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Volumn 434, Issue 7035, 2005, Pages 926-933

Structure of the apoptotic protease-activating factor 1 bound to ADP

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; CYTOLOGY; HYDROLYSIS; METABOLITES; MOLECULAR BIOLOGY; NUCLEIC ACIDS; PHOSPHATES;

EID: 17244368276     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03465     Document Type: Article
Times cited : (296)

References (30)
  • 1
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl, S. J. & Shi, Y. Molecular mechanisms of caspase regulation during apoptosis. Nature Rev. Mol. Cell Biol. 5, 897-907 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 2
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15, 2922-2933 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2922-2933
    • Wang, X.1
  • 3
    • 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
  • 4
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou, H., Li, Y., Liu, X. & Wang, X. An APAF-1-cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J. Biol. Chem. 274, 11549-11556 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 5
    • 0034613302 scopus 로고    scopus 로고
    • Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1
    • Jiang, X. & Wang, X. Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1. J. Biol. Chem. 275, 31199-31203 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 31199-31203
    • Jiang, X.1    Wang, X.2
  • 6
    • 0344348821 scopus 로고    scopus 로고
    • Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis
    • Hu, Y., Benedict, M. A., Ding, L. & Nunez, G. Role of cytochrome c and dATP/ATP hydrolysis in Apaf-1-mediated caspase-9 activation and apoptosis. EMBO J. 18, 3586-3595 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3586-3595
    • Hu, Y.1    Benedict, M.A.2    Ding, L.3    Nunez, G.4
  • 7
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • Saleh, A., Srinivasula, S. M., Acharya, S., Fishel, R. & Alnemri, E. S. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J. Biol. Chem. 274, 17941-17945 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3    Fishel, R.4    Alnemri, E.S.5
  • 8
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and Apaf-1 form an active holoenzyme
    • Rodriguez, J. & Lazebnik, Y. Caspase-9 and Apaf-1 form an active holoenzyme. Genes Dev. 13, 3179-3184 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 9
    • 0035474227 scopus 로고    scopus 로고
    • The NOD: A signaling module that regulates apoptosis and host defense against pathogens
    • Inohara, N. & Nunez, G. The NOD: a signaling module that regulates apoptosis and host defense against pathogens. Oncogene 20, 6473-6481 (2001).
    • (2001) Oncogene , vol.20 , pp. 6473-6481
    • Inohara, N.1    Nunez, G.2
  • 10
    • 0032509354 scopus 로고    scopus 로고
    • WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation
    • Hu, Y., Ding, L., Spencer, D. M. & Nunez, G. WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation. J. Biol. Chem. 273, 33489-33494 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33489-33494
    • Hu, Y.1    Ding, L.2    Spencer, D.M.3    Nunez, G.4
  • 11
  • 12
    • 17344379513 scopus 로고    scopus 로고
    • Five years on the wings of fork head
    • Kaufmann, E. & Knöchel, W. Five years on the wings of fork head. Mech. Dev. 57, 3-20 (1996).
    • (1996) Mech. Dev. , vol.57 , pp. 3-20
    • Kaufmann, E.1    Knöchel, W.2
  • 13
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 14
    • 0032555745 scopus 로고    scopus 로고
    • Crystal structure of the hexamerization domain of N-ethylmaleimide- sensitive fusion protein
    • Lenzen, C. U., Steinmann, D., Whiteheart, S. W. & Weis, W. I. Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein. Cell 94, 525-536 (1998).
    • (1998) Cell , vol.94 , pp. 525-536
    • Lenzen, C.U.1    Steinmann, D.2    Whiteheart, S.W.3    Weis, W.I.4
  • 15
    • 0034502514 scopus 로고    scopus 로고
    • Structure of the AAA ATPase p97
    • Zhang, X. et al. Structure of the AAA ATPase p97. Mol. Cell 6, 1473-1484 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 1473-1484
    • Zhang, X.1
  • 17
    • 0034658130 scopus 로고    scopus 로고
    • ATP-activated oligomerization as a mechanism for apoptosis regulation: Fold and mechanism prediction for CED-4
    • Jaroszewski, L., Rychlewski, L., Reed, J. C. & Godzik, A. ATP-activated oligomerization as a mechanism for apoptosis regulation: fold and mechanism prediction for CED-4. Proteins 39, 197-203 (2000).
    • (2000) Proteins , vol.39 , pp. 197-203
    • Jaroszewski, L.1    Rychlewski, L.2    Reed, J.C.3    Godzik, A.4
  • 18
    • 0033542482 scopus 로고    scopus 로고
    • Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1
    • Qin, H. et al. Structural basis of procaspase-9 recruitment by the apoptotic protease-activating factor 1. Nature 399, 547-555 (1999).
    • (1999) Nature , vol.399 , pp. 547-555
    • Qin, H.1
  • 19
    • 0034614551 scopus 로고    scopus 로고
    • Nucleotide requirements for the in vitro activation of the apoptosis protein-activating factor-1-mediated caspase pathway
    • Genini, D. et al. Nucleotide requirements for the in vitro activation of the apoptosis protein-activating factor-1-mediated caspase pathway. J. Biol. Chem. 275, 29-34 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 29-34
    • Genini, D.1
  • 20
    • 0032483010 scopus 로고    scopus 로고
    • Induction of an apoptotic program in cell-free extracts by 2-chloro-2′-deoxyadenosine 5′-triphosphate and cytochrome c
    • Leoni, L. M. et al. Induction of an apoptotic program in cell-free extracts by 2-chloro-2′-deoxyadenosine 5′-triphosphate and cytochrome c. Proc. Natl Acad. Sci. USA 95, 9567-9571 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9567-9571
    • Leoni, L.M.1
  • 21
    • 0033529634 scopus 로고    scopus 로고
    • Caspase activation involves the formation of the aposome, a large (∼700 kDa) caspase-activating complex
    • Cain, K., Brown, D. G., Langlais, C. & Cohen, G. M. Caspase activation involves the formation of the aposome, a large (∼700 kDa) caspase-activating complex. J. Biol. Chem. 274, 22686-22692 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22686-22692
    • Cain, K.1    Brown, D.G.2    Langlais, C.3    Cohen, G.M.4
  • 22
    • 0034677361 scopus 로고    scopus 로고
    • The structures of HsIU and the ATP-dependent protease HsIU-HsIV
    • Bochtler, M. et al. The structures of HsIU and the ATP-dependent protease HsIU-HsIV. Nature 403, 800-805 (2000).
    • (2000) Nature , vol.403 , pp. 800-805
    • Bochtler, M.1
  • 23
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai, D., Zhao, R., Li, D., Finkielstein, C. V. & Chen, X. S. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119, 47-60 (2004).
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 24
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding and activation
    • Acehan, D. et al. Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding and activation. Mol. Cell 9, 423-432 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0033119895 scopus 로고    scopus 로고
    • Automated structure solution for MIR and MAD
    • Terwilliger, T. C. & Berendzen, J. Automated structure solution for MIR and MAD. Acta Crystallogr. D 55, 849-861 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 27
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 28
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 29
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 30
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11, 281-296 (1991).
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.