메뉴 건너뛰기




Volumn 2, Issue 10, 2005, Pages 771-777

Caspase-specific and nonspecific in vivo protein processing during Fas-induced apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CASPASE; CASPASE 3; CASPASE 7; CASPASE 8; DYNAMIN; FAS ANTIBODY; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; OXYGEN; OXYGEN 18; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; PROTEINASE; RECOMBINANT ENZYME; SYNTHETASE; TRANSCRIPTION FACTOR;

EID: 27144473929     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth792     Document Type: Article
Times cited : (209)

References (31)
  • 1
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J.C. et al. The sequence of the human genome. Science 291, 1304-1351 (2001).
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 2
    • 0042630561 scopus 로고    scopus 로고
    • Secretases as targets for the treatment of Alzheimer's disease: The prospects
    • Dewachter I. & Van Leuven, F. Secretases as targets for the treatment of Alzheimer's disease: The prospects. Lancet Neurol. 1, 409-416 (2002).
    • (2002) Lancet Neurol. , vol.1 , pp. 409-416
    • Dewachter, I.1    Van Leuven, F.2
  • 3
    • 1542604677 scopus 로고    scopus 로고
    • Cysteine proteases as disease markers
    • Berdowska, I. Cysteine proteases as disease markers. Clin. Chim. Acta 342, 41-69 (2004).
    • (2004) Clin. Chim. Acta , vol.342 , pp. 41-69
    • Berdowska, I.1
  • 6
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer, U., Janicke, R.U. & Schulze-Osthoff, K. Many cuts to ruin: A comprehensive update of caspase substrates. Cell Death Differ. 10, 76-100 (2003).
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 7
    • 0030701527 scopus 로고    scopus 로고
    • Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy
    • Cryns, V.L. et al. Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy. J. Biol. Chem. 272, 29449-29453 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 29449-29453
    • Cryns, V.L.1
  • 8
    • 0032555262 scopus 로고    scopus 로고
    • A cloning method for caspase substrates that uses the yeast two-hybrid system: Cloning of the antiapoptotic gene gelsolin
    • Kamada, S. et al. A cloning method for caspase substrates that uses the yeast two-hybrid system: Cloning of the antiapoptotic gene gelsolin. Proc. Natl. Acad. Sci. USA 95, 8532-8537 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8532-8537
    • Kamada, S.1
  • 9
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme
    • Kuida, K. et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1β converting enzyme. Science 267, 2000-2003 (1995).
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1
  • 10
    • 0028984948 scopus 로고
    • Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock
    • Li, P. et al. Mice deficient in IL-1β-converting enzyme are defective in production of mature IL-1β and resistant to endotoxic shock. Cell 80, 401-411 (1995).
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1
  • 11
    • 0034671735 scopus 로고    scopus 로고
    • The Fas-induced apoptosis analyzed by high throughput proteome analysis
    • Gerner, C. et al. The Fas-induced apoptosis analyzed by high throughput proteome analysis. J. Biol. Chem. 275, 39018-39026 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39018-39026
    • Gerner, C.1
  • 12
    • 0035854661 scopus 로고    scopus 로고
    • Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis
    • Thiede, B., Dimmler, C., Siejak, F. & Rudel, T. Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J. Biol. Chem. 276, 26044-26050 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 26044-26050
    • Thiede, B.1    Dimmler, C.2    Siejak, F.3    Rudel, T.4
  • 13
    • 0035987478 scopus 로고    scopus 로고
    • Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation
    • Gerner, C. et al. Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation. Cell Death Differ. 9 671-681 (2002).
    • (2002) Cell Death Differ. , vol.9 , pp. 671-681
    • Gerner, C.1
  • 14
    • 0036668524 scopus 로고    scopus 로고
    • Prediction of translocation and cleavage of heterogeneous ribonuclear proteins and Rho guanine nucleotide dissociation inhibitor 2 during apoptosis by subcellular proteome analysis
    • Thiede, B., Siejak, F., Dimmler, C. & Rudel, T. Prediction of translocation and cleavage of heterogeneous ribonuclear proteins and Rho guanine nucleotide dissociation inhibitor 2 during apoptosis by subcellular proteome analysis. Proteomics 2, 996-1006 (2002).
    • (2002) Proteomics , vol.2 , pp. 996-1006
    • Thiede, B.1    Siejak, F.2    Dimmler, C.3    Rudel, T.4
  • 15
    • 0037204952 scopus 로고    scopus 로고
    • The Fas signalling pathway: More than a paradigm
    • Wajant, H. The Fas signalling pathway: More than a paradigm. Science 296, 1635-1636 (2002).
    • (2002) Science , vol.296 , pp. 1635-1636
    • Wajant, H.1
  • 16
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert, K. et al. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21, 566-569 (2003).
    • (2003) Nat. Biotechnol. , vol.21 , pp. 566-569
    • Gevaert, K.1
  • 17
    • 4444271864 scopus 로고    scopus 로고
    • Global differential non-gel proteomics by quantitative and stable labelling of tryptic peptides with oxygen-18
    • Staes, A. et al. Global differential non-gel proteomics by quantitative and stable labelling of tryptic peptides with oxygen-18. J. Proteome. Res. 3, 786-791 (2004).
    • (2004) J. Proteome Res. , vol.3 , pp. 786-791
    • Staes, A.1
  • 18
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry, N.A. et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J. Biol. Chem. 272, 17907-17911 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1
  • 19
    • 0032484008 scopus 로고    scopus 로고
    • Inhibition of human caspases by peptide-based and macromolecular inhibitors
    • Garcia-Calvo, M. et al. Inhibition of human caspases by peptide-based and macromolecular inhibitors. J. Biol. Chem. 273 32608-32613 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32608-32613
    • Garcia-Calvo, M.1
  • 20
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson, D.W. et al. Identification and inhibition of the ICE/ CED-3 protease necessary for mammalian apoptosis. Nature 376 37-43 (1995).
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1
  • 21
    • 0035884195 scopus 로고    scopus 로고
    • Targeting of the transcription factor Max during apoptosis: Phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1
    • Krippner-Heidenreich, A. et al. Targeting of the transcription factor Max during apoptosis: Phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem. J. 358, 705-715 (2001).
    • (2001) Biochem. J. , vol.358 , pp. 705-715
    • Krippner-Heidenreich, A.1
  • 22
    • 0037023680 scopus 로고    scopus 로고
    • Apoptotic release of histones from nucleosomes
    • Wu, D. et al. Apoptotic release of histones from nucleosomes. J. Biol. Chem. 277, 12001-12008 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12001-12008
    • Wu, D.1
  • 23
    • 0034928793 scopus 로고    scopus 로고
    • SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis
    • Galande, S., Dickinson, L.A., Mian, I.S., Sikorska, M. & Kohwi-Shigematsu, T. SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis. Mol. Cell. Biol. 21, 5591-5604 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5591-5604
    • Galande, S.1    Dickinson, L.A.2    Mian, I.S.3    Sikorska, M.4    Kohwi-Shigematsu, T.5
  • 24
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara, S. et al. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature 401, 168-173 (1999).
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1
  • 25
    • 20044386174 scopus 로고    scopus 로고
    • Shotgun proteome analysis of protein cleavage in apoptotic cells
    • Thiede, B., Treumann, A., Kretschmer, A., Sohlke, J. & Rudel, T. Shotgun proteome analysis of protein cleavage in apoptotic cells. Proteomics 5, 2123-2130 (2005).
    • (2005) Proteomics , vol.5 , pp. 2123-2130
    • Thiede, B.1    Treumann, A.2    Kretschmer, A.3    Sohlke, J.4    Rudel, T.5
  • 26
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti, E. & Baralle, F.E. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J. Biol. Chem. 276, 36337-36343 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 27
    • 0037013146 scopus 로고    scopus 로고
    • Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45
    • Lallena, M.J., Chalmers, K.J., Llamazares, S., Lamond, A.I. & Valcarcel, J. Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45. Cell 109, 285-296 (2002).
    • (2002) Cell , vol.109 , pp. 285-296
    • Lallena, M.J.1    Chalmers, K.J.2    Llamazares, S.3    Lamond, A.I.4    Valcarcel, J.5
  • 28
    • 0037068447 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human spliceosome
    • Zhou, Z., Licklider, L.J., Gygi, S.P. & Reed, R. Comprehensive proteomic analysis of the human spliceosome. Nature 419, 182-185 (2002).
    • (2002) Nature , vol.419 , pp. 182-185
    • Zhou, Z.1    Licklider, L.J.2    Gygi, S.P.3    Reed, R.4
  • 29
    • 0344406975 scopus 로고    scopus 로고
    • ASAP, a novel protein complex involved in RNA processing and apoptosis
    • Schwerk, C. et al. ASAP, a novel protein complex involved in RNA processing and apoptosis. Mol. Cell Biol. 23, 2981-2990 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 2981-2990
    • Schwerk, C.1
  • 30
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signalling domains
    • Schultz, J., Milpetz, F., Bork, P. & Ponting, C.P. SMART, a simple modular architecture research tool: Identification of signalling domains. Proc. Natl. Acad. Sci. USA 95, 5857-5864 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 31
    • 0032914182 scopus 로고    scopus 로고
    • Alternative splicing and programmed cell death
    • Jiang, Z.H. & Wu, J.Y. Alternative splicing and programmed cell death. Proc. Soc. Exp. Biol. Med. 220, 64-72 (1999).
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 64-72
    • Jiang, Z.H.1    Wu, J.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.