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Volumn 85, Issue , 2015, Pages 127-137

Insights into the importance for designing curcumin-inspired anticancer agents by a prooxidant strategy: The case of diarylpentanoids

Author keywords

Apoptosis; Curcumin; Electrophilicity; Prooxidant; Thioredoxin reductase

Indexed keywords

ANTINEOPLASTIC AGENT; CASPASE 3; CASPASE 9; CURCUMIN; DIARYLPENTANOID; DRUG ANALOG; REACTIVE OXYGEN METABOLITE; THIOREDOXIN REDUCTASE; UNCLASSIFIED DRUG; VALERIC ACID DERIVATIVE;

EID: 84930946260     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2015.04.017     Document Type: Article
Times cited : (78)

References (95)
  • 1
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • B.C. Dickinson, and C.J. Chang Chemistry and biology of reactive oxygen species in signaling or stress responses Nat. Chem. Biol. 7 2011 504 511
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 2
    • 42249088093 scopus 로고    scopus 로고
    • Reconciling the chemistry and biology of reactive oxygen species
    • C.C. Winterbourn Reconciling the chemistry and biology of reactive oxygen species Nat. Chem. Biol. 4 2008 278 286
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 278-286
    • Winterbourn, C.C.1
  • 3
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autréaux, and M.B. Toledano ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat. Rev. Mol. Cell Biol. 8 2007 813 824
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autréaux, B.1    Toledano, M.B.2
  • 4
    • 84882684320 scopus 로고    scopus 로고
    • The tumor microenvironment: Characterization, redox considerations, and novel approaches for reactive oxygen species-targeted gene therapy
    • L.L. Policastro, I.L. Ibañez, C. Notcovich, H.A. Duran, and O.L. Podhajcer The tumor microenvironment: characterization, redox considerations, and novel approaches for reactive oxygen species-targeted gene therapy Antioxid. Redox Signal. 19 2013 854 895
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 854-895
    • Policastro, L.L.1    Ibañez, I.L.2    Notcovich, C.3    Duran, H.A.4    Podhajcer, O.L.5
  • 5
    • 84875181661 scopus 로고    scopus 로고
    • Oxidants, antioxidants and the current incurability of metastatic cancers
    • J. Watson Oxidants, antioxidants and the current incurability of metastatic cancers Open Biol 3 2013 120144
    • (2013) Open Biol , vol.3 , pp. 120144
    • Watson, J.1
  • 6
    • 84859864623 scopus 로고    scopus 로고
    • Upsides and downsides of reactive oxygen species for cancer: The roles of reactive oxygen species in tumorigenesis, prevention, and therapy
    • S.C. Gupta, D. Hevia, S. Patchva, B. Park, W. Koh, and B.B. Aggarwal Upsides and downsides of reactive oxygen species for cancer: the roles of reactive oxygen species in tumorigenesis, prevention, and therapy Antioxid. Redox Signal. 16 2012 1295 1322
    • (2012) Antioxid. Redox Signal. , vol.16 , pp. 1295-1322
    • Gupta, S.C.1    Hevia, D.2    Patchva, S.3    Park, B.4    Koh, W.5    Aggarwal, B.B.6
  • 7
    • 80055022374 scopus 로고    scopus 로고
    • Runaway ROS as a selective anticancer strategy
    • E.I. Parkinson, and P.J. Hergenrother Runaway ROS as a selective anticancer strategy ChemMedChem 6 2011 1957 1959
    • (2011) ChemMedChem , vol.6 , pp. 1957-1959
    • Parkinson, E.I.1    Hergenrother, P.J.2
  • 8
    • 67650071137 scopus 로고    scopus 로고
    • Targeting cancer cells by ROS-mediated mechanisms: A radical therapeutic approach?
    • D. Trachootham, J. Alexandre, and P. Huang Targeting cancer cells by ROS-mediated mechanisms: a radical therapeutic approach? Nat. Rev. Drug Discov. 8 2009 579 591
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 579-591
    • Trachootham, D.1    Alexandre, J.2    Huang, P.3
  • 9
    • 70449107252 scopus 로고    scopus 로고
    • Redox-directed cancer therapeutics: Molecular mechanisms and opportunities
    • G.T. Wondrak Redox-directed cancer therapeutics: molecular mechanisms and opportunities Antioxid. Redox Signal. 11 2009 3013 3069
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 3013-3069
    • Wondrak, G.T.1
  • 10
    • 58549089871 scopus 로고    scopus 로고
    • Elevated copper and oxidative stress in cancer cells as a target for cancer treatment
    • A. Gupte, and R.J. Mumper Elevated copper and oxidative stress in cancer cells as a target for cancer treatment Cancer Treat. Rev. 35 2009 32 46
    • (2009) Cancer Treat. Rev. , vol.35 , pp. 32-46
    • Gupte, A.1    Mumper, R.J.2
  • 11
    • 58149105356 scopus 로고    scopus 로고
    • Cancer cell killing via ROS: To increase or decrease, that is the question
    • J. Wang, and J. Yi Cancer cell killing via ROS: to increase or decrease, that is the question Cancer Biol. Ther. 7 2008 1875 1884
    • (2008) Cancer Biol. Ther. , vol.7 , pp. 1875-1884
    • Wang, J.1    Yi, J.2
  • 13
    • 36849034493 scopus 로고    scopus 로고
    • Experimental therapeutics: Targeting the redox Achilles heel of cancer
    • C.M. Cabello, W.B. Bair III, and G.T. Wondrak Experimental therapeutics: targeting the redox Achilles heel of cancer Curr. Opin. Investig. Drug 8 2007 1022 1037
    • (2007) Curr. Opin. Investig. Drug , vol.8 , pp. 1022-1037
    • Cabello, C.M.1    Bair, W.B.2    Wondrak, G.T.3
  • 14
    • 2942593991 scopus 로고    scopus 로고
    • ROS stress in cancer cells and therapeutic implications
    • H. Pelicano, D. Carney, and P. Huang ROS stress in cancer cells and therapeutic implications Drug Resist. Updates 7 2004 97 110
    • (2004) Drug Resist. Updates , vol.7 , pp. 97-110
    • Pelicano, H.1    Carney, D.2    Huang, P.3
  • 15
    • 33748165596 scopus 로고    scopus 로고
    • Reactive oxygen species in cancer cells: Live by the sword, die by the sword
    • P.T. Schumacker Reactive oxygen species in cancer cells: live by the sword, die by the sword Cancer Cell 10 2006 175 176
    • (2006) Cancer Cell , vol.10 , pp. 175-176
    • Schumacker, P.T.1
  • 16
    • 33847349283 scopus 로고    scopus 로고
    • Reactive oxygen species: A breath of life or death?
    • J.P. Fruehauf, and F.L. Meyskens Reactive oxygen species: a breath of life or death? Clin. Cancer Res. 13 2007 789 794
    • (2007) Clin. Cancer Res. , vol.13 , pp. 789-794
    • Fruehauf, J.P.1    Meyskens, F.L.2
  • 19
    • 4644364745 scopus 로고    scopus 로고
    • Effect of curcumin on normal and tumor cells: Role of glutathione and bcl-2
    • C. Syng-Ai, A.L. Kumari, and A. Khar Effect of curcumin on normal and tumor cells: role of glutathione and bcl-2 Mol. Cancer Ther 3 2004 1101 1108
    • (2004) Mol. Cancer Ther , vol.3 , pp. 1101-1108
    • Syng-Ai, C.1    Kumari, A.L.2    Khar, A.3
  • 21
    • 84876007871 scopus 로고    scopus 로고
    • Selective induction of tumor cell apoptosis by a novel P450-mediated reactive oxygen species (ROS) inducer methyl 3-(4-nitrophenyl) propiolate
    • X. Sun, M. Ai, Y. Wang, S. Shen, Y. Gu, Y. Jin, Z. Zhou, Y. Long, and Q. Yu Selective induction of tumor cell apoptosis by a novel P450-mediated reactive oxygen species (ROS) inducer methyl 3-(4-nitrophenyl) propiolate J. Biol. Chem. 288 2013 8826 8837
    • (2013) J. Biol. Chem. , vol.288 , pp. 8826-8837
    • Sun, X.1    Ai, M.2    Wang, Y.3    Shen, S.4    Gu, Y.5    Jin, Y.6    Zhou, Z.7    Long, Y.8    Yu, Q.9
  • 22
    • 34248582844 scopus 로고    scopus 로고
    • Novel action of paclitaxel against cancer cells: Bystander effect mediated by reactive oxygen species
    • J. Alexandre, Y. Hu, W. Lu, H. Pelicano, and P. Huang Novel action of paclitaxel against cancer cells: bystander effect mediated by reactive oxygen species Cancer Res. 67 2007 3512 3517
    • (2007) Cancer Res. , vol.67 , pp. 3512-3517
    • Alexandre, J.1    Hu, Y.2    Lu, W.3    Pelicano, H.4    Huang, P.5
  • 23
    • 0033568238 scopus 로고    scopus 로고
    • Arsenic trioxide selectively induces acute promyelocytic leukemia cell apoptosis via a hydrogen peroxide-dependent pathway
    • Y. Jing, J. Dai, R.M. Chalmers-Redman, W.G. Tatton, and S. Waxman Arsenic trioxide selectively induces acute promyelocytic leukemia cell apoptosis via a hydrogen peroxide-dependent pathway Blood 94 1999 2102 2111
    • (1999) Blood , vol.94 , pp. 2102-2111
    • Jing, Y.1    Dai, J.2    Chalmers-Redman, R.M.3    Tatton, W.G.4    Waxman, S.5
  • 24
    • 84875716554 scopus 로고    scopus 로고
    • Principles in redox signaling: From chemistry to functional significance
    • A. Bindoli, and M.P. Rigobello Principles in redox signaling: from chemistry to functional significance Antioxid. Redox Signal. 18 2013 1557 1593
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 1557-1593
    • Bindoli, A.1    Rigobello, M.P.2
  • 25
    • 84867711090 scopus 로고    scopus 로고
    • Thioredoxin system in cell death progression
    • J. Lu, and A. Holmgren Thioredoxin system in cell death progression Antioxid. Redox Signal. 17 2012 1738 1747
    • (2012) Antioxid. Redox Signal. , vol.17 , pp. 1738-1747
    • Lu, J.1    Holmgren, A.2
  • 26
    • 84868328588 scopus 로고    scopus 로고
    • Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose
    • Y. Du, H. Zhang, J. Lu, and A. Holmgren Glutathione and glutaredoxin act as a backup of human thioredoxin reductase 1 to reduce thioredoxin 1 preventing cell death by aurothioglucose J. Biol. Chem. 287 2012 38210 38219
    • (2012) J. Biol. Chem. , vol.287 , pp. 38210-38219
    • Du, Y.1    Zhang, H.2    Lu, J.3    Holmgren, A.4
  • 27
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
    • L. Zhong, E.S. Arnér, and A. Holmgren Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence Proc. Natl. Acad. Sci. USA 97 2000 5854 5859
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arnér, E.S.2    Holmgren, A.3
  • 29
    • 58149352993 scopus 로고    scopus 로고
    • Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy
    • K.F. Tonissen, and G.D. Trapani Thioredoxin system inhibitors as mediators of apoptosis for cancer therapy Mol. Nutr. Food Res. 53 2009 87 103
    • (2009) Mol. Nutr. Food Res. , vol.53 , pp. 87-103
    • Tonissen, K.F.1    Trapani, G.D.2
  • 30
    • 34548067718 scopus 로고    scopus 로고
    • Thioredoxin signaling as a target for cancer therapy
    • G. Powis, and D.L. Kirkpatrick Thioredoxin signaling as a target for cancer therapy Curr. Opin. Pharmacol. 7 2007 392 397
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 392-397
    • Powis, G.1    Kirkpatrick, D.L.2
  • 31
    • 33751181030 scopus 로고    scopus 로고
    • On the potential of thioredoxin reductase inhibitors for cancer therapy
    • S. Urig, and K. Becker On the potential of thioredoxin reductase inhibitors for cancer therapy Semin. Cancer Biol. 16 2006 452 465
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 452-465
    • Urig, S.1    Becker, K.2
  • 32
    • 0242277285 scopus 로고    scopus 로고
    • The thioredoxin system - From science to clinic
    • S. Gromer, S. Urig, and K. Becker The thioredoxin system - from science to clinic Med. Res. Rev. 24 2004 40 89
    • (2004) Med. Res. Rev. , vol.24 , pp. 40-89
    • Gromer, S.1    Urig, S.2    Becker, K.3
  • 36
    • 0030499036 scopus 로고
    • Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia
    • M. Berggren, A. Gallegos, J. Gasdaska, P. Gasdaska, J. Warneke, and G. Powis Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia Anticancer Res. 16 1995 3459 3466
    • (1995) Anticancer Res. , vol.16 , pp. 3459-3466
    • Berggren, M.1    Gallegos, A.2    Gasdaska, J.3    Gasdaska, P.4    Warneke, J.5    Powis, G.6
  • 38
    • 21644477778 scopus 로고    scopus 로고
    • Thioredoxin reductase is irreversibly modified by curcumin a novel molecular mechanism for its anticancer activity
    • J. Fang, J. Lu, and A. Holmgren Thioredoxin reductase is irreversibly modified by curcumin a novel molecular mechanism for its anticancer activity J. Biol. Chem. 280 2005 25284 25290
    • (2005) J. Biol. Chem. , vol.280 , pp. 25284-25290
    • Fang, J.1    Lu, J.2    Holmgren, A.3
  • 39
    • 33244472848 scopus 로고    scopus 로고
    • Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo
    • J., Fang, and A. Holmgren Inhibition of thioredoxin and thioredoxin reductase by 4-hydroxy-2-nonenal in vitro and in vivo J. Am. Chem. Soc. 128 2006 1879 1885
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 1879-1885
    • Fang, J.1    Holmgren, A.2
  • 41
    • 84884687097 scopus 로고    scopus 로고
    • Identification of Michael acceptor-centric pharmacophores with substituents that yield strong thioredoxin reductase inhibitory character correlated to antiproliferative activity
    • F.-F. Gan, K.K. Kaminska, H. Yang, C.-Y. Liew, P.-C. Leow, C.-L. So, L.N. Tu, A. Roy, C.-W. Yap, and T.-S. Kang Identification of Michael acceptor-centric pharmacophores with substituents that yield strong thioredoxin reductase inhibitory character correlated to antiproliferative activity Antioxid. Redox Signal. 19 2013 1149 1165
    • (2013) Antioxid. Redox Signal. , vol.19 , pp. 1149-1165
    • Gan, F.-F.1    Kaminska, K.K.2    Yang, H.3    Liew, C.-Y.4    Leow, P.-C.5    So, C.-L.6    Tu, L.N.7    Roy, A.8    Yap, C.-W.9    Kang, T.-S.10
  • 42
    • 84884843703 scopus 로고    scopus 로고
    • A diterpenoid derivate compound targets selenocysteine of thioredoxin reductases and induces Bax/Bak-independent apoptosis
    • J. Liu, C. Mu, W. Yue, J. Li, B. Ma, L. Zhao, L. Liu, Q. Chen, C. Yan, and H. Liu A diterpenoid derivate compound targets selenocysteine of thioredoxin reductases and induces Bax/Bak-independent apoptosis Free Radic. Biol. Med. 63 2013 485 494
    • (2013) Free Radic. Biol. Med. , vol.63 , pp. 485-494
    • Liu, J.1    Mu, C.2    Yue, W.3    Li, J.4    Ma, B.5    Zhao, L.6    Liu, L.7    Chen, Q.8    Yan, C.9    Liu, H.10
  • 43
    • 84893502890 scopus 로고    scopus 로고
    • Gambogic acid induces apoptosis in hepatocellular carcinoma SMMC-7721 cells by targeting cytosolic thioredoxin reductase
    • D. Duan, B. Zhang, J. Yao, Y. Liu, J. Sun, C. Ge, S. Peng, and J. Fang Gambogic acid induces apoptosis in hepatocellular carcinoma SMMC-7721 cells by targeting cytosolic thioredoxin reductase Free Radic. Biol. Med. 69 2014 15 25
    • (2014) Free Radic. Biol. Med. , vol.69 , pp. 15-25
    • Duan, D.1    Zhang, B.2    Yao, J.3    Liu, Y.4    Sun, J.5    Ge, C.6    Peng, S.7    Fang, J.8
  • 44
    • 55949095821 scopus 로고    scopus 로고
    • Modulation of anti-apoptotic and survival pathways by curcumin as a strategy to induce apoptosis in cancer cells
    • S. Reuter, S. Eifes, M. Dicato, B.B. Aggarwal, and M. Diederich Modulation of anti-apoptotic and survival pathways by curcumin as a strategy to induce apoptosis in cancer cells Biochem. Pharmacol. 76 2008 1340 1351
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1340-1351
    • Reuter, S.1    Eifes, S.2    Dicato, M.3    Aggarwal, B.B.4    Diederich, M.5
  • 45
    • 53449094405 scopus 로고    scopus 로고
    • Anticancer and carcinogenic properties of curcumin: Considerations for its clinical development as a cancer chemopreventive and chemotherapeutic agent
    • references therein
    • M. López-Lázaro Anticancer and carcinogenic properties of curcumin: considerations for its clinical development as a cancer chemopreventive and chemotherapeutic agent Mol. Nutr. Food Res. 52 2008 S103 S127 and references therein
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. S103-S127
    • López-Lázaro, M.1
  • 46
    • 40949089329 scopus 로고    scopus 로고
    • Mitochondria reactive oxygen species affect sensitivity to curcumin-induced apoptosis
    • N. Hail Jr Mitochondria reactive oxygen species affect sensitivity to curcumin-induced apoptosis Free Radic. Biol. Med. 44 2008 1382 1393
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1382-1393
    • Hail, Jr.N.1
  • 48
    • 33747880401 scopus 로고    scopus 로고
    • Curcumin mediates ceramide generation via the de novo pathway in colon cancer cells
    • M. Moussavi, K. Assi, A. Gómez-Muñoz, and B. Salh Curcumin mediates ceramide generation via the de novo pathway in colon cancer cells Carcinogenesis 27 2006 1636 1644
    • (2006) Carcinogenesis , vol.27 , pp. 1636-1644
    • Moussavi, M.1    Assi, K.2    Gómez-Muñoz, A.3    Salh, B.4
  • 49
    • 33845945097 scopus 로고    scopus 로고
    • Curcumin-induced apoptosis of human colon cancer colo 205 cells through the production of ROS, Ca2+ and the activation of caspase-3
    • C.-C. Su, J.-G. Lin, T.-M. Li, J.-G. Chung, J.-S. Yang, S.-W. Ip, W.-C. Lin, and G.-W. Chen Curcumin-induced apoptosis of human colon cancer colo 205 cells through the production of ROS, Ca2+ and the activation of caspase-3 Anticancer Res. 26 2006 4379 4389
    • (2006) Anticancer Res. , vol.26 , pp. 4379-4389
    • Su, C.-C.1    Lin, J.-G.2    Li, T.-M.3    Chung, J.-G.4    Yang, J.-S.5    Ip, S.-W.6    Lin, W.-C.7    Chen, G.-W.8
  • 50
    • 15744370742 scopus 로고    scopus 로고
    • Curcumin-induced histone hypoacetylation: The role of reactive oxygen species
    • J. Kang, J. Chen, Y. Shi, J. Jia, and Y. Zhang Curcumin-induced histone hypoacetylation: the role of reactive oxygen species Biochem. Pharmacol. 69 2005 1205 1213
    • (2005) Biochem. Pharmacol. , vol.69 , pp. 1205-1213
    • Kang, J.1    Chen, J.2    Shi, Y.3    Jia, J.4    Zhang, Y.5
  • 51
    • 8844261849 scopus 로고    scopus 로고
    • Curcumin-induced GADD153 gene up-regulation in human colon cancer cells
    • D.W. Scott, and G. Loo Curcumin-induced GADD153 gene up-regulation in human colon cancer cells Carcinogenesis 25 2004 2155 2164
    • (2004) Carcinogenesis , vol.25 , pp. 2155-2164
    • Scott, D.W.1    Loo, G.2
  • 52
    • 0042169007 scopus 로고    scopus 로고
    • Molecular mechanisms of curcumin-induced cytotoxicity: Induction of apoptosis through generation of reactive oxygen species, down-regulation of Bcl-XL and IAP, the release of cytochrome c and inhibition of Akt
    • J.-H. Woo, Y.-H. Kim, Y.-J. Choi, D.-G. Kim, K.-S. Lee, J.H. Bae, J.-S. Chang, Y.-J. Jeong, Y.H. Lee, and J.-W. Park Molecular mechanisms of curcumin-induced cytotoxicity: induction of apoptosis through generation of reactive oxygen species, down-regulation of Bcl-XL and IAP, the release of cytochrome c and inhibition of Akt Carcinogenesis 24 2003 1199 1208
    • (2003) Carcinogenesis , vol.24 , pp. 1199-1208
    • Woo, J.-H.1    Kim, Y.-H.2    Choi, Y.-J.3    Kim, D.-G.4    Lee, K.-S.5    Bae, J.H.6    Chang, J.-S.7    Jeong, Y.-J.8    Lee, Y.H.9    Park, J.-W.10
  • 53
    • 0032815637 scopus 로고    scopus 로고
    • Curcumin mediated apoptosis in AK-5 tumor cells involves the production of reactive oxygen intermediates
    • S. Bhaumik, R. Anjum, N. Rangaraj, B. Pardhasaradhi, and A. Khar Curcumin mediated apoptosis in AK-5 tumor cells involves the production of reactive oxygen intermediates FEBS Lett. 456 1999 311 314
    • (1999) FEBS Lett. , vol.456 , pp. 311-314
    • Bhaumik, S.1    Anjum, R.2    Rangaraj, N.3    Pardhasaradhi, B.4    Khar, A.5
  • 55
    • 84934436443 scopus 로고    scopus 로고
    • Highly active anticancer curcumin analogues
    • references therein
    • C.A. Mosley, D.C. Liotta, and J.P. Snyder Highly active anticancer curcumin analogues Adv. Exp. Med. Biol. 595 2007 77 103 and references therein
    • (2007) Adv. Exp. Med. Biol. , vol.595 , pp. 77-103
    • Mosley, C.A.1    Liotta, D.C.2    Snyder, J.P.3
  • 57
    • 79957533842 scopus 로고    scopus 로고
    • Synthesis of 86 species of 1, 5-diaryl-3-oxo-1, 4-pentadienes analogs of curcumin can yield a good lead in vivo
    • C. Kudo, H. Yamakoshi, A. Sato, H. Nanjo, H. Ohori, C. Ishioka, Y. Iwabuchi, and H. Shibata Synthesis of 86 species of 1, 5-diaryl-3-oxo-1, 4-pentadienes analogs of curcumin can yield a good lead in vivo BMC Pharmacol 11 4 2011 http://dx.doi.org/10.1186/1471-2210-11-4
    • (2011) BMC Pharmacol , vol.11 , Issue.4
    • Kudo, C.1    Yamakoshi, H.2    Sato, A.3    Nanjo, H.4    Ohori, H.5    Ishioka, C.6    Iwabuchi, Y.7    Shibata, H.8
  • 58
    • 79958116796 scopus 로고    scopus 로고
    • A novel monocarbonyl analogue of curcumin, (1 E, 4 E)-1, 5-bis (2, 3-dimethoxyphenyl) penta-1, 4-dien-3-one, induced cancer cell H460 apoptosis via activation of endoplasmic reticulum stress signaling pathway
    • Y. Wang, J. Xiao, H. Zhou, S. Yang, X. Wu, C. Jiang, Y. Zhao, D. Liang, X. Li, and G. Liang A novel monocarbonyl analogue of curcumin, (1 E, 4 E)-1, 5-bis (2, 3-dimethoxyphenyl) penta-1, 4-dien-3-one, induced cancer cell H460 apoptosis via activation of endoplasmic reticulum stress signaling pathway J. Med. Chem. 54 2011 3768 3778
    • (2011) J. Med. Chem. , vol.54 , pp. 3768-3778
    • Wang, Y.1    Xiao, J.2    Zhou, H.3    Yang, S.4    Wu, X.5    Jiang, C.6    Zhao, Y.7    Liang, D.8    Li, X.9    Liang, G.10
  • 60
    • 62149086696 scopus 로고    scopus 로고
    • Exploration and synthesis of curcumin analogues with improved structural stability both in vitro and in vivo as cytotoxic agents
    • G. Liang, L. Shao, Y. Wang, C. Zhao, Y. Chu, J. Xiao, Y. Zhao, X. Li, and S. Yang Exploration and synthesis of curcumin analogues with improved structural stability both in vitro and in vivo as cytotoxic agents Bioorg. Med. Chem. 17 2009 2623 2631
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 2623-2631
    • Liang, G.1    Shao, L.2    Wang, Y.3    Zhao, C.4    Chu, Y.5    Xiao, J.6    Zhao, Y.7    Li, X.8    Yang, S.9
  • 63
    • 84865259421 scopus 로고    scopus 로고
    • CuII ions and the stilbene-chroman hybrid with a catechol moiety synergistically induced DNA damage, and cell cycle arrest and apoptosis of HepG2 cells: An interesting acid/base-promoted prooxidant reaction
    • G.Y. Liu, J. Yang, F. Dai, W.J. Yan, Q. Wang, X.Z. Li, D.J. Ding, X.Y. Cao, and B. Zhou CuII ions and the stilbene-chroman hybrid with a catechol moiety synergistically induced DNA damage, and cell cycle arrest and apoptosis of HepG2 cells: an interesting acid/base-promoted prooxidant reaction Chem. Eur. J 18 2012 11100 11106
    • (2012) Chem. Eur. J , vol.18 , pp. 11100-11106
    • Liu, G.Y.1    Yang, J.2    Dai, F.3    Yan, W.J.4    Wang, Q.5    Li, X.Z.6    Ding, D.J.7    Cao, X.Y.8    Zhou, B.9
  • 64
    • 71549158194 scopus 로고    scopus 로고
    • Hydroxycinnamic acids as DNA-cleaving agents in the presence of CuII Ions: Mechanism, structure-activity relationship, and biological implications
    • G.J. Fan, X.L. Jin, Y.P. Qian, Q. Wang, R.T. Yang, F. Dai, J.J. Tang, Y.J. Shang, L.X. Cheng, J. Yang, and B. Zhou Hydroxycinnamic acids as DNA-cleaving agents in the presence of CuII Ions: mechanism, structure-activity relationship, and biological implications Chem. Eur. J 15 2009 12889 12899
    • (2009) Chem. Eur. J , vol.15 , pp. 12889-12899
    • Fan, G.J.1    Jin, X.L.2    Qian, Y.P.3    Wang, Q.4    Yang, R.T.5    Dai, F.6    Tang, J.J.7    Shang, Y.J.8    Cheng, L.X.9    Yang, J.10    Zhou, B.11
  • 65
    • 33751509078 scopus 로고    scopus 로고
    • DNA damage induced by resveratrol and its synthetic analogues in the presence of Cu (II) ions: Mechanism and structure-activity relationship
    • L.-F. Zheng, Q.-Y. Wei, Y.-J. Cai, J.-G. Fang, B. Zhou, L. Yang, and Z.-L. Liu DNA damage induced by resveratrol and its synthetic analogues in the presence of Cu (II) ions: mechanism and structure-activity relationship Free Radic. Biol. Med. 41 2006 1807 1816
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1807-1816
    • Zheng, L.-F.1    Wei, Q.-Y.2    Cai, Y.-J.3    Fang, J.-G.4    Zhou, B.5    Yang, L.6    Liu, Z.-L.7
  • 66
    • 84878384095 scopus 로고    scopus 로고
    • Ortho-dihydroxychalcones as cupric ion-dependent prooxidants: Activity and mechanisms
    • Q. Wang, Y.-P. Qian, F. Dai, D.-L. Lu, W.-J. Yan, Y. Chen, and B. Zhou Ortho-dihydroxychalcones as cupric ion-dependent prooxidants: activity and mechanisms Food Chem. 141 2013 1259 1266
    • (2013) Food Chem. , vol.141 , pp. 1259-1266
    • Wang, Q.1    Qian, Y.-P.2    Dai, F.3    Lu, D.-L.4    Yan, W.-J.5    Chen, Y.6    Zhou, B.7
  • 68
  • 71
    • 43049141516 scopus 로고    scopus 로고
    • The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: Two new functionals and systematic testing of four M06-class functionals and 12 other functionals
    • Y. Zhao, and D.G. Truhlar The M06 suite of density functionals for main group thermochemistry, thermochemical kinetics, noncovalent interactions, excited states, and transition elements: two new functionals and systematic testing of four M06-class functionals and 12 other functionals Theor. Chem. Acc. 120 2008 215 241
    • (2008) Theor. Chem. Acc. , vol.120 , pp. 215-241
    • Zhao, Y.1    Truhlar, D.G.2
  • 73
    • 84892164605 scopus 로고    scopus 로고
    • Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells
    • L. Zhang, D. Duan, Y. Liu, C. Ge, X. Cui, J. Sun, and J. Fang Highly selective off-on fluorescent probe for imaging thioredoxin reductase in living cells J. Am. Chem. Soc. 136 2013 226 233
    • (2013) J. Am. Chem. Soc. , vol.136 , pp. 226-233
    • Zhang, L.1    Duan, D.2    Liu, Y.3    Ge, C.4    Cui, X.5    Sun, J.6    Fang, J.7
  • 74
    • 0027946067 scopus 로고
    • A microtiter plate assay for total glutathione and glutathione disulfide contents in cultured/isolated cells: Performance study of a new miniaturized protocol
    • C. Vandeputte, I. Guizon, I. Genestie-Denis, B. Vannier, and G. Lorenzon A microtiter plate assay for total glutathione and glutathione disulfide contents in cultured/isolated cells: performance study of a new miniaturized protocol Cell Biol. Toxicol. 10 1994 415 421
    • (1994) Cell Biol. Toxicol. , vol.10 , pp. 415-421
    • Vandeputte, C.1    Guizon, I.2    Genestie-Denis, I.3    Vannier, B.4    Lorenzon, G.5
  • 75
    • 0001519365 scopus 로고    scopus 로고
    • Measurement of intracellular calcium ions by flow cytometry
    • C.H. June, R. Abe, and P.S. Rabinovitch Measurement of intracellular calcium ions by flow cytometry Curr. Protoc. Cytometry 2 9.8 2001 9.8.1 9.8.19
    • (2001) Curr. Protoc. Cytometry , vol.2 , Issue.8-9 , pp. 981-9819
    • June, C.H.1    Abe, R.2    Rabinovitch, P.S.3
  • 76
    • 0025127633 scopus 로고
    • Determination of aldehydic lipid peroxidation products: Malonaldehyde and 4-hydroxynonenal
    • H. Esterbauer, and K.H. Cheeseman Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal Method. Enzymol 186 1990 407 421
    • (1990) Method. Enzymol , vol.186 , pp. 407-421
    • Esterbauer, H.1    Cheeseman, K.H.2
  • 77
    • 84884726738 scopus 로고    scopus 로고
    • Curcumin analog 1, 5-bis (2-trifluoromethylphenyl)-1, 4-pentadien-3-one exhibits enhanced ability on Nrf2 activation and protection against acrolein-induced ARPE-19 cell toxicity
    • Y. Li, X. Zou, K. Cao, J. Xu, T. Yue, F. Dai, B. Zhou, W. Lu, Z. Feng, and J. Liu Curcumin analog 1, 5-bis (2-trifluoromethylphenyl)-1, 4-pentadien-3-one exhibits enhanced ability on Nrf2 activation and protection against acrolein-induced ARPE-19 cell toxicity Toxicol. Appl. Pharmacol. 272 2013 726 735
    • (2013) Toxicol. Appl. Pharmacol. , vol.272 , pp. 726-735
    • Li, Y.1    Zou, X.2    Cao, K.3    Xu, J.4    Yue, T.5    Dai, F.6    Zhou, B.7    Lu, W.8    Feng, Z.9    Liu, J.10
  • 78
    • 0035853101 scopus 로고    scopus 로고
    • Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups
    • A.T. Dinkova-Kostova, M.A. Massiah, R.E. Bozak, R.J. Hicks, and P. Talalay Potency of Michael reaction acceptors as inducers of enzymes that protect against carcinogenesis depends on their reactivity with sulfhydryl groups Proc. Natl. Acad. Sci. USA 98 2001 3404 3409
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3404-3409
    • Dinkova-Kostova, A.T.1    Massiah, M.A.2    Bozak, R.E.3    Hicks, R.J.4    Talalay, P.5
  • 81
    • 84919629589 scopus 로고    scopus 로고
    • Moving free radical and redox biology ahead in the next decade(s)
    • G.R. Buettner Moving free radical and redox biology ahead in the next decade(s) Free Radic. Biol. Med. 78 2015 236 238
    • (2015) Free Radic. Biol. Med. , vol.78 , pp. 236-238
    • Buettner, G.R.1
  • 82
  • 83
    • 49449097238 scopus 로고    scopus 로고
    • The many roles for fluorine in medicinal chemistry
    • W.K. Hagmann The many roles for fluorine in medicinal chemistry J. Med. Chem. 51 2008 4359 4369
    • (2008) J. Med. Chem. , vol.51 , pp. 4359-4369
    • Hagmann, W.K.1
  • 84
    • 83055177179 scopus 로고    scopus 로고
    • Trifluoromethylation of arenes and heteroarenes by means of photoredox catalysis
    • D.A. Nagib, and D.W. MacMillan Trifluoromethylation of arenes and heteroarenes by means of photoredox catalysis Nature 480 2011 224 228
    • (2011) Nature , vol.480 , pp. 224-228
    • Nagib, D.A.1    Macmillan, D.W.2
  • 85
    • 0033862305 scopus 로고    scopus 로고
    • A threshold concept for cancer therapy
    • Q. Kong, J. Beel, and K. Lillehei A threshold concept for cancer therapy Med. Hypotheses 55 2000 29 35
    • (2000) Med. Hypotheses , vol.55 , pp. 29-35
    • Kong, Q.1    Beel, J.2    Lillehei, K.3
  • 87
    • 84861494386 scopus 로고    scopus 로고
    • Synthesis, chemical reactivity as Michael acceptors, and biological potency of monocyclic cyanoenones, novel and highly potent anti-inflammatory and cytoprotective agents (1)
    • S. Zheng, Y. Santosh Laxmi, E. David, A.T. Dinkova-Kostova, K.H. Shiavoni, Y. Ren, Y. Zheng, I. Trevino, R. Bumeister, and I. Ojima Synthesis, chemical reactivity as Michael acceptors, and biological potency of monocyclic cyanoenones, novel and highly potent anti-inflammatory and cytoprotective agents (1) J. Med. Chem. 55 2012 4837 4846
    • (2012) J. Med. Chem. , vol.55 , pp. 4837-4846
    • Zheng, S.1    Santosh Laxmi, Y.2    David, E.3    Dinkova-Kostova, A.T.4    Shiavoni, K.H.5    Ren, Y.6    Zheng, Y.7    Trevino, I.8    Bumeister, R.9    Ojima, I.10
  • 88
    • 84887566303 scopus 로고    scopus 로고
    • Profound methyl effects in drug discovery and a call for new C-H methylation reactions
    • H. Schönherr, and T. Cernak Profound methyl effects in drug discovery and a call for new C-H methylation reactions Angew. Chem. Int. Ed. 52 2013 12256 12267
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 12256-12267
    • Schönherr, H.1    Cernak, T.2
  • 89
    • 0032545445 scopus 로고    scopus 로고
    • Diphenyleneiodonium, an NAD (P) H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production
    • Y. Li, and M.A. Trush Diphenyleneiodonium, an NAD (P) H oxidase inhibitor, also potently inhibits mitochondrial reactive oxygen species production Biochem. Biophys. Res. Commun. 253 1998 295 299
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 295-299
    • Li, Y.1    Trush, M.A.2
  • 90
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • F.Q. Schafer, and G.R. Buettner Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple Free Radic. Biol. Med. 30 2001 1191 1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 91
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiols metabolism
    • D.A. Dickinson, and H.J. Forman Cellular glutathione and thiols metabolism Biochem. Pharmacol. 64 2002 1019 1026
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1019-1026
    • Dickinson, D.A.1    Forman, H.J.2
  • 92
    • 0032531818 scopus 로고    scopus 로고
    • Calcium-a life and death signal
    • M.J. Berridge, M.D. Bootman, and P. Lipp Calcium-a life and death signal Nature 395 1998 645 648
    • (1998) Nature , vol.395 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 93
  • 94
    • 84865407060 scopus 로고    scopus 로고
    • Reversible covalent inhibition of a protein target
    • C.-U. Lee, and T.N. Grossmann Reversible covalent inhibition of a protein target Angew. Chem. Int. Ed. 51 2012 8699 8700
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 8699-8700
    • Lee, C.-U.1    Grossmann, T.N.2


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