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Volumn 228, Issue , 2015, Pages 69-78

6-Shogaol enhances renal carcinoma Caki cells to TRAIL-induced apoptosis through reactive oxygen species-mediated cytochrome c release and down-regulation of c-FLIP(L) expression

Author keywords

6 Shogaol; Apoptosis; c FLIP(L); ROS; TRAIL

Indexed keywords

(6) GINGEROL; CYTOCHROME C; FLICE INHIBITORY PROTEIN; GLUTATHIONE; GLUTATHIONE DISULFIDE; PROTEIN BAX; REACTIVE OXYGEN METABOLITE; RHODAMINE 123; SHOGAOL; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; ANTINEOPLASTIC AGENT; CATECHOL DERIVATIVE; CFLAR PROTEIN, HUMAN; TNFSF10 PROTEIN, HUMAN;

EID: 84921996881     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2015.01.020     Document Type: Article
Times cited : (29)

References (47)
  • 1
    • 0346792725 scopus 로고    scopus 로고
    • TRAIL and apoptosis induction by TNF-family death receptors
    • S. Wang, and W.S. El-Deiry TRAIL and apoptosis induction by TNF-family death receptors Oncogene 22 2003 8628 8633
    • (2003) Oncogene , vol.22 , pp. 8628-8633
    • Wang, S.1    El-Deiry, W.S.2
  • 2
    • 0035216008 scopus 로고    scopus 로고
    • TRAIL/Apo-2L: Mechanisms and clinical applications in cancer
    • R.K. Srivastava TRAIL/Apo-2L: mechanisms and clinical applications in cancer Neoplasia 3 2001 535 546
    • (2001) Neoplasia , vol.3 , pp. 535-546
    • Srivastava, R.K.1
  • 3
    • 14644437742 scopus 로고    scopus 로고
    • Mechanisms of resistance to TRAIL-induced apoptosis in cancer
    • L. Zhang, and B. Fang Mechanisms of resistance to TRAIL-induced apoptosis in cancer Cancer Gene Ther. 12 2005 228 237
    • (2005) Cancer Gene Ther. , vol.12 , pp. 228-237
    • Zhang, L.1    Fang, B.2
  • 4
    • 57749097095 scopus 로고    scopus 로고
    • TRAIL resistance of breast cancer cells is associated with constitutive endocytosis of death receptors 4 and 5
    • Y. Zhang, and B. Zhang TRAIL resistance of breast cancer cells is associated with constitutive endocytosis of death receptors 4 and 5 Mol. Cancer Res. 6 2008 1861 1871
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1861-1871
    • Zhang, Y.1    Zhang, B.2
  • 6
    • 26844536133 scopus 로고    scopus 로고
    • Surface TRAIL decoy receptor-4 expression is correlated with TRAIL resistance in MCF7 breast cancer cells
    • A.D. Sanlioglu, E. Dirice, C. Aydin, N. Erin, S. Koksoy, and S. Sanlioglu Surface TRAIL decoy receptor-4 expression is correlated with TRAIL resistance in MCF7 breast cancer cells BMC Cancer 5 2005 54
    • (2005) BMC Cancer , vol.5 , pp. 54
    • Sanlioglu, A.D.1    Dirice, E.2    Aydin, C.3    Erin, N.4    Koksoy, S.5    Sanlioglu, S.6
  • 7
    • 70249107161 scopus 로고    scopus 로고
    • Cancer cells with high expression of CD133 exert FLIP upregulation and resistance to TRAIL-induced apoptosis
    • R. Zobalova, M. Stantic, K. Prokopova, L.F. Dong, and J. Neuzil Cancer cells with high expression of CD133 exert FLIP upregulation and resistance to TRAIL-induced apoptosis BioFactors 34 2008 231 235
    • (2008) BioFactors , vol.34 , pp. 231-235
    • Zobalova, R.1    Stantic, M.2    Prokopova, K.3    Dong, L.F.4    Neuzil, J.5
  • 8
    • 22044441646 scopus 로고    scopus 로고
    • Accelerated degradation of caspase-8 protein correlates with TRAIL resistance in a DLD1 human colon cancer cell line
    • L. Zhang, H. Zhu, F. Teraishi, J.J. Davis, W. Guo, Z. Fan, and B. Fang Accelerated degradation of caspase-8 protein correlates with TRAIL resistance in a DLD1 human colon cancer cell line Neoplasia 7 2005 594 602
    • (2005) Neoplasia , vol.7 , pp. 594-602
    • Zhang, L.1    Zhu, H.2    Teraishi, F.3    Davis, J.J.4    Guo, W.5    Fan, Z.6    Fang, B.7
  • 9
    • 84863171959 scopus 로고    scopus 로고
    • Simultaneously targeting Bcl-2 and Akt pathways reverses resistance of nasopharyngeal carcinoma to TRAIL synergistically
    • S.S. Li, Q.L. Tang, S.H. Wang, Y.H. Chen, J.J. Liu, and X.M. Yang Simultaneously targeting Bcl-2 and Akt pathways reverses resistance of nasopharyngeal carcinoma to TRAIL synergistically Tumori 97 2011 762 770
    • (2011) Tumori , vol.97 , pp. 762-770
    • Li, S.S.1    Tang, Q.L.2    Wang, S.H.3    Chen, Y.H.4    Liu, J.J.5    Yang, X.M.6
  • 10
    • 54249159248 scopus 로고    scopus 로고
    • Targeting XIAP bypasses Bcl-2-mediated resistance to TRAIL and cooperates with TRAIL to suppress pancreatic cancer growth in vitro and in vivo
    • M. Vogler, H. Walczak, D. Stadel, T.L. Haas, F. Genze, M. Jovanovic, J.E. Gschwend, T. Simmet, K.M. Debatin, and S. Fulda Targeting XIAP bypasses Bcl-2-mediated resistance to TRAIL and cooperates with TRAIL to suppress pancreatic cancer growth in vitro and in vivo Cancer Res. 68 2008 7956 7965
    • (2008) Cancer Res. , vol.68 , pp. 7956-7965
    • Vogler, M.1    Walczak, H.2    Stadel, D.3    Haas, T.L.4    Genze, F.5    Jovanovic, M.6    Gschwend, J.E.7    Simmet, T.8    Debatin, K.M.9    Fulda, S.10
  • 11
    • 79951556892 scopus 로고    scopus 로고
    • Sensitization of human bladder tumor cells to TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis with a small molecule IAP antagonist
    • T.S. Griffith, T.A. Kucaba, M.A. O'Donnell, J. Burns, C. Benetatos, M.A. McKinlay, S. Condon, and S. Chunduru Sensitization of human bladder tumor cells to TNF-related apoptosis-inducing ligand (TRAIL)-induced apoptosis with a small molecule IAP antagonist Apoptosis 16 2011 13 26
    • (2011) Apoptosis , vol.16 , pp. 13-26
    • Griffith, T.S.1    Kucaba, T.A.2    O'Donnell, M.A.3    Burns, J.4    Benetatos, C.5    McKinlay, M.A.6    Condon, S.7    Chunduru, S.8
  • 12
    • 37349127807 scopus 로고    scopus 로고
    • Some phytochemical, pharmacological and toxicological properties of ginger (Zingiber officinale Roscoe): A review of recent research
    • B.H. Ali, G. Blunden, M.O. Tanira, and A. Nemmar Some phytochemical, pharmacological and toxicological properties of ginger (Zingiber officinale Roscoe): a review of recent research Food Chem. Toxicol. 46 2008 409 420
    • (2008) Food Chem. Toxicol. , vol.46 , pp. 409-420
    • Ali, B.H.1    Blunden, G.2    Tanira, M.O.3    Nemmar, A.4
  • 15
    • 84863897014 scopus 로고    scopus 로고
    • In vitro antioxidant and anti-inflammatory activities of 1-dehydro-[6]-gingerdione, 6-shogaol, 6-dehydroshogaol and hexahydrocurcumin
    • F. Li, V. Nitteranon, X. Tang, J. Liang, G. Zhang, K.L. Parkin, and Q. Hu In vitro antioxidant and anti-inflammatory activities of 1-dehydro-[6]-gingerdione, 6-shogaol, 6-dehydroshogaol and hexahydrocurcumin Food Chem. 135 2012 332 337
    • (2012) Food Chem. , vol.135 , pp. 332-337
    • Li, F.1    Nitteranon, V.2    Tang, X.3    Liang, J.4    Zhang, G.5    Parkin, K.L.6    Hu, Q.7
  • 16
    • 73749087460 scopus 로고    scopus 로고
    • Comparative antioxidant and anti-inflammatory effects of [6]-gingerol, [8]-gingerol, [10]-gingerol and [6]-shogaol
    • S. Dugasani, M.R. Pichika, V.D. Nadarajah, M.K. Balijepalli, S. Tandra, and J.N. Korlakunta Comparative antioxidant and anti-inflammatory effects of [6]-gingerol, [8]-gingerol, [10]-gingerol and [6]-shogaol J. Ethnopharmacol. 127 2010 515 520
    • (2010) J. Ethnopharmacol. , vol.127 , pp. 515-520
    • Dugasani, S.1    Pichika, M.R.2    Nadarajah, V.D.3    Balijepalli, M.K.4    Tandra, S.5    Korlakunta, J.N.6
  • 17
    • 34247842982 scopus 로고    scopus 로고
    • 6-shogaol (alkanone from ginger) induces apoptotic cell death of human hepatoma p53 mutant Mahlavu subline via an oxidative stress-mediated caspase-dependent mechanism
    • C.Y. Chen, T.Z. Liu, Y.W. Liu, W.C. Tseng, R.H. Liu, F.J. Lu, Y.S. Lin, S.H. Kuo, and C.H. Chen 6-shogaol (alkanone from ginger) induces apoptotic cell death of human hepatoma p53 mutant Mahlavu subline via an oxidative stress-mediated caspase-dependent mechanism J. Agric. Food Chem. 55 2007 948 954
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 948-954
    • Chen, C.Y.1    Liu, T.Z.2    Liu, Y.W.3    Tseng, W.C.4    Liu, R.H.5    Lu, F.J.6    Lin, Y.S.7    Kuo, S.H.8    Chen, C.H.9
  • 18
    • 84863091501 scopus 로고    scopus 로고
    • 6-Shogaol induces apoptosis in human hepatocellular carcinoma cells and exhibits anti-tumor activity in vivo through endoplasmic reticulum stress
    • R. Hu, P. Zhou, Y.B. Peng, X. Xu, J. Ma, Q. Liu, L. Zhang, X.D. Wen, L.W. Qi, N. Gao, and P. Li 6-Shogaol induces apoptosis in human hepatocellular carcinoma cells and exhibits anti-tumor activity in vivo through endoplasmic reticulum stress PLoS ONE 7 2012 e39664
    • (2012) PLoS ONE , vol.7 , pp. e39664
    • Hu, R.1    Zhou, P.2    Peng, Y.B.3    Xu, X.4    Ma, J.5    Liu, Q.6    Zhang, L.7    Wen, X.D.8    Qi, L.W.9    Gao, N.10    Li, P.11
  • 19
    • 48649093632 scopus 로고    scopus 로고
    • 6-Shogaol induces apoptosis in human colorectal carcinoma cells via ROS production, caspase activation, and GADD 153 expression
    • M.H. Pan, M.C. Hsieh, J.M. Kuo, C.S. Lai, H. Wu, S. Sang, and C.T. Ho 6-Shogaol induces apoptosis in human colorectal carcinoma cells via ROS production, caspase activation, and GADD 153 expression Mol. Nutr. Food Res. 52 2008 527 537
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 527-537
    • Pan, M.H.1    Hsieh, M.C.2    Kuo, J.M.3    Lai, C.S.4    Wu, H.5    Sang, S.6    Ho, C.T.7
  • 20
    • 84887303412 scopus 로고    scopus 로고
    • 6-Shogaol induces apoptosis in human leukemia cells through a process involving caspase-mediated cleavage of eIF2α
    • Q. Liu, Y.B. Peng, P. Zhou, L.W. Qi, M. Zhang, N. Gao, E.H. Liu, and P. Li 6-Shogaol induces apoptosis in human leukemia cells through a process involving caspase-mediated cleavage of eIF2α Mol. Cancer 12 2013 135
    • (2013) Mol. Cancer , vol.12 , pp. 135
    • Liu, Q.1    Peng, Y.B.2    Zhou, P.3    Qi, L.W.4    Zhang, M.5    Gao, N.6    Liu, E.H.7    Li, P.8
  • 23
    • 57549097842 scopus 로고    scopus 로고
    • 6-Shogaol suppressed lipopolysaccharide-induced up-expression of iNOS and COX-2 in murine macrophages
    • M.H. Pan, M.C. Hsieh, P.C. Hsu, S.Y. Ho, C.S. Lai, H. Wu, S. Sang, and C.T. Ho 6-Shogaol suppressed lipopolysaccharide-induced up-expression of iNOS and COX-2 in murine macrophages Mol. Nutr. Food Res. 52 2008 1467 1477
    • (2008) Mol. Nutr. Food Res. , vol.52 , pp. 1467-1477
    • Pan, M.H.1    Hsieh, M.C.2    Hsu, P.C.3    Ho, S.Y.4    Lai, C.S.5    Wu, H.6    Sang, S.7    Ho, C.T.8
  • 24
    • 77957077028 scopus 로고    scopus 로고
    • 6-Shogaol is more effective than 6-gingerol and curcumin in inhibiting 12-O-tetradecanoylphorbol 13-acetate-induced tumor promotion in mice
    • H. Wu, M.C. Hsieh, C.Y. Lo, C.B. Liu, S. Sang, C.T. Ho, and M.H. Pan 6-Shogaol is more effective than 6-gingerol and curcumin in inhibiting 12-O-tetradecanoylphorbol 13-acetate-induced tumor promotion in mice Mol. Nutr. Food Res. 54 2010 1296 1306
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1296-1306
    • Wu, H.1    Hsieh, M.C.2    Lo, C.Y.3    Liu, C.B.4    Sang, S.5    Ho, C.T.6    Pan, M.H.7
  • 25
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • F. Tietze Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues Anal. Biochem. 27 1969 502 522
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 26
    • 0019740345 scopus 로고
    • Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples
    • T.P. Akerboom, and H. Sies Assay of glutathione, glutathione disulfide, and glutathione mixed disulfides in biological samples Methods Enzymol. 77 1981 373 382
    • (1981) Methods Enzymol. , vol.77 , pp. 373-382
    • Akerboom, T.P.1    Sies, H.2
  • 27
    • 0022272493 scopus 로고
    • Determination of glutathione and glutathione disulfide in biological samples
    • M.E. Anderson Determination of glutathione and glutathione disulfide in biological samples Methods Enzymol. 113 1985 548 555
    • (1985) Methods Enzymol. , vol.113 , pp. 548-555
    • Anderson, M.E.1
  • 29
    • 0037401695 scopus 로고    scopus 로고
    • Substrate access and processing by the 20S proteasome core particle
    • M. Groll, and R. Huber Substrate access and processing by the 20S proteasome core particle Int. J. Biochem. Cell Biol. 35 2003 606 616
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 606-616
    • Groll, M.1    Huber, R.2
  • 30
    • 84868139074 scopus 로고    scopus 로고
    • Calyculin A causes sensitization to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by ROS-mediated down-regulation of cellular FLICE-inhibiting protein (c-FLIP) and by enhancing death receptor 4 mRNA stabilization
    • S.M. Woo, K.J. Min, and T.K. Kwon Calyculin A causes sensitization to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced apoptosis by ROS-mediated down-regulation of cellular FLICE-inhibiting protein (c-FLIP) and by enhancing death receptor 4 mRNA stabilization Apoptosis 17 2012 1223 1234
    • (2012) Apoptosis , vol.17 , pp. 1223-1234
    • Woo, S.M.1    Min, K.J.2    Kwon, T.K.3
  • 31
    • 77953811663 scopus 로고    scopus 로고
    • Compound C sensitizes Caki renal cancer cells to TRAIL-induced apoptosis through reactive oxygen species-mediated down-regulation of c-FLIPL and Mcl-1
    • J.H. Jang, T.J. Lee, E.S. Yang, S. Min do, Y.H. Kim, S.H. Kim, Y.H. Choi, J.W. Park, K.S. Choi, and T.K. Kwon Compound C sensitizes Caki renal cancer cells to TRAIL-induced apoptosis through reactive oxygen species-mediated down-regulation of c-FLIPL and Mcl-1 Exp. Cell Res. 316 2010 2194 2203
    • (2010) Exp. Cell Res. , vol.316 , pp. 2194-2203
    • Jang, J.H.1    Lee, T.J.2    Yang, E.S.3    Min Do, S.4    Kim, Y.H.5    Kim, S.H.6    Choi, Y.H.7    Park, J.W.8    Choi, K.S.9    Kwon, T.K.10
  • 32
    • 67349228750 scopus 로고    scopus 로고
    • Withaferin A sensitizes TRAIL-induced apoptosis through reactive oxygen species-mediated up-regulation of death receptor 5 and down-regulation of c-FLIP
    • T.J. Lee, H.J. Um, S. Min do, J.W. Park, K.S. Choi, and T.K. Kwon Withaferin A sensitizes TRAIL-induced apoptosis through reactive oxygen species-mediated up-regulation of death receptor 5 and down-regulation of c-FLIP Free Radic. Biol. Med. 46 2009 1639 1649
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1639-1649
    • Lee, T.J.1    Um, H.J.2    Min Do, S.3    Park, J.W.4    Choi, K.S.5    Kwon, T.K.6
  • 34
    • 84865117886 scopus 로고    scopus 로고
    • Molecular mechanism inhibiting human hepatocarcinoma cell invasion by 6-shogaol and 6-gingerol
    • C.J. Weng, C.P. Chou, C.T. Ho, and G.C. Yen Molecular mechanism inhibiting human hepatocarcinoma cell invasion by 6-shogaol and 6-gingerol Mol. Nutr. Food Res. 56 2012 1304 1314
    • (2012) Mol. Nutr. Food Res. , vol.56 , pp. 1304-1314
    • Weng, C.J.1    Chou, C.P.2    Ho, C.T.3    Yen, G.C.4
  • 35
    • 78349245958 scopus 로고    scopus 로고
    • Anti-invasion effects of 6-shogaol and 6-gingerol, two active components in ginger, on human hepatocarcinoma cells
    • C.J. Weng, C.F. Wu, H.W. Huang, C.T. Ho, and G.C. Yen Anti-invasion effects of 6-shogaol and 6-gingerol, two active components in ginger, on human hepatocarcinoma cells Mol. Nutr. Food Res. 54 2010 1618 1627
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 1618-1627
    • Weng, C.J.1    Wu, C.F.2    Huang, H.W.3    Ho, C.T.4    Yen, G.C.5
  • 36
    • 78649411147 scopus 로고    scopus 로고
    • 6-Shogaol, an active constituent of ginger, inhibits breast cancer cell invasion by reducing matrix metalloproteinase-9 expression via blockade of nuclear factor-κB activation
    • H. Ling, H. Yang, S.H. Tan, W.K. Chui, and E.H. Chew 6-Shogaol, an active constituent of ginger, inhibits breast cancer cell invasion by reducing matrix metalloproteinase-9 expression via blockade of nuclear factor-κB activation Br. J. Pharmacol. 161 2010 1763 1777
    • (2010) Br. J. Pharmacol. , vol.161 , pp. 1763-1777
    • Ling, H.1    Yang, H.2    Tan, S.H.3    Chui, W.K.4    Chew, E.H.5
  • 37
    • 70350317873 scopus 로고    scopus 로고
    • 6-Shogaol, an active constituent of dietary ginger, induces autophagy by inhibiting the AKT/mTOR pathway in human non-small cell lung cancer A549 cells
    • J.Y. Hung, Y.L. Hsu, C.T. Li, Y.C. Ko, W.C. Ni, M.S. Huang, and P.L. Kuo 6-Shogaol, an active constituent of dietary ginger, induces autophagy by inhibiting the AKT/mTOR pathway in human non-small cell lung cancer A549 cells J. Agric. Food Chem. 57 2009 9809 9816
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 9809-9816
    • Hung, J.Y.1    Hsu, Y.L.2    Li, C.T.3    Ko, Y.C.4    Ni, W.C.5    Huang, M.S.6    Kuo, P.L.7
  • 38
    • 0026734484 scopus 로고
    • Enzymatic reduction of shogaol: A novel biotransformation pathway for the alpha,beta-unsaturated ketone system
    • Y.J. Surh, and S.S. Lee Enzymatic reduction of shogaol: a novel biotransformation pathway for the alpha,beta-unsaturated ketone system Biochem. Int. 27 1992 179 187
    • (1992) Biochem. Int. , vol.27 , pp. 179-187
    • Surh, Y.J.1    Lee, S.S.2
  • 39
    • 0014347894 scopus 로고
    • Enzymes catalysing conjugations of glutathione with alpha-beta-unsaturated carbonyl compounds
    • E. Boyland, and L.F. Chasseaud Enzymes catalysing conjugations of glutathione with alpha-beta-unsaturated carbonyl compounds Biochem. J. 109 1968 651 661
    • (1968) Biochem. J. , vol.109 , pp. 651-661
    • Boyland, E.1    Chasseaud, L.F.2
  • 40
    • 0025304632 scopus 로고
    • Conjugation of 9-deoxy-delta 9,delta 12(E)-prostaglandin D2 with intracellular glutathione and enhancement of its antiproliferative activity by glutathione depletion
    • J. Atsmon, M.L. Freeman, M.J. Meredith, B.J. Sweetman, and L.J. Roberts 2nd Conjugation of 9-deoxy-delta 9,delta 12(E)-prostaglandin D2 with intracellular glutathione and enhancement of its antiproliferative activity by glutathione depletion Cancer Res. 50 1990 1879 1885
    • (1990) Cancer Res. , vol.50 , pp. 1879-1885
    • Atsmon, J.1    Freeman, M.L.2    Meredith, M.J.3    Sweetman, B.J.4    Roberts, L.J.5
  • 41
    • 34547137901 scopus 로고    scopus 로고
    • Exposure to hydrogen peroxide diminishes NF-kappaB activation, IkappaB-alpha degradation, and proteasome activity in neutrophils
    • J.W. Zmijewski, X. Zhao, Z. Xu, and E. Abraham Exposure to hydrogen peroxide diminishes NF-kappaB activation, IkappaB-alpha degradation, and proteasome activity in neutrophils Am. J. Physiol. Cell Physiol. 293 2007 C255 C266
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293 , pp. C255-C266
    • Zmijewski, J.W.1    Zhao, X.2    Xu, Z.3    Abraham, E.4
  • 42
    • 79251477528 scopus 로고    scopus 로고
    • Dual regulation of hepatocyte apoptosis by reactive oxygen species: Increases in transcriptional expression and decreases in proteasomal degradation of BimEL
    • Y. Ishihara, K. Takeuchi, F. Ito, and N. Shimamoto Dual regulation of hepatocyte apoptosis by reactive oxygen species: increases in transcriptional expression and decreases in proteasomal degradation of BimEL J. Cell. Physiol. 226 2011 1007 1016
    • (2011) J. Cell. Physiol. , vol.226 , pp. 1007-1016
    • Ishihara, Y.1    Takeuchi, K.2    Ito, F.3    Shimamoto, N.4
  • 43
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Y.P. Li, Y. Chen, A.S. Li, and M.B. Reid Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes Am. J. Physiol. Cell Physiol. 285 2003 C806 C812
    • (2003) Am. J. Physiol. Cell Physiol. , vol.285 , pp. C806-C812
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 44
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated
    • F. Shang, X. Gong, and A. Taylor Activity of ubiquitin-dependent pathway in response to oxidative stress. Ubiquitin-activating enzyme is transiently up-regulated J. Biol. Chem. 272 1997 23086 23093
    • (1997) J. Biol. Chem. , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 45
    • 84896748716 scopus 로고    scopus 로고
    • Antipsychotic agent thioridazine sensitizes renal carcinoma Caki cells to TRAIL-induced apoptosis through reactive oxygen species-mediated inhibition of Akt signaling and downregulation of Mcl-1 and c-FLIP(L)
    • K.J. Min, B.R. Seo, Y.C. Bae, Y.H. Yoo, and T.K. Kwon Antipsychotic agent thioridazine sensitizes renal carcinoma Caki cells to TRAIL-induced apoptosis through reactive oxygen species-mediated inhibition of Akt signaling and downregulation of Mcl-1 and c-FLIP(L) Cell Death Dis. 5 2014 e1063
    • (2014) Cell Death Dis. , vol.5 , pp. e1063
    • Min, K.J.1    Seo, B.R.2    Bae, Y.C.3    Yoo, Y.H.4    Kwon, T.K.5
  • 46
    • 84875472185 scopus 로고    scopus 로고
    • MTOR complex 2 is involved in regulation of Cbl-dependent c-FLIP degradation and sensitivity of TRAIL-induced apoptosis
    • L. Zhao, P. Yue, F.R. Khuri, and S.Y. Sun MTOR complex 2 is involved in regulation of Cbl-dependent c-FLIP degradation and sensitivity of TRAIL-induced apoptosis Cancer Res. 73 2013 1946 1957
    • (2013) Cancer Res. , vol.73 , pp. 1946-1957
    • Zhao, L.1    Yue, P.2    Khuri, F.R.3    Sun, S.Y.4
  • 47
    • 32044447161 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover
    • L. Chang, H. Kamata, G. Solinas, J.L. Luo, S. Maeda, K. Venuprasad, Y.C. Liu, and M. Karin The E3 ubiquitin ligase itch couples JNK activation to TNFalpha-induced cell death by inducing c-FLIP(L) turnover Cell 124 2006 601 613
    • (2006) Cell , vol.124 , pp. 601-613
    • Chang, L.1    Kamata, H.2    Solinas, G.3    Luo, J.L.4    Maeda, S.5    Venuprasad, K.6    Liu, Y.C.7    Karin, M.8


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