메뉴 건너뛰기




Volumn 34, Issue 3, 2009, Pages 104-107

A caspase homolog keeps CED-3 in check

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CASPASE 3; PROTEINASE;

EID: 63149094761     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.11.003     Document Type: Short Survey
Times cited : (7)

References (24)
  • 1
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 2
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl S.J., and Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 5 (2004) 897-907
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 3
    • 33244471589 scopus 로고    scopus 로고
    • Developmental apoptosis in C. elegans: a complex CEDnario
    • Lettre G., and Hengartner M.O. Developmental apoptosis in C. elegans: a complex CEDnario. Nat. Rev. Mol. Cell Biol. 7 (2006) 97-108
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 97-108
    • Lettre, G.1    Hengartner, M.O.2
  • 4
    • 53549089865 scopus 로고    scopus 로고
    • Inhibition of CED-3 zymogen activation and apoptosis in Caenorhabditis elegans by caspase homolog CSP-3
    • Geng X., et al. Inhibition of CED-3 zymogen activation and apoptosis in Caenorhabditis elegans by caspase homolog CSP-3. Nat. Struct. Mol. Biol. 15 (2008) 1094-1101
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1094-1101
    • Geng, X.1
  • 5
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • Miura M., et al. Induction of apoptosis in fibroblasts by IL-1 β-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3. Cell 75 (1993) 653-660
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1
  • 6
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzyme
    • Yuan J., et al. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzyme. Cell 75 (1993) 641-652
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1
  • 7
    • 0027973061 scopus 로고
    • CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β-converting enzyme
    • Fernandes-Alnemri T., et al. CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 β-converting enzyme. J. Biol. Chem. 269 (1994) 30761-30764
    • (1994) J. Biol. Chem. , vol.269 , pp. 30761-30764
    • Fernandes-Alnemri, T.1
  • 8
    • 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
    • Xue D., et al. 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
  • 9
    • 26844485563 scopus 로고    scopus 로고
    • Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans
    • Yan N., et al. Structure of the CED-4-CED-9 complex provides insights into programmed cell death in Caenorhabditis elegans. Nature 437 (2005) 831-837
    • (2005) Nature , vol.437 , pp. 831-837
    • Yan, N.1
  • 10
    • 33646024628 scopus 로고    scopus 로고
    • The apoptosome activates caspase-9 by dimerization
    • Pop C., et al. The apoptosome activates caspase-9 by dimerization. Mol. Cell 22 (2006) 269-275
    • (2006) Mol. Cell , vol.22 , pp. 269-275
    • Pop, C.1
  • 12
    • 53249133039 scopus 로고    scopus 로고
    • Inhibitor of apoptosis proteins in eukaryotic evolution and development: a model of thematic conservation
    • O'Riordan M.X.D., et al. Inhibitor of apoptosis proteins in eukaryotic evolution and development: a model of thematic conservation. Dev. Cell 15 (2008) 497-508
    • (2008) Dev. Cell , vol.15 , pp. 497-508
    • O'Riordan, M.X.D.1
  • 13
    • 0033602489 scopus 로고    scopus 로고
    • Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis
    • Fraser A.G., et al. Caenorhabditis elegans inhibitor of apoptosis protein (IAP) homologue BIR-1 plays a conserved role in cytokinesis. Curr. Biol. 9 (1999) 292-301
    • (1999) Curr. Biol. , vol.9 , pp. 292-301
    • Fraser, A.G.1
  • 14
    • 0033588273 scopus 로고    scopus 로고
    • The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID
    • Wang S.L., et al. The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID. Cell 98 (1999) 453-463
    • (1999) Cell , vol.98 , pp. 453-463
    • Wang, S.L.1
  • 15
    • 33845483887 scopus 로고    scopus 로고
    • Caspases in cell survival, proliferation and differentiation
    • Lamkanfi M., et al. Caspases in cell survival, proliferation and differentiation. Cell Death Differ. 14 (2007) 44-55
    • (2007) Cell Death Differ. , vol.14 , pp. 44-55
    • Lamkanfi, M.1
  • 16
    • 0032567405 scopus 로고    scopus 로고
    • Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades
    • Shaham S. Identification of multiple Caenorhabditis elegans caspases and their potential roles in proteolytic cascades. J. Biol. Chem. 273 (1998) 35109-35117
    • (1998) J. Biol. Chem. , vol.273 , pp. 35109-35117
    • Shaham, S.1
  • 17
    • 0035860780 scopus 로고    scopus 로고
    • Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing
    • Lee S.H., et al. Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 activation processing. J. Biol. Chem. 276 (2001) 34495-34500
    • (2001) J. Biol. Chem. , vol.276 , pp. 34495-34500
    • Lee, S.H.1
  • 18
    • 10644270650 scopus 로고    scopus 로고
    • INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1β generation
    • Lamkanfi M., et al. INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1β generation. J. Biol. Chem. 279 (2004) 51729-51738
    • (2004) J. Biol. Chem. , vol.279 , pp. 51729-51738
    • Lamkanfi, M.1
  • 19
    • 0034730325 scopus 로고    scopus 로고
    • ICEBERG: a novel inhibitor of interleukin-1β generation
    • Humke E.W., et al. ICEBERG: a novel inhibitor of interleukin-1β generation. Cell 103 (2000) 99-111
    • (2000) Cell , vol.103 , pp. 99-111
    • Humke, E.W.1
  • 20
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler M., et al. Inhibition of death receptor signals by cellular FLIP. Nature 388 (1997) 190-195
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1
  • 21
    • 54249133441 scopus 로고    scopus 로고
    • FLIP and the death effector domain family
    • Yu J.W., and Shi Y. FLIP and the death effector domain family. Oncogene 27 (2008) 6216-6227
    • (2008) Oncogene , vol.27 , pp. 6216-6227
    • Yu, J.W.1    Shi, Y.2
  • 22
    • 37749030247 scopus 로고    scopus 로고
    • A phylogenetic and functional overview of inflammatory caspases and caspase-1-related CARD-only proteins
    • Kersse K., et al. A phylogenetic and functional overview of inflammatory caspases and caspase-1-related CARD-only proteins. Biochem. Soc. Trans. 35 (2007) 1508-1511
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 1508-1511
    • Kersse, K.1
  • 23
    • 0032524885 scopus 로고    scopus 로고
    • The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9
    • Conradt B., and Horvitz H.R. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 93 (1998) 519-529
    • (1998) Cell , vol.93 , pp. 519-529
    • Conradt, B.1    Horvitz, H.R.2
  • 24
    • 0032509238 scopus 로고    scopus 로고
    • Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation
    • del Peso L., et al. Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation. J. Biol. Chem. 273 (1998) 33495-33500
    • (1998) J. Biol. Chem. , vol.273 , pp. 33495-33500
    • del Peso, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.