, A Lutschg and X Wang (1997) Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90 405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 22
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • P Li, D Nijhawan, I Budihardjo, SM Srinivasula, M Ahmad, ES Alnemri and X Wang (1997) Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 23
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • P Fuentes-Prior and GS Salvesen (2004) The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem J 384 201-232.
    • (2004) Biochem J , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 24
    • 0029787268 scopus 로고    scopus 로고
    • Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases
    • K Orth, K O’Rourke, GS Salvesen and VM Dixit (1996) Molecular ordering of apoptotic mammalian CED-3/ICE-like proteases. J Biol Chem 271 20,977-20,980.
    • (1996) J Biol Chem , vol.271 , pp. 20,977-20,980
    • Orth, K.1    O’Rourke, K.2    Salvesen, G.S.3    Dixit, V.M.4
  • 25
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • HR Stennicke and GS Salvesen (1997) Biochemical characteristics of caspases-3, -6, -7, and -8. J Biol Chem 272 25,719-25,723.
    • (1997) J Biol Chem , vol.272 , pp. 25,719-25,723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 27
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • SJ Riedl and GS Salvesen (2007) The apoptosome: signalling platform of cell death. Nat Rev Mol Cell Biol 5 405-413.
    • (2007) Nat Rev Mol Cell Biol , vol.5 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 30
    • 33646024628 scopus 로고    scopus 로고
    • The apoptosome activates caspase-9 by dimerization
    • C Pop, J Timmer, S Sperandio and GS Salvesen (2006) The apoptosome activates caspase-9 by dimerization. Mol Cell 22 269-275.
    • (2006) Mol Cell , vol.22 , pp. 269-275
    • Pop, C.1    Timmer, J.2    Sperandio, S.3    Salvesen, G.S.4
  • 31
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism for caspase-8 activation
    • M Donepudi, A Mac Sweeney, C Briand and MG Gruetter (2003) Insights into the regulatory mechanism for caspase-8 activation. Mol Cell 11 543-549.
    • (2003) Mol Cell , vol.11 , pp. 543-549
    • Donepudi, M.1    Mac Sweeney, A.2    Briand, C.3    Gruetter, M.G.4
  • 34
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen. Mechanisms of activation and substrate binding
    • J Chai, Q Wu, E Shiozaki, SM Srinivasula, ES Alnemri and Y Shi (2001) Crystal structure of a procaspase-7 zymogen. Mechanisms of activation and substrate binding. Cell 107 399-407.
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 36
    • 0036470319 scopus 로고    scopus 로고
    • Reprieval from execution: The molecular basis of caspase inhibition
    • HR Stennicke, CA Ryan and GS Salvesen (2002) Reprieval from execution: the molecular basis of caspase inhibition. Trends Biochem Sci 27 94-101.
    • (2002) Trends Biochem Sci , vol.27 , pp. 94-101
    • Stennicke, H.R.1    Ryan, C.A.2    Salvesen, G.S.3
  • 37
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • SJ Riedl and Y Shi (2004) Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mol Cell Biol 5 897-907.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 38
    • 33845472476 scopus 로고    scopus 로고
    • Caspase inhibitors: Viral, cellular and chemical
    • BA Callus and DL Vaux (2007) Caspase inhibitors: viral, cellular and chemical. Cell Death Differ 14 73-78.
    • (2007) Cell Death Differ , vol.14 , pp. 73-78
    • Callus, B.A.1    Vaux, D.L.2
  • 39
    • 0036088471 scopus 로고    scopus 로고
    • IAP proteins: Blocking the road to death’s door
    • GS Salvesen and CS Duckett (2002) IAP proteins: blocking the road to death’s door. Nat Rev Mol Cell Biol 3 401-410.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 40
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: Why XIAP is the black sheep of the family
    • BP Eckelman, GS Salvesen and FL Scott (2006) Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family. EMBO Rep 7 988-994.
    • (2006) EMBO Rep , vol.7 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 41
    • 0032078249 scopus 로고    scopus 로고
    • Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts
    • AG Uren, EJ Coulson and DL Vaux (1998) Conservation of baculovirus inhibitor of apoptosis repeat proteins (BIRPs) in viruses, nematodes, vertebrates and yeasts. Trends Biochem Sci 23 159-162.
    • (1998) Trends Biochem Sci , vol.23 , pp. 159-162
    • Uren, A.G.1    Coulson, E.J.2    Vaux, D.L.3
  • 42
    • 33644853217 scopus 로고    scopus 로고
    • Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases
    • T Samuel, K Welsh, T Lober, SH Togo, JM Zapata and JC Reed (2006) Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases. J Biol Chem 281 1080-1090.
    • (2006) J Biol Chem , vol.281 , pp. 1080-1090
    • Samuel, T.1    Welsh, K.2    Lober, T.3    Togo, S.H.4    Zapata, J.M.5    Reed, J.C.6
  • 43
    • 33749389926 scopus 로고    scopus 로고
    • The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kappaB activation independently of TRAF1 AND TRAF2
    • E Varfolomeev, SM Wayson, VM Dixit, WJ Fairbrother and D Vucic (2006) The inhibitor of apoptosis protein fusion c-IAP2.MALT1 stimulates NF-kappaB activation independently of TRAF1 AND TRAF2. J Biol Chem 281 29,022-29,029.
    • (2006) J Biol Chem , vol.281 , pp. 29,022-29,029
    • Varfolomeev, E.1    Wayson, S.M.2    Dixit, V.M.3    Fairbrother, W.J.4    Vucic, D.5
  • 45
    • 0035831022 scopus 로고    scopus 로고
    • Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
    • Y Huang, YC Park, RL Rich, D Segal, DG Myszka and H Wu (2001) Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain. Cell 104 781-790.
    • (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
  • 49
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • A Ashkenazi and VM Dixit (1998) Death receptors: signaling and modulation. Science 281 1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 50
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • DR Green and JC Reed (1998) Mitochondria and apoptosis. Science 281 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 53
    • 0036566395 scopus 로고    scopus 로고
    • Unrestrained caspase-dependent cell death caused by loss of Diap1 function requires the Drosophila Apaf-1 homolog, Dark
    • A Rodriguez, P Chen, H Oliver and JM Abrams (2002) Unrestrained caspase-dependent cell death caused by loss of Diap1 function requires the Drosophila Apaf-1 homolog, Dark. EMBO J 21 2189-2197.
    • (2002) EMBO J , vol.21 , pp. 2189-2197
    • Rodriguez, A.1    Chen, P.2    Oliver, H.3    Abrams, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.