메뉴 건너뛰기




Volumn 36, Issue 6, 2015, Pages 696-706

Fisetin, a dietary flavonoid, induces apoptosis of cancer cells by inhibiting HSF1 activity through blocking its binding to the hsp70 promoter

Author keywords

[No Author keywords available]

Indexed keywords

BCL 2 ASSOCIATED ATHANOGENE DOMAIN 3 PROTEIN; FISETIN; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70; HEAT SHOCK TRANSCRIPTION FACTOR 1; LUCIFERASE; PROTEIN; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; APOPTOSIS REGULATORY PROTEIN; BAG3 PROTEIN, HUMAN; DNA BINDING PROTEIN; FLAVONOID; HEAT SHOCK TRANSCRIPTION FACTOR; HSPB1 PROTEIN, HUMAN; MCL1 PROTEIN, HUMAN; PROTEIN BCL 2; PROTEIN BCL X; PROTEIN BINDING; PROTEIN MCL 1; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 84941618262     PISSN: 01433334     EISSN: 14602180     Source Type: Journal    
DOI: 10.1093/carcin/bgv045     Document Type: Article
Times cited : (68)

References (52)
  • 1
    • 0031928015 scopus 로고    scopus 로고
    • Nutraceuticals: poised for a healthy slice of the healthcare market? Nat
    • Brower, V. (1998) Nutraceuticals: poised for a healthy slice of the healthcare market? Nat. Biotechnol., 16, 728-731.
    • (1998) Biotechnol. , vol.16 , pp. 728-731
    • Brower, V.1
  • 2
    • 0033578922 scopus 로고    scopus 로고
    • Regulation of "nutraceuticals"
    • Zeisel, S.H. (1999) Regulation of "nutraceuticals". Science, 285, 1853-1855.
    • (1999) Science , vol.285 , pp. 1853-1855
    • Zeisel, S.H.1
  • 3
    • 33746736380 scopus 로고    scopus 로고
    • Flavonoids protect human retinal pigment epithelial cells from oxidative-stress-induced death
    • Hanneken, A. et al. (2006) Flavonoids protect human retinal pigment epithelial cells from oxidative-stress-induced death. Invest Ophthalmol. Vis. Sci., 47, 3164-3177.
    • (2006) Invest Ophthalmol. Vis. Sci. , vol.47 , pp. 3164-3177
    • Hanneken, A.1
  • 4
    • 0038518110 scopus 로고    scopus 로고
    • Fisetin, a flavonol, inhibits TH2-type cytokine production by activated human basophils
    • Higa, S. et al. (2003) Fisetin, a flavonol, inhibits TH2-type cytokine production by activated human basophils. J. Allergy Clin. Immunol., 111, 1299-1306.
    • (2003) J. Allergy Clin. Immunol. , vol.111 , pp. 1299-1306
    • Higa, S.1
  • 5
    • 0033850592 scopus 로고    scopus 로고
    • Dietary intakes of flavonols, flavones and isoflavones by Japanese women and the inverse correlation between quercetin intake and plasma LDL cholesterol concentration
    • Arai, Y. et al. (2000) Dietary intakes of flavonols, flavones and isoflavones by Japanese women and the inverse correlation between quercetin intake and plasma LDL cholesterol concentration. J. Nutr., 130, 2243-2250.
    • (2000) J. Nutr. , vol.130 , pp. 2243-2250
    • Arai, Y.1
  • 6
    • 47249134657 scopus 로고    scopus 로고
    • Fisetin, a novel dietary flavonoid, causes apoptosis and cell cycle arrest in human prostate cancer LNCaP cells
    • Khan, N. et al. (2008) Fisetin, a novel dietary flavonoid, causes apoptosis and cell cycle arrest in human prostate cancer LNCaP cells. Carcinogenesis, 29, 1049-1056.
    • (2008) Carcinogenesis , vol.29 , pp. 1049-1056
    • Khan, N.1
  • 7
    • 54249097888 scopus 로고    scopus 로고
    • A novel dietary flavonoid fisetin inhibits androgen receptor signaling and tumor growth in athymic nude mice
    • Khan, N. et al. (2008) A novel dietary flavonoid fisetin inhibits androgen receptor signaling and tumor growth in athymic nude mice. Cancer Res., 68, 8555-8563.
    • (2008) Cancer Res. , vol.68 , pp. 8555-8563
    • Khan, N.1
  • 8
    • 79955998411 scopus 로고    scopus 로고
    • Inhibition of human melanoma cell growth by the dietary flavonoid fisetin is associated with disruption of Wnt/ß-catenin signaling and decreased Mitf levels
    • Syed, D.N. et al. (2011) Inhibition of human melanoma cell growth by the dietary flavonoid fisetin is associated with disruption of Wnt/ß-catenin signaling and decreased Mitf levels. J. Invest Dermatol., 131, 1291-1299.
    • (2011) J. Invest Dermatol. , vol.131 , pp. 1291-1299
    • Syed, D.N.1
  • 9
    • 66749159615 scopus 로고    scopus 로고
    • Dietary flavonoid fisetin induces a forced exit from mitosis by targeting the mitotic spindle checkpoint
    • Salmela, A.L. et al. (2009) Dietary flavonoid fisetin induces a forced exit from mitosis by targeting the mitotic spindle checkpoint. Carcinogenesis, 30, 1032-1040.
    • (2009) Carcinogenesis , vol.30 , pp. 1032-1040
    • Salmela, A.L.1
  • 10
    • 70349881605 scopus 로고    scopus 로고
    • Fisetin, a natural flavonoid, targets chemoresistant human pancreatic cancer AsPC-1 cells through DR3-mediated inhibition of NF-kappaB
    • Murtaza, I. et al. (2009) Fisetin, a natural flavonoid, targets chemoresistant human pancreatic cancer AsPC-1 cells through DR3-mediated inhibition of NF-kappaB. Int. J. Cancer, 125, 2465-2473.
    • (2009) Int. J. Cancer , vol.125 , pp. 2465-2473
    • Murtaza, I.1
  • 11
    • 77955355798 scopus 로고    scopus 로고
    • Fisetin induces autophagic cell death through suppression of mTOR signaling pathway in prostate cancer cells
    • Suh, Y. et al. (2010) Fisetin induces autophagic cell death through suppression of mTOR signaling pathway in prostate cancer cells. Carcinogenesis, 31, 1424-1433.
    • (2010) Carcinogenesis , vol.31 , pp. 1424-1433
    • Suh, Y.1
  • 12
    • 84856329735 scopus 로고    scopus 로고
    • Dual inhibition of phosphatidylinositol 3-kinase/Akt and mammalian target of rapamycin signaling in human nonsmall cell lung cancer cells by a dietary flavonoid fisetin
    • Khan, N. et al. (2012) Dual inhibition of phosphatidylinositol 3-kinase/Akt and mammalian target of rapamycin signaling in human nonsmall cell lung cancer cells by a dietary flavonoid fisetin. Int. J. Cancer, 130, 1695-1705.
    • (2012) Int. J. Cancer , vol.130 , pp. 1695-1705
    • Khan, N.1
  • 13
    • 84925498001 scopus 로고    scopus 로고
    • Fisetin induces apoptosis in human nonsmall lung cancer cells via a mitochondria-mediated pathway
    • Kang, K.A. et al. (2015) Fisetin induces apoptosis in human nonsmall lung cancer cells via a mitochondria-mediated pathway. In Vitro Cell. Dev. Biol. Anim., 51, 300-309.
    • (2015) In Vitro Cell. Dev. Biol. Anim. , vol.51 , pp. 300-309
    • Kang, K.A.1
  • 14
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R.I. (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev., 22, 1427-1438.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 15
    • 43249125196 scopus 로고    scopus 로고
    • New insights into the mechanism of heat shock response activation
    • Shamovsky, I. et al. (2008) New insights into the mechanism of heat shock response activation. Cell. Mol. Life Sci., 65, 855-861.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 855-861
    • Shamovsky, I.1
  • 16
    • 0028961801 scopus 로고
    • Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells
    • Jäättelä, M. (1995) Over-expression of hsp70 confers tumorigenicity to mouse fibrosarcoma cells. Int. J. Cancer, 60, 689-693.
    • (1995) Int. J. Cancer , vol.60 , pp. 689-693
    • Jäättelä, M.1
  • 17
    • 0032404094 scopus 로고    scopus 로고
    • Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones
    • Garrido, C. et al. (1998) Heat shock protein 27 enhances the tumorigenicity of immunogenic rat colon carcinoma cell clones. Cancer Res., 58, 5495-5499.
    • (1998) Cancer Res. , vol.58 , pp. 5495-5499
    • Garrido, C.1
  • 18
    • 33644841943 scopus 로고    scopus 로고
    • Ha-ras(val12) induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Haras(val12)-transformed cells
    • Stanhill, A. et al. (2006) Ha-ras(val12) induces HSP70b transcription via the HSE/HSF1 system, but HSP70b expression is suppressed in Haras(val12)-transformed cells. Oncogene, 25, 1485-1495.
    • (2006) Oncogene , vol.25 , pp. 1485-1495
    • Stanhill, A.1
  • 19
    • 0021721180 scopus 로고
    • Regulation of heat shock protein 70 gene expression by c-myc
    • Kingston, R.E. et al. (1984) Regulation of heat shock protein 70 gene expression by c-myc. Nature, 312, 280-282.
    • (1984) Nature , vol.312 , pp. 280-282
    • Kingston, R.E.1
  • 20
    • 0022995620 scopus 로고
    • Binding of polyomavirus large T antigen to the human hsp70 promoter is not required for trans activation
    • Kingston, R.E. et al. (1986) Binding of polyomavirus large T antigen to the human hsp70 promoter is not required for trans activation. Mol. Cell. Biol., 6, 3180-3190.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3180-3190
    • Kingston, R.E.1
  • 21
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis
    • Dai, C. et al. (2007) Heat shock factor 1 is a powerful multifaceted modifier of carcinogenesis. Cell, 130, 1005-1018.
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1
  • 22
    • 79959947025 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 is a key determinant of HCC development by regulating hepatic steatosis and metabolic syndrome
    • Jin, X. et al. (2011) Heat shock transcription factor 1 is a key determinant of HCC development by regulating hepatic steatosis and metabolic syndrome. Cell Metab., 14, 91-103.
    • (2011) Cell Metab. , vol.14 , pp. 91-103
    • Jin, X.1
  • 23
    • 28544433004 scopus 로고    scopus 로고
    • Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin
    • Guo, F. et al. (2005) Abrogation of heat shock protein 70 induction as a strategy to increase antileukemia activity of heat shock protein 90 inhibitor 17-allylamino-demethoxy geldanamycin. Cancer Res., 65, 10536-10544.
    • (2005) Cancer Res. , vol.65 , pp. 10536-10544
    • Guo, F.1
  • 24
    • 28244456529 scopus 로고    scopus 로고
    • Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis
    • Rocchi, P. et al. (2005) Increased Hsp27 after androgen ablation facilitates androgen-independent progression in prostate cancer via signal transducers and activators of transcription 3-mediated suppression of apoptosis. Cancer Res., 65, 11083-11093.
    • (2005) Cancer Res. , vol.65 , pp. 11083-11093
    • Rocchi, P.1
  • 25
    • 66149118221 scopus 로고    scopus 로고
    • HSF1-mediated BAG3 expression attenuates apoptosis in 4-hydroxynonenal-treated colon cancer cells via stabilization of anti-apoptotic Bcl-2 proteins
    • Jacobs, A.T. et al. (2009) HSF1-mediated BAG3 expression attenuates apoptosis in 4-hydroxynonenal-treated colon cancer cells via stabilization of anti-apoptotic Bcl-2 proteins. J. Biol. Chem., 284, 9176-9183.
    • (2009) J. Biol. Chem. , vol.284 , pp. 9176-9183
    • Jacobs, A.T.1
  • 26
    • 0028847915 scopus 로고
    • Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity
    • Takayama, S. et al. (1995) Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity. Cell, 80, 279-284.
    • (1995) Cell , vol.80 , pp. 279-284
    • Takayama, S.1
  • 27
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
    • Lüders, J. et al. (2000) The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. J. Biol. Chem., 275, 4613-4617.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4613-4617
    • Lüders, J.1
  • 28
    • 0042208135 scopus 로고    scopus 로고
    • CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins
    • Doong, H. et al. (2003) CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins. J. Biol. Chem., 278, 28490-28500.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28490-28500
    • Doong, H.1
  • 29
    • 78751505781 scopus 로고    scopus 로고
    • KRIBB11 inhibits HSP70 synthesis through inhibition of heat shock factor 1 function by impairing the recruitment of positive transcription elongation factor b to the hsp70 promoter
    • Yoon, Y.J. et al. (2011) KRIBB11 inhibits HSP70 synthesis through inhibition of heat shock factor 1 function by impairing the recruitment of positive transcription elongation factor b to the hsp70 promoter. J. Biol. Chem., 286, 1737-1747.
    • (2011) J. Biol. Chem. , vol.286 , pp. 1737-1747
    • Yoon, Y.J.1
  • 30
    • 0025678202 scopus 로고
    • Flavonoids inhibit the expression of heat shock proteins
    • Hosokawa, N. et al. (1990) Flavonoids inhibit the expression of heat shock proteins. Cell Struct. Funct., 15, 393-401.
    • (1990) Cell Struct. Funct. , vol.15 , pp. 393-401
    • Hosokawa, N.1
  • 31
    • 0029664396 scopus 로고    scopus 로고
    • Modulation of prostaglandin A1-induced thermotolerance by quercetin in human leukemic cells: role of heat shock protein 70
    • Elia, G. et al. (1996) Modulation of prostaglandin A1-induced thermotolerance by quercetin in human leukemic cells: role of heat shock protein 70. Cancer Res., 56, 210-217.
    • (1996) Cancer Res. , vol.56 , pp. 210-217
    • Elia, G.1
  • 32
    • 0031590444 scopus 로고    scopus 로고
    • Quercetin inhibits heat shock protein induction but not heat shock factor DNA-binding in human breast carcinoma cells
    • Hansen, R.K. et al. (1997) Quercetin inhibits heat shock protein induction but not heat shock factor DNA-binding in human breast carcinoma cells. Biochem. Biophys. Res. Commun., 239, 851-856.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 851-856
    • Hansen, R.K.1
  • 33
    • 84864585171 scopus 로고    scopus 로고
    • HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers
    • Mendillo, M.L. et al. (2012) HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell, 150, 549-562.
    • (2012) Cell , vol.150 , pp. 549-562
    • Mendillo, M.L.1
  • 34
    • 0029947346 scopus 로고    scopus 로고
    • Basal regulatory promoter elements of the hsp27 gene in human breast cancer cells
    • Oesterreich, S. et al. (1996) Basal regulatory promoter elements of the hsp27 gene in human breast cancer cells. Biochem. Biophys. Res. Commun., 222, 155-163.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 155-163
    • Oesterreich, S.1
  • 35
    • 0028798425 scopus 로고
    • Response of heat shock element within the human HSP70 promoter to mutated p53 genes
    • Tsutsumi-Ishii, Y. et al. (1995) Response of heat shock element within the human HSP70 promoter to mutated p53 genes. Cell Growth Differ., 6, 1-8.
    • (1995) Cell Growth Differ. , vol.6 , pp. 1-8
    • Tsutsumi-Ishii, Y.1
  • 36
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell, L. et al. (2009) Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin. Ther. Targets, 13, 469-478.
    • (2009) Expert Opin. Ther. Targets , vol.13 , pp. 469-478
    • Whitesell, L.1
  • 37
    • 0035100834 scopus 로고    scopus 로고
    • Pre-clinical and clinical study of QC12, a water-soluble, pro-drug of quercetin
    • Mulholland, P.J. et al. (2001) Pre-clinical and clinical study of QC12, a water-soluble, pro-drug of quercetin. Ann. Oncol., 12, 245-248.
    • (2001) Ann. Oncol. , vol.12 , pp. 245-248
    • Mulholland, P.J.1
  • 38
    • 0034212740 scopus 로고    scopus 로고
    • Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells
    • Yokota, S. et al. (2000) Benzylidene lactam compound, KNK437, a novel inhibitor of acquisition of thermotolerance and heat shock protein induction in human colon carcinoma cells. Cancer Res., 60, 2942-2948.
    • (2000) Cancer Res. , vol.60 , pp. 2942-2948
    • Yokota, S.1
  • 39
    • 0032762599 scopus 로고    scopus 로고
    • Stresgenin B, an inhibitor of heat-induced heat shock protein gene expression, produced by Streptomyces sp. AS-9
    • Akagawa, H. et al. (1999) Stresgenin B, an inhibitor of heat-induced heat shock protein gene expression, produced by Streptomyces sp. AS-9. J. Antibiot. (Tokyo)., 52, 960-970.
    • (1999) J. Antibiot. (Tokyo). , vol.52 , pp. 960-970
    • Akagawa, H.1
  • 40
    • 33646900838 scopus 로고    scopus 로고
    • Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death
    • Westerheide, S.D. et al. (2006) Triptolide, an inhibitor of the human heat shock response that enhances stress-induced cell death. J. Biol. Chem., 281, 9616-9622.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9616-9622
    • Westerheide, S.D.1
  • 41
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur, N. et al. (2006) Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors. Cancer Res., 66, 1783-1791.
    • (2006) Cancer Res. , vol.66 , pp. 1783-1791
    • Zaarur, N.1
  • 42
    • 84876098921 scopus 로고    scopus 로고
    • Targeting heat shock proteins by phenethyl isothiocyanate results in cell-cycle arrest and apoptosis of human breast cancer cells
    • Sarkars, R. et al. (2013) Targeting heat shock proteins by phenethyl isothiocyanate results in cell-cycle arrest and apoptosis of human breast cancer cells. Nutr. Cancer, 65, 480-493.
    • (2013) Nutr. Cancer , vol.65 , pp. 480-493
    • Sarkars, R.1
  • 43
    • 84880438841 scopus 로고    scopus 로고
    • Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state
    • Santagata, S. et al. (2013) Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state. Science, 341, 1238303.
    • (2013) Science , vol.341 , pp. 1238303
    • Santagata, S.1
  • 44
    • 84885415875 scopus 로고    scopus 로고
    • The natural compound cantharidin induces cancer cell death through inhibition of heat shock protein 70 (HSP70) and Bcl-2-associated athanogene domain 3 (BAG3) expression by blocking heat shock factor 1 (HSF1) binding to promoters
    • Kim, J.A. et al. (2013) The natural compound cantharidin induces cancer cell death through inhibition of heat shock protein 70 (HSP70) and Bcl-2-associated athanogene domain 3 (BAG3) expression by blocking heat shock factor 1 (HSF1) binding to promoters. J. Biol. Chem., 288, 28713-28726.
    • (2013) J. Biol. Chem. , vol.288 , pp. 28713-28726
    • Kim, J.A.1
  • 45
    • 48549086880 scopus 로고    scopus 로고
    • Triptolide-induced transcriptional arrest is associated with changes in nuclear substructure
    • Leuenroth, S.J. et al. (2008) Triptolide-induced transcriptional arrest is associated with changes in nuclear substructure. Cancer Res., 68, 5257-5266.
    • (2008) Cancer Res. , vol.68 , pp. 5257-5266
    • Leuenroth, S.J.1
  • 46
    • 79961166833 scopus 로고    scopus 로고
    • Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins
    • Wang, R.E. et al. (2011) Biotinylated quercetin as an intrinsic photoaffinity proteomics probe for the identification of quercetin target proteins. Bioorg. Med. Chem., 19, 4710-4720.
    • (2011) Bioorg. Med. Chem. , vol.19 , pp. 4710-4720
    • Wang, R.E.1
  • 47
    • 57049157033 scopus 로고    scopus 로고
    • BCL-2 family antagonists for cancer therapy
    • Lessene, G. et al. (2008) BCL-2 family antagonists for cancer therapy. Nat. Rev. Drug Discov., 7, 989-1000.
    • (2008) Nat. Rev. Drug Discov. , vol.7 , pp. 989-1000
    • Lessene, G.1
  • 48
    • 84881091005 scopus 로고    scopus 로고
    • Decoding and unlocking the BCL-2 dependency of cancer cells
    • Juin, P. et al. (2013) Decoding and unlocking the BCL-2 dependency of cancer cells. Nat. Rev. Cancer, 13, 455-465.
    • (2013) Nat. Rev. Cancer , vol.13 , pp. 455-465
    • Juin, P.1
  • 49
    • 33750834023 scopus 로고    scopus 로고
    • The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized
    • van Delft, M.F. et al. (2006) The BH3 mimetic ABT-737 targets selective Bcl-2 proteins and efficiently induces apoptosis via Bak/Bax if Mcl-1 is neutralized. Cancer Cell, 10, 389-399.
    • (2006) Cancer Cell , vol.10 , pp. 389-399
    • van Delft, M.F.1
  • 50
    • 33846674886 scopus 로고    scopus 로고
    • Mcl-1 down-regulation potentiates ABT-737 lethality by cooperatively inducing Bak activation and Bax translocation
    • Chen, S. et al. (2007) Mcl-1 down-regulation potentiates ABT-737 lethality by cooperatively inducing Bak activation and Bax translocation. Cancer Res., 67, 782-791.
    • (2007) Cancer Res. , vol.67 , pp. 782-791
    • Chen, S.1
  • 51
    • 68949099384 scopus 로고    scopus 로고
    • RNA silencing of Mcl-1 enhances ABT-737-mediated apoptosis in melanoma: role for a caspase-8-dependent pathway
    • Keuling, A.M. et al. (2009) RNA silencing of Mcl-1 enhances ABT-737-mediated apoptosis in melanoma: role for a caspase-8-dependent pathway. PLoS One, 4, e6651.
    • (2009) PLoS One , vol.4
    • Keuling, A.M.1
  • 52
    • 77249119762 scopus 로고    scopus 로고
    • The landscape of somatic copy-number alteration across human cancers
    • Beroukhim, R. et al. (2010) The landscape of somatic copy-number alteration across human cancers. Nature, 463, 899-905.
    • (2010) Nature , vol.463 , pp. 899-905
    • Beroukhim, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.