메뉴 건너뛰기




Volumn 287, Issue 40, 2012, Pages 33781-33795

Fibrils colocalize caspase-3 with procaspase-3 to foster maturation

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL MECHANISMS; CASPASE-3; CELLULAR SIGNALING; COLOCALIZATION; COLOCALIZE; IN-VITRO; LIMITED PROTEOLYSIS; NANO-FIBRILS; SELF-ACTIVATION; SMALL MOLECULES; TRACE AMOUNTS;

EID: 84866931834     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.386128     Document Type: Article
Times cited : (43)

References (86)
  • 1
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases. Successes, failures, and future prospects
    • Turk, B. (2006) Targeting proteases. Successes, failures, and future prospects. Nat. Rev. Drug Discov. 5, 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 2
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan, A. R., and James, M. N. (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
  • 4
    • 77954600981 scopus 로고    scopus 로고
    • Allosteric regulation of protease activity by small molecules
    • Shen, A. (2010) Allosteric regulation of protease activity by small molecules. Mol. Biosyst. 6, 1431-1443
    • (2010) Mol. Biosyst. , vol.6 , pp. 1431-1443
    • Shen, A.1
  • 5
    • 0037058964 scopus 로고    scopus 로고
    • Structure and zymogen activation of caspases
    • DOI 10.1016/S0301-4622(02)00151-5, PII S0301462202001515
    • Donepudi, M., and Grütter, M. G. (2002) Structure and zymogen activation of caspases. Biophys. Chem. 101, 145-153 (Pubitemid 35462043)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 145-153
    • Donepudi, M.1    Grutter, M.G.2
  • 7
    • 77955620283 scopus 로고    scopus 로고
    • Activation of specific apoptotic caspases with an engineered small molecule-activated protease
    • Gray, D. C., Mahrus, S., and Wells, J. A. (2010) Activation of specific apoptotic caspases with an engineered small molecule-activated protease. Cell 142, 637-646
    • (2010) Cell , vol.142 , pp. 637-646
    • Gray, D.C.1    Mahrus, S.2    Wells, J.A.3
  • 9
    • 54249096028 scopus 로고    scopus 로고
    • Caspases in apoptosis and beyond
    • Li, J., and Yuan, J. (2008) Caspases in apoptosis and beyond. Oncogene 27, 6194-6206
    • (2008) Oncogene , vol.27 , pp. 6194-6206
    • Li, J.1    Yuan, J.2
  • 10
    • 80051519507 scopus 로고    scopus 로고
    • The Holo-apoptosome. Activation of procaspase-9 and interactions with caspase-3
    • Yuan, S., Yu, X., Asara, J. M., Heuser, J. E., Ludtke, S. J., and Akey, C. W. (2011) The Holo-apoptosome. Activation of procaspase-9 and interactions with caspase-3. Structure 19, 1084-1096
    • (2011) Structure , vol.19 , pp. 1084-1096
    • Yuan, S.1    Yu, X.2    Asara, J.M.3    Heuser, J.E.4    Ludtke, S.J.5    Akey, C.W.6
  • 12
    • 0037291890 scopus 로고    scopus 로고
    • Insights into the regulatory mechanism for caspase-8 activation
    • DOI 10.1016/S1097-2765(03)00059-5
    • Donepudi, M., Mac Sweeney, A., Briand, C., and Grütter, M. G. (2003) Insights into the regulatory mechanism for caspase-8 activation. Mol. Cell 11, 543-549 (Pubitemid 36297058)
    • (2003) Molecular Cell , vol.11 , Issue.2 , pp. 543-549
    • Donepudi, M.1    Sweeney, A.M.2    Briand, C.3    Grutter, M.G.4
  • 13
    • 0031615875 scopus 로고    scopus 로고
    • Autoproteolytic activation of pro-caspases by oligomerization
    • Yang, X., Chang, H. Y., and Baltimore, D. (1998) Autoproteolytic activation of pro-caspases by oligomerization. Mol. Cell 1, 319-325 (Pubitemid 128378672)
    • (1998) Molecular Cell , vol.1 , Issue.2 , pp. 319-325
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 14
    • 33645237577 scopus 로고    scopus 로고
    • Caspase-7 is directly activated by the ∼700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 ∼200-kDa complex
    • DOI 10.1074/jbc.M507393200
    • Twiddy, D., Cohen, G. M., Macfarlane, M., and Cain, K. (2006) Caspase-7 is directly activated by the approximately 700-kDa apoptosome complex and is released as a stable XIAP-caspase-7 approximately 200-kDa complex. J. Biol. Chem. 281, 3876-3888 (Pubitemid 43847811)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.7 , pp. 3876-3888
    • Twiddy, D.1    Cohen, G.M.2    MacFarlane, M.3    Cain, K.4
  • 15
    • 33646068739 scopus 로고    scopus 로고
    • Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine
    • Yin, Q., Park, H. H., Chung, J. Y., Lin, S. C., Lo, Y. C., da Graca, L. S., Jiang, X., and Wu, H. (2006) Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Mol. Cell 22, 259-268
    • (2006) Mol. Cell , vol.22 , pp. 259-268
    • Yin, Q.1    Park, H.H.2    Chung, J.Y.3    Lin, S.C.4    Lo, Y.C.5    Da Graca, L.S.6    Jiang, X.7    Wu, H.8
  • 16
    • 0031018914 scopus 로고    scopus 로고
    • FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens
    • DOI 10.1074/jbc.272.5.2952
    • Muzio, M., Salvesen, G. S., and Dixit, V. M. (1997) FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J. Biol. Chem. 272, 2952-2956 (Pubitemid 27053346)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.5 , pp. 2952-2956
    • Muzio, M.1    Salvesen, G.S.2    Dixit, V.M.3
  • 17
    • 52649141086 scopus 로고    scopus 로고
    • Global sequencing of proteolytic cleavage sites in apoptosis by specific labeling of protein N termini
    • Mahrus, S., Trinidad, J. C., Barkan, D. T., Sali, A., Burlingame, A. L., and Wells, J. A. (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
  • 18
    • 49549113643 scopus 로고    scopus 로고
    • Global mapping of the topography and magnitude of proteolytic events in apoptosis
    • Dix, M. M., Simon, G. M., and Cravatt, B. F. (2008) Global mapping of the topography and magnitude 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
  • 19
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: A searchable database of caspase substrates
    • DOI 10.1038/sj.cdd.4402103, PII 4402103
    • Lüthi, A. U., and Martin, S. J. (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
  • 21
    • 80052307868 scopus 로고    scopus 로고
    • A bifunctional allosteric site in the dimer interface of procaspase-3
    • Schipper, J. L., MacKenzie, S. H., Sharma, A., and Clark, A. C. (2011) A bifunctional allosteric site in the dimer interface of procaspase-3. Biophys. Chem. 159, 100-109
    • (2011) Biophys. Chem. , vol.159 , pp. 100-109
    • Schipper, J.L.1    MacKenzie, S.H.2    Sharma, A.3    Clark, A.C.4
  • 22
    • 70449372265 scopus 로고    scopus 로고
    • Small molecule activators of a proenzyme
    • Wolan, D. W., Zorn, J. A., Gray, D. C., and Wells, J. A. (2009) Small molecule activators of a proenzyme. Science 326, 853-858
    • (2009) Science , vol.326 , pp. 853-858
    • Wolan, D.W.1    Zorn, J.A.2    Gray, D.C.3    Wells, J.A.4
  • 23
    • 83055197029 scopus 로고    scopus 로고
    • Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation
    • Zorn, J. A., Wille, H., Wolan, D. W., and Wells, J. A. (2011) Self-assembling small molecules form nanofibrils that bind procaspase-3 to promote activation. J. Am. Chem. Soc. 133, 19630-19633
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 19630-19633
    • Zorn, J.A.1    Wille, H.2    Wolan, D.W.3    Wells, J.A.4
  • 24
    • 60549089207 scopus 로고    scopus 로고
    • APP binds DR6 to trigger axon pruning and neuron death via distinct caspases
    • Nikolaev, A., McLaughlin, T., O'Leary, D. D., and Tessier-Lavigne, M. (2009) APP binds DR6 to trigger axon pruning and neuron death via distinct caspases. Nature 457, 981-989
    • (2009) Nature , vol.457 , pp. 981-989
    • Nikolaev, A.1    McLaughlin, T.2    O'Leary, D.D.3    Tessier-Lavigne, M.4
  • 27
    • 0033953015 scopus 로고    scopus 로고
    • Caspases and neurodegeneration: On the cutting edge of new therapeutic approaches
    • DOI 10.1034/j.1399-0004.2000.570101.x
    • Wellington, C. L., and Hayden, M. R. (2000) Caspases and neurodegeneration. On the cutting edge of new therapeutic approaches. Clin. Genet. 57, 1-10 (Pubitemid 30105555)
    • (2000) Clinical Genetics , vol.57 , Issue.1 , pp. 1-10
    • Wellington, C.L.1    Hayden, M.R.2
  • 28
    • 79955601720 scopus 로고    scopus 로고
    • Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo
    • Umeda, T., Tomiyama, T., Sakama, N., Tanaka, S., Lambert, M. P., Klein, W. L., and Mori, H. (2011) Intraneuronal amyloid β oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J. Neurosci. Res. 89, 1031-1042
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1031-1042
    • Umeda, T.1    Tomiyama, T.2    Sakama, N.3    Tanaka, S.4    Lambert, M.P.5    Klein, W.L.6    Mori, H.7
  • 29
    • 77249133010 scopus 로고    scopus 로고
    • Prion-like mechanisms in neurodegenerative diseases
    • Frost, B., and Diamond, M. I. (2010) Prion-like mechanisms in neurodegenerative diseases. Nat. Rev. Neurosci. 11, 155-159
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 155-159
    • Frost, B.1    Diamond, M.I.2
  • 32
    • 1542289716 scopus 로고    scopus 로고
    • Intermediate Filaments Control the Intracellular Distribution of Caspases during Apoptosis
    • Dinsdale, D., Lee, J. C., Dewson, G., Cohen, G. M., and Peter, M. E. (2004) Intermediate filaments control the intracellular distribution of caspases during apoptosis. Am. J. Pathol. 164, 395-407 (Pubitemid 38364656)
    • (2004) American Journal of Pathology , vol.164 , Issue.2 , pp. 395-407
    • Dinsdale, D.1    Lee, J.C.2    Dewson, G.3    Cohen, G.M.4    Peter, M.E.5
  • 35
    • 0032500552 scopus 로고    scopus 로고
    • Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain
    • DOI 10.1074/jbc.273.41.26566
    • Colussi, P. A., Harvey, N. L., Shearwin-Whyatt, L. M., and Kumar, S. (1998) Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 prodomain. J. Biol. Chem. 273, 26566-26570 (Pubitemid 28471667)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26566-26570
    • Colussi, P.A.1    Harvey, N.L.2    Shearwin-Whyatt, L.M.3    Kumar, S.4
  • 36
    • 45549088468 scopus 로고    scopus 로고
    • Expression, purification, and characterization of caspases
    • Chapter 21, Unit 21.13
    • Denault, J. B., and Salvesen, G. S. (2003) Expression, purification, and characterization of caspases. Curr. Protoc. Protein Sci. Chapter 21, Unit 21.13
    • (2003) Curr. Protoc. Protein Sci.
    • Denault, J.B.1    Salvesen, G.S.2
  • 37
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • DOI 10.1074/jbc.272.41.25719
    • Stennicke, H. R., and Salvesen, G. S. (1997) Biochemical characteristics of caspases-3, -6, -7, and -8. J. Biol. Chem. 272, 25719-25723 (Pubitemid 27438890)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 39
    • 0032762563 scopus 로고    scopus 로고
    • Catalytic properties of the caspases
    • Stennicke, H. R., and Salvesen, G. S. (1999) Catalytic properties of the caspases. Cell Death Differ. 6, 1054-1059
    • (1999) Cell Death Differ. , vol.6 , pp. 1054-1059
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 40
    • 33646024628 scopus 로고    scopus 로고
    • The apoptosome activates caspase-9 by dimerization
    • Pop, C., Timmer, J., Sperandio, S., and Salvesen, G. S. (2006) The apoptosome activates caspase-9 by dimerization. Mol. Cell 22, 269-275
    • (2006) Mol. Cell , vol.22 , pp. 269-275
    • Pop, C.1    Timmer, J.2    Sperandio, S.3    Salvesen, G.S.4
  • 41
    • 0029002823 scopus 로고
    • Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β-converting enzyme (ICE)
    • Graybill, T. L., Dolle, R. E., Helaszek, C. T., Ator, M. A., and Strasters, J. (1995) Synthesis and evaluation of diacylhydrazines as inhibitors of the interleukin-1β-converting enzyme (ICE). Bioorg. Med. Chem. Lett. 5, 1197-1202
    • (1995) Bioorg. Med. Chem. Lett. , vol.5 , pp. 1197-1202
    • Graybill, T.L.1    Dolle, R.E.2    Helaszek, C.T.3    Ator, M.A.4    Strasters, J.5
  • 42
    • 47749106894 scopus 로고    scopus 로고
    • Stoichiometry and physical chemistry of promiscuous aggregate-based inhibitors
    • DOI 10.1021/ja802977h
    • Coan, K. E., and Shoichet, B. K. (2008) Stoichiometry and physical chemistry of promiscuous aggregate-based inhibitors. J. Am. Chem. Soc. 130, 9606-9612 (Pubitemid 352031174)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.29 , pp. 9606-9612
    • Coan, K.E.D.1    Shoichet, B.K.2
  • 43
    • 18744391410 scopus 로고    scopus 로고
    • Pulse proteolysis: A simple method for quantitative determination of protein stability and ligand binding
    • DOI 10.1038/nmeth740
    • Park, C., and Marqusee, S. (2005) Pulse proteolysis. A simple method for quantitative determination of protein stability and ligand binding. Nat. Methods 2, 207-212 (Pubitemid 41122128)
    • (2005) Nature Methods , vol.2 , Issue.3 , pp. 207-212
    • Park, C.1    Marqusee, S.2
  • 45
    • 50349089817 scopus 로고    scopus 로고
    • Caspase assays. Identifying caspase activity and substrates in vitro and in vivo
    • Pop, C., Salvesen, G. S., and Scott, F. L. (2008) Caspase assays. Identifying caspase activity and substrates in vitro and in vivo. Methods Enzymol. 446, 351-367
    • (2008) Methods Enzymol. , vol.446 , pp. 351-367
    • Pop, C.1    Salvesen, G.S.2    Scott, F.L.3
  • 46
    • 33750968798 scopus 로고    scopus 로고
    • Inhibition of β-amyloid fibrillization by directed evolution of a β-sheet presenting miniature protein
    • DOI 10.1021/ja065557e
    • Smith, T. J., Stains, C. I., Meyer, S. C., and Ghosh, I. (2006) Inhibition of β-amyloid fibrillization by directed evolution of a β-sheet presenting miniature protein. J. Am. Chem. Soc. 128, 14456-14457 (Pubitemid 44749835)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.45 , pp. 14456-14457
    • Smith, T.J.1    Stains, C.I.2    Meyer, S.C.3    Ghosh, I.4
  • 47
    • 0034830096 scopus 로고    scopus 로고
    • Kinetic analysis of a simplified scheme of autocatalytic zymogen activation
    • DOI 10.1046/j.1432-1327.2001.01914.x
    • Wu, J. W., Wu, Y., and Wang, Z. X. (2001) Kinetic analysis of a simplified scheme of autocatalytic zymogen activation. Eur. J. Biochem. 268, 1547-1553 (Pubitemid 32862686)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.6 , pp. 1547-1553
    • Wu, J.-W.1    Wu, Y.2    Wang, Z.-X.3
  • 48
    • 0015917607 scopus 로고
    • Zymogens of proteolytic enzymes
    • Kassell, B., and Kay, J. (1973) Zymogens of proteolytic enzymes. Science 180, 1022-1027
    • (1973) Science , vol.180 , pp. 1022-1027
    • Kassell, B.1    Kay, J.2
  • 49
    • 48849103642 scopus 로고    scopus 로고
    • Quantitative determination of protein stability and ligand binding by pulse proteolysis
    • Chapter 20, Unit 20.11
    • Park, C., and Marqusee, S. (2006) Quantitative determination of protein stability and ligand binding by pulse proteolysis. Curr. Protoc. Protein Sci. Chapter 20, Unit 20.11
    • (2006) Curr. Protoc. Protein Sci.
    • Park, C.1    Marqusee, S.2
  • 50
    • 0035960678 scopus 로고    scopus 로고
    • Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer
    • DOI 10.1021/bi011037e
    • Pop, C., Chen, Y. R., Smith, B., Bose, K., Bobay, B., Tripathy, A., Franzen, S., and Clark, A. C. (2001) Removal of the prodomain does not affect the conformation of the procaspase-3 dimer. Biochemistry 40, 14224-14235 (Pubitemid 33081626)
    • (2001) Biochemistry , vol.40 , Issue.47 , pp. 14224-14235
    • Pop, C.1    Chen, Y.-R.2    Smith, B.3    Bose, K.4    Bobay, B.5    Tripathy, A.6    Franzen, S.7    Clark, A.C.8
  • 52
    • 0142063420 scopus 로고    scopus 로고
    • Mutations in the Procaspase-3 Dimer Interface Affect the Activity of the Zymogen
    • DOI 10.1021/bi034999p
    • Pop, C., Feeney, B., Tripathy, A., and Clark, A. C. (2003) Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. Biochemistry 42, 12311-12320 (Pubitemid 37296507)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12311-12320
    • Pop, C.1    Feeney, B.2    Tripathy, A.3    Clark, A.C.4
  • 53
    • 33745260957 scopus 로고    scopus 로고
    • Extended Substrate Recognition in Caspase-3 Revealed by High Resolution X-ray Structure Analysis
    • DOI 10.1016/j.jmb.2006.04.051, PII S0022283606005304
    • Ganesan, R., Mittl, P. R., Jelakovic, S., and Grütter, M. G. (2006) Extended substrate recognition in caspase-3 revealed by high resolution x-ray structure analysis. J. Mol. Biol. 359, 1378-1388 (Pubitemid 43922445)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.5 , pp. 1378-1388
    • Ganesan, R.1    Mittl, P.R.E.2    Jelakovic, S.3    Grutter, M.G.4
  • 54
  • 55
    • 0030970351 scopus 로고    scopus 로고
    • Activation of pro-caspase-7 by serine proteases includes a non-canonical specificity
    • Zhou, Q., and Salvesen, G. S. (1997) Activation of procaspase-7 by serine proteases includes a noncanonical specificity. Biochem. J. 324, 361-364 (Pubitemid 27267975)
    • (1997) Biochemical Journal , vol.324 , Issue.2 , pp. 361-364
    • Zhou, Q.1    Salvesen, G.S.2
  • 56
    • 33747011616 scopus 로고    scopus 로고
    • Engineered Hybrid Dimers: Tracking the Activation Pathway of Caspase-7
    • DOI 10.1016/j.molcel.2006.06.020, PII S1097276506004448
    • Denault, J. B., Békés, M., Scott, F. L., Sexton, K. M., Bogyo, M., and Salvesen, G. S. (2006) Engineered hybrid dimers. Tracking the activation pathway of caspase-7. Mol. Cell 23, 523-533 (Pubitemid 44205487)
    • (2006) Molecular Cell , vol.23 , Issue.4 , pp. 523-533
    • Denault, J.-B.1    Bekes, M.2    Scott, F.L.3    Sexton, K.M.B.4    Bogyo, M.5    Salvesen, G.S.6
  • 57
    • 33746972404 scopus 로고    scopus 로고
    • Identification of Early Intermediates of Caspase Activation Using Selective Inhibitors and Activity-Based Probes
    • DOI 10.1016/j.molcel.2006.06.021, PII S1097276506004357
    • Berger, A. B., Witte, M. D., Denault, J. B., Sadaghiani, A. M., Sexton, K. M., Salvesen, G. S., and Bogyo, M. (2006) Identification of early intermediates of caspase activation using selective inhibitors and activity-based probes. Mol. Cell 23, 509-521 (Pubitemid 44205485)
    • (2006) Molecular Cell , vol.23 , Issue.4 , pp. 509-521
    • Berger, A.B.1    Witte, M.D.2    Denault, J.-B.3    Sadaghiani, A.M.4    Sexton, K.M.B.5    Salvesen, G.S.6    Bogyo, M.7
  • 58
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation. The induced-proximity model
    • Salvesen, G. S., and Dixit, V. M. (1999) Caspase activation. The induced-proximity model. Proc. Natl. Acad. Sci. U.S.A. 96, 10964-10967
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 59
    • 84860389674 scopus 로고    scopus 로고
    • Amyloid-β forms fibrils by nucleated conformational conversion of oligomers
    • Lee, J., Culyba, E. K., Powers, E. T., and Kelly, J. W. (2011) Amyloid-β forms fibrils by nucleated conformational conversion of oligomers. Nat. Chem. Biol. 7, 602-609
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 602-609
    • Lee, J.1    Culyba, E.K.2    Powers, E.T.3    Kelly, J.W.4
  • 60
    • 84934439037 scopus 로고    scopus 로고
    • Preparing synthetic Aβ in different aggregation states
    • Stine, W. B., Jungbauer, L., Yu, C., and LaDu, M. J. (2011) Preparing synthetic Aβ in different aggregation states. Methods Mol. Biol. 670, 13-32
    • (2011) Methods Mol. Biol. , vol.670 , pp. 13-32
    • Stine, W.B.1    Jungbauer, L.2    Yu, C.3    LaDu, M.J.4
  • 61
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K., and Tschopp, J. (2010) The inflammasomes. Cell 140, 821-832
    • (2010) Cell , vol.140 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 62
    • 0032085941 scopus 로고    scopus 로고
    • Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization
    • Srinivasula, S. M., Ahmad, M., Fernandes-Alnemri, T., and Alnemri, E. S. (1998) Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization. Mol. Cell 1, 949-957 (Pubitemid 128379256)
    • (1998) Molecular Cell , vol.1 , Issue.7 , pp. 949-957
    • Srinivasula, S.M.1    Ahmad, M.2    Fernandes-Alnemri, T.3    Alnemri, E.S.4
  • 63
    • 84862281453 scopus 로고    scopus 로고
    • Caspase-8 isoform 6 promotes death effector filament formation independent of microtubules
    • Yuan, R. T., Young, S., Liang, J., Schmid, M. C., Mielgo, A., and Stupack, D. G. (2012) Caspase-8 isoform 6 promotes death effector filament formation independent of microtubules. Apoptosis 17, 229-235
    • (2012) Apoptosis , vol.17 , pp. 229-235
    • Yuan, R.T.1    Young, S.2    Liang, J.3    Schmid, M.C.4    Mielgo, A.5    Stupack, D.G.6
  • 64
    • 0032101371 scopus 로고    scopus 로고
    • Death-effector filaments: Novel cytoplasmic structures that recruit caspases and trigger apoptosis
    • DOI 10.1083/jcb.141.5.1243
    • Siegel, R. M., Martin, D. A., Zheng, L., Ng, S. Y., Bertin, J., Cohen, J., and Lenardo, M. J. (1998) Death-effector filaments. Novel cytoplasmic structures that recruit caspases and trigger apoptosis. J. Cell Biol. 141, 1243-1253 (Pubitemid 28265617)
    • (1998) Journal of Cell Biology , vol.141 , Issue.5 , pp. 1243-1253
    • Siegel, R.M.1    Martin, D.A.2    Zheng, L.3    Ng, S.Y.4    Bertin, J.5    Cohen, J.6    Lenardo, M.J.7
  • 67
    • 0028928084 scopus 로고
    • In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid β-peptide analogues
    • Kingston, I. B., Castro, M. J., and Anderson, S. (1995) In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid β-peptide analogues. Nat. Med. 1, 138-142
    • (1995) Nat. Med. , vol.1 , pp. 138-142
    • Kingston, I.B.1    Castro, M.J.2    Anderson, S.3
  • 68
    • 0029800327 scopus 로고    scopus 로고
    • Converting tissue-type plasminogen activator into a zymogen
    • DOI 10.1074/jbc.271.46.28749
    • Tachias, K., and Madison, E. L. (1996) Converting tissue-type plasminogen activator into a zymogen. J. Biol. Chem. 271, 28749-28752 (Pubitemid 26382568)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 28749-28752
    • Tachias, K.1    Madison, E.L.2
  • 69
    • 0024532410 scopus 로고
    • The single-chain form of tissue-type plasminogen activator has catalytic activity: Studies with a mutant enzyme that lacks the cleavage site
    • DOI 10.1021/bi00428a033
    • Boose, J. A., Kuismanen, E., Gerard, R., Sambrook, J., and Gething, M. J. (1989) The single-chain form of tissue-type plasminogen activator has catalytic activity. Studies with a mutant enzyme that lacks the cleavage site. Biochemistry 28, 635-643 (Pubitemid 19047101)
    • (1989) Biochemistry , vol.28 , Issue.2 , pp. 635-643
    • Boose, J.A.1    Kuismanen, E.2    Gerard, R.3    Sambrook, J.4    Gething, M.-J.5
  • 70
    • 0023101988 scopus 로고
    • Functional role of proteolytic cleavage at arginine-275 of human tissue plasminogen activator as assessed by site-directed mutagenesis
    • DOI 10.1021/bi00376a002
    • Tate, K. M., Higgins, D. L., Holmes, W. E., Winkler, M. E., Heyneker, H. L., and Vehar, G. A. (1987) Functional role of proteolytic cleavage at arginine 275 of human tissue plasminogen activator as assessed by site-directed mutagenesis. Biochemistry 26, 338-343 (Pubitemid 17022102)
    • (1987) Biochemistry , vol.26 , Issue.2 , pp. 338-343
    • Tate, K.M.1    Higgins, D.L.2    Holmes, W.E.3
  • 71
    • 0027496219 scopus 로고
    • Converting tissue plasminogen activator to a zymogen: A regulatory triad of Asp-His-Ser
    • Madison, E. L., Kobe, A., Gething, M. J., Sambrook, J. F., and Goldsmith, E. J. (1993) Converting tissue plasminogen activator to a zymogen. A regulatory triad of Asp-His-Ser. Science 262, 419-421 (Pubitemid 23353383)
    • (1993) Science , vol.262 , Issue.5132 , pp. 419-421
    • Madison, E.L.1    Kobe, A.2    Gething, M.-J.3    Sambrook, J.F.4    Goldsmith, E.J.5
  • 72
    • 0027520151 scopus 로고
    • Probing structure-function relationships of tissue-type plasminogen activator by oligonucleotide-mediated site-specific mutagenesis
    • Madison, E. L., and Sambrook, J. E. (1993) Probing structure-function relationships of tissue-type plasminogen activator by oligonucleotide-mediated site-specific mutagenesis. Methods Enzymol. 223, 249-271
    • (1993) Methods Enzymol. , vol.223 , pp. 249-271
    • Madison, E.L.1    Sambrook, J.E.2
  • 73
    • 0015939420 scopus 로고
    • The relation of the -amino group of trypsin to enzyme function and zymogen activation
    • Robinson, N. C., Neurath, H., and Walsh, K. A. (1973) The relation of the -amino group of trypsin to enzyme function and zymogen activation. Biochemistry 12, 420-426
    • (1973) Biochemistry , vol.12 , pp. 420-426
    • Robinson, N.C.1    Neurath, H.2    Walsh, K.A.3
  • 74
    • 0016390558 scopus 로고
    • Catalysis by chymotrypsinogen. Demonstration of an acyl-zymogen intermediate
    • Gertler, A., Walsh, K. A., and Neurath, H. (1974) Catalysis by chymotrypsinogen. Demonstration of an acyl-zymogen intermediate. Biochemistry 13, 1302-1310
    • (1974) Biochemistry , vol.13 , pp. 1302-1310
    • Gertler, A.1    Walsh, K.A.2    Neurath, H.3
  • 75
    • 0019952023 scopus 로고
    • Enzymatic activities of activated and zymogen forms of human Hageman factor (factor XII)
    • Silverberg, M., and Kaplan, A. P. (1982) Enzymatic activities of activated and zymogen forms of human Hageman factor (factor XII). Blood 60, 64-70 (Pubitemid 12085921)
    • (1982) Blood , vol.60 , Issue.1 , pp. 64-70
    • Silverberg, M.1    Kaplan, A.P.2
  • 76
    • 0005292810 scopus 로고
    • Role of proteolytic enzymes in biological regulation (a review)
    • Neurath, H., and Walsh, K. A. (1976) Role of proteolytic enzymes in biological regulation (a review). Proc. Natl. Acad. Sci. U.S.A. 73, 3825-3832
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 3825-3832
    • Neurath, H.1    Walsh, K.A.2
  • 77
    • 0017860586 scopus 로고
    • Probes of the mechanism of zymogen catalysis
    • Lonsdale-Eccles, J. D., Neurath, H., and Walsh, K. A. (1978) Probes of the mechanism of zymogen catalysis. Biochemistry 17, 2805-2809 (Pubitemid 8385281)
    • (1978) Biochemistry , vol.17 , Issue.14 , pp. 2805-2809
    • Lonsdale-Eccles, J.D.1    Neurath, H.2    Walsh, K.A.3
  • 78
    • 0015150785 scopus 로고
    • The autoactivation of trypsinogen
    • Kay, J., and Kassell, B. (1971) The autoactivation of trypsinogen. J. Biol. Chem. 246, 6661-6665
    • (1971) J. Biol. Chem. , vol.246 , pp. 6661-6665
    • Kay, J.1    Kassell, B.2
  • 80
    • 53749083462 scopus 로고    scopus 로고
    • Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain
    • Lupardus, P. J., Shen, A., Bogyo, M., and Garcia, K. C. (2008) Small molecule-induced allosteric activation of the Vibrio cholerae RTX cysteine protease domain. Science 322, 265-268
    • (2008) Science , vol.322 , pp. 265-268
    • Lupardus, P.J.1    Shen, A.2    Bogyo, M.3    Garcia, K.C.4
  • 84
    • 0034710984 scopus 로고    scopus 로고
    • Intracellular antibody caspase-mediated cell killing. An approach for application in cancer therapy
    • Tse, E., and Rabbitts, T. H. (2000) Intracellular antibody caspase-mediated cell killing. An approach for application in cancer therapy. Proc. Natl. Acad. Sci. U.S.A. 97, 12266-12271
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12266-12271
    • Tse, E.1    Rabbitts, T.H.2
  • 85
    • 77952784381 scopus 로고    scopus 로고
    • Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation
    • Oberst, A., Pop, C., Tremblay, A. G., Blais, V., Denault, J. B., Salvesen, G. S., and Green, D. R.(2010) Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation. J. Biol. Chem. 285, 16632-16642
    • (2010) J. Biol. Chem. , vol.285 , pp. 16632-16642
    • Oberst, A.1    Pop, C.2    Tremblay, A.G.3    Blais, V.4    Denault, J.B.5    Salvesen, G.S.6    Green, D.R.7
  • 86
    • 0042466637 scopus 로고    scopus 로고
    • Interdimer processing mechanism of procaspase-8 activation
    • DOI 10.1093/emboj/cdg414
    • Chang, D. W., Xing, Z., Capacio, V. L., Peter, M. E., and Yang, X. (2003) Interdimer processing mechanism of procaspase-8 activation. EMBO J. 22, 4132-4142 (Pubitemid 37021742)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4132-4142
    • Chang, D.W.1    Xing, Z.2    Capacio, V.L.3    Peter, M.E.4    Yang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.