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Volumn 52, Issue 18, 2009, Pages 5721-5731

Procaspase-3 activation as an anti-cancer strategy: Structure-activity relationship of procaspase-activating compound 1 (PAC-1) and its cellular co-localization with caspase-3

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DERIVATIVE; ANTINEOPLASTIC AGENT; CASPASE 3; DNA; FLUORESCENT DYE; HYDRAZIDE DERIVATIVE; PROCASPASE 3; PROCASPASE ACTIVATING COMPOUND 1; RABBIT ANTISERUM; UNCLASSIFIED DRUG; ZINC ION;

EID: 70349433777     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm900722z     Document Type: Article
Times cited : (140)

References (73)
  • 2
    • 1542436776 scopus 로고    scopus 로고
    • Classical chemotherapy: Mechanisms, toxicities and the therapeutic window
    • Malhotra, V.; Perry, M. C. Classical chemotherapy: mechanisms, toxicities and the therapeutic window. Cancer Biol. Ther. 2003, 2, S2-4.
    • (2003) Cancer Biol. Ther. , vol.2
    • Malhotra, V.1    Perry, M.C.2
  • 3
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D.; Weinberg, R. A. The hallmarks of cancer. Cell 2000, 100, 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 4
    • 0036547417 scopus 로고    scopus 로고
    • Death and anti-death: Tumor resistance to apoptosis
    • Igney, F. H.; Krammer, P. H. Death and anti-death: tumor resistance to apoptosis. Nature Rev. Cancer 2002, 2, 277-288.
    • (2002) Nature Rev. Cancer , vol.2 , pp. 277-288
    • Igney, F.H.1    Krammer, P.H.2
  • 6
    • 28544443984 scopus 로고    scopus 로고
    • Promoting apoptosis as a strategy for cancer drug discovery
    • Fesik, S. W. Promoting apoptosis as a strategy for cancer drug discovery. Nat. Rev. Cancer 2005, 5, 876-885.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 876-885
    • Fesik, S.W.1
  • 7
    • 33746741050 scopus 로고    scopus 로고
    • Targeted induction of apoptosis for cancer therapy: Current progress and prospects
    • Bremer, E.; van Dam, G.; Kroesen, B. J.; de Leij, L.; Helfrich, W. Targeted induction of apoptosis for cancer therapy: current progress and prospects. Trends Mol. Med. 2006, 12, 382-393.
    • (2006) Trends Mol. Med. , vol.12 , pp. 382-393
    • Bremer, E.1    Van Dam, G.2    Kroesen, B.J.3    De Leij, L.4    Helfrich, W.5
  • 8
    • 26444434342 scopus 로고    scopus 로고
    • Pharmacological manipulation of cell death: Clinical applications in sight?
    • Green, D. R.; Kroemer, G. Pharmacological manipulation of cell death: clinical applications in sight? J. Clin. Invest. 2005, 115, 2610-2617.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2610-2617
    • Green, D.R.1    Kroemer, G.2
  • 9
    • 4644244279 scopus 로고    scopus 로고
    • Targeting apoptotic pathways in cancer cells
    • DOI 10.1126/science.1102974
    • Denicourt, C.; Dowdy, S. F. Targeting apoptotic pathways in cancer cells. Science 2004, 305, 1411-1413. (Pubitemid 39167648)
    • (2004) Science , vol.305 , Issue.5689 , pp. 1411-1413
    • Denicourt, C.1    Dowdy, S.F.2
  • 13
    • 4444243683 scopus 로고    scopus 로고
    • A small molecule Smac mimic potentiates TRAIL- And TNFalpha-mediated cell death
    • Li, L.; Thomas, R. M.; Suzuki, H.; De Brabander, J. K.; Wang, X.; Harran, P. G. A small molecule Smac mimic potentiates TRAIL- and TNFalpha-mediated cell death. Science 2004, 305, 1471-1474.
    • (2004) Science , vol.305 , pp. 1471-1474
    • Li, L.1    Thomas, R.M.2    Suzuki, H.3    De Brabander, J.K.4    Wang, X.5    Harran, P.G.6
  • 15
    • 34548574823 scopus 로고    scopus 로고
    • YM155, a novel small-molecule survivin suppressant, induces regression of established human hormone-refractory prostate tumor xenografts
    • DOI 10.1158/0008-5472.CAN-07-1343
    • Nakahara, T.; Takeuchi, M.; Kinoyama, I.; Minematsu, T.; Shirasuna, K.; Matsuhisa, A.; Kita, A.; Tominaga, F.; Yamanaka, K.; Kudoh, M.; Sasamata, M. YM155, a novel small-molecule survivin suppressant, induces regression of established human hormone-refractory prostate tumor xenografts. Cancer Res. 2007, 67, 8014-8021. (Pubitemid 47395135)
    • (2007) Cancer Research , vol.67 , Issue.17 , pp. 8014-8021
    • Nakahara, T.1    Takeuchi, M.2    Kinoyama, I.3    Minematsu, T.4    Shirasuna, K.5    Matsuhisa, A.6    Kita, A.7    Tominaga, F.8    Yamanaka, K.9    Kudoh, M.10    Sasamata, M.11
  • 18
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • Earnshaw, W. C.; Martins, L. M.; Kaufmann, S. H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 1999, 68, 383-424.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 19
    • 33750690511 scopus 로고    scopus 로고
    • Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3
    • Feeney, B.; Pop, C.; Swartz, P.; Mattos, C.; Clark, A. C. Role of loop bundle hydrogen bonds in the maturation and activity of (Pro)caspase-3. Biochemistry 2006, 45, 13249-13263.
    • (2006) Biochemistry , vol.45 , pp. 13249-13263
    • Feeney, B.1    Pop, C.2    Swartz, P.3    Mattos, C.4    Clark, A.C.5
  • 20
    • 0142063420 scopus 로고    scopus 로고
    • Mutations in the procaspase-3 dimer interface affect the activity of the zymogen
    • Pop, C.; Feeney, B.; Tripathy, A.; Clark, A. C. Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. Biochemistry 2003, 42, 12311-12320.
    • (2003) Biochemistry , vol.42 , pp. 12311-12320
    • Pop, C.1    Feeney, B.2    Tripathy, A.3    Clark, A.C.4
  • 21
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • DOI 10.1016/S1097-2765(02)00442-2
    • Acehan, D.; Jiang, X.; Morgan, D. G.; Heuser, J. E.; Wang, X.; Akey, C. W. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell 2002, 9, 423-432. (Pubitemid 34195566)
    • (2002) Molecular Cell , vol.9 , Issue.2 , pp. 423-432
    • Acehan, D.1    Jiang, X.2    Morgan, D.G.3    Heuser, J.E.4    Wang, X.5    Akey, C.W.6
  • 22
    • 22744436580 scopus 로고    scopus 로고
    • Engineering a dimeric caspase-9: A re-evaluation of the induced proximity model for caspase activation
    • DOI 10.1371/journal.pbio.0030183, e183
    • Chao, Y.; Shiozaki, E. N.; Srinivasula, S. M.; Rigotti, D. J.; Fairman, R.; Shi, Y. Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation. PLoS Biol. 2005, 3, e183. (Pubitemid 41032217)
    • (2005) PLoS Biology , vol.3 , Issue.6 , pp. 1079-1087
    • Chao, Y.1    Shiozaki, E.N.2    Srinivasula, S.M.3    Rigotti, D.J.4    Fairman, R.5    Shi, Y.6
  • 23
    • 61449175831 scopus 로고    scopus 로고
    • Structural and biochemical studies on procaspase-8: New insights on initiator caspase activation
    • Keller, N.; Mares, J.; Zerbe, O.; Grutter, M. G. Structural and biochemical studies on procaspase-8: new insights on initiator caspase activation. Structure 2009, 17, 438-448.
    • (2009) Structure , vol.17 , pp. 438-448
    • Keller, N.1    Mares, J.2    Zerbe, O.3    Grutter, M.G.4
  • 25
    • 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.; Wu, H. Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. Mol. Cell 2006, 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
  • 26
    • 33947426526 scopus 로고    scopus 로고
    • The CASBAH: A searchable database of caspase substrates
    • Luthi, A. U.; Martin, S. J. The CASBAH: a searchable database of caspase substrates. Cell Death Differ. 2007, 14, 641-650.
    • (2007) Cell Death Differ. , vol.14 , pp. 641-650
    • Luthi, A.U.1    Martin, S.J.2
  • 29
    • 0035831473 scopus 로고    scopus 로고
    • Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis
    • Slee, E. A.; Adrain, C.; Martin, S. J. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis. J. Biol. Chem. 2001, 276, 7320-7326.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7320-7326
    • Slee, E.A.1    Adrain, C.2    Martin, S.J.3
  • 31
    • 33749186347 scopus 로고    scopus 로고
    • A pro-chelator triggered by hydrogen peroxide inhibits iron-promoted hydroxyl radical formation
    • Charkoudian, L. K.; Pham, D. M.; Franz, K. J. A pro-chelator triggered by hydrogen peroxide inhibits iron-promoted hydroxyl radical formation. J. Am. Chem. Soc. 2006, 128, 12424-12425.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12424-12425
    • Charkoudian, L.K.1    Pham, D.M.2    Franz, K.J.3
  • 32
    • 0030881603 scopus 로고    scopus 로고
    • Biochemical characteristics of caspases-3, -6, -7, and -8
    • Stennicke, H. R.; Salvesen, G. S. Biochemical characteristics of caspases-3, -6, -7, and -8. J. Biol. Chem. 1997, 272, 25719-25723.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25719-25723
    • Stennicke, H.R.1    Salvesen, G.S.2
  • 34
    • 34347230544 scopus 로고    scopus 로고
    • Sulforhodamine B colorimetric assay for cytotoxicity screening
    • Vichai, V.; Kirtikara, K. Sulforhodamine B colorimetric assay for cytotoxicity screening. Nat. Protoc. 2006, 1, 1112-1116.
    • (2006) Nat. Protoc. , vol.1 , pp. 1112-1116
    • Vichai, V.1    Kirtikara, K.2
  • 35
    • 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
    • Bose, K.; Pop, C.; Feeney, B.; Clark, A. C. An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. Biochemistry 2003, 42, 12298-12310.
    • (2003) Biochemistry , vol.42 , pp. 12298-12310
    • Bose, K.1    Pop, C.2    Feeney, B.3    Clark, A.C.4
  • 36
    • 36849031775 scopus 로고    scopus 로고
    • Highly sensitive fluorescent probes for zinc ion based on triazolyl-containing tetradentate coordination motifs
    • Huang, S.; Clark, R. J.; Zhu, L. Highly sensitive fluorescent probes for zinc ion based on triazolyl-containing tetradentate coordination motifs. Org. Lett. 2007, 9, 4999-5002.
    • (2007) Org. Lett. , vol.9 , pp. 4999-5002
    • Huang, S.1    Clark, R.J.2    Zhu, L.3
  • 37
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisen cycloaddition process: Copper(I)-catalyzed regio-selective "ligation" of azides and terminal alkynes
    • Rostovtsev, V. V.; Green, L. G.; Fokin, V. V.; Sharpless, K. B. A stepwise Huisen cycloaddition process: copper(I)-catalyzed regio-selective "ligation" of azides and terminal alkynes. Angew. Chem., Int. Ed. 2002, 41, 2596-2599.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 38
    • 0036386378 scopus 로고    scopus 로고
    • Intracellular zinc distribution and transport in C6 rat glioma cells
    • Haase, H.; Beyersmann, D. Intracellular zinc distribution and transport in C6 rat glioma cells. Biochem. Biophys. Res. Commun. 2002, 296, 923-928.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 923-928
    • Haase, H.1    Beyersmann, D.2
  • 39
    • 0033572730 scopus 로고    scopus 로고
    • Aqueous coordination chemistry of quinoline-based fluorescence probes for the biological chemistry of zinc
    • Fahrni, C. J.; O'Halloran, T. V. Aqueous coordination chemistry of quinoline-based fluorescence probes for the biological chemistry of zinc. J. Am. Chem. Soc. 1999, 121, 11448-11458.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11448-11458
    • Fahrni, C.J.1    O'Halloran, T.V.2
  • 40
    • 0034533678 scopus 로고    scopus 로고
    • Visualization of labile zinc and its role in apoptosis of primary airway epithelial cells and cell lines
    • Truong-Tran, A. Q.; Ruffin, R. E.; Zalewski, P. D. Visualization of labile zinc and its role in apoptosis of primary airway epithelial cells and cell lines. Am. J. Physiol.: Lung Cell Mol. Physiol. 2000, 279, L1172-L1183.
    • (2000) Am. J. Physiol.: Lung Cell Mol. Physiol. , vol.279
    • Truong-Tran, A.Q.1    Ruffin, R.E.2    Zalewski, P.D.3
  • 41
    • 0027501386 scopus 로고
    • Correlation of apoptosis with change in intracellular labile Zn(II) using Zinquin [(2-methyl-8-p-toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II)
    • Zalewski, P. D.; Forbes, I. J.; Betts, W. H. Correlation of apoptosis with change in intracellular labile Zn(II) using Zinquin [(2-methyl-8-p- toluenesulphonamido-6-quinolyloxy)acetic acid], a new specific fluorescent probe for Zn(II). Biochem. J. 1993, 296 (Pt 2), 403-408.
    • (1993) Biochem. J. , vol.296 , Issue.PART 2 , pp. 403-408
    • Zalewski, P.D.1    Forbes, I.J.2    Betts, W.H.3
  • 42
    • 0035696301 scopus 로고    scopus 로고
    • Functions of zinc in signaling, proliferation and differentiation of mammalian cells
    • DOI 10.1023/A:1012905406548
    • Beyersmann, D.; Haase, H. Functions of zinc in signaling, proliferation and differentiation of mammalian cells. BioMetals 2001, 14, 331-341. (Pubitemid 34066636)
    • (2001) BioMetals , vol.14 , Issue.3-4 , pp. 331-341
    • Beyersmann, D.1    Haase, H.2
  • 43
    • 4444316699 scopus 로고    scopus 로고
    • Exchangeable zinc ions transiently accumulate in a vesicular compartment in the yeast Saccharomyces cerevisiae
    • Devirgiliis, C.; Murgia, C.; Danscher, G.; Perozzi, G. Exchangeable zinc ions transiently accumulate in a vesicular compartment in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 2004, 323, 58-64.
    • (2004) Biochem. Biophys. Res. Commun. , vol.323 , pp. 58-64
    • Devirgiliis, C.1    Murgia, C.2    Danscher, G.3    Perozzi, G.4
  • 45
    • 56349095210 scopus 로고    scopus 로고
    • High intracellular Zn2+ ions modulate the VHR, ZAP-70 and ERK activities of LNCaP prostate cancer cells
    • Wong, P.-F.; Abubakar, S. High intracellular Zn2+ ions modulate the VHR, ZAP-70 and ERK activities of LNCaP prostate cancer cells. Cell. Mol. Biol. Lett. 2008, 13, 375-390.
    • (2008) Cell. Mol. Biol. Lett. , vol.13 , pp. 375-390
    • Wong, P.-F.1    Abubakar, S.2
  • 46
    • 0034714009 scopus 로고    scopus 로고
    • Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): Correlation with DNA fragmentation
    • Bedner, E.; Smolewski, P.; Amstad, P.; Darzynkiewicz, Z. Activation of caspases measured in situ by binding of fluorochrome-labeled inhibitors of caspases (FLICA): correlation with DNA fragmentation. Exp. Cell Res. 2000, 259, 308-313.
    • (2000) Exp. Cell Res. , vol.259 , pp. 308-313
    • Bedner, E.1    Smolewski, P.2    Amstad, P.3    Darzynkiewicz, Z.4
  • 47
    • 0035340652 scopus 로고    scopus 로고
    • Detection of caspases activation by fluorochrome-labeled inhibitors: Multiparameter analysis by laser scanning cytometry
    • DOI 10.1002/1097-0320(20010501)44:1<73::AID-CYTO1084>3.0.CO;2-S
    • Smolewski, P.; Bedner, E.; Du, L.; Hsieh, T. C.; Wu, J. M.; Phelps, D. J.; Darzynkiewicz, Z. Detection of caspases activation by fluorochrome-labeled inhibitors: Multiparameter analysis by laser scanning cytometry. Cytometry 2001, 44, 73-82. (Pubitemid 32434005)
    • (2001) Cytometry , vol.44 , Issue.1 , pp. 73-82
    • Smolewski, P.1    Bedner, E.2    Du, L.3    Hsieh, T.-C.4    Wu, J.M.5    Phelps, D.J.6    Darzynkiewicz, Z.7
  • 48
    • 0035489015 scopus 로고    scopus 로고
    • Stathmo-apoptosis: Arresting apoptosis by fluorochrome-labeled inhibitor of caspases
    • Smolewski, P.; Grabarek, J.; Phelps, D. J.; Darzynkiewicz, Z. Stathmo-apoptosis: arresting apoptosis by fluorochrome-labeled inhibitor of caspases. Int. J. Oncol. 2001, 19, 657-663.
    • (2001) Int. J. Oncol. , vol.19 , pp. 657-663
    • Smolewski, P.1    Grabarek, J.2    Phelps, D.J.3    Darzynkiewicz, Z.4
  • 49
    • 12544256390 scopus 로고    scopus 로고
    • Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s)
    • Kamada, S.; Kikkawa, U.; Tsujimoto, Y.; Hunter, T. Nuclear translocation of caspase-3 is dependent on its proteolytic activation and recognition of a substrate-like protein(s). J. Biol. Chem. 2005, 280, 857-860.
    • (2005) J. Biol. Chem. , vol.280 , pp. 857-860
    • Kamada, S.1    Kikkawa, U.2    Tsujimoto, Y.3    Hunter, T.4
  • 50
    • 33845764296 scopus 로고    scopus 로고
    • A guided tour into subcellular colocalization analysis in light microscopy
    • Bolte, S.; Cordelieres, F. P. A guided tour into subcellular colocalization analysis in light microscopy. J. Microsc. 2006, 224, 213-232.
    • (2006) J. Microsc. , vol.224 , pp. 213-232
    • Bolte, S.1    Cordelieres, F.P.2
  • 51
    • 0031985647 scopus 로고    scopus 로고
    • Annexin V-affinity assay: A review on an apoptosis detection system based on phosphatidylserine exposure
    • van Engeland, M.; Nieland, L. J.; Ramaekers, F. C.; Schutte, B.; Reutelingsperger, C. P. Annexin V-affinity assay: a review on an apoptosis detection system based on phosphatidylserine exposure. Cytometry 1998, 31, 1-9.
    • (1998) Cytometry , vol.31 , pp. 1-9
    • Van Engeland, M.1    Nieland, L.J.2    Ramaekers, F.C.3    Schutte, B.4    Reutelingsperger, C.P.5
  • 52
    • 0037437796 scopus 로고    scopus 로고
    • Pyridoxal isonicotinoyl hydrazone analogs induce apoptosis in hematopoietic cells due to their iron-chelating properties
    • Buss, J. L.; Neuzil, J.; Gellert, N.; Weber, C.; Ponka, P. Pyridoxal isonicotinoyl hydrazone analogs induce apoptosis in hematopoietic cells due to their iron-chelating properties. Biochem. Pharmacol. 2003, 65, 161-172.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 161-172
    • Buss, J.L.1    Neuzil, J.2    Gellert, N.3    Weber, C.4    Ponka, P.5
  • 53
    • 26044432230 scopus 로고    scopus 로고
    • Direct and derivative spectrophotometric determination of zinc with 2,4-dihydroxybenzaldehyde isonicotinoyl hydrazone in potable water and pharmaceutical samples
    • Sivaramaiah, S.; Reddy, P. R. Direct and derivative spectrophotometric determination of zinc with 2,4-dihydroxybenzaldehyde isonicotinoyl hydrazone in potable water and pharmaceutical samples. J. Anal. Chem. 2005, 60, 828-832.
    • (2005) J. Anal. Chem. , vol.60 , pp. 828-832
    • Sivaramaiah, S.1    Reddy, P.R.2
  • 55
    • 56449087813 scopus 로고    scopus 로고
    • In vitro antileukemia, antibacterial and antifungal activities of some 3d metal complexes: Chemical synthesis and structure-activity relationships
    • Gulea, A.; Poirier, D.; Roy, J.; Stavila, V.; Bulimestru, I.; Tapcov, V.; Birca, M.; Popovschi, L. In vitro antileukemia, antibacterial and antifungal activities of some 3d metal complexes: chemical synthesis and structure-activity relationships. J. Enzyme Inhib. Med. Chem. 2008, 23, 806-818.
    • (2008) J. Enzyme Inhib. Med. Chem. , vol.23 , pp. 806-818
    • Gulea, A.1    Poirier, D.2    Roy, J.3    Stavila, V.4    Bulimestru, I.5    Tapcov, V.6    Birca, M.7    Popovschi, L.8
  • 56
    • 43049126234 scopus 로고    scopus 로고
    • Transition metal complexes of isonicotinic acid (2-hydroxybenzylidene) hydrazide
    • Abou-Melha, K. S. Transition metal complexes of isonicotinic acid (2-hydroxybenzylidene)hydrazide. Spectrochim. Acta, Part A 2008, 70, 162-170.
    • (2008) Spectrochim. Acta, Part a , vol.70 , pp. 162-170
    • Abou-Melha, K.S.1
  • 57
    • 0032469763 scopus 로고    scopus 로고
    • Complexes of salicylaldehyde acylhydrazones: Cytotoxicity, QSAR and crystal structure of the sterically hindered t-butyl dimer
    • Koh, L. L.; Kon, O. L.; Loh, K. W.; Long, Y. C.; Ranford, J. D.; Tan, A. L.; Tjan, Y. Y. Complexes of salicylaldehyde acylhydrazones: cytotoxicity, QSAR and crystal structure of the sterically hindered t-butyl dimer. J. Inorg. Biochem. 1998, 72, 155-162.
    • (1998) J. Inorg. Biochem. , vol.72 , pp. 155-162
    • Koh, L.L.1    Kon, O.L.2    Loh, K.W.3    Long, Y.C.4    Ranford, J.D.5    Tan, A.L.6    Tjan, Y.Y.7
  • 58
    • 0031000566 scopus 로고    scopus 로고
    • Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
    • Borkow, G.; Fletcher, R. S.; Barnard, J.; Arion, D.; Motakis, D.; Dmitrienko, G. I.; Parniak, M. A. Inhibition of the ribonuclease H and DNA polymerase activities of HIV-1 reverse transcriptase by N-(4-tert-butylbenzoyl)- 2-hydroxy-1-naphthaldehyde hydrazone. Biochemistry 1997, 36, 3179-3185.
    • (1997) Biochemistry , vol.36 , pp. 3179-3185
    • Borkow, G.1    Fletcher, R.S.2    Barnard, J.3    Arion, D.4    Motakis, D.5    Dmitrienko, G.I.6    Parniak, M.A.7
  • 59
    • 0035298087 scopus 로고    scopus 로고
    • Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases
    • Shikama, Y.; U, M.; Miyashita, T.; Yamada, M. Comprehensive studies on subcellular localizations and cell death-inducing activities of eight GFP-tagged apoptosis-related caspases. Exp. Cell Res. 2001, 264, 315-325.
    • (2001) Exp. Cell Res. , vol.264 , pp. 315-325
    • Shikama, Y.1    Miyashita, T.2    Yamada, M.3
  • 61
    • 1842636513 scopus 로고    scopus 로고
    • Increased expression of Apaf-1 and procaspase-3 and the functionality of intrinsic apoptosis apparatus in non-small cell lung carcinoma
    • Krepela, E.; Prochazka, J.; Liul, X.; Fiala, P.; Kinkor, Z. Increased expression of Apaf-1 and procaspase-3 and the functionality of intrinsic apoptosis apparatus in non-small cell lung carcinoma. Biol. Chem. 2004, 385, 153-168.
    • (2004) Biol. Chem. , vol.385 , pp. 153-168
    • Krepela, E.1    Prochazka, J.2    Liul, X.3    Fiala, P.4    Kinkor, Z.5
  • 63
    • 85078505211 scopus 로고    scopus 로고
    • Expression of caspase-3 and -7 does not correlate with the extent of apoptosis in primary breast carcinomas
    • Grigoriev, M. Y.; Pozharissky, K. M.; Hanson, K. P.; Imyanitov, E. N.; Zhivotovsky, B. Expression of caspase-3 and -7 does not correlate with the extent of apoptosis in primary breast carcinomas. Cell Cycle 2002, 1, 337-342.
    • (2002) Cell Cycle , vol.1 , pp. 337-342
    • Grigoriev, M.Y.1    Pozharissky, K.M.2    Hanson, K.P.3    Imyanitov, E.N.4    Zhivotovsky, B.5
  • 65
    • 34548572349 scopus 로고    scopus 로고
    • Caspase expression profile and functional activity in a panel of breast cancer cell lines
    • Yang, S.; Liu, J.; Thor, A. D.; Yang, X. Caspase expression profile and functional activity in a panel of breast cancer cell lines. Oncol. Rep. 2007, 17, 1229-1235.
    • (2007) Oncol. Rep. , vol.17 , pp. 1229-1235
    • Yang, S.1    Liu, J.2    Thor, A.D.3    Yang, X.4
  • 67
    • 0031691375 scopus 로고    scopus 로고
    • Zinc ions prevent processing of caspase-3 during apoptosis induced by geranylgeraniol in HL-60 cells
    • Aiuchi, T.; Mihara, S.; Nakaya, M.; Masuda, Y.; Nakajo, S.; Nakaya, K. Zinc ions prevent processing of caspase-3 during apoptosis induced by geranylgeraniol in HL-60 cells. J. Biochem. (Tokyo) 1998, 124, 300-303.
    • (1998) J. Biochem. (Tokyo) , vol.124 , pp. 300-303
    • Aiuchi, T.1    Mihara, S.2    Nakaya, M.3    Masuda, Y.4    Nakajo, S.5    Nakaya, K.6
  • 68
    • 0033043178 scopus 로고    scopus 로고
    • Regulation of caspase activation and apoptosis by cellular zinc fluxes and zinc deprivation: A review
    • Chai, F.; Truong-Tran, A. Q.; Ho, L. H.; Zalewski, P. D. Regulation of caspase activation and apoptosis by cellular zinc fluxes and zinc deprivation: A review. Immunol. Cell Biol. 1999, 77, 272-278.
    • (1999) Immunol. Cell Biol. , vol.77 , pp. 272-278
    • Chai, F.1    Truong-Tran, A.Q.2    Ho, L.H.3    Zalewski, P.D.4
  • 69
    • 0035400549 scopus 로고    scopus 로고
    • Role of cellular zinc in programmed cell death: Temporal relationship between zinc depletion, activation of caspases, and cleavage of Sp family transcription factors
    • Chimienti, F.; Seve, M.; Richard, S.; Mathieu, J.; Favier, A. Role of cellular zinc in programmed cell death: temporal relationship between zinc depletion, activation of caspases, and cleavage of Sp family transcription factors. Biochem. Pharmacol. 2001, 62, 51-62.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 51-62
    • Chimienti, F.1    Seve, M.2    Richard, S.3    Mathieu, J.4    Favier, A.5
  • 70
    • 0642345203 scopus 로고    scopus 로고
    • Apoptosis in the normal and inflamed airway epithelium: Role of zinc in epithelial protection and procaspase-3 regulation
    • Truong-Tran, A. Q.; Grosser, D.; Ruffin, R. E.; Murgia, C.; Zalewski, P. D. Apoptosis in the normal and inflamed airway epithelium: role of zinc in epithelial protection and procaspase-3 regulation. Biochem. Pharmacol. 2003, 66, 1459-1468.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1459-1468
    • Truong-Tran, A.Q.1    Grosser, D.2    Ruffin, R.E.3    Murgia, C.4    Zalewski, P.D.5
  • 72
    • 0032866138 scopus 로고    scopus 로고
    • Cytotoxic actions of the heavy metal chelator TPEN on NG108-15 neuroblastoma-glioma cells
    • Adler, M.; Shafer, H.; Hamilton, T.; Petrali, J. P. Cytotoxic actions of the heavy metal chelator TPEN on NG108-15 neuroblastoma-glioma cells. Neurotoxicology 1999, 20, 571-582.
    • (1999) Neurotoxicology , vol.20 , pp. 571-582
    • Adler, M.1    Shafer, H.2    Hamilton, T.3    Petrali, J.P.4


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