메뉴 건너뛰기




Volumn 159, Issue 1, 2011, Pages 100-109

A bifunctional allosteric site in the dimer interface of procaspase-3

Author keywords

Allosteric activator; Apoptosis; Cancer therapy; Caspase; Drug design

Indexed keywords

ENZYME PRECURSOR; PROCASPASE 3;

EID: 80052307868     PISSN: 03014622     EISSN: 18734200     Source Type: Journal    
DOI: 10.1016/j.bpc.2011.05.013     Document Type: Article
Times cited : (24)

References (50)
  • 1
    • 0035938924 scopus 로고    scopus 로고
    • What is apoptosis, and why is it important?
    • A.G. Renehan, C. Booth, and C.S. Potten What is apoptosis, and why is it important? British Medical Journal 322 2001 1536 1538 (Pubitemid 32588353)
    • (2001) British Medical Journal , vol.322 , Issue.7301 , pp. 1536-1538
    • Renehan, A.G.1    Booth, C.2    Potten, C.S.3
  • 2
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: Apoptosis, necrosis and autophagy
    • DOI 10.1016/j.ceb.2004.09.011, PII S0955067404001474
    • A.L. Edinger, and C.B. Thompson Death by design: apoptosis, necrosis and autophagy Current Opinion in Cell Biology 16 2004 663 669 (Pubitemid 39463117)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.6 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 3
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • DOI 10.1038/nrm2239, PII NRM2239
    • M.C. Maiuri, E. Zalckvar, A. Kimchi, and G. Kroemer Self-eating and self-killing: crosstalk between autophagy and apoptosis Molecular Cell Biology 8 2007 741 752 (Pubitemid 47312826)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.9 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3    Kroemer, G.4
  • 4
    • 34247345833 scopus 로고    scopus 로고
    • The apoptosome: Signalling platform of cell death
    • DOI 10.1038/nrm2153, PII NRM2153
    • S.J. Riedl, and G.S. Salvesen The apoptosome: signalling platform of cell death Molecular Cell Biology 8 2007 405 413 (Pubitemid 46643237)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.5 , pp. 405-413
    • Riedl, S.J.1    Salvesen, G.S.2
  • 5
    • 68349154339 scopus 로고    scopus 로고
    • Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival
    • M.A. Hughes, N. Harper, M. Butterworth, K. Cain, G.M. Cohen, and M. MacFarlane Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival Molecular Cell 35 2009 265 279
    • (2009) Molecular Cell , vol.35 , pp. 265-279
    • Hughes, M.A.1    Harper, N.2    Butterworth, M.3    Cain, K.4    Cohen, G.M.5    MacFarlane, M.6
  • 6
    • 0344309002 scopus 로고    scopus 로고
    • Mechanisms of caspase activation
    • DOI 10.1016/j.ceb.2003.10.009
    • K.M. Boatright, and G.S. Salvesen Mechanisms of caspase activation Current Opinion in Cell Biology 15 2003 725 731 (Pubitemid 37492933)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.6 , pp. 725-731
    • Boatright, K.M.1    Salvesen, G.S.2
  • 7
    • 0036205587 scopus 로고    scopus 로고
    • Mechanisms of caspase activation and inhibition during apoptosis
    • DOI 10.1016/S1097-2765(02)00482-3
    • Y. Shi Mechanisms of caspase activation and inhibition during apoptosis Molecular Cell 9 2002 459 470 (Pubitemid 34273778)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 459-470
    • Shi, Y.1
  • 8
    • 40449141956 scopus 로고    scopus 로고
    • Targeting cell death in tumors by activating caspases
    • DOI 10.2174/156800908783769391
    • S.H. MacKenzie, and A.C. Clark Targeting cell death in tumors by activating caspases Current Cancer Drug Targets 8 2008 98 109 (Pubitemid 351347245)
    • (2008) Current Cancer Drug Targets , vol.8 , Issue.2 , pp. 98-109
    • MacKenzie, S.H.1    Clark, A.C.2
  • 9
    • 69249100500 scopus 로고    scopus 로고
    • Human caspases: Activation, specificity, and regulation
    • C. Pop, and G.S. Salvesen Human caspases: activation, specificity, and regulation Journal of Biological Chemistry 33 2009 21777 21781
    • (2009) Journal of Biological Chemistry , vol.33 , pp. 21777-21781
    • Pop, C.1    Salvesen, G.S.2
  • 15
    • 34147178164 scopus 로고    scopus 로고
    • Role of proteolysis in caspase-8 activation and stabilization
    • DOI 10.1021/bi602623b
    • C. Pop, P. Fitzgerald, D.R. Green, and G.S. Salvesen Role of proteolysis in caspase-8 activation and stabilization Biochemistry 46 2007 4398 4407 (Pubitemid 46559405)
    • (2007) Biochemistry , vol.46 , Issue.14 , pp. 4398-4407
    • Pop, C.1    Fitzgerald, P.2    Green, D.R.3    Salvesen, G.S.4
  • 16
    • 77958493422 scopus 로고    scopus 로고
    • The caspase-8 dimerization/dissociation balance is a highly potent regulator of caspase-8, -3, -6 signaling
    • M.L. Wurstle, M.A. Laussmann, and M. Rehm The caspase-8 dimerization/dissociation balance is a highly potent regulator of caspase-8, -3, -6 signaling Journal of Biological Chemistry 285 2010 33209 33218
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 33209-33218
    • Wurstle, M.L.1    Laussmann, M.A.2    Rehm, M.3
  • 19
    • 0035960678 scopus 로고    scopus 로고
    • Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer
    • DOI 10.1021/bi011037e
    • C. Pop, Y.-R. Chen, B. Smith, K. Bose, B. Bobay, A. Tripathy, S. Franzen, and A.C. Clark Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer Biochemistry 40 2001 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
  • 20
    • 67650070345 scopus 로고    scopus 로고
    • L2' loop is critical for caspase-7 active site formation
    • W.A. Witkowski, and J.A. Hardy L2' loop is critical for caspase-7 active site formation Protein Science 18 2009 1459 1468
    • (2009) Protein Science , vol.18 , pp. 1459-1468
    • Witkowski, W.A.1    Hardy, J.A.2
  • 21
    • 70350033973 scopus 로고    scopus 로고
    • Dissecting an allosteric switch in caspase-7 using chemical and mutational probes
    • J.A. Hardy, and J.A. Wells Dissecting an allosteric switch in caspase-7 using chemical and mutational probes Journal of Biological Chemistry 284 2009 26063 26069
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 26063-26069
    • Hardy, J.A.1    Wells, J.A.2
  • 22
    • 77951625831 scopus 로고    scopus 로고
    • Colorectal cancer: National and international perspective on the burden of disease and public health impact
    • Z.F. Gellad, and D. Provenazle Colorectal cancer: national and international perspective on the burden of disease and public health impact Gastroenterology 138 2010 2177 2190
    • (2010) Gastroenterology , vol.138 , pp. 2177-2190
    • Gellad, Z.F.1    Provenazle, D.2
  • 23
    • 1542409979 scopus 로고    scopus 로고
    • Changes in the Apoptotic and Survival Signaling in Cancer Cells and Their Potential Therapeutic Implications
    • DOI 10.2174/1568009043481551
    • A.F. Kabore, J.B. Johnston, and S.B. Gibson Changes in the apoptotic and survival signaling in cancer cells and their potential therapeutic implications Current Cancer Drug Targets 4 2004 147 163 (Pubitemid 38332553)
    • (2004) Current Cancer Drug Targets , vol.4 , Issue.2 , pp. 147-163
    • Kabore, A.F.1    Johnston, J.B.2    Gibson, S.B.3
  • 24
    • 8844263797 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in cancer therapy
    • DOI 10.2174/1568009043332763
    • S. Fulda, and K.-M. Debatin Targeting apoptosis pathways in cancer therapy Current Cancer Drug Targets 4 2004 569 576 (Pubitemid 39536377)
    • (2004) Current Cancer Drug Targets , vol.4 , Issue.7 , pp. 569-576
    • Fulda, S.1    Debatin, K.-M.2
  • 25
    • 33750632135 scopus 로고    scopus 로고
    • Apoptosis in the treatment of cancer: A promise kept?
    • DOI 10.1016/j.ceb.2006.10.008, PII S095506740600161X
    • X.W. Meng, S.-H. Lee, and S.H. Kaufmann Apoptosis in the treatment of cancer: a promise kept? Current Opinion in Cell Biology 18 2006 668 676 (Pubitemid 44692481)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.6 , pp. 668-676
    • Meng, X.W.1    Lee, S.-H.2    Kaufmann, S.H.3
  • 26
    • 43249093771 scopus 로고    scopus 로고
    • Therapeutic targeting of death pathways in cancer: Mechanisms for activating cell death in cancer cells
    • R. Khosravi-Far, E. White, Springer Philadelphia
    • T.-T. Tan, and E. White Therapeutic targeting of death pathways in cancer: mechanisms for activating cell death in cancer cells R. Khosravi-Far, E. White, Programmed Cell Death in Cancer Progression 2008 Springer Philadelphia 81 104
    • (2008) Programmed Cell Death in Cancer Progression , pp. 81-104
    • Tan, T.-T.1    White, E.2
  • 27
    • 67349160732 scopus 로고    scopus 로고
    • Caspase-8 in cancer biology and therapy
    • S. Fulda Caspase-8 in cancer biology and therapy Cancer Letters 281 2009 128 133
    • (2009) Cancer Letters , vol.281 , pp. 128-133
    • Fulda, S.1
  • 29
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • DOI 10.1038/sj.onc.1207373
    • H.-G. Zhang, J. Wang, X. Yang, H.-C. Hsu, and J.D. Mountz Regulation of apoptosis proteins in cancer cells by ubiquitin Oncogene 23 2004 2009 2015 (Pubitemid 38496730)
    • (2004) Oncogene , vol.23 , Issue.REV. ISS. 1 , pp. 2009-2015
    • Zhang, H.-G.1    Wang, J.2    Yang, X.3    Hsu, H.-C.4    Mountz, J.D.5
  • 32
    • 0030932894 scopus 로고    scopus 로고
    • The Gibbs Conference on Biothermodynamics: Origins and evolution
    • DOI 10.1016/S0301-4622(96)02246-6, PII S0301462296022466
    • G.K. Ackers, and D.W. Bolen The Gibbs conference on biothermodynamics: origins and evolution Biophysical Chemistry 64 1997 3 5 (Pubitemid 27148651)
    • (1997) Biophysical Chemistry , vol.64 , Issue.1-3 , pp. 3-5
    • Ackers, G.K.1    Bolen, D.W.2
  • 36
    • 0142063422 scopus 로고    scopus 로고
    • An Uncleavable Procaspase-3 Mutant Has a Lower Catalytic Efficiency but an Active Site Similar to That of Mature Caspase-3
    • DOI 10.1021/bi034998x
    • K. Bose, C. Pop, B. Feeney, and A.C. Clark An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3 Biochemistry 42 2003 12298 12310 (Pubitemid 37296506)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12298-12310
    • Bose, K.1    Pop, C.2    Feeney, B.3    Clark, A.C.4
  • 37
    • 10944256201 scopus 로고    scopus 로고
    • Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3
    • DOI 10.1042/BJ20040693
    • B. Feeney, C. Pop, A. Tripathy, and A.C. Clark Ionic interactions near loop L4 are important for maintaining the active site environment and the dimer stability of (pro)caspase-3 Biochemical Journal 384 2004 515 525 (Pubitemid 40018965)
    • (2004) Biochemical Journal , vol.384 , Issue.3 , pp. 515-525
    • Feeney, B.1    Pop, C.2    Tripathy, A.3    Clark, A.C.4
  • 38
    • 28844472825 scopus 로고    scopus 로고
    • Reassembly of active caspase-3 is facilitated by the propeptide
    • DOI 10.1074/jbc.M505834200
    • B. Feeney, and A.C. Clark Reassembly of active caspase-3 is facilitated by the propeptide Journal of Biological Chemistry 280 2005 39772 39785 (Pubitemid 41779110)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39772-39785
    • Feeney, B.1    Clark, A.C.2
  • 39
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • DOI 10.1016/S0169-409X(00)00129-0, PII S0169409X00001290
    • C.A. Lipinski, F. Lombardo, B.W. Dominy, and P.J. Feeney Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings Advanced Drug Delivery Reviews 46 2001 3 26 (Pubitemid 33653411)
    • (2000) Advanced Drug Delivery Reviews , vol.46 , Issue.1-3 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 40
    • 0142063420 scopus 로고    scopus 로고
    • Mutations in the Procaspase-3 Dimer Interface Affect the Activity of the Zymogen
    • DOI 10.1021/bi034999p
    • C. Pop, B. Feeney, A. Tripathy, and A.C. Clark Mutations in the procaspase-3 dimer interface affect the activity of the zymogen Biochemistry 42 2003 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
  • 41
    • 70449372265 scopus 로고    scopus 로고
    • Small-molecule activators of a proenzyme
    • D.W. Wolan, J.A. Zorn, D.C. Gray, and J.A. Wells Small-molecule activators of a proenzyme Science 326 2009 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
  • 42
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • T. Wiseman, S. Williston, J.F. Brandts, and L. Lung-Nan Rapid measurement of binding constants and heats of binding using a new titration calorimeter Analytical Biochemistry 179 1989 131 137 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 43
    • 84856513620 scopus 로고    scopus 로고
    • National Center for Biotechnology Information. AID = 463141, Source = Scripps Research Institute Molecular Screening Center.
    • National Center for Biotechnology Information. PubChem BioAssay Database; AID = 463141, Source = Scripps Research Institute Molecular Screening Center, http://pubchem.ncbi.nlm.nih.gov/assay/assay.cgi?aid=463141.
    • PubChem BioAssay Database
  • 44
    • 84916211748 scopus 로고    scopus 로고
    • National Center for Biotechnology Information. SID = 49647539, Source = Scripps Research Institute Molecular Screening Center.
    • National Center for Biotechnology Information. PubChem Substance Database; SID = 49647539, Source = Scripps Research Institute Molecular Screening Center, http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi?sid= 49647539.
    • PubChem Substance Database
  • 45
    • 84856521159 scopus 로고    scopus 로고
    • N.C.f.B. Information, National Center for Biotechnology Information. CID = 3292253.
    • N.C.f.B. Information, National Center for Biotechnology Information. PubChem Compound Database; CID = 3292253, http://pubchem.ncbi.nlm.nih.gov/ summary/summary.cgi?cid=3292253.
    • PubChem Compound Database
  • 46
    • 2942557079 scopus 로고    scopus 로고
    • Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets
    • H. Ohtaka, S. Muzammil, A. Schon, A. Vaelazquez-Campoy, S. Vega, and E. Friere Thermodynamic rules for the design of high affinity HIV-1 protease inhibitors with adaptability to mutations and high selectivity towards unwanted targets International Journal of Biochemistry and Cell Biology 36 2004 1787 1789
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , pp. 1787-1789
    • Ohtaka, H.1    Muzammil, S.2    Schon, A.3    Vaelazquez-Campoy, A.4    Vega, S.5    Friere, E.6
  • 47
    • 0034093758 scopus 로고    scopus 로고
    • HIV-1 protease inhibitors: Enthalpic versus entropic optimization of the binding affinity
    • DOI 10.1021/bi992399d
    • A. Velazquez-Campoy, M.J. Todd, and E. Friere HIV-1 protease inhibitors: enthalpic versus entropic optimization of the binding affinity Biochemistry 39 2000 2201 2207 (Pubitemid 30130068)
    • (2000) Biochemistry , vol.39 , Issue.9 , pp. 2201-2207
    • Velazquez-Campoy, A.1    Todd, M.J.2    Freire, E.3
  • 48
    • 0019889063 scopus 로고
    • Thermodynamics of protein association reactions: Forces contributing to stability
    • P.D. Ross, and S. Subramanian Thermodynamics of protein association reactions: forces contributing to stability Biochemistry 20 1981 3096 3102
    • (1981) Biochemistry , vol.20 , pp. 3096-3102
    • Ross, P.D.1    Subramanian, S.2
  • 49
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • J.B. Chaires Calorimetry and thermodynamics in drug design Annual review of biophysics 37 2008 135 151
    • (2008) Annual Review of Biophysics , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 50
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • E. Friere Do enthalpy and entropy distinguish first in class from best in class? Drug Discovery Today 13 2008 869 874
    • (2008) Drug Discovery Today , vol.13 , pp. 869-874
    • Friere, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.