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Volumn 17, Issue 5, 2010, Pages 479-494

Thioredoxin system modulation by plant and fungal secondary metabolites

Author keywords

Fungal secondary metabolites; Plant secondary metabolites; Thioredoxin systems

Indexed keywords

1 METHYLPROPYL 2 IMIDAZOLYL DISULFIDE; 13 HYDROXY 15 OXO ZOAPATLIN; ANTHRACYCLINE; CATECHIN; CHALCONE; CURCUMIN; DAUNORUBICIN; FORSKOLIN; HELENALIN; JUGLONE; LUTEOLIN; MK 3018; MYRICETIN; PALMARUMYCIN; PELARGONIDIN; PLEUROTIN; POLYPHENOL DERIVATIVE; PROTEIN INHIBITOR; PX 12; PX 916; QUERCETIN; QUINONE DERIVATIVE; RESVERATROL; RIBONUCLEOTIDE REDUCTASE; SCUTELLARIN; TAXIFOLIN; TEPRENONE; TERPENE; TERPENOID DERIVATIVE; THIOREDOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 77950663504     PISSN: 09298673     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986710790226165     Document Type: Review
Times cited : (37)

References (106)
  • 2
    • 0033775891 scopus 로고    scopus 로고
    • Physiologic function of thioredoxin and thioredoxin reductase
    • Arner, E.S.; Holmgren, A. Physiologic function of thioredoxin and thioredoxin reductase. Eur. J. Biochem., 2000, 267, 6102-6109.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6102-6109
    • Arner, E.S.1    Holmgren, A.2
  • 3
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren, A. Thioredoxin and glutaredoxin systems. J. Biol. Chem., 1989, 264, 13963-13966.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 4
    • 34548067718 scopus 로고    scopus 로고
    • Thioredoxin signaling as a target for cancer therapy
    • DOI 10.1016/j.coph.2007.04.003, PII S1471489207000914, Cancer/Immunomodulation
    • Powis, J.; Kirkpatrick, D.L. Thioredoxin signalling as a target for cancer therapy. Curr. Opin. Pharmacol., 2007, 7, 392-397. (Pubitemid 47289261)
    • (2007) Current Opinion in Pharmacology , vol.7 , Issue.4 , pp. 392-397
    • Powis, G.1    Kirkpatrick, D.L.2
  • 6
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • DOI 10.1074/jbc.274.5.3182
    • Makino, J.; Yoshikawa, N.; Okamoto, K.; Hirota, K.; Yodoi, J.; Makino, I; Tanaka, H. Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem., 1999, 274, 3182-3188. (Pubitemid 29075407)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.5 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 7
    • 0030020576 scopus 로고    scopus 로고
    • A new selenoprotein from human lung and adenocarcinoma cells: Purification, properties, and thioredoxin reductase activity
    • Tamura, T.; Stadtman, T.C. A new selenoprotein from human lung and adenocarcinoma cells: purification, properties, and thioredoxin reductase activity. Proc. Natl. Acad. Sci. USA, 1996, 93, 1006-1011.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1006-1011
    • Tamura, T.1    Stadtman, T.C.2
  • 8
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • DOI 10.1074/jbc.M000690200
    • Zong, L.; Holmgren, A. Essential role of selenium in the catalytic activity of mammalian thioredoxin reductase revealed by characterization of recombinant enzyme with selenocisteine mutations. J. Biol. Chem., 2000, 275, 18121-18128. (Pubitemid 30414762)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.24 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2
  • 9
    • 0034652113 scopus 로고    scopus 로고
    • Thioredoxin reductase
    • Mustacich, D.; Powis, G. Thioredoxin reductase. Biochem. J., 2000, 346, 1-8.
    • (2000) Biochem. J. , vol.346 , pp. 1-8
    • Mustacich, D.1    Powis, G.2
  • 10
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidant, and the mammalian thioredoxin system
    • Nordberg, J.; Arner, E.S.J. Reactive oxygen species, antioxidant, and the mammalian thioredoxin system. Free Radical Bio. Med., 2001, 31, 1287-1312.
    • (2001) Free Radical Bio. Med. , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arner, E.S.J.2
  • 11
  • 12
    • 0042807630 scopus 로고    scopus 로고
    • The thioredoxin-thioredoxin reductase system: Over-expression in human cancer
    • Lincoln, D.T.; Eli Emadi, E.M.; Tonissen, K.F.; Clarke, F.M. The thioredoxin-thioredoxin reductase system: over-expression in human cancer. Anticancer Res., 2003, 23, 2425-2434.
    • (2003) Anticancer Res. , vol.23 , pp. 2425-2434
    • Lincoln, D.T.1    Eli Emadi, E.M.2    Tonissen, K.F.3    Clarke, F.M.4
  • 14
    • 31944432877 scopus 로고    scopus 로고
    • The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma
    • DOI 10.1016/j.lab.2005.09.001, PII S0022214305003100
    • Baker, A.F.; Dragovich, T.; Tate, W.R.; Ramanathan, R.K.; Roe, D.; Hsu, C.H.; Kirkpatrick, D.L.; Powis, G. The antitumor thioredoxin-1 inhibitor PX-12 (1-methylpropyl 2-imidazolyl disulfide) decreases thioredoxin-1 and VEGF levels in cancer patient plasma. J. Lab. Clin. Med., 2006, 147, 83-90. (Pubitemid 43189000)
    • (2006) Journal of Laboratory and Clinical Medicine , vol.147 , Issue.2 , pp. 83-90
    • Baker, A.F.1    Dragovich, T.2    Tate, W.R.3    Ramanathan, R.K.4    Roe, D.5    Hsu, C.-H.6    Kirkpatrick, D.L.7    Powis, G.8
  • 15
    • 11344292132 scopus 로고    scopus 로고
    • The role of natural product chemistry in drug discovery
    • DOI 10.1021/np040106y
    • Butler, M.S. The role of natural product chemistry in drug discovery. J. Nat. Prod., 2004, 67, 2141-2153. (Pubitemid 40092578)
    • (2004) Journal of Natural Products , vol.67 , Issue.12 , pp. 2141-2153
    • Butler, M.S.1
  • 16
    • 0026093041 scopus 로고
    • Pharmacology of Curcuma longa
    • Ammon, H.P.; Wahl, M.A. Pharmacology of Curcuma longa. Planta Med., 1991, 57, 1-7.
    • (1991) Planta Med. , vol.57 , pp. 1-7
    • Ammon, H.P.1    Wahl, M.A.2
  • 17
    • 33644901007 scopus 로고    scopus 로고
    • Multiple biological activities of curcumin: A short review
    • Maheswari, R.K.; Singh, A.K.; Gadippati, J.; Srimal, R.C. Multiple biological activities of curcumin: a short review. Life Sci., 2006, 78, 2081-2087.
    • (2006) Life Sci. , vol.78 , pp. 2081-2087
    • Maheswari, R.K.1    Singh, A.K.2    Gadippati, J.3    Srimal, R.C.4
  • 18
    • 21244498576 scopus 로고    scopus 로고
    • 2 phase of cell cycle in a p53-dependent manner
    • DOI 10.1074/jbc.M410670200
    • Choudhuri, T.; Pal, S.; Das, T.; Sa, G. Curcumin selectively induces apoptosis in deregulated cyclin D1-expressed cells at G2 phase of cell cycle in a p53-dependent manner. J. Biol. Chem., 2005, 280, 20059-20068. (Pubitemid 41379535)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.20 , pp. 20059-20068
    • Choudhuri, T.1    Pal, S.2    Das, T.3    Sa, G.4
  • 19
    • 21644477778 scopus 로고    scopus 로고
    • Thioredoxin reductase is irreversibly modified by curcumin: A novel molecular mechanism for its anticancer activity
    • DOI 10.1074/jbc.M414645200
    • Fang, J.; Lu, J.; Holmgren, A. Thioredoxin reductase is irreversibly modified by curcumin: a novel molecular mechanism for its anticancer activity. J. Biol. Chem., 2005, 280, 25284-25290. (Pubitemid 40934623)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25284-25290
    • Fang, J.1    Lu, J.2    Holmgren, A.3
  • 20
    • 0032080238 scopus 로고    scopus 로고
    • Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighbouring cysteine residue
    • Nordberg, J.; Zong, L.; Olmgren, A.; Arner, E.S. Mammalian thioredoxin reductase is irreversibly inhibited by dinitrohalobenzenes by alkylation of both the redox active selenocysteine and its neighbouring cysteine residue. J. Biol. Chem., 1998, 273, 10835-10842.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10835-10842
    • Nordberg, J.1    Zong, L.2    Olmgren, A.3    Arner, E.S.4
  • 24
    • 5644283296 scopus 로고    scopus 로고
    • Role of chemopreventive agents in cancer therapy
    • DOI 10.1016/j.canlet.2004.07.013, PII S0304383504005464
    • Dorai, T.; Aggarwal, B.B. Role of chemopreventive agents in cancer therapy. Cancer Lett., 2004, 215, 129-140. (Pubitemid 39370030)
    • (2004) Cancer Letters , vol.215 , Issue.2 , pp. 129-140
    • Dorai, T.1    Aggarwal, B.B.2
  • 25
    • 33646233781 scopus 로고    scopus 로고
    • Inhibition of mammalian thioredoxin reductase by some flavonoids: Implications for myricetin and quercetin anticancer activity
    • Lu, J.; Papp, L.V.; Fang, J.; Rodriguez-Nieto, S.; Zhivotovsky, B.; Holmgren, A. Inhibition of mammalian thioredoxin reductase by some flavonoids: implications for myricetin and quercetin anticancer activity. Cancer Res., 2006, 66, 4410-4418.
    • (2006) Cancer Res. , vol.66 , pp. 4410-4418
    • Lu, J.1    Papp, L.V.2    Fang, J.3    Rodriguez-Nieto, S.4    Zhivotovsky, B.5    Holmgren, A.6
  • 26
    • 0035010504 scopus 로고    scopus 로고
    • Electron transfer and oxidative stress as key factors in the design of drugs selectively active in hypoxia
    • Wardman, P. Electron transfer and oxidative stress as key factors in the design of drugs selectively active in hypoxia. Curr. Med. Chem., 2001, 8, 739-761. (Pubitemid 32427904)
    • (2001) Current Medicinal Chemistry , vol.8 , Issue.7 , pp. 739-761
    • Wardman, P.1
  • 27
    • 0031466528 scopus 로고    scopus 로고
    • Cell linedirected screening assay for inhibitors of thioredoxin reductase signalling as potential anticancer drugs
    • Kunkel, M.W.; Kirkpatrick, D.L.; Johnson, J.I.; Powis, J. Cell linedirected screening assay for inhibitors of thioredoxin reductase signalling as potential anticancer drugs. Anti-Cancer Drug Des., 1997, 12, 659-670.
    • (1997) Anti-Cancer Drug Des. , vol.12 , pp. 659-670
    • Kunkel, M.W.1    Kirkpatrick, D.L.2    Johnson, J.I.3    Powis, J.4
  • 29
    • 0031550840 scopus 로고    scopus 로고
    • 5 from coniothyrium palmarum: Structure elucidation, crystal structure analysis and determination of the absolute configuration by CD calculations
    • DOI 10.1016/S0040-4020(97)00066-5, PII S0040402097000665
    • Krohn, K.; Beckman, K.; Florke, U.; Aust, H.J.; Draiger, S.; Shulz, B.; Busemann, S.; Bringmann, G. Biologically active metabolites from fungi, 9. New palmarumycins CP4a and CP5 from Coniothyrium palmarum: structure elucidation, crystal structure analysis and determination of the absolute configuration by CD calculations. Tetrahedron, 1997, 53, 3101-3110. (Pubitemid 27087454)
    • (1997) Tetrahedron , vol.53 , Issue.9 , pp. 3101-3110
    • Krohn, K.1    Beckmann, K.2    Florke, U.3    Aust, H.-J.4    Draeger, S.5    Schulz, B.6    Busemann, S.7    Bringmann, G.8
  • 31
    • 33645466124 scopus 로고    scopus 로고
    • Molecular pharmacology and antitumor activity of palmarumycin-based inhibitors of thioredoxin reductase
    • Powis, G.; Wipf, P.; Lynch S.M.; Birmingham A.; Kirkpatrick, D.L. Molecular pharmacology and antitumor activity of palmarumycin-based inhibitors of thioredoxin reductase. Mol. Cancer Ther., 2006, 5, 630-636.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 630-636
    • Powis, G.1    Wipf, P.2    Lynch, S.M.3    Birmingham, A.4    Kirkpatrick, D.L.5
  • 32
    • 1642535437 scopus 로고    scopus 로고
    • Interactions of quinones with thioredoxin reductase a challenge to the antioxidant role of the mammalian selenoprotein
    • Cenas, N.; Nivinskas, H.; Anusevicius, Z.; Sarlauskas, J.; Lederer, F.; Arner, E.S.J. Interactions of quinones with thioredoxin reductase a challenge to the antioxidant role of the mammalian selenoprotein. J. Biol. Chem., 2004, 279, 2583-2592.
    • (2004) J. Biol. Chem. , vol.279 , pp. 2583-2592
    • Cenas, N.1    Nivinskas, H.2    Anusevicius, Z.3    Sarlauskas, J.4    Lederer, F.5    Arner, E.S.J.6
  • 35
    • 3042714351 scopus 로고    scopus 로고
    • Structure of kaurane-type diterpenes from Parinari sprucei and their potential anticancer activity
    • DOI 10.1055/s-2004-827155
    • Braca, A.; Armenise, A.; Morelli, I.; Mendez, J.; Mi, Q.; Chai, H.; Swanson, S. M.; Kinghorn A. D.; De Tommasi, N. Structure of kaurane-type diterpenes from Parinari sprucei and their potential anticancer activity. Planta Med., 2004, 70, 540-550. (Pubitemid 38887912)
    • (2004) Planta Medica , vol.70 , Issue.6 , pp. 540-550
    • Braca, A.1    Armenise, A.2    Morelli, I.3    Mendez, J.4    Mi, Q.5    Chai, H.-B.6    Swanson, S.M.7    Kinghorn, A.D.8    De Tommasi, N.9
  • 36
    • 0035930521 scopus 로고    scopus 로고
    • 2 DNA Damage Checkpoint Inhibition and Antimitotic Activity of 13-Hydroxy-15-oxozoapatlin
    • Rundle, N. T.; Xu, L., Andersen, R. J.; Roberge, M. G2 DNA damage checkpoint inhibition and antimitotic activity of 13-hydroxy-15-oxozoapatlin. J. Biol. Chem., 2001, 276, 48231-48236. (Pubitemid 37370727)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 48231-48236
    • Rundle, N.T.1    Xu, L.2    Andersen, R.J.3    Roberge, M.4
  • 37
    • 34948888792 scopus 로고    scopus 로고
    • 13-hydroxy-15-oxo-zoapatlin, an ent-kaurane diterpene, induces apoptosis in human leukemia cells, affecting thiol-mediated redox regulation
    • Dal Piaz, F.; Nigro, P.; Braca, A.; De Tommasi, N.; Belisario, M.A. 13-hydroxy-15-oxo-zoapatlin, an ent-kaurane diterpene, induces apoptosis in human leukemia cells, affecting thiol-mediated redox regulation. Free Radical Bio. Med., 2007, 43, 1409-1422.
    • (2007) Free Radical Bio. Med. , vol.43 , pp. 1409-1422
    • Dal Piaz, F.1    Nigro, P.2    Braca, A.3    De Tommasi, N.4    Belisario, M.A.5
  • 38
    • 54949103954 scopus 로고    scopus 로고
    • Inhibition of the thioredoxin system is a basis for the antileukemic potential of 13-hydroxy-15-oxo-zoapatlin
    • Nigro, P.; Dal Piaz, F.; Gallotta, D.; De Tommasi N.; Belisario, M.A. Inhibition of the thioredoxin system is a basis for the antileukemic potential of 13-hydroxy-15-oxo-zoapatlin. Free Radical Bio. Med., 2008, 45, 875-884.
    • (2008) Free Radical Bio. Med. , vol.45 , pp. 875-884
    • Nigro, P.1    Dal Piaz, F.2    Gallotta, D.3    De Tommasi, N.4    Belisario, M.A.5
  • 39
    • 0041856170 scopus 로고    scopus 로고
    • Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif
    • Watson, W.H.; Pohl, J.; Montfort, W.R.; Stuchlik, O.; Reed, M.S.; Powis, G.; Jones, D.P. Redox potential of human thioredoxin 1 and identification of a second dithiol/disulfide motif. J. Biol. Chem., 2003, 278, 33408-33415.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33408-33415
    • Watson, W.H.1    Pohl, J.2    Montfort, W.R.3    Stuchlik, O.4    Reed, M.S.5    Powis, G.6    Jones, D.P.7
  • 40
    • 0037297417 scopus 로고    scopus 로고
    • Non-reciprocal regulation of the redox state of the glutathione- glutaredoxin and thioredoxin systems
    • Trotter, E.W.; Grant, C.M. Non-reciprocal regulation of the redox state of the glutathione-glutaredoxin and thioredoxin systems. EMBO Rep., 2003, 4, 184-188.
    • (2003) EMBO Rep. , vol.4 , pp. 184-188
    • Trotter, E.W.1    Grant, C.M.2
  • 42
    • 77950680725 scopus 로고
    • Terpenes. LXXI. Helenalin -a further lactone of the guaianolide group
    • Herout, V.; Romanuk, M.; Sorm, F. Terpenes. LXXI. Helenalin -a further lactone of the guaianolide group. Chemicke Listy pro Vedu a Prumysl, 1956, 50, 985-987.
    • (1956) Chemicke Listy Pro Vedu a Prumysl , vol.50 , pp. 985-987
    • Herout, V.1    Romanuk, M.2    Sorm, F.3
  • 43
    • 4243585103 scopus 로고
    • Terpenes. VI. the structures of helenalin and isohelenalin
    • Buchi, G.; Rosenthal, D. Terpenes. VI. The structures of helenalin and isohelenalin. J. Am. Chem. Soc., 1956, 78, 3860-3861.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 3860-3861
    • Buchi, G.1    Rosenthal, D.2
  • 44
    • 0032696632 scopus 로고    scopus 로고
    • Toxic activities of sesquiterpene lactones-structural and biochemical aspects
    • Schmidt, T.J. Toxic activities of sesquiterpene lactones-structural and biochemical aspects. Curr. Org. Chem., 1999, 3, 577-605.
    • (1999) Curr. Org. Chem. , vol.3 , pp. 577-605
    • Schmidt, T.J.1
  • 45
    • 0023918670 scopus 로고
    • Inhibition of nucleic acid synthesis in P-388 lymphocytic leukaemia cells in culture by sesquiterpene lactones
    • Hall, I.H.; Williams, W.L.Jr.; Grippo, A.A.; Lee, K-H.; Holbrook, D.J.; Chaney, S.G. Inhibition of nucleic acid synthesis in P-388 lymphocytic leukaemia cells in culture by sesquiterpene lactones. Anticancer Res., 1988, 8, 33-42.
    • (1988) Anticancer Res. , vol.8 , pp. 33-42
    • Hall, I.H.1    Williams, W.L.J.2    Grippo, A.A.3    Lee, K.-H.4    Holbrook, D.J.5    Chaney, S.G.6
  • 47
    • 9644294597 scopus 로고    scopus 로고
    • NF-kappaB activation prevents apoptotic oxidative stress via an increase of both thioredoxin and MnSOD levels in TNFalpha-treated Ewing sarcoma cells
    • DOI 10.1016/j.febslet.2004.10.082, PII S0014579304013468
    • Djavaheri-Mergny, M.; Javelaud, D.; Wietzerbin, J.; Besançon, F. NF-kappaB activation prevents apoptotic oxidative stress via an increase of both thioredoxin and MnSOD levels in TNFalpha-treated Ewing sarcoma cells. FEBS Lett., 2004, 578, 111-115. (Pubitemid 39576110)
    • (2004) FEBS Letters , vol.578 , Issue.1-2 , pp. 111-115
    • Djavaheri-Mergny, M.1    Javelaud, D.2    Wietzerbin, J.3    Besancon, F.4
  • 48
    • 30044436438 scopus 로고    scopus 로고
    • Cathepsin D and H2O2 stimulate degradation of Thioredoxin- 1: Implication for endothelial cell apoptosis
    • Haendeler, J.; Popp, R.; Goy, C.; Tischler, V.; Zeiher, A.M.; Dimmeler S. Cathepsin D and H2O2 stimulate degradation of Thioredoxin- 1: implication for endothelial cell apoptosis. J Biol. Chem., 2005, 280, 42945-42951.
    • (2005) J Biol. Chem. , vol.280 , pp. 42945-42951
    • Haendeler, J.1    Popp, R.2    Goy, C.3    Tischler, V.4    Zeiher, A.M.5    Dimmeler, S.6
  • 49
    • 62349116477 scopus 로고    scopus 로고
    • The mitochondrial theory of aging: Insight from transgenic and knockout mouse models
    • Jang, Y.C.; Van Remme, H. The mitochondrial theory of aging: insight from transgenic and knockout mouse models. Exp. Gerontol., 2009, 44, 256-260.
    • (2009) Exp. Gerontol. , vol.44 , pp. 256-260
    • Van Remme, H.1
  • 51
    • 0033955352 scopus 로고    scopus 로고
    • Interaction of flavones from the roots of Scutellaria baicalensis with the benzodiazepine site
    • Hui, K.M.; Wang, X.H.; Xue, H. Interaction of flavones from the roots of Scutellaria baicalensis with the benzodiazepine site. Planta Med., 2000, 66, 91-93. (Pubitemid 30097295)
    • (2000) Planta Medica , vol.66 , Issue.1 , pp. 91-93
    • Kwok, M.H.1    Xi, H.W.2    Xue, H.3
  • 52
    • 51249087928 scopus 로고    scopus 로고
    • Antiinflammatory activity of the extracts and fractions from Erigeron multiradiatus through bioassay-guided procedures
    • Luo, P.; Zhang, Z.; Yi, T.; Zhang, H.; Liu, X.; Mo, Z. Antiinflammatory activity of the extracts and fractions from Erigeron multiradiatus through bioassay-guided procedures. J. Ethnopharmacol., 2008, 119, 232-237.
    • (2008) J. Ethnopharmacol. , vol.119 , pp. 232-237
    • Luo, P.1    Zhang, Z.2    Yi, T.3    Zhang, H.4    Liu, X.5    Mo, Z.6
  • 53
    • 44849101717 scopus 로고    scopus 로고
    • Scutellarein inhibits hypoxia- And moderately-high glucose-induced proliferation and VEGF expression in human retinal endothelial cells
    • DOI 10.1111/j.1745-7254.2008.00797.x
    • Gao, R.; Zhu, B.H.; Tang, S.B.; Wang, J.F.; Ren, J. Scutellarein inhibits hypoxia- and moderately-high glucose-induced proliferation and VEGF expression in human retinal endothelial cells. Acta Pharmacol. Sin., 2008, 29, 707-712. (Pubitemid 351799471)
    • (2008) Acta Pharmacologica Sinica , vol.29 , Issue.6 , pp. 707-712
    • Gao, R.1    Zhu, B.-H.2    Tang, S.-B.3    Wang, J.-F.4    Ren, J.5
  • 54
    • 1642424296 scopus 로고    scopus 로고
    • Protection against hydrogen peroxide-induced cytotoxicity in PC12 cells by scutellarin
    • DOI 10.1016/j.lfs.2003.09.074, PII S0024320504001432
    • Hong, H.; Liu, G.Q. Protection against hydrogen peroxide-induced cytotoxicity in PC12 cells by scutellarin. Life Sci., 2004, 74, 2959-2973. (Pubitemid 38402293)
    • (2004) Life Sciences , vol.74 , Issue.24 , pp. 2959-2973
    • Hong, H.1    Liu, G.-Q.2
  • 55
    • 0024418963 scopus 로고
    • Inhibition of reverse transcriptases by flavonoids
    • Spedding, G.; Ratty, A.; Middleton, E. Jr. Inhibition of reverse transcriptases by flavonoids. Antiviral. Res., 1989, 12, 99-110.
    • (1989) Antiviral. Res. , vol.12 , pp. 99-110
    • Spedding, G.1    Ratty, A.2    Middleton Jr., E.3
  • 56
    • 2542530655 scopus 로고    scopus 로고
    • Antagonistic effect of scutellarin on the toxicity of selenium in rat livers
    • DOI 10.1385/BTER:98:3:253
    • Elatayeb, A.A.; Liu, Q.; Gan, L.; Liu, H.; Xu, H. Antagonistic effect of scutellarin on the toxicity of selenium in rat livers. Biol. Trace Elem. Res., 2004, 98, 253-264. (Pubitemid 38703702)
    • (2004) Biological Trace Element Research , vol.98 , Issue.3 , pp. 253-264
    • Eltayeb, A.A.1    Liu, Q.2    Gan, L.U.3    Liu, H.4    Xu, H.5
  • 57
    • 0036400016 scopus 로고    scopus 로고
    • Dietary flavonoids: Bioavailability, metabolic effects, and safety
    • Ross, J.A.; Kasum, C.M. Dietary flavonoids: bioavailability, metabolic effects, and safety. Annu. Rev. Nutr., 2002, 22, 19-34.
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 19-34
    • Ross, J.A.1    Kasum, C.M.2
  • 58
    • 0028840931 scopus 로고
    • Tyrosine kinase activity is essential for interleukin-1 beta-stimulated production of interleukin-6 in U373 human astrocytoma cells
    • Carlson, R.O.; Aschmies, S.H. Tyrosine kinase activity is essential for interleukin-1 beta-stimulated production of interleukin-6 in U373 human astrocytoma cells. J. Neurochem., 1995, 65, 2491-2499.
    • (1995) J. Neurochem. , vol.65 , pp. 2491-2499
    • Carlson, R.O.1    Aschmies, S.H.2
  • 59
    • 29744458225 scopus 로고    scopus 로고
    • Quercetin protects C6 glial cells from oxidative stress induced by tertiary-butylhydroperoxide
    • DOI 10.1080/10715760500335447, PII T257243717406
    • Gitika, B.; Sai Ram, M.; Sharma, S.K.; Ilavazhagan, G.; Banerjee, P.K. Quercetin protects C6 glial cells from oxidative stress induced by tertiarybutylhydroperoxide. Free Radical Res., 2006, 40, 95-102. (Pubitemid 43023790)
    • (2006) Free Radical Research , vol.40 , Issue.1 , pp. 95-102
    • Gitika, B.1    Sairam, M.2    Sharma, S.K.3    Ilavazhagan, G.4    Banerjee, P.K.5
  • 60
    • 34248146559 scopus 로고    scopus 로고
    • Modulation of interleukin-1b mediated inflammatory response in human astrocytes by flavonoids: Implications in neuroprotection
    • DOI 10.1016/j.brainresbull.2007.01.016, PII S0361923007000664
    • Sharma, V.; Mishra, M.; Ghosh, S.; Tewari, R.; Basu, A.; Seth, P.; Sen, E. Modulation of interleukin-1b mediated inflammatory response in human astrocytes by flavonoids: implications in neuroprotection. Brain Res. Bull., 2007, 73, 55-63. (Pubitemid 46710246)
    • (2007) Brain Research Bulletin , vol.73 , Issue.1-3 , pp. 55-63
    • Sharma, V.1    Mishra, M.2    Ghosh, S.3    Tewari, R.4    Basu, A.5    Seth, P.6    Sen, E.7
  • 65
    • 0031913851 scopus 로고    scopus 로고
    • Synthesis and anti-inflammatory effect of chalcones and related compounds
    • DOI 10.1023/A:1011940401754
    • Hsieh, H.K.; Lee, T.H.; Wang, J.P.; Wang, J.J.; Lin, C.N. Synthesis and anti-inflammatory effect of chalcones and related compounds. Pharm. Res., 1998, 15, 39-46. (Pubitemid 28080864)
    • (1998) Pharmaceutical Research , vol.15 , Issue.1 , pp. 39-46
    • Hsieh, H.-K.1    Lee, T.-H.2    Wang, J.-P.3    Wang, J.-J.4    Lin, C.-N.5
  • 66
    • 17844405853 scopus 로고    scopus 로고
    • Blockade of vascular endothelial growth factor receptor signal pathway and antitumor activity of ON-III (2′,4′-dihydroxy-6′-methoxy- 3′,5′-dimethylchalcone), a component from Chinese herbal medicine
    • Zhu, X.F.; Xie, B.F.; Zhou, J.M.; Fengm G.K.; Liu, Z.C.; Wei, X.Y.; Zhang, F.X.; Liu, M.F., Zeng, Y.X. Blockade of vascular endothelial growth factor receptor signal pathway and antitumor activity of ON-III (2′,4′-dihydroxy-6′-methoxy-3′,5′- dimethylchalcone), a component from Chinese herbal medicine. Mol. Pharmacol., 2005, 67, 1444-1450.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1444-1450
    • Zhu, X.F.1    Xie, B.F.2    Zhou, J.M.3    Fengm, G.K.4    Liu, Z.C.5    Wei, X.Y.6    Zhang, F.X.7    Liu, M.F.8    Zeng, Y.X.9
  • 67
    • 0028798998 scopus 로고
    • Anticancer and antioxidant activity of synthetic chalcones and related compounds
    • Anto, R.J., Sukumaran, K.; Kuttan, G.; Rao, M.N. Subbaraju, V.; Kuttan, R. Anticancer and antioxidant activity of synthetic chalcones and related compounds. Cancer Lett., 1995, 97, 33-37.
    • (1995) Cancer Lett. , vol.97 , pp. 33-37
    • Anto, R.J.1    Sukumaran, K.2    Kuttan, G.3    Rao, M.N.4    Subbaraju, V.5    Kuttan, R.6
  • 69
    • 33847633373 scopus 로고    scopus 로고
    • Chalcone inhibits the activation of NF-κB and STAT3 in endothelial cells via endogenous electrophile
    • Liu, Y-C.; Hsieh, C.W.; Wu, C-C.; Wung, B-S. Chalcone inhibits the activation of NF-κB and STAT3 in endothelial cells via endogenous electrophile. Life Sci., 2007, 80, 1420-30.
    • (2007) Life Sci. , vol.80 , pp. 1420-1430
    • Liu, Y.-C.1    Hsieh, C.W.2    Wu, C.-C.3    Wung, B.-S.4
  • 70
    • 0031839670 scopus 로고    scopus 로고
    • Resveratrol, a phytoestrogen found in red wine. a possible explanation for the conundrum of the 'French paradox'?
    • Kopp, P. Resveratrol, a phytoestrogen found in red wine. A possible explanation for the conundrum of the 'French paradox'? Eur. J. Endocrinol., 1998, 138, 619-620.
    • (1998) Eur. J. Endocrinol. , vol.138 , pp. 619-620
    • Kopp, P.1
  • 71
    • 14844295766 scopus 로고    scopus 로고
    • Resveratrol and estradiol rapidly activate MAPK signaling through estrogen receptors alpha and beta in endothelial cells
    • Klinge, C.M.; Blankenship, K.A.; Risinger, K.E.; Bhatnager, S.; Noisin, E.L.; Sumanasekera W.K. Resveratrol and estradiol rapidly activate MAPK signaling through estrogen receptors alpha and beta in endothelial cells. J. Biol. Chem., 2005, 280, 7460-7468.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7460-7468
    • Klinge, C.M.1    Blankenship, K.A.2    Risinger, K.E.3    Bhatnager, S.4    Noisin, E.L.5    Sumanasekera, W.K.6
  • 74
    • 4143140856 scopus 로고    scopus 로고
    • Trans-3,4,5'-Trihydroxystibene inhibits hypoxia-inducible factor 1alpha and vascular endothelial growth factor expression in human ovarian cancer cells
    • DOI 10.1158/1078-0432.CCR-03-0588
    • Cao, Z.; Fang, J.; Xia, C.; Shi, X.; Jiang, B.H. trans-3,4,5'- Trihydroxystilbene inhibits hypoxia-inducible factor 1alpha and vascular endothelial growth factor expression in human ovarian cancer cells. Clin. Cancer Res., 2004, 10, 5253-5263. (Pubitemid 39099800)
    • (2004) Clinical Cancer Research , vol.10 , Issue.15 , pp. 5253-5263
    • Cao, Z.1    Fang, J.2    Xia, C.3    Shi, X.4    Jiang, B.-H.5
  • 75
    • 26844449558 scopus 로고    scopus 로고
    • Resveratrol enhances neovascularization in the infarcted rat myocardium through the induction of thioredoxin-1, heme oxygenase-1 and vascular endothelial growth factor
    • DOI 10.1016/j.yjmcc.2005.08.003, PII S0022282805002580
    • Kaga, S.; Zhan, L.; Matsumoto, M.; Maulik, N. Resveratrol enhances neovascularization in the infracted rat myocardium through the induction of thioredoxin-1, hemeoxygenase-1, and vascular endothelial growth factor. J. Mol. Cell. Cardiol., 2005, 39, 813-822. (Pubitemid 41464418)
    • (2005) Journal of Molecular and Cellular Cardiology , vol.39 , Issue.5 , pp. 813-822
    • Kaga, S.1    Zhan, L.2    Matsumoto, M.3    Maulik, N.4
  • 76
    • 34547101726 scopus 로고    scopus 로고
    • Resveratrol alleviates cardiac dysfunction in streptozotocin-induced diabetes: Role of nitric oxide, thioredoxin, and heme oxygenase
    • DOI 10.1016/j.freeradbiomed.2007.05.004, PII S0891584907003188
    • Thirunavukkarasu, M.; Penumathsa, S.; Koneru, V.; Bela, S.; Lijun, Z.; Otani, H.; Bagchi, D.; Das, D.K.; Maulik, N. Resveratrol alleviates cardiac dysfunction in streptozotocin-induced diabetes: role of nitric oxide, thioredoxin, and heme oxygenase. Free Radical Bio. Med., 2007, 43, 720-729. (Pubitemid 47102122)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.5 , pp. 720-729
    • Thirunavukkarasu, M.1    Penumathsa, S.V.2    Koneru, S.3    Juhasz, B.4    Zhan, L.5    Otani, H.6    Bagchi, D.7    Das, D.K.8    Maulik, N.9
  • 77
    • 0028850626 scopus 로고
    • Green-tea consumption and risk of stomach cancer: A populationbased case-control study in Shanghai, China
    • Yu, G.P.; Hsieh, C.C.; Wang, L.Y.; Yu, S.Z.; Li, X.L.; Jin, T.H. Green-tea consumption and risk of stomach cancer: a populationbased case-control study in Shanghai, China. Cancer Cause Control, 1995, 6, 532-553.
    • (1995) Cancer Cause Control , vol.6 , pp. 532-553
    • Yu, G.P.1    Hsieh, C.C.2    Wang, L.Y.3    Yu, S.Z.4    Li, X.L.5    Jin, T.H.6
  • 78
    • 33645977193 scopus 로고    scopus 로고
    • The relationship between green tea and total caffeine intake and risk for self-reported type 2 diabetes among Japanese adults
    • the JACC Study Group.
    • Iso, H.; Date, C.; Wakai, K.; Fukui, M.; Tamakoshi, A.; the JACC Study Group. The relationship between green tea and total caffeine intake and risk for self-reported type 2 diabetes among Japanese adults. Ann. Intern. Med., 2006, 144, 554-562.
    • (2006) Ann. Intern. Med. , vol.144 , pp. 554-562
    • Iso, H.1    Date, C.2    Wakai, K.3    Fukui, M.4    Tamakoshi, A.5
  • 79
    • 0141639855 scopus 로고    scopus 로고
    • Antioxidant activity of tea polyphenols in vitro: Evidence from animal studies
    • Frei, B.; Higdon, J.V. Antioxidant activity of tea polyphenols in vitro: evidence from animal studies. J. Nutr., 2003, 133, 3275S- 84S.
    • (2003) J. Nutr. , vol.133
    • Frei, B.1    Higdon, J.V.2
  • 80
    • 0038121053 scopus 로고    scopus 로고
    • Tea Catechins and Polyphenols: Health Effects, Metabolism, and Antioxidant Functions
    • DOI 10.1080/10408690390826464
    • Higdon, J.V.; Frei, B. Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Crit. Rev. Food Sci. Nutr., 2003, 43, 89-143. (Pubitemid 38552312)
    • (2003) Critical Reviews in Food Science and Nutrition , vol.43 , Issue.1 , pp. 89-143
    • Higdon, J.V.1    Frei, B.2
  • 82
    • 0034810264 scopus 로고    scopus 로고
    • Black tea is a powerful chemopreventor of reactive oxygen and nitrogen species: Comparison with its individual catechin constituents and green tea
    • DOI 10.1006/bbrc.2001.4944
    • Sarkar, A.; Bhaduri, A. Black tea is a powerful chemopreventor of reactive oxygen and nitrogen species: comparison with its individual catechin constituents and green tea. Biochem. Biophys. Res. Commun., 2001, 284, 173-178. (Pubitemid 32924324)
    • (2001) Biochemical and Biophysical Research Communications , vol.284 , Issue.1 , pp. 173-178
    • Sarkar, A.1    Bhaduri, A.2
  • 83
    • 12344282174 scopus 로고    scopus 로고
    • Enrichment of yeast thioredoxin by green tea extract through activation of Yap1 transcription factor in Saccharomyces cerevisiae
    • DOI 10.1021/jf048818h
    • Takatsume, Y.; Maeta, K.; Izawa, S.; Inoue, Y. Enrichment of yeast thioredoxin by green tea extract through activation of yap1 transcription factor in Saccharomyces cerevisiae. J. Agric. Food Chem., 2005, 53, 332-337. (Pubitemid 40129923)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.2 , pp. 332-337
    • Takatsume, Y.1    Maeta, K.2    Izawa, S.3    Inoue, Y.4
  • 84
    • 33846409869 scopus 로고    scopus 로고
    • Green tea polyphenols function as prooxidants to activate oxidative-stress-responsive transcription factors in yeasts
    • DOI 10.1128/AEM.01963-06
    • Maeta, K.; Nomura, W.; Takatsume, Y.; Izawa, S.; Inoue, Y. Green tea polyphenols function as prooxidants to activate oxidativestress- responsive transcription factors in yeasts. Appl. Environ. Microbiol., 2007, 73, 572-580. (Pubitemid 46147588)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.2 , pp. 572-580
    • Maeta, K.1    Nomura, W.2    Takatsume, Y.3    Izawa, S.4    Inoue, Y.5
  • 86
    • 0029206373 scopus 로고
    • Oxidant induced inactivation of protein kinase C in UC11MG cells
    • Brawn, M.K.; Chiou, W.J.; Leach, K.L. Oxidant induced inactivation of protein kinase C in UC11MG cells. Free Radical Res., 1995, 22, 23-37.
    • (1995) Free Radical Res. , vol.22 , pp. 23-37
    • Brawn, M.K.1    Chiou, W.J.2    Leach, K.L.3
  • 87
    • 0029758783 scopus 로고    scopus 로고
    • Redox modulation of tyrosine phosphorylation-dependent signal transduction pathways
    • DOI 10.1016/0891-5849(96)00051-2
    • Monteiro, H.P.; Stern, A. Redox modulation of tyrosine phosphorylation-dependent signal transduction pathways. Free Radical Bio. Med., 1996, 21, 323-333. (Pubitemid 26271722)
    • (1996) Free Radical Biology and Medicine , vol.21 , Issue.3 , pp. 323-333
    • Monteiro, H.P.1    Stern, A.2
  • 88
    • 0024517167 scopus 로고
    • Involvement of thiol transferase- And thioredoxin-dependent systems in the protection of 'essential' thiol groups of ornithine decarboxylase
    • Flamigni, F.; Marmiroli, S.; Caldarera, C.M.; Guarnieri, C. Involvement of thiol transferase and thioredoxin dependent systems in the protection of essential thiol groups of ornithine decarboxylase. Biochem. J., 1989, 259, 111-115. (Pubitemid 19100503)
    • (1989) Biochemical Journal , vol.259 , Issue.1 , pp. 111-115
    • Flamigni, F.1    Marmiroli, S.2    Caldarera, C.M.3    Guarnieri, C.4
  • 89
    • 0032824908 scopus 로고    scopus 로고
    • Induction of thioredoxin, thioredoxin reductase and glutaredoxin activity in mouse skin by TPA, a calcium ionophore and other tumor promoters
    • DOI 10.1093/carcin/20.9.1761
    • Kumar, S.; Holmgren, A. Induction of thioredoxin, thioredoxin reductase and glutaredoxin activity in mouse skin by TPA, a calcium ionophore and other tumor promoters. Carcinogenesis, 1999, 20, 1761-1767. (Pubitemid 29410556)
    • (1999) Carcinogenesis , vol.20 , Issue.9 , pp. 1761-1767
    • Kumar, S.1    Holmgren, A.2
  • 90
    • 0023052241 scopus 로고
    • Studies and perspectives of protein kinase C
    • Nishizuka,Y. Studies and perspectives of protein kinase C. Science, 1986, 233, 305-312.
    • (1986) Science , vol.233 , pp. 305-312
    • Nishizuka, Y.1
  • 91
    • 49349139162 scopus 로고
    • Structures and stereochemistry of new labdane diterpenoids from Coleus forskohlii Briq
    • Bhat, S.V.; Bajwa, B.S.; Dornauer, H.; DeSouza, N.J.; Fehlhaber, H.W. Structures and stereochemistry of new labdane diterpenoids from Coleus forskohlii Briq. Tetrahedron Lett., 1977, 18, 1669-1672.
    • (1977) Tetrahedron Lett. , vol.18 , pp. 1669-1672
    • Bhat, S.V.1    Bajwa, B.S.2    Dornauer, H.3    Desouza, N.J.4    Fehlhaber, H.W.5
  • 92
    • 28944433229 scopus 로고    scopus 로고
    • Simple and rapid method for the isolation of forskolin form Coleus forskohlii by characoal column chromatography
    • Saleem, A.M.; Dhasan, P.B.; Rafiullah, M.R.M. Simple and rapid method for the isolation of forskolin form Coleus forskohlii by characoal column chromatography. J. Chromatogr. A, 2006, 1101, 313-314.
    • (2006) J. Chromatogr. A , vol.1101 , pp. 313-314
    • Saleem, A.M.1    Dhasan, P.B.2    Rafiullah, M.R.M.3
  • 93
    • 0021083279 scopus 로고
    • Forskolin: A potential antimetastatic agent
    • Agarwal, K.C.; Parks, R.E. Jr. Forskolin: a potential antimetastatic agent. Int. J. Cancer, 1983, 32, 801-804.
    • (1983) Int. J. Cancer , vol.32 , pp. 801-804
    • Agarwal, K.C.1    Parks Jr., R.E.2
  • 94
    • 0024443061 scopus 로고
    • Forskolin: A specific stimulator of adenylyl cyclase or a diterpene with multiple sites of action?
    • Laurenza, A.; Sutkowski, E.M.; Seamon, K.B. Forskolin: a specific stimulator of adenylyl cyclase or a diterpene with multiple sites of action? Trends Pharmacol. Sci., 1989, 10, 442-447.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 442-447
    • Laurenza, A.1    Sutkowski, E.M.2    Seamon, K.B.3
  • 95
    • 0030670289 scopus 로고    scopus 로고
    • 1
    • DOI 10.1006/exer.1997.0370
    • Yamamoto, M.; Sato, N.; Tajima, H.; Furuke, K.; Ohira, A.; Honda, Y.; Yodoi, J. Induction of human thioredoxin in cultured human retinal pigment epithelial cells through cyclic AMPdependent pathway: involvement in the cytoprotective activity of prostaglandin E1. Exp. Eye Res., 1997, 65, 645-652. (Pubitemid 27489760)
    • (1997) Experimental Eye Research , vol.65 , Issue.5 , pp. 645-652
    • Yamamoto, M.1    Sato, N.2    Tajima, H.3    Furuke, K.4    Ohira, A.5    Honda, Y.6    Yodoi, J.7
  • 97
    • 0035949514 scopus 로고    scopus 로고
    • Avicins, a family of triterpenoid saponins from Acacia victoriae (Bentham), inhibit activation of NF-κB by inhibiting both its nuclear localization and ability to bind DNA
    • Haridas, V.; Arntzen, C.J.; Gutterman, J.U. Avicins, a family of triterpenoid saponins from Acacia victoriae (Bentham), inhibit activation of NF-κB by inhibiting both its nuclear localization and ability to bind DNA. Proc. Natl. Acad. Sci. USA, 2001, 98, 11557-11562.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11557-11562
    • Haridas, V.1    Arntzen, C.J.2    Gutterman, J.U.3
  • 99
    • 0023975549 scopus 로고
    • Correlation between endogenous glutathione content and sensitivity of cultured human skin cells to radiation at defined wavelengths in the solar ultraviolet range
    • Tyrrell, R.M.; Pidoux, M. Correlation between endogenous glutathione content and sensitivity of cultured human skin cells to radiation at defined wavelengths in the solar ultraviolet range. Photochem. Photobiol., 1988, 47, 405-412.
    • (1988) Photochem. Photobiol. , vol.47 , pp. 405-412
    • Tyrrell, R.M.1    Pidoux, M.2
  • 101
    • 0019834023 scopus 로고
    • Effect of acyclic polyisoprenoids on the biosynthesis of mannose-labeled glycolipids in rat liver microsomes
    • Murakami, M.; Muto, Y.; Moriwaki, H.; Ohgo, T. Effect of acyclic polyisoprenoids on the biosynthesis of mannose-labeled glycolipids in rat liver microsomes. Biochem. Biophys. Res. Commun., 1981, 103, 706-712.
    • (1981) Biochem. Biophys. Res. Commun. , vol.103 , pp. 706-712
    • Murakami, M.1    Muto, Y.2    Moriwaki, H.3    Ohgo, T.4
  • 102
    • 0022533634 scopus 로고
    • Protective action of tetraprenylacetone against ethanol-induced damage in rat gastric mucosa
    • Terano, A.; Shiga, J.; Hiraishi, H.; Ota, S.; Sugimoto, T. Protective action of tetraprenylacetone against ethanol-induced damage in rat gastric mucosa. Digestion, 1986, 35, 182-188.
    • (1986) Digestion , vol.35 , pp. 182-188
    • Terano, A.1    Shiga, J.2    Hiraishi, H.3    Ota, S.4    Sugimoto, T.5
  • 103
    • 0034618673 scopus 로고    scopus 로고
    • Geranylgeranylacetone enhances expression of thioredoxin and suppresses ethanol-induced cytotoxicity in cultured hepatocytes
    • Hirota, K.; Nakamura, H.; Arai, T.; Ishii, H.; Bai, J,; Itoh, T.; Fukuda, K.; Yodoi, J. Geranylgeranylacetone enhances expression of thioredoxin and suppresses ethanol-induced cytotoxicity in cultured hepatocytes. Biochem. Biophys. Res. Commun., 2000, 275, 825-830.
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 825-830
    • Hirota, K.1    Nakamura, H.2    Arai, T.3    Ishii, H.4    Bai, J.5    Itoh, T.6    Fukuda, K.7    Yodoi, J.8
  • 104
    • 0034899291 scopus 로고    scopus 로고
    • Geranylgeranylacetone promotes induction and secretion of thioredoxin in gastric mucosal cells and peripheral blood lymphocytes
    • Dekigai, H.; Nakamura, H.; Bai, J.; Tanito, M.; Masutani, H.; Hirota, K.; Matsui, H.; Murakami, M.; Yodoi J. Geranylgeranylacetone promotes induction and secretion of thioredoxin in gastric mucosal cells and peripheral blood lymphocytes. Free Radical Res., 2001, 35, 23-30. (Pubitemid 32725622)
    • (2001) Free Radical Research , vol.35 , Issue.1 , pp. 23-30
    • Dekigai, H.1    Nakamura, H.2    Bai, J.3    Tanito, M.4    Masutani, H.5    Hirota, K.6    Matsui, H.7    Murakami, M.8    Yodoi, J.9
  • 106
    • 34250175495 scopus 로고    scopus 로고
    • Discovery of gliotoxin as a new small molecule targeting thioredoxin redox system
    • Choi, H.S.; Shim, J.S.; Kim, J-A.; Kang, S.W.; Kwon, H.J. Discovery of gliotoxin as a new small molecule targeting thioredoxin redox system. Biochem. Biophys. Res. Commun., 2007, 359, 523-528.
    • (2007) Biochem. Biophys. Res. Commun. , vol.359 , pp. 523-528
    • Choi, H.S.1    Shim, J.S.2    Kim, J.-A.3    Kang, S.W.4    Kwon, H.J.5


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