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Volumn 2014, Issue 8, 2014, Pages 799-806

Measuring apoptosis: Caspase inhibitors and activity assays

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOTIC PROTEASE ACTIVATING FACTOR 1; CALPAIN; CASPASE; CASPASE INHIBITOR; CATHEPSIN; CELL EXTRACT; CYTOCHROME C; DEATH DOMAIN RECEPTOR SIGNALING ADAPTOR PROTEIN; GRANZYME B; INTERLEUKIN 1BETA; PROTEIN P53;

EID: 84922345634     PISSN: 19403402     EISSN: 15596095     Source Type: Journal    
DOI: 10.1101/pdb.top070359     Document Type: Article
Times cited : (33)

References (59)
  • 1
    • 8844224859 scopus 로고    scopus 로고
    • The biochemical mechanism of caspase-2 activation
    • Baliga BC, Read SH, Kumar S. 2004. The biochemical mechanism of caspase-2 activation. Cell Death Differ 11: 1234-1241.
    • (2004) Cell Death Differ , vol.11 , pp. 1234-1241
    • Baliga, B.C.1    Read, S.H.2    Kumar, S.3
  • 2
    • 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
  • 3
    • 33746972404 scopus 로고    scopus 로고
    • Identification of early intermediates of caspase activation using selective inhibitors and activity-based probes
    • Berger AB, Witte MD, Denault JB, Sadaghiani AM, Sexton KM, Salvesen GS, Bogyo M. 2006a. Identification of early intermediates of caspase activation using selective inhibitors and activity-based probes. Mol Cell 23: 509-521.
    • (2006) Mol Cell , vol.23 , pp. 509-521
    • Berger, A.B.1    Witte, M.D.2    Denault, J.B.3    Sadaghiani, A.M.4    Sexton, K.M.5    Salvesen, G.S.6    Bogyo, M.7
  • 4
    • 33845766627 scopus 로고    scopus 로고
    • Commonly used caspase inhibitors designed based on substrate specificity profiles lack selectivity
    • Berger AB, Sexton KB, Bogyo M. 2006b. Commonly used caspase inhibitors designed based on substrate specificity profiles lack selectivity. Cell Res 16: 961-963.
    • (2006) Cell Res , vol.16 , pp. 961-963
    • Berger, A.B.1    Sexton, K.B.2    Bogyo, M.3
  • 8
    • 0035798361 scopus 로고    scopus 로고
    • Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding
    • Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y. 2001. Crystal structure of a procaspase-7 zymogen: Mechanisms of activation and substrate binding. Cell 107: 399-407.
    • (2001) Cell , vol.107 , pp. 399-407
    • Chai, J.1    Wu, Q.2    Shiozaki, E.3    Srinivasula, S.M.4    Alnemri, E.S.5    Shi, Y.6
  • 13
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW, Bleackley RC. 1995. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 377: 446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 20
  • 21
    • 68349154339 scopus 로고    scopus 로고
    • Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival
    • Hughes MA, Harper N, Butterworth M, Cain K, Cohen GM, MacFarlane M. Reconstitution of the death-inducing signaling complex reveals a substrate switch that determines CD95-mediated death or survival. Mol Cell 35: 265-279.
    • Mol 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
  • 23
    • 33845480548 scopus 로고    scopus 로고
    • Caspase function in programmed cell death
    • Kumar S. 2007. Caspase function in programmed cell death. Cell Death Differ 14: 32-43.
    • (2007) Cell Death Differ , vol.14 , pp. 32-43
    • Kumar, S.1
  • 24
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. 1997. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91: 479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 25
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: A searchable database of caspase substrates
    • Luthi AU, Martin SJ. 2007. The CASBAH: A searchable database of caspase substrates. Cell Death Differ 14: 641-650.
    • (2007) Cell Death Differ , vol.14 , pp. 641-650
    • Luthi, A.U.1    Martin, S.J.2
  • 28
    • 67650455882 scopus 로고    scopus 로고
    • The Apaf-1* procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer
    • Malladi S, Challa-Malladi M, Fearnhead HO, Bratton SB. 2009. The Apaf-1* procaspase-9 apoptosome complex functions as a proteolytic-based molecular timer. EmBO J 28: 1916-1925.
    • (2009) Embo J , vol.28 , pp. 1916-1925
    • Malladi, S.1    Challa-Malladi, M.2    Fearnhead, H.O.3    Bratton, S.B.4
  • 29
    • 84923788859 scopus 로고    scopus 로고
    • Detection of caspase activity using antibody-based techniques
    • McStay GP, Green DR. 2014a. Detection of caspase activity using antibody-based techniques. Cold Spring Harb Protoc doi: 10.1101/pdb. prot080291.
    • (2014) Cold Spring Harb Protoc
    • McStay, G.P.1    Green, D.R.2
  • 30
    • 84923769280 scopus 로고    scopus 로고
    • Verification of a putative caspase substrate
    • McStay GP, Green DR. 2014b. Verification of a putative caspase substrate. Cold Spring Harb Protoc doi: 10.1101/pdb.prot080317.
    • (2014) Cold Spring Harb Protoc
    • McStay, G.P.1    Green, D.R.2
  • 31
    • 84923791988 scopus 로고    scopus 로고
    • Preparation ofcytosolic extract and activation of caspases by cytochrome c
    • McStay GP, Green DR. 2014c. Preparation ofcytosolic extract and activation of caspases by cytochrome c. Cold SpringHarb Protoc doi: 10.1101/pdb. prot080275.
    • (2014) Cold SpringHarb Protoc
    • McStay, G.P.1    Green, D.R.2
  • 33
    • 84923826183 scopus 로고    scopus 로고
    • Identification ofactive caspases usingaffinity-based probes
    • McStay GP, Green DR. 2014e. Identification ofactive caspases usingaffinity-based probes. Cold Spring Harb Protoc doi: 10.1101/pdb.prot080309.
    • (2014) Cold Spring Harb Protoc
    • McStay, G.P.1    Green, D.R.2
  • 34
    • 38049119903 scopus 로고    scopus 로고
    • Overlapping cleavage motifselec-tivity of caspases: Implications for analysis of apoptotic pathways
    • McStay GP, Salvesen GS, Green DR. 2008. Overlapping cleavage motifselec-tivity 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
  • 36
    • 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 AG, Blais V, Denault JB, Salvesen GS, Green DR. Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation. J Biol Chem 285: 16632-16642.
    • 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
  • 38
    • 56049116880 scopus 로고    scopus 로고
    • Some commonly used caspase substrates and inhibitors lack the specificity required to monitor individual caspase activity
    • Pereira NA, Song Z. 2008. Some commonly used caspase substrates and inhibitors lack the specificity required to monitor individual caspase activity. Biochem Biophys Res Commun 377: 873-877.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 873-877
    • Pereira, N.A.1    Song, Z.2
  • 39
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitor
    • (Database issue):
    • Rawlings ND. Barrett AJ, Bateman A. 2012. MEROPS: The database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res 40(Database issue): D343-D350.
    • (2012) Nucleic Acids Res , vol.40 , pp. D343-D350
    • Rawlings1    Barrett Bateman, N.D.A.J.A.2
  • 40
  • 41
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • Riedl SJ, Shi Y. 2004. Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mat Cell Biol 5: 897-907.
    • (2004) Nat Rev Mat Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 45
    • 84864507831 scopus 로고    scopus 로고
    • Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis
    • Shimbo K, Hsu GW, Nguyen H, Mahrus S, Trinidad JC, Burlingame AL, Wells JA. 2012. Quantitative profiling of caspase-cleaved substrates reveals different drug-induced and cell-type patterns in apoptosis. Proc Natl Acad Sci 109: 12432-12437.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 12432-12437
    • Shimbo, K.1    Hsu, G.W.2    Nguyen, H.3    Mahrus, S.4    Trinidad, J.C.5    Burlingame, A.L.6    Wells, J.A.7
  • 47
    • 0037009370 scopus 로고    scopus 로고
    • Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducingsignallingcomplexesinaFADD-dependentmannerbut can not functionallysubstitute caspase-8
    • Sprick MR, Rieser E, Stahl H, Grosse-Wilde A, Weigand MA, Walczak H.2002. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducingsignallingcomplexesinaFADD-dependentmannerbut can not functionallysubstitute caspase-8. EMBO J 21: 4520-4530.
    • (2002) EMBO J , vol.21 , pp. 4520-4530
    • Sprick, M.R.1    Rieser, E.2    Stahl, H.3    Grosse-Wilde, A.4    Weigand, M.A.5    Walczak, H.6
  • 48
    • 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: 563-568.
    • (2000) Biochem J , vol.350 , pp. 563-568
    • Stennicke, H.R.1    Renatus, M.2    Meldal, M.3    Salvesen, G.S.4
  • 52
    • 0028990125 scopus 로고
    • Yama/CPP32p, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M, Quan LT, O’Rourke K, Desnoyers S, Zeng Z, Beidler DR, Poirier GG, Salvesen GS, Dixit VM. 1995. Yama/CPP32p, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O’Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 55
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A, Tschopp J. 2004. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304: 843-846.
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 57
    • 0034929314 scopus 로고    scopus 로고
    • The history of Z-VAD-FMK, a tool for understanding the significance of caspase inhibition
    • Van Noorden CJ. 2001. The history of Z-VAD-FMK, a tool for understanding the significance of caspase inhibition. Acta Histochem 103: 241-251.
    • (2001) Acta Histochem , vol.103 , pp. 241-251
    • Van Noorden, C.J.1
  • 59
    • 36549063702 scopus 로고    scopus 로고
    • CASVM: Web-server for SVM based prediction of caspase substrates cleavage sites
    • Wee LJ, Tan TW, Ranganathan S. 2007. CASVM: Web-server for SVM based prediction of caspase substrates cleavage sites. Bioinformatics 23: 3241-3243.
    • (2007) Bioinformatics , vol.23 , pp. 3241-3243
    • Wee, L.J.1    Tan, T.W.2    Ranganathan, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.