메뉴 건너뛰기




Volumn 52, Issue 1, 2009, Pages 117-125

Total synthesis and cytoprotective properties of dykellic acid

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; DYKELLIC ACID DERIVATIVE; NATURAL PRODUCT; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; ALDEHYDE; ALKENE; DYKELLIC ACID; PHOSPHONIC ACID DERIVATIVE; PROPIONIC ACID DERIVATIVE; PYRONE DERIVATIVE;

EID: 59449101668     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm801169s     Document Type: Article
Times cited : (14)

References (110)
  • 1
    • 0142217555 scopus 로고    scopus 로고
    • Apoptosis: Target for novel drugs
    • Alam, J. J. Apoptosis: target for novel drugs. Trends Biotechnol. 2003, 21, 479-483.
    • (2003) Trends Biotechnol , vol.21 , pp. 479-483
    • Alam, J.J.1
  • 2
    • 0038265069 scopus 로고    scopus 로고
    • Recent advances in understanding apoptosis: New therapeutic opportunities in cancer chemotherapy
    • (a) Makin, G.; Dive, C. Recent advances in understanding apoptosis: new therapeutic opportunities in cancer chemotherapy. Trends Mol. Med. 2003, 9, 251-255.
    • (2003) Trends Mol. Med , vol.9 , pp. 251-255
    • Makin, G.1    Dive, C.2
  • 3
    • 33750632135 scopus 로고    scopus 로고
    • Apoptosis in the treatment of cancer: A promise kept?
    • (b) Meng, X. W.; Lee, S. H.; Kaufmann, S. H. Apoptosis in the treatment of cancer: a promise kept? Curr. Opin. Cell Biol. 2006, 18, 668-676.
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 668-676
    • Meng, X.W.1    Lee, S.H.2    Kaufmann, S.H.3
  • 4
    • 33749437310 scopus 로고    scopus 로고
    • Apoptotic cascades as possible targets for inhibiting cell death in Huntington's disease
    • (a) Pattison, L. R.; Kotter, M. R.; Fraga, D.; Bonelli, R. M. Apoptotic cascades as possible targets for inhibiting cell death in Huntington's disease. J. Neurol. 2006, 253, 1137-1142.
    • (2006) J. Neurol , vol.253 , pp. 1137-1142
    • Pattison, L.R.1    Kotter, M.R.2    Fraga, D.3    Bonelli, R.M.4
  • 5
    • 0038205745 scopus 로고    scopus 로고
    • Targeting programmed cell death in neurodegenerative diseases
    • (b) Vila, M.; Przedborski, S. Targeting programmed cell death in neurodegenerative diseases. Nat. Rev. Neurosci. 2003, 4, 365-375.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 365-375
    • Vila, M.1    Przedborski, S.2
  • 6
    • 0037377189 scopus 로고    scopus 로고
    • Prospects for antiapoptotic drug therapy of neurodegenerative diseases
    • Waldmeier, P. C. Prospects for antiapoptotic drug therapy of neurodegenerative diseases. Prog. Neuropsychopharmacol. Biol. Psychiatry 2003, 27, 303-321.
    • (2003) Prog. Neuropsychopharmacol. Biol. Psychiatry , vol.27 , pp. 303-321
    • Waldmeier, P.C.1
  • 7
    • 1242338861 scopus 로고    scopus 로고
    • Interrupting apoptosis in neurode- generative disease: Potential for effective therapy
    • Waldmeier, P. C.; Tatton, W. G. Interrupting apoptosis in neurode- generative disease: potential for effective therapy. Drug Discovery Today 2004, 9, 210-218.
    • (2004) Drug Discovery Today , vol.9 , pp. 210-218
    • Waldmeier, P.C.1    Tatton, W.G.2
  • 9
    • 33847194975 scopus 로고    scopus 로고
    • Kim, H. A.; Blanco, F. J. Cell death and apoptosis in osteoarthritic cartilage. Curr. Drug Targets 2007, 8, 333-345.
    • Kim, H. A.; Blanco, F. J. Cell death and apoptosis in osteoarthritic cartilage. Curr. Drug Targets 2007, 8, 333-345.
  • 10
    • 34548402079 scopus 로고    scopus 로고
    • Programmed death as a therapeutic target to reduce myocardial infarction
    • Webster, K. A. Programmed death as a therapeutic target to reduce myocardial infarction. Trends Pharmacol. Sci. 2007, 28, 492-499.
    • (2007) Trends Pharmacol. Sci , vol.28 , pp. 492-499
    • Webster, K.A.1
  • 11
    • 33745955359 scopus 로고    scopus 로고
    • Therapeutic strategies for the treatment of stroke
    • Green, A. R.; Shuaib, A. Therapeutic strategies for the treatment of stroke. Drug Discovery Today 2006, 11, 681-693.
    • (2006) Drug Discovery Today , vol.11 , pp. 681-693
    • Green, A.R.1    Shuaib, A.2
  • 12
    • 0842281645 scopus 로고    scopus 로고
    • Danial, N. N.; Korsmeyer, S. J. Cell death: critical control points. Cell 2004, 116, 205-219.
    • (a) Danial, N. N.; Korsmeyer, S. J. Cell death: critical control points. Cell 2004, 116, 205-219.
  • 13
    • 0345276414 scopus 로고    scopus 로고
    • Bcl-2- family proteins and the role of mitochondria in apoptosis
    • (b) Kuwana, T.; Newmeyer, D. D. Bcl-2- family proteins and the role of mitochondria in apoptosis. Curr. Qpin. Cell Biol. 2003, 15, 691-699.
    • (2003) Curr. Qpin. Cell Biol , vol.15 , pp. 691-699
    • Kuwana, T.1    Newmeyer, D.D.2
  • 14
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • (a) Ashkenazi, A.; Dixit, V. M. Death receptors: signaling and modulation. Science 1998, 281, 1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 17
    • 20344393200 scopus 로고    scopus 로고
    • Death receptor signals to mitochondria
    • (a) Khosravi-Far, R.; Esposti, M. D. Death receptor signals to mitochondria. Cancer Biol. Ther. 2004, 3, 1051-1057.
    • (2004) Cancer Biol. Ther , vol.3 , pp. 1051-1057
    • Khosravi-Far, R.1    Esposti, M.D.2
  • 18
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • (b) Kroemer, G.; Reed, J. C. Mitochondrial control of cell death. Nat. Med. 2000, 6, 513-519.
    • (2000) Nat. Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 19
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • (a) Fischer, U.; Janicke, R. U.; Schulze-Osthoff, K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 2003, 10, 76-100.
    • (2003) Cell Death Differ , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 21
    • 5344245984 scopus 로고    scopus 로고
    • Dipeptidyl aspartyl fluoromethylketones as potent caspase inhibitors: SAR of the N-protecting group
    • (a) Cai, S. X.; Guan, L.; Jia, S.; Wang, Y.; Yang, W.; Tseng, B.; Drewe, J. Dipeptidyl aspartyl fluoromethylketones as potent caspase inhibitors: SAR of the N-protecting group. Bioorg. Med. Chem. Lett. 2004, 14, 5295-5300.
    • (2004) Bioorg. Med. Chem. Lett , vol.14 , pp. 5295-5300
    • Cai, S.X.1    Guan, L.2    Jia, S.3    Wang, Y.4    Yang, W.5    Tseng, B.6    Drewe, J.7
  • 22
    • 0034669213 scopus 로고    scopus 로고
    • Protection against TNF-induced liver parenchymal cell apoptosis during endotoxemia by a novel caspase inhibitor in mice
    • (b) Jaeschke, H.; Farhood, A.; Cai, S. X.; Tseng, B. Y.; Bajt, M. L. Protection against TNF-induced liver parenchymal cell apoptosis during endotoxemia by a novel caspase inhibitor in mice. Toxicol. Appl. Pharmacol. 2000, 169, 77-83.
    • (2000) Toxicol. Appl. Pharmacol , vol.169 , pp. 77-83
    • Jaeschke, H.1    Farhood, A.2    Cai, S.X.3    Tseng, B.Y.4    Bajt, M.L.5
  • 23
    • 33845666247 scopus 로고    scopus 로고
    • Plantainoside D protects adriamycin-induced apoptosis in H9c2 cardiac muscle cells via the inhibition of ROS generation and NF-kappaB activation
    • (a) Kim, D. S.; Woo, E. R.; Chae, S. W.; Ha, K. C.; Lee, G. H.; Hong, S. T.; Kwon, D. Y.; Kim, M. S.; Jung, Y. K.; Kim, H. M.; Kim, H. K.;Kim, H. R.; Chae, H. J. Plantainoside D protects adriamycin-induced apoptosis in H9c2 cardiac muscle cells via the inhibition of ROS generation and NF-kappaB activation. Life Sci. 2007, 80, 314-323.
    • (2007) Life Sci , vol.80 , pp. 314-323
    • Kim, D.S.1    Woo, E.R.2    Chae, S.W.3    Ha, K.C.4    Lee, G.H.5    Hong, S.T.6    Kwon, D.Y.7    Kim, M.S.8    Jung, Y.K.9    Kim, H.M.10    Kim, H.K.11    Kim, H.R.12    Chae, H.J.13
  • 24
    • 33846249635 scopus 로고    scopus 로고
    • Pyruvate protects mitochondria from oxidative stress in human neuroblastoma SK-N-SH cells
    • (b) Wang, X.; Perez, E.; Liu, R.; Yan, L. J.; Mallet, R. T.; Yang, S. H. Pyruvate protects mitochondria from oxidative stress in human neuroblastoma SK-N-SH cells. Brain Res. 2007, 1132, 1-9.
    • (2007) Brain Res , vol.1132 , pp. 1-9
    • Wang, X.1    Perez, E.2    Liu, R.3    Yan, L.J.4    Mallet, R.T.5    Yang, S.H.6
  • 26
    • 38149033055 scopus 로고    scopus 로고
    • The 2007 Feinberg lecture: A new road map for neuroprotection
    • (a) Donnan, G. A. The 2007 Feinberg lecture: a new road map for neuroprotection. Stroke 2008, 39, 242-248.
    • (2008) Stroke , vol.39 , pp. 242-248
    • Donnan, G.A.1
  • 27
    • 34249942190 scopus 로고    scopus 로고
    • Future of neuroprotection for acute stroke: In the aftermath of the SAINT trials
    • (b) Savitz, S. I.; Fisher, M. Future of neuroprotection for acute stroke: in the aftermath of the SAINT trials. Ann. Neurol. 2007, 61, 396-402.
    • (2007) Ann. Neurol , vol.61 , pp. 396-402
    • Savitz, S.I.1    Fisher, M.2
  • 28
    • 31944440565 scopus 로고    scopus 로고
    • Jiang, Z. G.; Lu, X. C.; Nelson, V.; Yang, X.; Pan, W.; Chen, R. W.; Lebowitz, M. S.; Almassian, B.; Tortella, F. C.; Brady, R. O.; Ghanbari, H. A. A multifunctional cytoprotective agent that reduces neurodegeneration after ischemia. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 1581-1586.
    • Jiang, Z. G.; Lu, X. C.; Nelson, V.; Yang, X.; Pan, W.; Chen, R. W.; Lebowitz, M. S.; Almassian, B.; Tortella, F. C.; Brady, R. O.; Ghanbari, H. A. A multifunctional cytoprotective agent that reduces neurodegeneration after ischemia. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 1581-1586.
  • 29
    • 33845472476 scopus 로고    scopus 로고
    • Caspase inhibitors: Viral, cellular and chemical
    • Callus, B. A.; Vaux, D. L. Caspase inhibitors: viral, cellular and chemical. Cell Death Differ. 2007, 14, 73-78.
    • (2007) Cell Death Differ , vol.14 , pp. 73-78
    • Callus, B.A.1    Vaux, D.L.2
  • 31
    • 33645056953 scopus 로고    scopus 로고
    • Caspase inhibitors: A pharmaceutical industry perspective
    • (b) Linton, S. D. Caspase inhibitors: a pharmaceutical industry perspective. Curr. Top. Med. Chem. 2005, 5, 1697-1717.
    • (2005) Curr. Top. Med. Chem , vol.5 , pp. 1697-1717
    • Linton, S.D.1
  • 33
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • (b) Youle, R. J.; Strasser, A. The BCL-2 protein family: opposing activities that mediate cell death. Nat. Rev. Mol. Cell Biol. 2008, 9, 47-59.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 34
    • 0036479015 scopus 로고    scopus 로고
    • Mitochondrial involvement in the point of no return in neuronal apoptosis
    • (a) Chang, L. K.; Putcha, G. V.; Deshmukh, M.; Johnson, E. M., Jr. Mitochondrial involvement in the point of no return in neuronal apoptosis. Biochimie 2002, 84, 223-231.
    • (2002) Biochimie , vol.84 , pp. 223-231
    • Chang, L.K.1    Putcha, G.V.2    Deshmukh, M.3    Johnson Jr., E.M.4
  • 35
    • 37149039846 scopus 로고    scopus 로고
    • Apoptosis commitment-translating survival signals into decisions on mitochondria
    • (b) Keeble, J. A.; Gilmore, A. P. Apoptosis commitment-translating survival signals into decisions on mitochondria. Cell Res. 2007, 17, 976-984.
    • (2007) Cell Res , vol.17 , pp. 976-984
    • Keeble, J.A.1    Gilmore, A.P.2
  • 36
    • 0037427479 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: An introduction
    • Kroemer, G. Mitochondrial control of apoptosis: an introduction. Biochem. Biophys. Res. Commun. 2003, 304, 433-435.
    • (2003) Biochem. Biophys. Res. Commun , vol.304 , pp. 433-435
    • Kroemer, G.1
  • 37
    • 0033578727 scopus 로고    scopus 로고
    • Dykellic acid, a novel apoptosis inhibitor from Westerdykella multispora F50733
    • Lee, H.-J.; Lee, C.-H.; Chung, M.-C.; Chun, H.-K.; Rhee, J.-S.; Kho, Y.-H. Dykellic acid, a novel apoptosis inhibitor from Westerdykella multispora F50733. Tetrahedron Lett. 1999, 40, 6949-6950.
    • (1999) Tetrahedron Lett , vol.40 , pp. 6949-6950
    • Lee, H.-J.1    Lee, C.-H.2    Chung, M.-C.3    Chun, H.-K.4    Rhee, J.-S.5    Kho, Y.-H.6
  • 39
    • 0038407256 scopus 로고    scopus 로고
    • Dykellic acid inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting nuclear factor kappa B transcriptional activity
    • Woo, J. H.; Park, J. W.; Lee, S. H.; Kim, Y. H.; Lee, I. K.; Gabrielson, E.; Lee, S. H.; Lee, H. J.; Kho, Y. H.; Kwon, T. K. Dykellic acid inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting nuclear factor kappa B transcriptional activity. Cancer Res. 2003, 63, 3430-3434.
    • (2003) Cancer Res , vol.63 , pp. 3430-3434
    • Woo, J.H.1    Park, J.W.2    Lee, S.H.3    Kim, Y.H.4    Lee, I.K.5    Gabrielson, E.6    Lee, S.H.7    Lee, H.J.8    Kho, Y.H.9    Kwon, T.K.10
  • 41
    • 0001848341 scopus 로고
    • The Wittig olefination reaction and modifications involving phosphoryl-stabilized carbanions. Stereochemistry, mechanism, and selected synthetic aspects
    • Rev
    • (a) Maryanoff, B. E.; Reitz, A. B. The Wittig olefination reaction and modifications involving phosphoryl-stabilized carbanions. Stereochemistry, mechanism, and selected synthetic aspects. Chetm. Rev. 1989, 89, 863-927.
    • (1989) Chetm , vol.89 , pp. 863-927
    • Maryanoff, B.E.1    Reitz, A.B.2
  • 42
    • 33646066450 scopus 로고
    • Direct synthesis of Z-unsaturated esters. A useful modification of the Horner-Emmons olefination
    • (b) Still, W. C.; Gennari, C. Direct synthesis of Z-unsaturated esters. A useful modification of the Horner-Emmons olefination. Tetrahedron Lett. 1983, 24, 4405-4408.
    • (1983) Tetrahedron Lett , vol.24 , pp. 4405-4408
    • Still, W.C.1    Gennari, C.2
  • 43
    • 0037366617 scopus 로고    scopus 로고
    • Recent advances in the Baylis-Hillman reaction and applications
    • Basavaiah, D.; Rao, A. J.; Satyanarayana, T. Recent advances in the Baylis-Hillman reaction and applications. Chem. Rev. 2003,103, 811-892.
    • (2003) Chem. Rev , vol.103 , pp. 811-892
    • Basavaiah, D.1    Rao, A.J.2    Satyanarayana, T.3
  • 44
    • 4744362831 scopus 로고
    • Synthetic potential of the tertiary-amine- catalysed reaction of activated vinyl carbanions with aldehydes
    • Drewes, S. E.; Roos, G. H. P. Synthetic potential of the tertiary-amine- catalysed reaction of activated vinyl carbanions with aldehydes. Tetrahedron 1988, 44, 4653-4670.
    • (1988) Tetrahedron , vol.44 , pp. 4653-4670
    • Drewes, S.E.1    Roos, G.H.P.2
  • 45
    • 84985531959 scopus 로고
    • Preparation of2-(1-hydroxyalkyl)acrylic esters; simple three-step synthesis of mikanecic acid
    • Hoffmann, H. M. R.; Rabe, J. Preparation of2-(1-hydroxyalkyl)acrylic esters; simple three-step synthesis of mikanecic acid. Angew. Chem., Int. Ed. Engl. 1983, 22, 795-796.
    • (1983) Angew. Chem., Int. Ed. Engl , vol.22 , pp. 795-796
    • Hoffmann, H.M.R.1    Rabe, J.2
  • 46
    • 4644231912 scopus 로고    scopus 로고
    • Acrylamide in the Baylis- Hillman reaction: Expanded reaction scope and the unexpected superiority of DABCO over more basic tertiary amine catalysts
    • (a) Faltin, C.; Fleming, E. M.; Connon, S. J. Acrylamide in the Baylis- Hillman reaction: expanded reaction scope and the unexpected superiority of DABCO over more basic tertiary amine catalysts. J. Org. Chem. 2004, 69, 6496-6499.
    • (2004) J. Org. Chem , vol.69 , pp. 6496-6499
    • Faltin, C.1    Fleming, E.M.2    Connon, S.J.3
  • 47
    • 18744414203 scopus 로고    scopus 로고
    • Synthesis of alpha-substituted N-aryl acrylamide derivatives through Baylis- Hillman reaction
    • (b) Wei, G.; Weiwei, W.; Ningjua" F.; Zhengang, W.; Chizhong, X. Synthesis of alpha-substituted N-aryl acrylamide derivatives through Baylis- Hillman reaction. Synth. Com- mun. 2005, 35, 1239-1251.
    • (2005) Synth. Com- mun , vol.35 , pp. 1239-1251
    • Wei, G.1    Weiwei, W.2    Ningjua", F.3    Zhengang, W.4    Chizhong, X.5
  • 48
    • 39149111233 scopus 로고    scopus 로고
    • Synthesis of substituted 3-methylene-2-pyridones from Baylis-Hillman derivatives and its application for the generation of 2-pyridone substituted spiroisoxazolines
    • Singh, V.; Yadav, G. P.; Maulik, P. R.; Batra, S. Synthesis of substituted 3-methylene-2-pyridones from Baylis-Hillman derivatives and its application for the generation of 2-pyridone substituted spiroisoxazolines. Tetrahedron 2008, 64, 2979-2991.
    • (2008) Tetrahedron , vol.64 , pp. 2979-2991
    • Singh, V.1    Yadav, G.P.2    Maulik, P.R.3    Batra, S.4
  • 49
    • 33645349856 scopus 로고    scopus 로고
    • Tandem β-elimination-Morita-Baylis-Hillman reaction in α,β-unsaturated sugar aldehydes
    • (a) Areces, P. C.; Carrasco, E.; Mancha, A.; Plumet, J. Tandem β-elimination-Morita-Baylis-Hillman reaction in α,β-unsaturated sugar aldehydes. Synthesis 2006, 6, 946-948.
    • (2006) Synthesis , vol.6 , pp. 946-948
    • Areces, P.C.1    Carrasco, E.2    Mancha, A.3    Plumet, J.4
  • 50
    • 0005110135 scopus 로고
    • 1,2-Addition of activated vinyl carbanions to,β-unsaturatedcarbonyls
    • (b) Drewes, S. E.; Emslie, N. D.; Khan, A. A.; Roos, G. H. P. 1,2-Addition of activated vinyl carbanions to,β-unsaturatedcarbonyls. Synth.Commun. 1989,19, 959-964.
    • (1989) Synth.Commun , vol.19 , pp. 959-964
    • Drewes, S.E.1    Emslie, N.D.2    Khan, A.A.3    Roos, G.H.P.4
  • 51
    • 0028076115 scopus 로고
    • Preparation of multifunctional stereodefined dienes
    • Heerden, F. R. v.; Huyser, J. J.; Holzapfel, C. W. Preparation of multifunctional stereodefined dienes. Synth.Commun. 1994, 24, 2863-2872.
    • (1994) Synth.Commun , vol.24 , pp. 2863-2872
    • Heerden, F.R.V.1    Huyser, J.J.2    Holzapfel, C.W.3
  • 52
    • 2442695035 scopus 로고    scopus 로고
    • Baylis-Hillman reaction in [bdmim][PF6] ionic liquid
    • Hsu, J.-C.; Yen, Y.-H.; Chu, Y.-H. Baylis-Hillman reaction in [bdmim][PF6] ionic liquid. Tetrahedron Lett. 2004, 45, 4673-4676.
    • (2004) Tetrahedron Lett , vol.45 , pp. 4673-4676
    • Hsu, J.-C.1    Yen, Y.-H.2    Chu, Y.-H.3
  • 53
    • 27144521210 scopus 로고    scopus 로고
    • A Diels- Alder macrocyclization enables an efficient asymmetric synthesis of the antibacterial natural product abyssomicin C
    • Zapf, C. W.; Harrison, B. A.; Drahl, C.; Sorensen, E. J. A Diels- Alder macrocyclization enables an efficient asymmetric synthesis of the antibacterial natural product abyssomicin C. Angew. Chem. Int Ed. 2005, 44, 6533-6537.
    • (2005) Angew. Chem. Int Ed , vol.44 , pp. 6533-6537
    • Zapf, C.W.1    Harrison, B.A.2    Drahl, C.3    Sorensen, E.J.4
  • 54
    • 0035857267 scopus 로고    scopus 로고
    • Chromatography with silver nitrate
    • Williams, C. M.; Mander, L. N. Chromatography with silver nitrate. Tetrahedron 2001, 57, 425-447.
    • (2001) Tetrahedron , vol.57 , pp. 425-447
    • Williams, C.M.1    Mander, L.N.2
  • 55
    • 33644528891 scopus 로고
    • Readily accessible 12-I-5 oxidant for the conversion of primary and secondary alcohols to aldehydes and ketones
    • Dess, D. B.; Martin, J. C. Readily accessible 12-I-5 oxidant for the conversion of primary and secondary alcohols to aldehydes and ketones. J. Ore. Chem. 1983, 43, 4155-4156.
    • (1983) J. Ore. Chem , vol.43 , pp. 4155-4156
    • Dess, D.B.1    Martin, J.C.2
  • 56
    • 33748664603 scopus 로고
    • Oxidation of [alpha],[beta]- unsaturated aldehydes
    • Bal, B. S.; Childers, W. E.; Pinnick, H. W. Oxidation of [alpha],[beta]- unsaturated aldehydes. Tetrahedron 1981, 37, 2091-2096.
    • (1981) Tetrahedron , vol.37 , pp. 2091-2096
    • Bal, B.S.1    Childers, W.E.2    Pinnick, H.W.3
  • 57
    • 33747041690 scopus 로고    scopus 로고
    • Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: Comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection
    • Demidenko, Z. N.; Vivo, C.; Halicka, H. D.; Li, C. J.; Bhalla, K.; Broude, E. V.; Blagosklonny, M. V. Pharmacological induction of Hsp70 protects apoptosis-prone cells from doxorubicin: comparison with caspase-inhibitor- and cycle-arrest-mediated cytoprotection. Cell Death Differ. 2006, 13, 1434-1441.
    • (2006) Cell Death Differ , vol.13 , pp. 1434-1441
    • Demidenko, Z.N.1    Vivo, C.2    Halicka, H.D.3    Li, C.J.4    Bhalla, K.5    Broude, E.V.6    Blagosklonny, M.V.7
  • 58
    • 22744449640 scopus 로고    scopus 로고
    • Cytopro- tective and antioxidant activity of Rhodiola imbricata against tert- butyl hydroperoxide induced oxidative injury in U-937 human macrophages
    • Kanupriya; Prasad, D.; Ram, M. S.; Kumar, R.; Sawhney, R. C.; Sharma, S. K.; Ilavazhagan, G.; Kumar, D.; Banerjee, P. K. Cytopro- tective and antioxidant activity of Rhodiola imbricata against tert- butyl hydroperoxide induced oxidative injury in U-937 human macrophages. Mol. Cell. Biochem. 2005, 275, 1-6.
    • (2005) Mol. Cell. Biochem , vol.275 , pp. 1-6
    • Kanupriya1    Prasad, D.2    Ram, M.S.3    Kumar, R.4    Sawhney, R.C.5    Sharma, S.K.6    Ilavazhagan, G.7    Kumar, D.8    Banerjee, P.K.9
  • 60
    • 38049095656 scopus 로고    scopus 로고
    • Cytoprotective effects of phenolic antioxidants and essential fatty acids in human blood monocyte and neuroblastoma cell lines: Surrogates for neurological damage in vivo
    • (b) Young, J.; Wahle, K. W.; Boyle, S. P. Cytoprotective effects of phenolic antioxidants and essential fatty acids in human blood monocyte and neuroblastoma cell lines: surrogates for neurological damage in vivo. Prostaglandins, Leukotrienes Essent. Fatty Acids 2008, 78, 45-59.
    • (2008) Prostaglandins, Leukotrienes Essent. Fatty Acids , vol.78 , pp. 45-59
    • Young, J.1    Wahle, K.W.2    Boyle, S.P.3
  • 62
    • 34548257657 scopus 로고    scopus 로고
    • Nicotinic receptor activation by epibatidine induces heme oxygenase-1 and protects chromaffin cells against oxidative stress
    • (a) Egea, J.; Rosa, A. O.; Cuadrado, A.; Garcia, A. G.; Lopez, M. G. Nicotinic receptor activation by epibatidine induces heme oxygenase-1 and protects chromaffin cells against oxidative stress. J. Neurochem. 2007, 102, 1842-1852.
    • (2007) J. Neurochem , vol.102 , pp. 1842-1852
    • Egea, J.1    Rosa, A.O.2    Cuadrado, A.3    Garcia, A.G.4    Lopez, M.G.5
  • 63
    • 33750465828 scopus 로고    scopus 로고
    • D-beta-Hydroxybutyrate protects dopaminergic SH-SY5Y cells in a rotenone model of Parkinson's disease
    • (b) Imamura, K.; Takeshima, T.; Kashiwaya, Y.; Nakaso, K.; Nakashima, K. D-beta-Hydroxybutyrate protects dopaminergic SH-SY5Y cells in a rotenone model of Parkinson's disease. J. Neurosci. Res. 2006, 84, 1376-1384.
    • (2006) J. Neurosci. Res , vol.84 , pp. 1376-1384
    • Imamura, K.1    Takeshima, T.2    Kashiwaya, Y.3    Nakaso, K.4    Nakashima, K.5
  • 64
    • 2142811497 scopus 로고    scopus 로고
    • Neuroprotective effect of fraxetin and myricetin against rotenone- induced apoptosis in neuroblastoma cells
    • Molina-Jimenez, M. F.; Sanchez-Reus, M. I.; Andres, D.; Cascales, M.; Benedi, J. Neuroprotective effect of fraxetin and myricetin against rotenone- induced apoptosis in neuroblastoma cells. Brain Res. 2004, 1009,9-16.
    • (2004) Brain Res , vol.1009 , pp. 9-16
    • Molina-Jimenez, M.F.1    Sanchez-Reus, M.I.2    Andres, D.3    Cascales, M.4    Benedi, J.5
  • 65
    • 34547824188 scopus 로고    scopus 로고
    • Lifespan of etoposide-treated human neutrophils is affected by antioxidant ability of quercetin
    • (a) Kapiszewska, M.; Cierniak, A.; Elas, M.; Lankoff, A. Lifespan of etoposide-treated human neutrophils is affected by antioxidant ability of quercetin. Toxicol. in Vitro 2007, 21, 1020-1030.
    • (2007) Toxicol. in Vitro , vol.21 , pp. 1020-1030
    • Kapiszewska, M.1    Cierniak, A.2    Elas, M.3    Lankoff, A.4
  • 66
    • 34347240776 scopus 로고    scopus 로고
    • Lysophosphatidic acid prevents apoptosis of Caco-2 colon cancer cells via activation of mitogen-activated protein kinase and phosphorylation of Bad
    • (b) Rusovici, R.; Ghaleb, A.; Shim, H.; Yang, V. W.; Yun, C. C. Lysophosphatidic acid prevents apoptosis of Caco-2 colon cancer cells via activation of mitogen-activated protein kinase and phosphorylation of Bad. Biochim Biophys Acta 2007, 1770, 1194-1203.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 1194-1203
    • Rusovici, R.1    Ghaleb, A.2    Shim, H.3    Yang, V.W.4    Yun, C.C.5
  • 67
    • 34248233130 scopus 로고    scopus 로고
    • Loss of mitochondrial membrane potential is inhibited by bombesin in etoposide-induced apoptosis in PC-3 prostate carcinoma cells
    • Salido, M.; Gonzalez, J. L.; Vilches, J. Loss of mitochondrial membrane potential is inhibited by bombesin in etoposide-induced apoptosis in PC-3 prostate carcinoma cells. Mol. Cancer Ther. 2007, 6, 1292-1299.
    • (2007) Mol. Cancer Ther , vol.6 , pp. 1292-1299
    • Salido, M.1    Gonzalez, J.L.2    Vilches, J.3
  • 68
    • 0032923143 scopus 로고    scopus 로고
    • Protective effect of docosahexaenoic acid against hydrogen peroxide-induced oxidative stress in human lymphocytes
    • (a) Bechoua, S.; Dubois, M.; Dominguez, Z.; Goncalves, A.; Nemoz, G.; Lagarde, M.; Prigent, A. F. Protective effect of docosahexaenoic acid against hydrogen peroxide-induced oxidative stress in human lymphocytes. Biochem. Pharnacol 1999, 57, 1021-1030.
    • (1999) Biochem. Pharnacol , vol.57 , pp. 1021-1030
    • Bechoua, S.1    Dubois, M.2    Dominguez, Z.3    Goncalves, A.4    Nemoz, G.5    Lagarde, M.6    Prigent, A.F.7
  • 69
    • 33746632989 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced oxidative stress in MC3T3-E1 cells: The effects of glutamate and protection by purines
    • (b) Fatokun, A. A.; Stone, T. W.; Smith, R. A. Hydrogen peroxide-induced oxidative stress in MC3T3-E1 cells: the effects of glutamate and protection by purines. Bone 2006, 39, 542-551.
    • (2006) Bone , vol.39 , pp. 542-551
    • Fatokun, A.A.1    Stone, T.W.2    Smith, R.A.3
  • 70
    • 35448943937 scopus 로고    scopus 로고
    • N-Methyl- Ń-nitro-N-nitrosoguanidine activates multiple cell death mechanisms in human fibroblasts
    • Lee, M. W.; Kim, W. J.; Beardsley, D. I.; Brown, K. D. N-Methyl- Ń-nitro-N-nitrosoguanidine activates multiple cell death mechanisms in human fibroblasts. DNA Cell Biol. 2007, 26, 683-694.
    • (2007) DNA Cell Biol , vol.26 , pp. 683-694
    • Lee, M.W.1    Kim, W.J.2    Beardsley, D.I.3    Brown, K.D.4
  • 72
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • (a) Hengartner, M. O. The biochemistry of apoptosis. Nature 2000, 407, 770-776.
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 73
    • 39749182234 scopus 로고    scopus 로고
    • Apoptosis: Controlled demolition at the cellular level
    • (b) Taylor, R. C.; Cullen, S. P.; Martin, S. J. Apoptosis: controlled demolition at the cellular level. Nat. Rev. Mol. Cell Biol. 2008, 9, 231-241.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 231-241
    • Taylor, R.C.1    Cullen, S.P.2    Martin, S.J.3
  • 74
    • 8444220527 scopus 로고    scopus 로고
    • Molecular mechanisms of caspase regulation during apoptosis
    • (a) Riedl, S. J.; Shi, Y. Molecular mechanisms of caspase regulation during apoptosis. Nat. Rev. Mol. Cell Biol. 2004, 5, 897-907.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 897-907
    • Riedl, S.J.1    Shi, Y.2
  • 76
    • 0031977070 scopus 로고    scopus 로고
    • Caspase activation in MCF7 cells responding to etoposide treatment
    • (a) Benjamin, C. W.; Hiebsch, R. R.; Jones, D. A. Caspase activation in MCF7 cells responding to etoposide treatment. Mol. Pharmacol. 1998, 53, 446-450.
    • (1998) Mol. Pharmacol , vol.53 , pp. 446-450
    • Benjamin, C.W.1    Hiebsch, R.R.2    Jones, D.A.3
  • 78
    • 23944461510 scopus 로고    scopus 로고
    • Using peptidic inhibitors to systematically probe the S1' site of caspase-3 and caspase- 7
    • (a) Goode, D. R.; Sharma, A. K.; Hergenrother, P. J. Using peptidic inhibitors to systematically probe the S1' site of caspase-3 and caspase- 7. Org. Lett. 2005, 7, 3529-3532.
    • (2005) Org. Lett , vol.7 , pp. 3529-3532
    • Goode, D.R.1    Sharma, A.K.2    Hergenrother, P.J.3
  • 79
    • 10644225944 scopus 로고    scopus 로고
    • Design and synthesis of a potent and selective peptidomimetic inhibitor of caspase-3
    • (b) Micale, N.; Vairagoundar, R.; Yakovlev, A. G.; Kozikowski, A. P. Design and synthesis of a potent and selective peptidomimetic inhibitor of caspase-3. J. Med. Chem. 2004, 47, 6455-6458.
    • (2004) J. Med. Chem , vol.47 , pp. 6455-6458
    • Micale, N.1    Vairagoundar, R.2    Yakovlev, A.G.3    Kozikowski, A.P.4
  • 82
    • 34547593361 scopus 로고    scopus 로고
    • Isatin sulfonamide analogs containing a Michael addition acceptor: A new class of caspase 3/7 inhibitors
    • (b) Chu, W.; Rothfuss, J.; d'Avignon, A.; Zeng, C.; Zhou, D.; Hotchkiss, R. S.; Mach, R. H. Isatin sulfonamide analogs containing a Michael addition acceptor: a new class of caspase 3/7 inhibitors. J. Med. Chem. 2007, 50, 3751-3755.
    • (2007) J. Med. Chem , vol.50 , pp. 3751-3755
    • Chu, W.1    Rothfuss, J.2    d'Avignon, A.3    Zeng, C.4    Zhou, D.5    Hotchkiss, R.S.6    Mach, R.H.7
  • 83
    • 20144384669 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of 4-substituted 2-(2-acetyloxyethyl)-8- (morpholine-4-sulfonyl)pyrrolo[3,4- c]quinoline-1,3- diones as potent caspase-3 inhibitors
    • Kravchenko, D. V.; Kuzovkova, Y. A.; Kysil, V. M.; Tkachenko, S. E.; Maliarchouk, S.; Okun, I. M.; Balakin, K. V.; Ivachtchenko, A. V. Synthesis and structure-activity relationship of 4-substituted 2-(2-acetyloxyethyl)-8- (morpholine-4-sulfonyl)pyrrolo[3,4- c]quinoline-1,3- diones as potent caspase-3 inhibitors. J. Med. Chem. 2005, 48, 3680-3683.
    • (2005) J. Med. Chem , vol.48 , pp. 3680-3683
    • Kravchenko, D.V.1    Kuzovkova, Y.A.2    Kysil, V.M.3    Tkachenko, S.E.4    Maliarchouk, S.5    Okun, I.M.6    Balakin, K.V.7    Ivachtchenko, A.V.8
  • 86
    • 29244444522 scopus 로고    scopus 로고
    • Fluorescence probes used for detection of reactive oxygen species
    • (a) Gomes, A.; Fernandes, E.; Lima, J. L. Fluorescence probes used for detection of reactive oxygen species. J. Biochem. Biophys. Methods 2005, 65, 45-80.
    • (2005) J. Biochem. Biophys. Methods , vol.65 , pp. 45-80
    • Gomes, A.1    Fernandes, E.2    Lima, J.L.3
  • 87
    • 48849100392 scopus 로고    scopus 로고
    • The role of oxidative stress in acrolein-induced DNA damage in HepG2 cells
    • (b) Li, L.; Jiang, L.; Geng, C.; Cao, J.; Zhong, L. The role of oxidative stress in acrolein-induced DNA damage in HepG2 cells. Free Radical Res. 2008, 42, 354-361.
    • (2008) Free Radical Res , vol.42 , pp. 354-361
    • Li, L.1    Jiang, L.2    Geng, C.3    Cao, J.4    Zhong, L.5
  • 88
    • 0028887591 scopus 로고
    • Flow cytometric analysis of the granulocyte respiratory burst: A comparison study of fluorescent probes
    • Vowells, S. J.; Sekhsaria, S.; Malech, H. L.; Shalit, M.; Fleisher, T. A. Flow cytometric analysis of the granulocyte respiratory burst: a comparison study of fluorescent probes. J. Immunol. Methods 1995, 178,89-97.
    • (1995) J. Immunol. Methods , vol.178 , pp. 89-97
    • Vowells, S.J.1    Sekhsaria, S.2    Malech, H.L.3    Shalit, M.4    Fleisher, T.A.5
  • 89
    • 0030008052 scopus 로고    scopus 로고
    • Superoxide production in rat hippocampal neurons: Selective imaging with hydroethidine
    • (a) Bindokas, V. P.; Jordan, J.; Lee, C. C.; Miller, R. J. Superoxide production in rat hippocampal neurons: selective imaging with hydroethidine. J. Neurosci. 1996, 16, 1324-1336.
    • (1996) J. Neurosci , vol.16 , pp. 1324-1336
    • Bindokas, V.P.1    Jordan, J.2    Lee, C.C.3    Miller, R.J.4
  • 90
    • 34547802699 scopus 로고    scopus 로고
    • Superoxide (*O2-) production in CA1 neurons of rat hippocampal slices exposed to graded levels of oxygen
    • (b) D'Agostino, D. P.; Putnam, R. W.; Dean, J. B. Superoxide (*O2-) production in CA1 neurons of rat hippocampal slices exposed to graded levels of oxygen. J. Neurophysiol. 2007, 98, 1030-1041.
    • (2007) J. Neurophysiol , vol.98 , pp. 1030-1041
    • D'Agostino, D.P.1    Putnam, R.W.2    Dean, J.B.3
  • 91
    • 44349085313 scopus 로고    scopus 로고
    • Aldosterone and the autocrine modulation of potassium currents and oxidative stress in the diabetic rat heart
    • Shimoni, Y.; Chen, K.; Emmett, T.; Kargacin, G. Aldosterone and the autocrine modulation of potassium currents and oxidative stress in the diabetic rat heart. Br. J. Pharmacol. 2008, 154, 675-687.
    • (2008) Br. J. Pharmacol , vol.154 , pp. 675-687
    • Shimoni, Y.1    Chen, K.2    Emmett, T.3    Kargacin, G.4
  • 92
    • 34249868200 scopus 로고    scopus 로고
    • Vitamin E, antioxidant and nothing more
    • Traber, M. G.; Atkinson, J. Vitamin E, antioxidant and nothing more. Free Radical Biol. Med. 2007, 43, 4-15.
    • (2007) Free Radical Biol. Med , vol.43 , pp. 4-15
    • Traber, M.G.1    Atkinson, J.2
  • 93
    • 34247383146 scopus 로고    scopus 로고
    • c-Jun N-terminal kinase mediates hydrogen peroxide-induced cell death via sustained poly(ADP-ribose) polymerase-1 activation
    • Zhang, S.; Lin, Y.; Kim, Y. S.; Hande, M. P.; Liu, Z. G.; Shen, H. M. c-Jun N-terminal kinase mediates hydrogen peroxide-induced cell death via sustained poly(ADP-ribose) polymerase-1 activation. Cell Death Differ. 2007, 14, 1001-1010.
    • (2007) Cell Death Differ , vol.14 , pp. 1001-1010
    • Zhang, S.1    Lin, Y.2    Kim, Y.S.3    Hande, M.P.4    Liu, Z.G.5    Shen, H.M.6
  • 94
    • 0037470042 scopus 로고    scopus 로고
    • A two-drug model for etoposide action against human topoisomerase IIalpha
    • Bromberg, K. D.; Burgin, A. B.; Osheroff, N. A two-drug model for etoposide action against human topoisomerase IIalpha. J. Biol. Chem. 2003, 278, 7406-7412.
    • (2003) J. Biol. Chem , vol.278 , pp. 7406-7412
    • Bromberg, K.D.1    Burgin, A.B.2    Osheroff, N.3
  • 95
    • 33746565261 scopus 로고    scopus 로고
    • Topoisomerase II inhibitors
    • Hande, K. R. Topoisomerase II inhibitors. Update Cancer Ther. 2006, 1, 3-15.
    • (2006) Update Cancer Ther , vol.1 , pp. 3-15
    • Hande, K.R.1
  • 97
    • 34248137349 scopus 로고    scopus 로고
    • Protein tyrosine nitration and poly(ADP-ribose) polymerase activation in N-methyl-N-nitro-N-nitrosoguanidine-treated thymocytes: Implication for cytotoxicity
    • Bai, P.; Hegedus, C.; Erdelyi, K.; Szabo, E.; Bakondi, E.; Gergely, S.; Szabo, C.; Virag, L. Protein tyrosine nitration and poly(ADP-ribose) polymerase activation in N-methyl-N-nitro-N-nitrosoguanidine-treated thymocytes: implication for cytotoxicity. Toxicol. Lett. 2007, 170, 203-213.
    • (2007) Toxicol. Lett , vol.170 , pp. 203-213
    • Bai, P.1    Hegedus, C.2    Erdelyi, K.3    Szabo, E.4    Bakondi, E.5    Gergely, S.6    Szabo, C.7    Virag, L.8
  • 100
    • 34347344991 scopus 로고    scopus 로고
    • Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis
    • (b) Moubarak, R. S.; Yuste, V. J.; Artus, C.; Bouharrour, A.; Greer, P. A.; Menissier-de Murcia, J.; Susin, S. A. Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis. Mol. Cell. Biol. 2007, 27, 4844-4862.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 4844-4862
    • Moubarak, R.S.1    Yuste, V.J.2    Artus, C.3    Bouharrour, A.4    Greer, P.A.5    Menissier-de Murcia, J.6    Susin, S.A.7
  • 103
    • 19444364781 scopus 로고    scopus 로고
    • (ADP-ribosyl)ation and stroke
    • (a) Chiarugi, A. Poly(ADP-ribosyl)ation and stroke. Pharmacol. Res. 2005, 52, 15-24.
    • (2005) Pharmacol. Res , vol.52 , pp. 15-24
    • Chiarugi, A.P.1
  • 104
    • 33845292554 scopus 로고    scopus 로고
    • Neither energy collapse nor transcription underlie in vitro neuro- toxicity of poly(ADP-ribose) polymerase hyper-activation
    • (b) Fossati, S.; Cipriani, G.; Moroni, F.; Chiarugi, A. Neither energy collapse nor transcription underlie in vitro neuro- toxicity of poly(ADP-ribose) polymerase hyper-activation. Neurochem. Int 2007, 50, 203-210.
    • (2007) Neurochem. Int , vol.50 , pp. 203-210
    • Fossati, S.1    Cipriani, G.2    Moroni, F.3    Chiarugi, A.4
  • 105
    • 38649092421 scopus 로고    scopus 로고
    • (ADP-ribose)polymerase 1 (PARP-1) and postischemic brain damage
    • Moroni, F. Poly(ADP-ribose)polymerase 1 (PARP-1) and postischemic brain damage. Curr. Qpin. Pharmacol. 2008, 8, 96-103.
    • (2008) Curr. Qpin. Pharmacol , vol.8 , pp. 96-103
    • Moroni, F.P.1
  • 106
    • 0036940204 scopus 로고    scopus 로고
    • Synthesis and MMP-inhibitory activity of gelastatin analogues
    • (a) Cho, J.-H; Ko, S. Y. Synthesis and MMP-inhibitory activity of gelastatin analogues. Helv. Chim. Acta 2002, 85, 3994-3999.
    • (2002) Helv. Chim. Acta , vol.85 , pp. 3994-3999
    • Cho, J.-H.1    Ko, S.Y.2
  • 108
    • 19444386259 scopus 로고    scopus 로고
    • Synthesis of arylidene-substituted gelastatin analogues and their screening for MMP-2 inhibitory activity
    • Kim, E. J.; Ko, S. Y. Synthesis of arylidene-substituted gelastatin analogues and their screening for MMP-2 inhibitory activity. Bioorg. Med. Chem. 2005,13, 4103-4112.
    • (2005) Bioorg. Med. Chem , vol.13 , pp. 4103-4112
    • Kim, E.J.1    Ko, S.Y.2
  • 109
    • 0032838953 scopus 로고    scopus 로고
    • Gelastatins, new inhibitors of matrix metalloproteinases from Westerdykella multispora F50733
    • Lee, H. J.; Chung, M. C.; Lee, C. H.; Chun, H. K.; Rhee, J. S.; Kho, Y. H. Gelastatins, new inhibitors of matrix metalloproteinases from Westerdykella multispora F50733. Ann. N.Y. Acad. Sci. 1999, 878, 635-637.
    • (1999) Ann. N.Y. Acad. Sci , vol.878 , pp. 635-637
    • Lee, H.J.1    Chung, M.C.2    Lee, C.H.3    Chun, H.K.4    Rhee, J.S.5    Kho, Y.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.