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Volumn 80, Issue , 2011, Pages 1055-1087

Caspase substrates and cellular remodeling

Author keywords

apoptosis; biomarkers; degradomics; differentiation; erythropoiesis; proteasome

Indexed keywords

ABELSON KINASE; CASPASE; CASPASE 10; CASPASE 12; CASPASE 14; CASPASE 2; CASPASE 3; CASPASE 4; CASPASE 5; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; INHIBITOR OF APOPTOSIS PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME; PROTEASOME; TRANSCRIPTION FACTOR GATA 1; UBIQUITIN; X LINKED INHIBITOR OF APOPTOSIS;

EID: 79959461070     PISSN: 00664154     EISSN: 00664154     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-061809-121639     Document Type: Article
Times cited : (257)

References (200)
  • 1
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • DOI 10.1016/S1534-5807(03)00120-5, PII S1534580703001205
    • Arama E, Agapite J, Steller H. 2003. Caspase activity and a specific cytochrome c are required for sperm differentiation in Drosophila. Dev. Cell 4:687-697. (Pubitemid 36564899)
    • (2003) Developmental Cell , vol.4 , Issue.5 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 3
  • 5
    • 2542475112 scopus 로고    scopus 로고
    • Caspase-3 has a nonapoptotic function in erythroid maturation
    • DOI 10.1182/blood-2003-09-3362
    • Carlile GW, Smith DH, Wiedmann M. 2004. Caspase-3 has a nonapoptotic function in erythroid maturation. Blood 103:4310-316. (Pubitemid 38685378)
    • (2004) Blood , vol.103 , Issue.11 , pp. 4310-4316
    • Carlile, G.W.1    Smith, D.H.2    Wiedmann, M.3
  • 6
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan AR, James MN. 1998. Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7:815-836. (Pubitemid 28216525)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 815-836
    • Khan, A.R.1    James, M.N.G.2
  • 9
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • DOI 10.1042/BJ20041142
    • Fuentes-Prior P, Salvesen GS. 2004. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384:201-232. (Pubitemid 39656233)
    • (2004) Biochemical Journal , vol.384 , Issue.2 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 13
    • 68149114498 scopus 로고    scopus 로고
    • Can't live without them, can live with them: Roles of caspases during vital cellular processes
    • Feinstein-Rotkopf Y, Arama E. 2009. Can't live without them, can live with them: roles of caspases during vital cellular processes. Apoptosis 14:980-995.
    • (2009) Apoptosis , vol.14 , pp. 980-995
    • Feinstein-Rotkopf, Y.1    Arama, E.2
  • 14
    • 58149464289 scopus 로고    scopus 로고
    • The Jekyll and Hyde functions of caspases
    • Yi CH, Yuan J. 2009. The Jekyll and Hyde functions of caspases. Dev. Cell 16:21-34.
    • (2009) Dev. Cell , vol.16 , pp. 21-34
    • Yi, C.H.1    Yuan, J.2
  • 15
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1βprocessing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, et al. 1992. A novel heterodimeric cysteine protease is required for interleukin- 1βprocessing in monocytes. Nature 356:768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5
  • 16
    • 2542457495 scopus 로고    scopus 로고
    • Inflammatory caspases: Linking an intracellular innate immune system to autoinflammatory diseases
    • DOI 10.1016/j.cell.2004.05.004, PII S0092867404004908
    • Martinon F, Tschopp J. 2004. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 117:561-574. (Pubitemid 38692523)
    • (2004) Cell , vol.117 , Issue.5 , pp. 561-574
    • Martinon, F.1    Tschopp, J.2
  • 18
    • 77951805919 scopus 로고    scopus 로고
    • Inflammatory stimuli regulate caspase substrate profiles
    • Agard NJ, Maltby D, Wells JA. 2010. Inflammatory stimuli regulate caspase substrate profiles. Mol. Cell. Proteomics 9:880-893.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 880-893
    • Agard, N.J.1    Maltby, D.2    Wells, J.A.3
  • 20
    • 0036385828 scopus 로고    scopus 로고
    • Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation
    • Chien AJ, Presland RB, Kuechle MK. 2002. Processing of native caspase-14 occurs at an atypical cleavage site in normal epidermal differentiation. Biochem. Biophys. Res. Commun. 296:911-917.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 911-917
    • Chien, A.J.1    Presland, R.B.2    Kuechle, M.K.3
  • 25
    • 46649096691 scopus 로고    scopus 로고
    • Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire
    • Eckhart L, Ballaun C, Hermann M, VandeBerg JL, Sipos W, et al. 2008. Identification of novel mammalian caspases reveals an important role of gene loss in shaping the human caspase repertoire. Mol. Biol. Evol. 25:831-841.
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 831-841
    • Eckhart, L.1    Ballaun, C.2    Hermann, M.3    Vande Berg, J.L.4    Sipos, W.5
  • 26
    • 0036302814 scopus 로고    scopus 로고
    • Protease degradomics: A new challenge for proteomics
    • DOI 10.1038/nrm858
    • Ĺopez-Otín C, Overall CM. 2002. Protease degradomics: a new challenge for proteomics. Nat. Rev. Mol. Cell Biol. 3:509-519. (Pubitemid 34733432)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.7 , pp. 509-519
    • Lopez-Otin, C.1    Overall, C.M.2
  • 27
    • 70549111633 scopus 로고    scopus 로고
    • Methods for the proteomic identification of protease substrates
    • Agard NJ, Wells JA. 2009. Methods for the proteomic identification of protease substrates. Curr. Opin. Chem. Biol. 13:503-9.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 503-509
    • Agard, N.J.1    Wells, J.A.2
  • 28
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: A searchable database of caspase substrates
    • DOI 10.1038/sj.cdd.4402103, PII 4402103
    • L̈uthi AU, Martin SJ. 2007. The CASBAH: a searchable database of caspase substrates. Cell Death Differ. 14:641-650. (Pubitemid 46444502)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 641-650
    • Luthi, A.U.1    Martin, S.J.2
  • 31
  • 32
    • 0032898735 scopus 로고    scopus 로고
    • Non-specific effects of methyl ketone peptide inhibitors of caspases
    • DOI 10.1016/S0014-5793(98)01640-8, PII S0014579398016408
    • Schotte P, DeclercqW, Van Huffel S, Vandenabeele P, Beyaert R. 1999. Non-specific effects of methyl ketone peptide inhibitors of caspases. FEBS Lett. 442:117-121. (Pubitemid 29065390)
    • (1999) FEBS Letters , vol.442 , Issue.1 , pp. 117-121
    • Schotte, P.1    Declercq, W.2    Van Huffel, S.3    Vandenabeele, P.4    Beyaert, R.5
  • 34
    • 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. 2001. Predominant identification of RNA-binding proteins in Fas-induced apoptosis by proteome analysis. J. Biol. Chem. 276:26044-050.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26044-26050
    • Thiede, B.1    Dimmler, C.2    Siejak, F.3    Rudel, T.4
  • 35
    • 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, RudelT. 2002. 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) Proteomics , vol.2 , pp. 996-1006
    • Thiede, B.1    Siejak, F.2    Dimmler, C.3    Rudel, T.4
  • 37
    • 0032561365 scopus 로고    scopus 로고
    • Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line: Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3
    • DOI 10.1074/jbc.273.43.28057
    • Brockstedt E, Rickers A, Kostka S, Laubersheimer A, D̈orken B, et al. 1998. Identification of apoptosisassociated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3. J. Biol. Chem. 273:28057-064. (Pubitemid 28496099)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 28057-28064
    • Brockstedt, E.1    Rickers, A.2    Kostka, S.3    Laubersheimer, A.4    Dorken, B.5    Wittmann-Liebold, B.6    Bommert, K.7    Otto, A.8
  • 38
    • 8744269434 scopus 로고    scopus 로고
    • Identification of caspase-3 degradome by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis
    • DOI 10.1002/pmic.200400979
    • Lee AY, Park BC, Jang M, Cho S, Lee DH, et al. 2004. Identification of caspase-3 degradome by twodimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 4:3429-436. (Pubitemid 39525292)
    • (2004) Proteomics , vol.4 , Issue.11 , pp. 3429-3436
    • Ah, Y.L.1    Byoung, C.P.2    Jang, M.3    Cho, S.4    Do, H.L.5    Sang, C.L.6    Pyung, K.M.7    Sung, G.P.8
  • 39
    • 53749104277 scopus 로고    scopus 로고
    • Mining of caspase-7 substrates using a degradomic approach
    • Jang M, Park BC, Kang S, Lee D, ChoS, Lee SC. 2008. Mining of caspase-7 substrates using a degradomic approach. Mol. Cells 26:152-157.
    • (2008) Mol. Cells , vol.26 , pp. 152-157
    • Jang, M.1    Park, B.C.2    Kang, S.3    Lee, D.4    Chos Lee, S.C.5
  • 40
    • 34447509998 scopus 로고    scopus 로고
    • Establishing a blueprint for CED-3-dependent killing through identification of multiple substrates for this protease
    • DOI 10.1074/jbc.M611051200
    • Taylor RC, Brumatti G, Ito S, HengartnerMO, Derry WB, Martin SJ. 2007. Establishing a blueprint for CED-3-dependent killing through identification of multiple substrates for this protease. J. Biol. Chem. 282:15011-021. (Pubitemid 47093383)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 15011-15021
    • Taylor, R.C.1    Brumatti, G.2    Ito, S.3    Hengartner, M.O.4    Derry, W.B.5    Martin, S.J.6
  • 42
    • 49549113643 scopus 로고    scopus 로고
    • Globalmapping of the topography andmagnitude of proteolytic events in apoptosis
    • DixMM, SimonGM, Cravatt BF. 2008. Globalmapping of the topography andmagnitude of proteolytic events in apoptosis. Cell 134:679-691.
    • (2008) Cell , vol.134 , pp. 679-691
    • Dix, M.M.1    Simon, G.M.2    Cravatt, B.F.3
  • 43
    • 0017293834 scopus 로고
    • Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nα-acetylated
    • Brown JL, Roberts WK. 1976. Evidence that approximately eighty per cent of the soluble proteins from Ehrlich ascites cells are Nα-acetylated. J. Biol. Chem. 251:1009-014.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1009-1014
    • Brown, J.L.1    Roberts, W.K.2
  • 45
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • DOI 10.1038/nbt810
    • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, et al. 2003. Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat. Biotechnol. 21:566-569. (Pubitemid 36532024)
    • (2003) Nature Biotechnology , vol.21 , Issue.5 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5    Thomas, G.R.6    Vandekerckhove, J.7
  • 46
    • 75149167437 scopus 로고    scopus 로고
    • Proteome-wide substrate analysis indicates substrate exclusion as a mechanism to generate caspase-7 versus caspase-3 specificity
    • Demon D, Van Damme P, Vanden Berghe T, Deceuninck A, Van Durme J, et al. 2009. Proteome-wide substrate analysis indicates substrate exclusion as a mechanism to generate caspase-7 versus caspase-3 specificity. Mol. Cell. Proteomics 8:2700-714.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 2700-2714
    • Demon, D.1    Van Damme, P.2    Vanden Berghe, T.3    Deceuninck, A.4    Van Durme, J.5
  • 47
    • 77957992099 scopus 로고    scopus 로고
    • A quantitative proteomics design for systematic identification of protease cleavage events
    • Impens F, Colaert N, Helsens K, Ghesquìere B, Timmerman E, et al. 2010. A quantitative proteomics design for systematic identification of protease cleavage events. Mol. Cell. Proteomics 9:2327-333.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2327-2333
    • Impens, F.1    Colaert, N.2    Helsens, K.3    Ghesquìere, B.4    Timmerman, E.5
  • 48
    • 0025757012 scopus 로고
    • Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution
    • Abrahmśen L, Tom J, Burnier J, Butcher KA, Kossiakoff A, Wells JA. 1991. Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution. Biochemistry 30:4151-159.
    • (1991) Biochemistry , vol.30 , pp. 4151-4159
    • Abrahmśen, L.1    Tom, J.2    Burnier, J.3    Butcher, K.A.4    Kossiakoff, A.5    Wells, J.A.6
  • 49
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • Jackson DY, Burnier J, Quan C, Stanley M, Tom J, Wells JA. 1994. A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266:243-247. (Pubitemid 24343508)
    • (1994) Science , vol.266 , Issue.5183 , pp. 243-247
    • Jackson, D.Y.1    Burnier, J.2    Quan, C.3    Stanley, M.4    Tom, J.5    Wells, J.A.6
  • 51
    • 52649141086 scopus 로고    scopus 로고
    • Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini
    • Mahrus S, Trinidad JC, Barkan DT, Sali A, Burlingame AL, Wells JA. 2008. Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini. Cell 134:866-876.
    • (2008) Cell , vol.134 , pp. 866-876
    • Mahrus, S.1    Trinidad, J.C.2    Barkan, D.T.3    Sali, A.4    Burlingame, A.L.5    Wells, J.A.6
  • 54
    • 73349138618 scopus 로고    scopus 로고
    • Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini
    • Xu G, Shin SB, Jaffrey SR. 2009. Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc. Natl. Acad. Sci. USA 106:19310-315.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 19310-19315
    • Xu, G.1    Shin, S.B.2    Jaffrey, S.R.3
  • 55
    • 54249137225 scopus 로고    scopus 로고
    • Proteolytic needles in the cellular haystack
    • Enoksson M, Salvesen GS. 2008. Proteolytic needles in the cellular haystack. Nat. Chem. Biol. 4:651-652.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 651-652
    • Enoksson, M.1    Salvesen, G.S.2
  • 56
    • 67649286454 scopus 로고    scopus 로고
    • Comparative assessment of large-scale proteomic studies of apoptotic proteolysis
    • Simon GM, Dix MM, Cravatt BF. 2009. Comparative assessment of large-scale proteomic studies of apoptotic proteolysis. ACS Chem. Biol. 4:401-8.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 401-408
    • Simon, G.M.1    Dix, M.M.2    Cravatt, B.F.3
  • 57
    • 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
    • DOI 10.1042/0264-6021:3580705
    • Krippner-Heidenreich A, Talanian RV, Sekul R, Kraft R, Thole H, et al. 2001. 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. (Pubitemid 32896958)
    • (2001) Biochemical Journal , vol.358 , Issue.3 , pp. 705-715
    • Krippner-Heidenreich, A.1    Talanian, R.V.2    Sekul, R.3    Kraft, R.4    Thole, H.5    Ottleben, H.6    Luscher, B.7
  • 58
    • 0034282666 scopus 로고    scopus 로고
    • The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM
    • Hawkins CJ, Yoo SJ, Peterson EP, Wang SL. 2000. The Drosophila caspase DRONC cleaves following glutamate or aspartate and is regulated by DIAP1, HID, and GRIM. J. Biol. 275:27084-093.
    • (2000) J. Biol. , vol.275 , pp. 27084-27093
    • Hawkins, C.J.1    Yoo, S.J.2    Peterson, E.P.3    Wang, S.L.4
  • 59
    • 42149169031 scopus 로고    scopus 로고
    • Activation mechanism and substrate specificity of the Drosophila initiator caspase DRONC
    • DOI 10.1038/cdd.2008.23, PII CDD200823
    • Snipas SJ, Drag M, Stennicke HR, Salvesen GS. 2008. Activation mechanism and substrate specificity of the Drosophila initiator caspase DRONC. Cell Death Differ. 15:938-945. (Pubitemid 351524435)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.5 , pp. 938-945
    • Snipas, S.J.1    Drag, M.2    Stennicke, H.R.3    Salvesen, G.S.4
  • 60
    • 39449094293 scopus 로고    scopus 로고
    • A biochemical analysis of the activation of the Drosophila caspase DRONC
    • DOI 10.1038/sj.cdd.4402288, PII 4402288
    • Dorstyn L, Kumar S. 2008. A biochemical analysis of the activation of the Drosophila caspase DRONC. Cell Death Differ. 15:461-470. (Pubitemid 351267297)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.3 , pp. 461-470
    • Dorstyn, L.1    Kumar, S.2
  • 61
    • 21444436375 scopus 로고    scopus 로고
    • Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells
    • DOI 10.1074/jbc.M501206200
    • Muro I, Means JC, Clem RJ. 2005. Cleavage of the apoptosis inhibitor DIAP1 by the apical caspase DRONC in both normal and apoptotic Drosophila cells. J. Biol. Chem. 280:18683-688. (Pubitemid 41379568)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 18683-18688
    • Muro, I.1    Means, J.C.2    Clem, R.J.3
  • 65
    • 0034283578 scopus 로고    scopus 로고
    • Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8
    • Stennicke HR, Renatus M, Meldal M, Salvesen GS. 2000. Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8. Biochem. J. 350(Pt. 2):563-68.
    • (2000) Biochem. J. , vol.350 , Issue.PART. 2 , pp. 563-68
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 66
    • 23144444029 scopus 로고    scopus 로고
    • GraBCas: A bioinformatics tool for score-based prediction of caspase- and granzyme B-cleavage sites in protein sequences
    • DOI 10.1093/nar/gki433
    • Backes C, Kuentzer J, Lenhof HP, Comtesse N, Meese E. 2005. GraBCas: a bioinformatics tool for score-based prediction of caspase-and granzyme B-cleavage sites in protein sequences. Nucleic Acids Res. 33:W208-213. (Pubitemid 44529910)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Backes, C.1    Kuentzer, J.2    Lenhof, H.-P.3    Comtesse, N.4    Meese, E.5
  • 67
    • 44949142150 scopus 로고    scopus 로고
    • Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites
    • DOI 10.1038/nbt1408, PII NBT1408
    • Schilling O, Overall C. 2008. Proteome-derived, database-searchable peptide libraries for identifying protease cleavage sites. Nat. Biotechnol. 26:685-694. (Pubitemid 351809596)
    • (2008) Nature Biotechnology , vol.26 , Issue.6 , pp. 685-694
    • Schilling, O.1    Overall, C.M.2
  • 69
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motif selectivity of caspases: Implications for analysis of apoptotic pathways
    • McStay GP, Salvesen GS, Green DR. 2008. Overlapping cleavage motif selectivity of caspases: implications for analysis of apoptotic pathways. Cell Death Differ. 15:322-331.
    • (2008) Cell Death Differ. , vol.15 , pp. 322-331
    • McStay, G.P.1    Salvesen, G.S.2    Green, D.R.3
  • 70
    • 0345826185 scopus 로고    scopus 로고
    • Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis
    • DOI 10.1074/jbc.M306653200
    • Fluhrer R, Friedlein A, Haass C, Walter J. 2004. Phosphorylation of presenilin 1 at the caspase recognition site regulates its proteolytic processing and the progression of apoptosis. J. Biol. Chem. 279:1585-593. (Pubitemid 38084422)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 1585-1593
    • Fluhrer, R.1    Friedlein, A.2    Haass, C.3    Walter, J.4
  • 72
    • 0030613770 scopus 로고    scopus 로고
    • Phosphorylation of IκB-α inhibits its cleavage by caspase CPP32 in vitro
    • DOI 10.1074/jbc.272.47.29419
    • Barkett M, Xue D, Horvitz HR, Gilmore TD. 1997. Phosphorylation of IkappaB-alpha inhibits its cleavage by caspase CPP32 in vitro. J. Biol. Chem. 272:29419-422. (Pubitemid 27508021)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.47 , pp. 29419-29422
    • Barkett, M.1    Xue, D.2    Horvitz, H.3    Gilmore, T.D.4
  • 73
    • 38049064947 scopus 로고    scopus 로고
    • Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site
    • Schweigreiter R, Stasyk T, Contarini I, Frauscher S, Oertle T, et al. 2007. Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site. Proteomics 7:4457-467.
    • (2007) Proteomics , vol.7 , pp. 4457-4467
    • Schweigreiter, R.1    Stasyk, T.2    Contarini, I.3    Frauscher, S.4    Oertle, T.5
  • 75
    • 69249206534 scopus 로고    scopus 로고
    • Evaluation of recombinant caspase specificity by competitive substrates
    • Benkova B, Lozanov V, Ivanov IP, Mitev V. 2009. Evaluation of recombinant caspase specificity by competitive substrates. Anal. Biochem. 394:68-74.
    • (2009) Anal. Biochem. , vol.394 , pp. 68-74
    • Benkova, B.1    Lozanov, V.2    Ivanov, I.P.3    Mitev, V.4
  • 76
  • 77
    • 33745644229 scopus 로고    scopus 로고
    • Structural and kinetic analysis of caspase-3 reveals role for s5 binding site in substrate recognition
    • DOI 10.1016/j.jmb.2006.05.041, PII S002228360600622X
    • Fang B, Boross PI, Tozser J, Weber IT. 2006. Structural and kinetic analysis of caspase-3 reveals role for S5 binding site in substrate recognition. J. Mol. Biol. 360:654-666. (Pubitemid 43975116)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.3 , pp. 654-666
    • Fang, B.1    Boross, P.I.2    Tozser, J.3    Weber, I.T.4
  • 79
    • 6344285316 scopus 로고    scopus 로고
    • Probing the high energy states in proteins by proteolysis
    • DOI 10.1016/j.jmb.2004.08.085, PII S002228360401085X
    • Park C, Marqusee S. 2004. Probing the high energy states in proteins by proteolysis. J. Mol. Biol. 343:1467-476. (Pubitemid 39387837)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1467-1476
    • Park, C.1    Marqusee, S.2
  • 80
    • 0021782926 scopus 로고
    • The application of neutron crystallography to the study of dynamic and hydration properties of proteins
    • Kossiakoff A. 1985. The application of neutron crystallography to the study of dynamic and hydration properties of proteins. Annu. Rev. Biochem. 54:1195-227.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 1195-1227
    • Kossiakoff, A.1
  • 81
    • 29144473665 scopus 로고    scopus 로고
    • CaSPredictor: A new computer-based tool for caspase substrate prediction
    • DOI 10.1093/bioinformatics/bti1034
    • Garay-Malpartida HM, Occhiucci JM, Alves J, Beliźario JE. 2005. CaSPredictor: a new computer-based tool for caspase substrate prediction. Bioinformatics 21:i169-176. (Pubitemid 41794487)
    • (2005) Bioinformatics , vol.21 , Issue.SUPPL. 1
    • Garay-Malpartida, H.M.1    Occhiucci, J.M.2    Alves, J.3    Belizario, J.E.4
  • 82
    • 84871967410 scopus 로고    scopus 로고
    • SVM-based prediction of caspase substrate cleavage sites
    • Wee LJ, Tan TW, Ranganathan S. 2006. SVM-based prediction of caspase substrate cleavage sites.BMC Bioinform. 7(Suppl. 5):S14.
    • (2006) BMC Bioinform. , vol.7 , Issue.SUPPL. 5
    • Wee, L.J.1    Tan, T.W.2    Ranganathan, S.3
  • 83
    • 77954481626 scopus 로고    scopus 로고
    • Prediction of protease substrates using sequence and structure features
    • Barkan DT, Hostetter DR, Mahrus S, Pieper U, Wells JA, et al. 2010. Prediction of protease substrates using sequence and structure features. Bioinformatics 26:1714-722.
    • (2010) Bioinformatics , vol.26 , pp. 1714-1722
    • Barkan, D.T.1    Hostetter, D.R.2    Mahrus, S.3    Pieper, U.4    Wells, J.A.5
  • 84
    • 0035932465 scopus 로고    scopus 로고
    • Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex
    • DOI 10.1038/35068604
    • Xu G, Cirilli M, Huang Y, Rich RL, Myszka DG, Wu H. 2001. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 410:494-497. (Pubitemid 32240052)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 494-497
    • Xu, G.1    Cirilli, M.2    Huang, Y.3    Rich, R.L.4    Myszka, D.G.5    Wu, H.6
  • 86
    • 0036741135 scopus 로고    scopus 로고
    • Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites
    • Overall CM. 2002. Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites. Mol. Biotechnol. 22:51-86.
    • (2002) Mol. Biotechnol. , vol.22 , pp. 51-86
    • Overall, C.M.1
  • 87
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • DOI 10.1111/j.1538-7836.2004.01021.x
    • Krishnaswamy S. 2005. Exosite-driven substrate specificity and function in coagulation. J. Thromb. Haemost. 3:54-67. (Pubitemid 41647115)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.1 , pp. 54-67
    • Krishnaswamy, S.1
  • 88
    • 55049133250 scopus 로고    scopus 로고
    • Metadegradomics: Toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome
    • Doucet A, Butler GS, Rodríguez D, Prudova A, Overall CM. 2008. Metadegradomics: toward in vivo quantitative degradomics of proteolytic post-translational modifications of the cancer proteome. Mol. Cell. Proteomics 7:1925-951.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1925-1951
    • Doucet, A.1    Butler, G.S.2    Rodríguez, D.3    Prudova, A.4    Overall, C.M.5
  • 89
    • 0033214624 scopus 로고    scopus 로고
    • Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7
    • Germain M, Affar EB, D'AmoursD, DixitVM, Salvesen GS, PoirierGG.1999. Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. Evidence for involvement of caspase-7. J. Biol. Chem. 274:28379-384.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28379-28384
    • Germain, M.1    Affar, E.B.2    D'Amours, D.3    Dixit, V.M.4    Salvesen, G.S.5    Poirier, G.G.6
  • 91
    • 19644375921 scopus 로고    scopus 로고
    • Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G
    • DOI 10.1002/jcb.20409
    • Widlak P, Garrard WT. 2005. Discovery, regulation, and action of the major apoptotic nucleases DFF40/CAD and endonuclease G. J. Cell Biochem. 94:1078-087. (Pubitemid 41420231)
    • (2005) Journal of Cellular Biochemistry , vol.94 , Issue.6 , pp. 1078-1087
    • Widlak, P.1    Garrard, W.T.2
  • 92
    • 77951195672 scopus 로고    scopus 로고
    • Caspase-dependent conversion of Dicer ribonuclease into a death-promoting deoxyribonuclease
    • Nakagawa A, Shi Y, Kage-Nakadai E, Mitani S, Xue D. 2010. Caspase-dependent conversion of Dicer ribonuclease into a death-promoting deoxyribonuclease. Science 328:327-334.
    • (2010) Science , vol.328 , pp. 327-334
    • Nakagawa, A.1    Shi, Y.2    Kage-Nakadai, E.3    Mitani, S.4    Xue, D.5
  • 93
    • 69449095860 scopus 로고    scopus 로고
    • Caspases and kinases in a death grip
    • Kurokawa M, Kornbluth S. 2009. Caspases and kinases in a death grip. Cell 138:838-854.
    • (2009) Cell , vol.138 , pp. 838-854
    • Kurokawa, M.1    Kornbluth, S.2
  • 94
    • 0036311492 scopus 로고    scopus 로고
    • On the origin, evolution, and nature of programmed cell death: A timeline of four billion years
    • DOI 10.1038/sj.cdd.4400950
    • Ameisen JC. 2002. On the origin, evolution, and nature of programmed cell death: a timeline of four billion years. Cell Death Differ. 9:367-393. (Pubitemid 34822817)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.4 , pp. 367-393
    • Ameisen, J.C.1
  • 96
    • 63749094517 scopus 로고    scopus 로고
    • Bicaudal is a conserved substrate for Drosophila and mammalian caspases and is essential for cell survival
    • Creagh EM, Brumatti G, SheridanC, Duriez PJ, Taylor RC, et al. 2009. Bicaudal is a conserved substrate for Drosophila and mammalian caspases and is essential for cell survival. PLoS One 4:e5055.
    • (2009) PLoS One , vol.4
    • Creagh, E.M.1    Brumatti, G.2    Sheridanc Duriez, P.J.3    Taylor, R.C.4
  • 99
    • 68149132463 scopus 로고    scopus 로고
    • Cell death: What can we learn from flies? Editorial for the special review issue on Drosophila apoptosis
    • Mollereau B. 2009. Cell death: What can we learn from flies? Editorial for the special review issue on Drosophila apoptosis. Apoptosis 14:929-934.
    • (2009) Apoptosis , vol.14 , pp. 929-934
    • Mollereau, B.1
  • 101
    • 0034647504 scopus 로고    scopus 로고
    • Identification and developmental expression of inhibitor of caspase- activated DNase (ICAD) in Drosophila melanogaster
    • DOI 10.1074/jbc.M909611199
    • Mukae N, Yokoyama H, Yokokura T, Sakoyama Y, Sakahira H, Nagata S. 2000. Identification and developmental expression of inhibitor of caspase-activated DNase (ICAD) in Drosophila melanogaster. J. Biol. Chem. 275:21402-8. (Pubitemid 30481841)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21402-21408
    • Mukae, N.1    Yokoyama, H.2    Yokokura, T.3    Sakoyama, Y.4    Sakahira, H.5    Nagata, S.6
  • 102
    • 0034724949 scopus 로고    scopus 로고
    • A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster
    • DOI 10.1074/jbc.275.17.12978
    • Yokoyama H, Mukae N, Sakahira H, Okawa K, Iwamatsu A, Nagata S. 2000. A novel activation mechanism of caspase-activated DNase from Drosophila melanogaster. J. Biol. Chem. 275:12978-986. (Pubitemid 30241456)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.17 , pp. 12978-12986
    • Yokoyama, H.1    Mukae, N.2    Sakahira, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 103
    • 65649133944 scopus 로고    scopus 로고
    • Activation of sterol regulatory element-binding protein by the caspase Drice in Drosophila larvae
    • Amarneh B, Matthews KA, Rawson RB. 2009. Activation of sterol regulatory element-binding protein by the caspase Drice in Drosophila larvae. J. Biol. Chem. 284:9674-682.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9674-9682
    • Amarneh, B.1    Matthews, K.A.2    Rawson, R.B.3
  • 104
    • 0028978248 scopus 로고
    • Purification of an interleukin-1 beta converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains
    • Wang X, Pai JT, Wiedenfeld EA, Medina JC, Slaughter CA, et al. 1995. Purification of an interleukin-1 beta converting enzyme-related cysteine protease that cleaves sterol regulatory element-binding proteins between the leucine zipper and transmembrane domains. J. Biol. Chem. 270:18044-050.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18044-18050
    • Wang, X.1    Pai, J.T.2    Wiedenfeld, E.A.3    Medina, J.C.4    Slaughter, C.A.5
  • 105
    • 0035667902 scopus 로고    scopus 로고
    • Apoptosis-induced release of mature sterol regulatory element-binding proteins activates sterol-responsive genes
    • Higgins ME, Ioannou YA. 2001. Apoptosis-induced release ofmature sterol regulatory element-binding proteins activates sterol-responsive genes. J. Lipid. Res. 42:1939-946. (Pubitemid 34001042)
    • (2001) Journal of Lipid Research , vol.42 , Issue.12 , pp. 1939-1946
    • Higgins, M.E.1    Ioannou, Y.A.2
  • 106
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis HM, Horvitz HR. 1986. Genetic control of programmed cell death in the nematode C. elegans. Cell 44:817-829. (Pubitemid 16045328)
    • (1986) Cell , vol.44 , Issue.6 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 107
    • 38949170938 scopus 로고    scopus 로고
    • Analysis of the minimal specificity of CED-3 using a yeast transcriptional reporter system
    • DOI 10.1016/j.bbamcr.2007.10.003, PII S0167488907002376
    • Westein SJ, Scott FL, Hawkins CJ. 2008. Analysis of the minimal specificity of CED-3 using a yeast transcriptional reporter system. Biochim. Biophys. Acta 1783:448-454. (Pubitemid 351232061)
    • (2008) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1783 , Issue.3 , pp. 448-454
    • Westein, S.J.1    Scott, F.L.2    Hawkins, C.J.3
  • 108
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • Uren AG, O'Rourke K, Aravind LA, Pisabarro MT, Seshagiri S, et al. 2000. Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma. Mol. Cell 6:961-967.
    • (2000) Mol. Cell , vol.6 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5
  • 110
    • 77950517098 scopus 로고    scopus 로고
    • Death proteases: Alive and kicking
    • Woltering EJ. 2010. Death proteases: alive and kicking. Trends Plant. Sci. 15:185-188.
    • (2010) Trends Plant. Sci. , vol.15 , pp. 185-188
    • Woltering, E.J.1
  • 111
    • 33846285777 scopus 로고    scopus 로고
    • Caspases in yeast apoptosis-like death: Facts and artefacts
    • DOI 10.1111/j.1567-1364.2006.00137.x
    • V́achov́a L, Palkov́a Z. 2007. Caspases in yeast apoptosis-like death: facts and artefacts. FEMS Yeast Res. 7:12-21. (Pubitemid 46122026)
    • (2007) FEMS Yeast Research , vol.7 , Issue.1 , pp. 12-21
    • Vachova, L.1    Palkova, Z.2
  • 112
    • 14744275580 scopus 로고    scopus 로고
    • Many ways to exit? Cell death categories in plants
    • DOI 10.1016/j.tplants.2005.01.006
    • van Doorn WG, Woltering EJ. 2005. Many ways to exit? Cell death categories in plants. Trends Plant Sci. 10:117-122. (Pubitemid 40323295)
    • (2005) Trends in Plant Science , vol.10 , Issue.3 , pp. 117-122
    • Van Doorn, W.G.1    Woltering, E.J.2
  • 116
    • 70449529844 scopus 로고    scopus 로고
    • Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome
    • Sundstr̈om JF, Vaculova A, Smertenko AP, Savenkov EI, Golovko A, et al. 2009. Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome. Nat. Cell Biol. 11:1347-354.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1347-1354
    • Sundstr̈om Jf, V.1
  • 117
    • 46549090119 scopus 로고    scopus 로고
    • Caspase-dependent apoptosis in yeast
    • Mazzoni C, Falcone C. 2008. Caspase-dependent apoptosis in yeast. Biochim. Biophys. Acta 1783:1320-327.
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1320-1327
    • Mazzoni, C.1    Falcone, C.2
  • 118
    • 77955620283 scopus 로고    scopus 로고
    • Activation of specific apoptotic caspases with an engineered smallmolecule- activated protease
    • Gray DC, Mahrus S, Wells JA. 2010. Activation of specific apoptotic caspases with an engineered smallmolecule- activated protease. Cell 142:637-646.
    • (2010) Cell , vol.142 , pp. 637-646
    • Gray, D.C.1    Mahrus, S.2    Wells, J.A.3
  • 119
    • 41549132691 scopus 로고    scopus 로고
    • Quantitative Analysis of pathways controlling extrinsic apoptosis in single cells
    • DOI 10.1016/j.molcel.2008.02.012, PII S1097276508001317
    • Albeck JG, Burke JM, Aldridge BB, ZhangM, Lauffenburger DA, Sorger PK. 2008. Quantitative analysis of pathways controlling extrinsic apoptosis in single cells. Mol. Cell 30:11-25. (Pubitemid 351470145)
    • (2008) Molecular Cell , vol.30 , Issue.1 , pp. 11-25
    • Albeck, J.G.1    Burke, J.M.2    Aldridge, B.B.3    Zhang, M.4    Lauffenburger, D.A.5    Sorger, P.K.6
  • 120
    • 66249136447 scopus 로고    scopus 로고
    • Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis
    • Spencer SL, Gaudet S, Albeck JG, Burke JM, Sorger PK. 2009. Non-genetic origins of cell-to-cell variability in TRAIL-induced apoptosis. Nature 459:428-432.
    • (2009) Nature , vol.459 , pp. 428-432
    • Spencer, S.L.1    Gaudet, S.2    Albeck, J.G.3    Burke, J.M.4    Sorger, P.K.5
  • 121
    • 0032785022 scopus 로고    scopus 로고
    • The proteolytic procaspase activation network: An in vitro analysis
    • Van de CraenM, DeclercqW. 1999. The proteolytic procaspase activation network: an in vitro analysis. Cell Death Differ. 6:1117-124.
    • (1999) Cell Death Differ. , vol.6 , pp. 1117-1124
    • Van De Craen, M.1    Declercq, W.2
  • 122
    • 70549100903 scopus 로고    scopus 로고
    • Regulation of cell death by the ubiquitin-proteasome system
    • BaderM, Steller H. 2009. Regulation of cell death by the ubiquitin-proteasome system. Curr. Opin. Cell Biol. 21:878-884.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 878-884
    • Bader, M.1    Steller, H.2
  • 123
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: Why XIAP is the black sheep of the family
    • DOI 10.1038/sj.embor.7400795, PII 7400795
    • Eckelman BP, Salvesen GS, Scott FL. 2006. Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family. EMBO Rep. 7:988-994. (Pubitemid 44480512)
    • (2006) EMBO Reports , vol.7 , Issue.10 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 124
    • 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
    • DOI 10.1073/pnas.161506698
    • Suzuki Y, Nakabayashi Y, Takahashi R. 2001. 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 98:8662-667. (Pubitemid 32678084)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.15 , pp. 8662-8667
    • Suzuki, Y.1    Nakabayashi, Y.2    Takahashi, R.3
  • 126
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • Schile AJ, García-Ferńandez M, Steller H. 2008. Regulation of apoptosis by XIAP ubiquitin-ligase activity. Genes Dev. 22:2256-266.
    • (2008) Genes Dev. , vol.22 , pp. 2256-2266
    • Schile, A.J.1    García-Ferńandez, M.2    Steller, H.3
  • 127
    • 55949118522 scopus 로고    scopus 로고
    • Inactivation of effector caspases through nondegradative polyubiquitylation
    • Ditzel M, BroemerM, Tenev T, Bolduc C, Lee TV, et al. 2008. Inactivation of effector caspases through nondegradative polyubiquitylation. Mol. Cell 32:540-553.
    • (2008) Mol. Cell , vol.32 , pp. 540-553
    • Ditzel, M.1    Broemer, M.2    Tenev, T.3    Bolduc, C.4    Lee, T.V.5
  • 128
    • 0037654554 scopus 로고    scopus 로고
    • Caspase activity and a specific cytochrome C are required for sperm differentiation in Drosophila
    • DOI 10.1016/S1534-5807(03)00120-5, PII S1534580703001205
    • Arama E, Agapite J, Steller H. 2003. Caspase activity and a specific cytochrome c are required for sperm differentiation in Drosophila. Dev. Cell 4:687-697. (Pubitemid 36564899)
    • (2003) Developmental Cell , vol.4 , Issue.5 , pp. 687-697
    • Arama, E.1    Agapite, J.2    Steller, H.3
  • 130
    • 61449134122 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of apoptosis
    • Broemer M, Meier P. 2009. Ubiquitin-mediated regulation of apoptosis. Trends Cell Biol. 19:130-140.
    • (2009) Trends Cell Biol. , vol.19 , pp. 130-140
    • Broemer, M.1    Meier, P.2
  • 131
    • 0033215040 scopus 로고    scopus 로고
    • Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases
    • DOI 10.1093/emboj/18.19.5242
    • Deveraux QL, Leo E, Stennicke HR, Welsh K, Salvesen GS, Reed JC. 1999. Cleavage of human inhibitor of apoptosis protein XIAP results in fragments with distinct specificities for caspases. EMBO J. 18:5242-251. (Pubitemid 29465575)
    • (1999) EMBO Journal , vol.18 , Issue.19 , pp. 5242-5251
    • Deveraux, Q.L.1    Leo, E.2    Stennicke, H.R.3    Welsh, K.4    Salvesen, G.S.5    Reed, J.C.6
  • 132
    • 0035831533 scopus 로고    scopus 로고
    • C-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment
    • Clem RJ, Sheu TT, Richter BW, He WW, Thornberry NA, et al. 2001. c-IAP1 is cleaved by caspases to produce a proapoptotic C-terminal fragment. J. Biol. Chem. 276:7602-8.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7602-7608
    • Clem, R.J.1    Sheu, T.T.2    Richter, B.W.3    He, W.W.4    Thornberry, N.A.5
  • 133
    • 2942674780 scopus 로고    scopus 로고
    • Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase
    • DOI 10.1016/j.molcel.2004.05.018, PII S1097276504003041
    • Bartke T, Pohl C, Pyrowolakis G, Jentsch S. 2004. Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. Mol. Cell 14:801-811. (Pubitemid 38780853)
    • (2004) Molecular Cell , vol.14 , Issue.6 , pp. 801-811
    • Bartke, T.1    Pohl, C.2    Pyrowolakis, G.3    Jentsch, S.4
  • 134
    • 0037936841 scopus 로고    scopus 로고
    • Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis
    • DOI 10.1038/ncb984
    • Ditzel M, Wilson R, Tenev T, Zachariou A, Paul A, et al. 2003. Degradation of DIAP1 by the N-end rule pathway is essential for regulating apoptosis. Nat. Cell Biol. 5:467-473. (Pubitemid 36592271)
    • (2003) Nature Cell Biology , vol.5 , Issue.5 , pp. 467-473
    • Ditzel, M.1    Wilson, R.2    Tenev, T.3    Zachariou, A.4    Paul, A.5    Deas, E.6    Meier, P.7
  • 135
    • 33947384611 scopus 로고    scopus 로고
    • Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways
    • DOI 10.1038/sj.cdd.4402079, PII 4402079
    • Herman-BachinskyY, Ryoo H-D, Ciechanover A, GonenH. 2007. Regulation of the Drosophila ubiquitin ligase DIAP1 is mediated via several distinct ubiquitin system pathways. Cell Death Differ. 14:861-871. (Pubitemid 46444523)
    • (2007) Cell Death and Differentiation , vol.14 , Issue.4 , pp. 861-871
    • Herman-Bachinsky, Y.1    Ryoo, H.-D.2    Ciechanover, A.3    Gonen, H.4
  • 137
    • 70349329714 scopus 로고    scopus 로고
    • Smac mimetics as new cancer therapeutics
    • Chen DJ, Huerta S. 2009. Smac mimetics as new cancer therapeutics. Anti-Cancer Drugs 20:646-658.
    • (2009) Anti-Cancer Drugs , vol.20 , pp. 646-658
    • Chen, D.J.1    Huerta, S.2
  • 138
  • 139
    • 78049264771 scopus 로고    scopus 로고
    • The 26S proteasome: Assembly and function of a destructive machine
    • Gallastegui N, Groll M. 2010. The 26S proteasome: assembly and function of a destructive machine. Trends Biochem. Sci. 35:634-642.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 634-642
    • Gallastegui, N.1    Groll, M.2
  • 140
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Paradigm review of a selfcompartmentalizing protease
    • Baumeister W, Walz J, Z̈uhl F, Seem̈uller E. 1998. The proteasome: paradigm review of a selfcompartmentalizing protease. Cell 92:367-390.
    • (1998) Cell , vol.92 , pp. 367-390
    • Baumeister, W.1    Walz, J.2    Z̈uhl, F.3    Seem̈uller, E.4
  • 142
    • 1842472483 scopus 로고    scopus 로고
    • Caspase activation inhibits proteasome function during apoptosis
    • DOI 10.1016/S1097-2765(04)00156-X, PII S109727650400156X
    • Sun XM, Butterworth M, MacFarlane M, Dubiel W, Ciechanover A, Cohen GM. 2004. Caspase activation inhibits proteasome function during apoptosis. Mol. Cell 14:81-93. (Pubitemid 38469911)
    • (2004) Molecular Cell , vol.14 , Issue.1 , pp. 81-93
    • Sun, X.-M.1    Butterworth, M.2    MacFarlane, M.3    Dubiel, W.4    Ciechanover, A.5    Cohen, G.M.6
  • 143
    • 77954356573 scopus 로고    scopus 로고
    • Caspase-3 cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity
    • Wang XH, Zhang L, Mitch WE, LeDoux JM, Hu J, Du J. 2010. Caspase-3 cleaves specific 19 S proteasome subunits in skeletal muscle stimulating proteasome activity. J. Biol. Chem. 285:21249-257.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21249-21257
    • Wang, X.H.1    Zhang, L.2    Mitch, W.E.3    Ledoux, J.M.4    Hu, J.5    Du, J.6
  • 144
    • 4344598382 scopus 로고    scopus 로고
    • Caspase-dependent inactivation of proteasome function during programmed cell death in Drosophila and man
    • DOI 10.1074/jbc.M402638200
    • Adrain C, Creagh EM, Cullen SP, Martin SJ. 2004. Caspase-dependent inactivation of proteasome function during programmed cell death in Drosophila and man. J. Biol. Chem. 279:36923-930. (Pubitemid 39129042)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36923-36930
    • Adrain, C.1    Creagh, E.M.2    Cullen, S.P.3    Martin, S.J.4
  • 146
    • 20044386174 scopus 로고    scopus 로고
    • Shotgun proteome analysis of protein cleavage in apoptotic cells
    • DOI 10.1002/pmic.200401110
    • Thiede B, Treumann A, Kretschmer A, S̈ohlke J, Rudel T. 2005. Shotgun proteome analysis of protein cleavage in apoptotic cells. Proteomics 5:2123-130. (Pubitemid 40770576)
    • (2005) Proteomics , vol.5 , Issue.8 , pp. 2123-2130
    • Thiede, B.1    Treumann, A.2    Kretschmer, A.3    Sohlke, J.4    Rudel, T.5
  • 147
    • 0036122710 scopus 로고    scopus 로고
    • Yeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28γ as an effector caspase substrate
    • DOI 10.1038/sj.cdd.4400949
    • Araya R, Takahashi R, Nomura Y. 2002. Yeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28gamma as an effector caspase substrate. Cell Death Differ. 9:322-328. (Pubitemid 34223875)
    • (2002) Cell Death and Differentiation , vol.9 , Issue.3 , pp. 322-328
    • Araya, R.1    Takahashi, R.2    Nomura, Y.3
  • 148
    • 70450227260 scopus 로고    scopus 로고
    • Proteasome inhibitors in the treatment of multiple myeloma
    • Shah JJ, Orlowski RZ. 2009. Proteasome inhibitors in the treatment of multiple myeloma. Leukemia 23:1964-979.
    • (2009) Leukemia , vol.23 , pp. 1964-1979
    • Shah, J.J.1    Orlowski, R.Z.2
  • 149
    • 0034693878 scopus 로고    scopus 로고
    • Regulation of cell death by the Abl tyrosine kinase
    • Wang JY. 2000. Regulation of cell death by the Abl tyrosine kinase. Oncogene 19:5643-650.
    • (2000) Oncogene , vol.19 , pp. 5643-5650
    • Wang, J.Y.1
  • 150
    • 0029879676 scopus 로고    scopus 로고
    • The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products
    • Wen ST, Jackson PK, Van Etten RA. 1996. The cytostatic function of c-Abl is controlled by multiple nuclear localization signals and requires the p53 and Rb tumor suppressor gene products. EMBO J. 15:1583-595. (Pubitemid 26112380)
    • (1996) EMBO Journal , vol.15 , Issue.7 , pp. 1583-1595
    • Wen, S.-T.1    Jackson, P.K.2    Van Etten, R.A.3
  • 153
    • 1542269715 scopus 로고    scopus 로고
    • Requirement of caspase-mediated cleavage of c-Abl during stress-induced apoptosis
    • DOI 10.1038/sj.cdd.4401336
    • Machuy N, Rajalingam K, Rudel T. 2004. Requirement of caspase-mediated cleavage of c-Abl during stress-induced apoptosis. Cell Death Differ. 11:290-300. (Pubitemid 38313138)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.3 , pp. 290-300
    • Machuy, N.1    Rajalingam, K.2    Rudel, T.3
  • 154
    • 0030462563 scopus 로고    scopus 로고
    • Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis
    • J̈anicke RU, Walker PA, Lin XY, Porter AG. 1996. Specific cleavage of the retinoblastoma protein by an ICE-like protease in apoptosis. EMBO J. 15:6969-978. (Pubitemid 27023268)
    • (1996) EMBO Journal , vol.15 , Issue.24 , pp. 6969-6978
    • Janicke, R.U.1    Walker, P.A.2    Lin, X.Y.3    Porter, A.G.4
  • 155
    • 0035942496 scopus 로고    scopus 로고
    • Sequential two-step cleavage of the retinoblastoma protein by caspase-3/-7 during etoposide-induced apoptosis
    • DOI 10.1038/sj.onc.1204414
    • Fattman CL, Delach SM, Dou QP, Johnson DE. 2001. Sequential two-step cleavage of the retinoblastoma protein by caspase-3/-7 during etoposide-induced apoptosis. Oncogene 20:2918-926. (Pubitemid 33027759)
    • (2001) Oncogene , vol.20 , Issue.23 , pp. 2918-2926
    • Fattman, C.L.1    Delach, S.M.2    Dou, Q.P.3    Johnson, D.E.4
  • 156
    • 0032031417 scopus 로고    scopus 로고
    • The caspase-RB connection in cell death
    • DOI 10.1016/S0962-8924(97)01208-7
    • Tan X, Wang JY. 1998. The caspase-RB connection in cell death. Trends Cell Biol. 8:116-120. (Pubitemid 28077736)
    • (1998) Trends in Cell Biology , vol.8 , Issue.3 , pp. 116-120
    • Tan, X.1    Wang, J.Y.J.2
  • 158
    • 46049090743 scopus 로고    scopus 로고
    • Nuclear trafficking of pro-apoptotic kinases in response to DNA damage
    • Yoshida K. 2008. Nuclear trafficking of pro-apoptotic kinases in response to DNA damage. Trends Mol. Med. 14:305-313.
    • (2008) Trends Mol. Med. , vol.14 , pp. 305-313
    • Yoshida, K.1
  • 159
    • 70449700091 scopus 로고    scopus 로고
    • Controlling subcellular localization to alter function: Sending oncogenic Bcr-Abl to the nucleus causes apoptosis
    • Dixon AS, KakarM, Schneider KMH, Constance JE, Paullin BC, Lim CS. 2009. Controlling subcellular localization to alter function: Sending oncogenic Bcr-Abl to the nucleus causes apoptosis. J. Control. Release 140:245-249.
    • (2009) J. Control. Release , vol.140 , pp. 245-249
    • Dixon, A.S.1    Kakar, M.2    Schneider, K.M.H.3    Constance, J.E.4    Paullin, B.C.5    Lim, C.S.6
  • 160
    • 0035122485 scopus 로고    scopus 로고
    • Induction of apoptosis in chronic myelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase
    • DOI 10.1038/84683
    • Vigneri P, Wang JY. 2001. Induction of apoptosis in chronicmyelogenous leukemia cells through nuclear entrapment of BCR-ABL tyrosine kinase. Nat. Med. 7:228-234. (Pubitemid 32148491)
    • (2001) Nature Medicine , vol.7 , Issue.2 , pp. 228-234
    • Vigneri, P.1    Wang, J.Y.J.2
  • 161
    • 26244439708 scopus 로고    scopus 로고
    • Active relocation of chromatin and endoplasmic reticulum into blebs in late apoptotic cells
    • DOI 10.1242/jcs.02529
    • Lane JD, Allan VJ, Woodman PG. 2005. Active relocation of chromatin and endoplasmic reticulum into blebs in late apoptotic cells. J. Cell Sci. 118:4059-071. (Pubitemid 41410287)
    • (2005) Journal of Cell Science , vol.118 , Issue.17 , pp. 4059-4071
    • Lane, J.D.1    Allan, V.J.2    Woodman, P.G.3
  • 163
    • 24744456935 scopus 로고    scopus 로고
    • Nuclear substructure reorganization during late-stage erythropoiesis is selective and does not involve caspase cleavage of major nuclear substructural proteins
    • DOI 10.1182/blood-2005-04-1357
    • Krauss SW, Lo AJ, Short SA, Koury MJ, Mohandas N, Chasis JA. 2005. Nuclear substructure reorganization during late-stage erythropoiesis is selective and does not involve caspase cleavage ofmajor nuclear substructural proteins. Blood 106:2200-5. (Pubitemid 41291741)
    • (2005) Blood , vol.106 , Issue.6 , pp. 2200-2205
    • Krauss, S.W.1    Lo, A.J.2    Short, S.A.3    Koury, M.J.4    Mohandas, N.5    Chasis, J.A.6
  • 164
    • 0030465544 scopus 로고    scopus 로고
    • Lamin proteolysis facilitates nuclear events during apoptosis
    • DOI 10.1083/jcb.135.6.1441
    • Rao L, Perez D, White E. 1996. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol. 135:1441-455. (Pubitemid 26427643)
    • (1996) Journal of Cell Biology , vol.135 , Issue.6 , pp. 1441-1455
    • Rao, L.1    Perez, D.2    White, E.3
  • 165
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • DOI 10.1074/jbc.271.28.16443
    • Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM. 1996. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J. Biol. Chem. 271:16443-446. (Pubitemid 26238991)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.28 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 166
    • 0030683619 scopus 로고    scopus 로고
    • DrlCE is an essential caspase required for apoptotic activity in Drosophila cells
    • DOI 10.1093/emboj/16.20.6192
    • Fraser AG, McCarthy NJ, Evan GI. 1997. drICE is an essential caspase required for apoptotic activity in Drosophila cells. EMBO J. 16:6192-199. (Pubitemid 27458339)
    • (1997) EMBO Journal , vol.16 , Issue.20 , pp. 6192-6199
    • Fraser, A.G.1    McCarthy, N.J.2    Evan, G.I.3
  • 167
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee EA, Adrain C, Martin SJ. 2001. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 276:7320-326.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 168
    • 0037090614 scopus 로고    scopus 로고
    • Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation
    • DOI 10.1093/emboj/21.8.1967
    • Ruchaud S, Korfali N, Villa P, Kottke TJ, Dingwall C, et al. 2002. Caspase-6 gene disruption reveals a requirement for lamin A cleavage in apoptotic chromatin condensation. EMBO J. 21:1967-977. (Pubitemid 34437194)
    • (2002) EMBO Journal , vol.21 , Issue.8 , pp. 1967-1977
    • Ruchaud, S.1    Korfali, N.2    Villa, P.3    Kottke, T.J.4    Dingwall, C.5    Kaufmann, S.H.6    Earnshaw, W.C.7
  • 169
    • 67549118622 scopus 로고    scopus 로고
    • Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway
    • Inoue S, Browne G, Melino G, Cohen GM. 2009. Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway. Cell Death Differ. 16:1053-061.
    • (2009) Cell Death Differ. , vol.16 , pp. 1053-1061
    • Inoue, S.1    Browne, G.2    Melino, G.3    Cohen, G.M.4
  • 170
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: Controlled demolition at the cellular level
    • DOI 10.1038/nrm2312, PII NRM2312
    • Taylor RC, Cullen SP, Martin SJ. 2008. Apoptosis: controlled demolition at the cellular level. Nat. Rev. Mol. Cell Biol. 9:231-241. (Pubitemid 351301823)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.3 , pp. 231-241
    • Taylor, R.C.1    Cullen, S.P.2    Martin, S.J.3
  • 171
    • 84984100297 scopus 로고
    • Role of the reticular cells during maturation process of the erythroblast. 3. The fate of phagocytized nucleus
    • Seki M, Shirasawa H. 1965. Role of the reticular cells during maturation process of the erythroblast. 3. The fate of phagocytized nucleus. Acta Pathol. Jpn. 15:387-405.
    • (1965) Acta Pathol. Jpn. , vol.15 , pp. 387-405
    • Seki, M.1    Shirasawa, H.2
  • 172
    • 0025343574 scopus 로고
    • Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells
    • Koury MJ, Bondurant MC. 1990. Erythropoietin retards DNA breakdown and prevents programmed death in erythroid progenitor cells. Science 248:378-381.
    • (1990) Science , vol.248 , pp. 378-381
    • Koury, M.J.1    Bondurant, M.C.2
  • 173
    • 0030854080 scopus 로고    scopus 로고
    • The roles of Bcl-X(L) and apopain in the control of erythropoiesis by erythropoietin
    • Gregoli PA, Bondurant MC. 1997. The roles of Bcl-X(L) and apopain in the control of erythropoiesis by erythropoietin. Blood 90:630-640. (Pubitemid 27299103)
    • (1997) Blood , vol.90 , Issue.2 , pp. 630-640
    • Gregoli, P.A.1    Bondurant, M.C.2
  • 174
    • 0028800317 scopus 로고
    • Transcription factor GATA-1 permits survival and maturation of erythroid precursors by preventing apoptosis
    • Weiss MJ, Orkin SH. 1995. Transcription factor GATA-1 permits survival and maturation of erythroid precursors by preventing apoptosis. Proc. Natl. Acad. Sci. USA 92:9623-627.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9623-9627
    • Weiss, M.J.1    Orkin, S.H.2
  • 176
    • 60049084978 scopus 로고    scopus 로고
    • A non-apoptotic role for Fas/FasL in erythropoiesis
    • Carlile GW, Smith DH, WiedmannM. 2009. A non-apoptotic role for Fas/FasL in erythropoiesis. FEBS Lett. 583:848-854.
    • (2009) FEBS Lett. , vol.583 , pp. 848-854
    • Carlile, G.W.1    Smith, D.H.2    Wiedmann, M.3
  • 178
    • 70350347711 scopus 로고    scopus 로고
    • A non-apoptotic function of caspase-3 in pharmacologically-induced differentiation of K562 cells
    • Sztiller-Sikorska M, Jakubowska J, Wozniak M, Stasiak M, Czyz M. 2009. A non-apoptotic function of caspase-3 in pharmacologically-induced differentiation of K562 cells. Br. J. Pharmacol. 157:1451-462.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 1451-1462
    • Sztiller-Sikorska, M.1    Jakubowska, J.2    Wozniak, M.3    Stasiak, M.4    Czyz, M.5
  • 179
    • 2542475112 scopus 로고    scopus 로고
    • Caspase-3 has a nonapoptotic function in erythroid maturation
    • DOI 10.1182/blood-2003-09-3362
    • Carlile GW, Smith DH, Wiedmann M. 2004. Caspase-3 has a nonapoptotic function in erythroid maturation. Blood 103:4310-316. (Pubitemid 38685378)
    • (2004) Blood , vol.103 , Issue.11 , pp. 4310-4316
    • Carlile, G.W.1    Smith, D.H.2    Wiedmann, M.3
  • 180
    • 0033619265 scopus 로고    scopus 로고
    • Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1
    • De Maria R, Zeuner A, Eramo A, Domenichelli C, Bonci D, et al. 1999. Negative regulation of erythropoiesis by caspase-mediated cleavage of GATA-1. Nature 401:489-493.
    • (1999) Nature , vol.401 , pp. 489-493
    • De Maria, R.1    Zeuner, A.2    Eramo, A.3    Domenichelli, C.4    Bonci, D.5
  • 182
    • 62349088789 scopus 로고    scopus 로고
    • Apoptosis versus cell differentiation: Role of heat shock proteins HSP90, HSP70 and HSP27
    • Lanneau D, de Thonel A, Maurel S, Didelot C, Garrido C. 2007. Apoptosis versus cell differentiation: role of heat shock proteins HSP90, HSP70 and HSP27. Prion 1:53-60.
    • (2007) Prion , vol.1 , pp. 53-60
    • Lanneau, D.1    De Thonel, A.2    Maurel, S.3    Didelot, C.4    Garrido, C.5
  • 183
    • 64049118936 scopus 로고    scopus 로고
    • SCL and associated proteins distinguish active from repressive GATA transcription factor complexes
    • Tripic T, Deng W, Cheng Y, Zhang Y, Vakoc CR, et al. 2009. SCL and associated proteins distinguish active from repressive GATA transcription factor complexes. Blood 113:2191-201.
    • (2009) Blood , vol.113 , pp. 2191-2201
    • Tripic, T.1    Deng, W.2    Cheng, Y.3    Zhang, Y.4    Vakoc, C.R.5
  • 186
    • 77249169281 scopus 로고    scopus 로고
    • Turning enzymes on with small molecules
    • Zorn JA, Wells JA. 2010. Turning enzymes ON with small molecules. Nat. Chem. Biol. 6:179-188.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 179-188
    • Zorn, J.A.1    Wells, J.A.2
  • 187
    • 14644407525 scopus 로고    scopus 로고
    • The role of apoptosis in cancer development and treatment response
    • DOI 10.1038/nrc1570
    • Brown JM, Attardi LD. 2005. The role of apoptosis in cancer development and treatment response. Nat. Rev. Cancer 5:231-237. (Pubitemid 40314954)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.3 , pp. 231-237
    • Brown, J.M.1    Attardi, L.D.2
  • 189
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulín C, Salvesen GS, Oshima RG. 1997. Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. J. Cell Biol. 138:1379-394.
    • (1997) J. Cell Biol. , vol.138 , pp. 1379-1394
    • Caulín C, S.1
  • 191
    • 0346035003 scopus 로고    scopus 로고
    • Measurement of an apoptotic product in the sera of breast cancer patients
    • DOI 10.1016/S0959-8049(02)00865-1
    • Ueno T, Toi M, Biv́en K, Bando H, Ogawa T, Linder S. 2003. Measurement of an apoptotic product in the sera of breast cancer patients. Eur. J. Cancer 39:769-774. (Pubitemid 36315993)
    • (2003) European Journal of Cancer , vol.39 , Issue.6 , pp. 769-774
    • Ueno, T.1    Toi, M.2    Biven, K.3    Bando, H.4    Ogawa, T.5    Linder, S.6
  • 193
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-βprecursor protein and amyloidogenic Aβpeptide formation
    • Gervais FG, Xu D, Robertson GS, Vaillancourt JP, Zhu Y, et al. 1999. Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-βprecursor protein and amyloidogenic Aβpeptide formation. Cell 97:395-406.
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.G.1    Xu, D.2    Robertson, G.S.3    Vaillancourt, J.P.4    Zhu, Y.5
  • 194
    • 0036968953 scopus 로고    scopus 로고
    • Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain
    • DOI 10.1006/nbdi.2002.0549
    • Rohn TT, Rissman RA, Davis MC, Kim YE, Cotman CW, Head E. 2002. Caspase-9 activation and caspase cleavage of tau in the Alzheimer's disease brain. Neurobiol. Dis. 11:341-354. (Pubitemid 36135697)
    • (2002) Neurobiology of Disease , vol.11 , Issue.2 , pp. 341-354
    • Rohn, T.T.1    Rissman, R.A.2    Davis, M.C.3    Kim, Y.E.4    Cotman, C.W.5    Head, E.6
  • 195
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC. 2004. Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am. J. Pathol. 165:523-531. (Pubitemid 38971382)
    • (2004) American Journal of Pathology , vol.165 , Issue.2 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    LeBlanc, A.C.6
  • 197
    • 0031930313 scopus 로고    scopus 로고
    • Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease
    • Yang F, Sun X, BeechW, Teter B, WuS, et al. 1998. Antibody to caspase-cleaved actin detects apoptosis in differentiated neuroblastoma and plaque-associated neurons and microglia in Alzheimer's disease. Am. J. Pathol. 152:379-389. (Pubitemid 28106384)
    • (1998) American Journal of Pathology , vol.152 , Issue.2 , pp. 379-389
    • Yang, F.1    Sun, X.2    Beech, W.3    Teter, B.4    Wu, S.5    Sigel, J.6    Vinters, H.V.7    Frautschy, S.A.8    Cole, G.M.9
  • 198
  • 199
    • 72149118728 scopus 로고    scopus 로고
    • Alterations in cellular proteome and secretome upon differentiation from monocyte to macrophage by treatment with phorbol myristate acetate: Insights into biological processes
    • Sintiprungrat K, Singhto N, Sinchaikul S, Chen S-T, Thongboonkerd V. 2010. Alterations in cellular proteome and secretome upon differentiation from monocyte to macrophage by treatment with phorbol myristate acetate: insights into biological processes. J. Proteomics 73:602-618.
    • (2010) J. Proteomics , vol.73 , pp. 602-618
    • Sintiprungrat, K.1    Singhto, N.2    Sinchaikul, S.3    Chen, S.-T.4    Thongboonkerd, V.5
  • 200
    • 37549002511 scopus 로고    scopus 로고
    • The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock
    • Shao W, Yeretssian G, Doiron K, Hussain SN, Saleh M. 2007. The caspase-1 digestome identifies the glycolysis pathway as a target during infection and septic shock. J. Biol. Chem. 282:36321-29
    • (2007) J. Biol. Chem. , vol.282 , pp. 36321-29
    • Shao, W.1    Yeretssian, G.2    Doiron, K.3    Hussain, S.N.4    Saleh, M.5


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