메뉴 건너뛰기




Volumn 2, Issue 1, 2016, Pages

Correction to: A Bowman–Birk inhibitor induces apoptosis in human breast adenocarcinoma through mitochondrial impairment and oxidative damage following proteasome 20S inhibition (Cell Death Di scovery, (2016), 2, 1, (15067), 10.1038/cddiscovery.2015.67);A bowman–birk inhibitor induces apoptosis in human breast adenocarcinoma through mitochondrial impairment and oxidative damage following proteasome 20S inhibition

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85009182975     PISSN: None     EISSN: 20587716     Source Type: Journal    
DOI: 10.1038/s41420-024-02155-4     Document Type: Erratum
Times cited : (41)

References (74)
  • 2
    • 0025166613 scopus 로고
    • Suppression of dimethylhydrazine-induced carcinogenesis in mice by dietary addition of the Bowman-Birk protease inhibitor
    • St Clair WH, Billings PC, Carew JA, Keller-McGandy C, Newberne P, Kennedy AR. Suppression of dimethylhydrazine-induced carcinogenesis in mice by dietary addition of the Bowman-Birk protease inhibitor. Cancer Res 1990; 50: 580–586.
    • (1990) Cancer Res , vol.50 , pp. 580-586
    • St Clair, W.H.1    Billings, P.C.2    Carew, J.A.3    Keller-McGandy, C.4    Newberne, P.5    Kennedy, A.R.6
  • 3
    • 0025348693 scopus 로고
    • Protease inhibitor suppression of colon and anal gland carcinogenesis induced by dimethylhydrazine
    • Billings PC, Newberne PM, Kennedy AR. Protease inhibitor suppression of colon and anal gland carcinogenesis induced by dimethylhydrazine. Carcinogenesis 1990; 11: 1083–1086.
    • (1990) Carcinogenesis , vol.11 , pp. 1083-1086
    • Billings, P.C.1    Newberne, P.M.2    Kennedy, A.R.3
  • 4
    • 77649316496 scopus 로고    scopus 로고
    • The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases
    • Clemente A, Moreno FJ, Marin-Manzano Mdel C, Jimenez E, Domoney C. The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases. Mol Nutr Food Res 2010; 54: 396–405.
    • (2010) Mol Nutr Food Res , vol.54 , pp. 396-405
    • Clemente, A.1    Moreno, F.J.2    Marin-Manzano Mdel, C.3    Jimenez, E.4    Domoney, C.5
  • 5
    • 0027318686 scopus 로고
    • Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA
    • Kennedy AR, Billings PC, Maki PA, Newberne P. Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA. Nutr Cancer 1993; 19: 191–200.
    • (1993) Nutr Cancer , vol.19 , pp. 191-200
    • Kennedy, A.R.1    Billings, P.C.2    Maki, P.A.3    Newberne, P.4
  • 8
    • 0034486550 scopus 로고    scopus 로고
    • Clinical modulation of oral leukoplakia and protease activity by Bowman-Birk inhibitor concentrate in a phase IIa chemoprevention trial
    • Armstrong WB, Kennedy AR, Wan XS, Taylor TH, Nguyen QA, Jensen J et al. Clinical modulation of oral leukoplakia and protease activity by Bowman-Birk inhibitor concentrate in a phase IIa chemoprevention trial. Clin Cancer Res 2000; 6: 4684–4691.
    • (2000) Clin Cancer Res , vol.6 , pp. 4684-4691
    • Armstrong, W.B.1    Kennedy, A.R.2    Wan, X.S.3    Taylor, T.H.4    Nguyen, Q.A.5    Jensen, J.6
  • 10
    • 0025945685 scopus 로고
    • Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor
    • von Hofe E, Newberne PM, Kennedy AR. Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor. Carcinogenesis 1991; 12: 2147–2150.
    • (1991) Carcinogenesis , vol.12 , pp. 2147-2150
    • von Hofe, E.1    Newberne, P.M.2    Kennedy, A.R.3
  • 11
    • 0033920566 scopus 로고    scopus 로고
    • Protease inhibitor-induced apoptosis: Accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition
    • An WG, Hwang SG, Trepel JB, Blagosklonny MV. Protease inhibitor-induced apoptosis: accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition. Leukemia 2000; 14: 1276–1283.
    • (2000) Leukemia , vol.14 , pp. 1276-1283
    • An, W.G.1    Hwang, S.G.2    Trepel, J.B.3    Blagosklonny, M.V.4
  • 12
    • 0035876208 scopus 로고    scopus 로고
    • Effects of Bowman-Birk inhibitor concentrate (BBIC) in patients with benign prostatic hyperplasia
    • Malkowicz SB, McKenna WG, Vaughn DJ, Wan XS, Propert KJ, Rockwell K et al. Effects of Bowman-Birk inhibitor concentrate (BBIC) in patients with benign prostatic hyperplasia. Prostate 2001; 48: 16–28.
    • (2001) Prostate , vol.48 , pp. 16-28
    • Malkowicz, S.B.1    McKenna, W.G.2    Vaughn, D.J.3    Wan, X.S.4    Propert, K.J.5    Rockwell, K.6
  • 13
    • 77952425329 scopus 로고    scopus 로고
    • Apoptosis and lysosome membrane permeabilization induction on breast cancer cells by an anticarcinogenic Bowman-Birk protease inhibitor from Vigna unguiculata seeds
    • Joanitti GA, Azevedo RB, Freitas SM. Apoptosis and lysosome membrane permeabilization induction on breast cancer cells by an anticarcinogenic Bowman-Birk protease inhibitor from Vigna unguiculata seeds. Cancer Lett 2010; 293: 73–81.
    • (2010) Cancer Lett , vol.293 , pp. 73-81
    • Joanitti, G.A.1    Azevedo, R.B.2    Freitas, S.M.3
  • 14
    • 22844434892 scopus 로고    scopus 로고
    • Bowman-Birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1
    • Chen YW, Huang SC, Lin-Shiau SY, Lin JK. Bowman-Birk inhibitor abates proteasome function and suppresses the proliferation of MCF7 breast cancer cells through accumulation of MAP kinase phosphatase-1. Carcinogenesis 2005; 26: 1296–1306.
    • (2005) Carcinogenesis , vol.26 , pp. 1296-1306
    • Chen, Y.W.1    Huang, S.C.2    Lin-Shiau, S.Y.3    Lin, J.K.4
  • 16
    • 9544239345 scopus 로고    scopus 로고
    • Involvement of the proteasome in the programmed cell death of NGF-deprived sympathetic neurons
    • Sadoul R, Fernandez PA, Quiquerez AL, Martinou I, Maki M, Schroter M et al. Involvement of the proteasome in the programmed cell death of NGF-deprived sympathetic neurons. EMBO J 1996; 15: 3845–3852.
    • (1996) EMBO J , vol.15 , pp. 3845-3852
    • Sadoul, R.1    Fernandez, P.A.2    Quiquerez, A.L.3    Martinou, I.4    Maki, M.5    Schroter, M.6
  • 17
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler HC. Activation of the cell death program by inhibition of proteasome function. Proc Natl Acad Sci USA 1997; 94: 855–860.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 855-860
    • Drexler, H.C.1
  • 18
    • 0030962262 scopus 로고    scopus 로고
    • P53-dependent induction of apoptosis by proteasome inhibitors
    • Lopes UG, Erhardt P, Yao R, Cooper GM. p53-dependent induction of apoptosis by proteasome inhibitors. J Biol Chem 1997; 272: 12893–12896.
    • (1997) J Biol Chem , vol.272 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 19
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana NR, Zemskov EA, Wang G, Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 2001; 10: 1049–1059.
    • (2001) Hum Mol Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 20
    • 1642564603 scopus 로고    scopus 로고
    • Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway
    • Jana NR, Dikshit P, Goswami A, Nukina N. Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway. J Biol Chem 2004; 279: 11680–11685.
    • (2004) J Biol Chem , vol.279 , pp. 11680-11685
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Nukina, N.4
  • 21
    • 0036855056 scopus 로고    scopus 로고
    • Proteasome inhibitors as new anticancer drugs
    • Adams J. Proteasome inhibitors as new anticancer drugs. Curr Opin Oncol 2002; 14: 628–634.
    • (2002) Curr Opin Oncol , vol.14 , pp. 628-634
    • Adams, J.1
  • 22
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004; 4: 349–360.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 23
    • 84905227469 scopus 로고    scopus 로고
    • Mitochondrial impairment triggers cytosolic oxidative stress and cell death following proteasome inhibition
    • Maharjan S, Oku M, Tsuda M, Hoseki J, Sakai Y. Mitochondrial impairment triggers cytosolic oxidative stress and cell death following proteasome inhibition. Sci Rep 2014; 4: 5896.
    • (2014) Sci Rep , vol.4 , pp. 5896
    • Maharjan, S.1    Oku, M.2    Tsuda, M.3    Hoseki, J.4    Sakai, Y.5
  • 24
    • 32544448056 scopus 로고    scopus 로고
    • Role of mitochondria as the gardens of cell death
    • Kim R, Emi M, Tanabe K. Role of mitochondria as the gardens of cell death. Cancer Chemother Pharmacol 2006; 57: 545–553.
    • (2006) Cancer Chemother Pharmacol , vol.57 , pp. 545-553
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 25
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon HU, Haj-Yehia A, Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis 2000; 5: 415–418.
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3
  • 26
    • 0029886786 scopus 로고    scopus 로고
    • Cancer risk and oxidative DNA damage in man
    • Loft S, Poulsen HE. Cancer risk and oxidative DNA damage in man. J Mol Med (Berl) 1996; 74: 297–312.
    • (1996) J Mol Med (Berl) , vol.74 , pp. 297-312
    • Loft, S.1    Poulsen, H.E.2
  • 27
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An B, Goldfarb RH, Siman R, Dou QP. Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ 1998; 5: 1062–1075.
    • (1998) Cell Death Differ , vol.5 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Dou, Q.P.4
  • 28
  • 29
    • 84929655210 scopus 로고    scopus 로고
    • Nelfinavir, an HIV protease inhibitor, induces apoptosis and cell cycle arrest in human cervical cancer cells via the ROS-dependent mitochondrial pathway
    • Xiang T, Du L, Pham P, Zhu B, Jiang S. Nelfinavir, an HIV protease inhibitor, induces apoptosis and cell cycle arrest in human cervical cancer cells via the ROS-dependent mitochondrial pathway. Cancer Lett 2015; 364: 79–88.
    • (2015) Cancer Lett , vol.364 , pp. 79-88
    • Xiang, T.1    Du, L.2    Pham, P.3    Zhu, B.4    Jiang, S.5
  • 30
    • 84989827781 scopus 로고    scopus 로고
    • Cathepsin D protects colorectal cancer cells from acetate-induced apoptosis through autophagy-independent degradation of damaged mitochondria
    • Oliveira CS, Pereira H, Alves S, Castro L, Baltazar F, Chaves SR et al. Cathepsin D protects colorectal cancer cells from acetate-induced apoptosis through autophagy-independent degradation of damaged mitochondria. Cell Death Dis 2015; 6: e1788.
    • (2015) Cell Death Dis , vol.6 , pp. e1788
    • Oliveira, C.S.1    Pereira, H.2    Alves, S.3    Castro, L.4    Baltazar, F.5    Chaves, S.R.6
  • 31
    • 34250804439 scopus 로고    scopus 로고
    • Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death
    • Papa L, Gomes E, Rockwell P. Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death. Apoptosis 2007; 12: 1389–1405.
    • (2007) Apoptosis , vol.12 , pp. 1389-1405
    • Papa, L.1    Gomes, E.2    Rockwell, P.3
  • 32
    • 41149164588 scopus 로고    scopus 로고
    • Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition
    • Papa L, Rockwell P. Persistent mitochondrial dysfunction and oxidative stress hinder neuronal cell recovery from reversible proteasome inhibition. Apoptosis 2008; 13: 588–599.
    • (2008) Apoptosis , vol.13 , pp. 588-599
    • Papa, L.1    Rockwell, P.2
  • 33
    • 84939252024 scopus 로고    scopus 로고
    • Chronic oxidative stress causes estrogen-independent aggressive phenotype, and epigenetic inactivation of estrogen receptor alpha in MCF-7 breast cancer cells
    • Mahalingaiah PK, Ponnusamy L, Singh KP. Chronic oxidative stress causes estrogen-independent aggressive phenotype, and epigenetic inactivation of estrogen receptor alpha in MCF-7 breast cancer cells. Breast Cancer Res Treat 2015.
    • (2015) Breast Cancer Res Treat
    • Mahalingaiah, P.K.1    Ponnusamy, L.2    Singh, K.P.3
  • 34
    • 84861161546 scopus 로고    scopus 로고
    • SIRT3 is a mitochondrial tumor suppressor: A scientific tale that connects aberrant cellular ROS, the Warburg effect, and carcinogenesis
    • Haigis MC, Deng CX, Finley LW, Kim HS, Gius D. SIRT3 is a mitochondrial tumor suppressor: a scientific tale that connects aberrant cellular ROS, the Warburg effect, and carcinogenesis. Cancer Res 2012; 72: 2468–2472.
    • (2012) Cancer Res , vol.72 , pp. 2468-2472
    • Haigis, M.C.1    Deng, C.X.2    Finley, L.W.3    Kim, H.S.4    Gius, D.5
  • 35
    • 84880822964 scopus 로고    scopus 로고
    • Mitochondrial dysfunction promotes breast cancer cell migration and invasion through HIF1alpha accumulation via increased production of reactive oxygen species
    • Ma J, Zhang Q, Chen S, Fang B, Yang Q, Chen C et al. Mitochondrial dysfunction promotes breast cancer cell migration and invasion through HIF1alpha accumulation via increased production of reactive oxygen species. PloS One 2013; 8: e69485.
    • (2013) Plos One , vol.8
    • Ma, J.1    Zhang, Q.2    Chen, S.3    Fang, B.4    Yang, Q.5    Chen, C.6
  • 36
    • 33847785970 scopus 로고    scopus 로고
    • Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases
    • Barbosa JA, Silva LP, Teles RC, Esteves GF, Azevedo RB, Ventura MM et al. Crystal structure of the Bowman-Birk Inhibitor from Vigna unguiculata seeds in complex with beta-trypsin at 1.55 A resolution and its structural properties in association with proteinases. Biophys J 2007; 92: 1638–1650.
    • (2007) Biophys J , vol.92 , pp. 1638-1650
    • Barbosa, J.A.1    Silva, L.P.2    Teles, R.C.3    Esteves, G.F.4    Azevedo, R.B.5    Ventura, M.M.6
  • 38
    • 0345757570 scopus 로고    scopus 로고
    • Thermal stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI)
    • Silva LP, Liete JR SA, Bloch Jr C, Freitas SM. Thermal stability of a black eyed pea trypsin/chymotrypsin inhibitor (BTCI). Protein Pept Lett 2001; 7: 397–401.
    • (2001) Protein Pept Lett , vol.7 , pp. 397-401
    • Silva, L.P.1    Liete, J.R.S.A.2    Bloch, C.3    Freitas, S.M.4
  • 39
    • 0004978724 scopus 로고
    • Trypsin and chymotrypsin inhibitor from black-eyed pea (V. Sinensis L.) I. Purification and partial characterization
    • Ventura MM X-FJ. Trypsin and chymotrypsin inhibitor from black-eyed pea (V. Sinensis L.) I. Purification and partial characterization. An Acad Bras Cienc 1966; 38: 553–566.
    • (1966) An Acad Bras Cienc , vol.38 , pp. 553-566
    • Ventura, M.M.1
  • 40
    • 84899959826 scopus 로고    scopus 로고
    • Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells
    • Souza Lda C, Camargo R, Demasi M, Santana JM, de Sa CM, de Freitas SM. Effects of an anticarcinogenic Bowman-Birk protease inhibitor on purified 20S proteasome and MCF-7 breast cancer cells. PloS One 2014; 9: e86600.
    • (2014) Plos One , vol.9
    • Souza Lda, C.1    Camargo, R.2    Demasi, M.3    Santana, J.M.4    de Sa, C.M.5    de Freitas, S.M.6
  • 41
    • 0015021414 scopus 로고
    • A trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna sinensis L.). II. Further studies on its characterization and a reevaluation of earlier results
    • Ventura MM, Xavier Filho J, Moreira RA, Aquino Ade M, Pinheiro PA. A trypsin and chymotrypsin inhibitor from black-eyed pea (Vigna sinensis L.). II. Further studies on its characterization and a reevaluation of earlier results. An Acad Bras Cienc 1971; 43: 233–242.
    • (1971) An Acad Bras Cienc , vol.43 , pp. 233-242
    • Ventura, M.M.1    Xavier Filho, J.2    Moreira, R.A.3    Aquino Ade, M.4    Pinheiro, P.A.5
  • 42
    • 0028809235 scopus 로고
    • The evidence for soybean products as cancer preventive agents
    • Kennedy AR. The evidence for soybean products as cancer preventive agents. J Nutr 1995; 125(3 Suppl): 733S–743S.
    • (1995) J Nutr , vol.125 , Issue.3 , pp. 733S-743S
    • Kennedy, A.R.1
  • 43
    • 0031741056 scopus 로고    scopus 로고
    • The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent
    • Suppl
    • Kennedy AR. The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. Am J Clin Nutr 1998; 68(6 Suppl): 1406S–1412S.
    • (1998) Am J Clin Nutr , vol.68 , Issue.6 , pp. 1406S-1412S
    • Kennedy, A.R.1
  • 48
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. Acidophilum at 3.4 A resolution
    • Lowe J, Stock D, Jap B, Zwickl P, Baumeister W, Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution. Science 1995; 268: 533–539.
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 50
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999; 68: 1015–1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 51
    • 84929169182 scopus 로고    scopus 로고
    • Breast cancer cell line MCF7 escapes from G1/S arrest induced by proteasome inhibition through a GSK-3beta dependent mechanism
    • Gavilan E, Giraldez S, Sanchez-Aguayo I, Romero F, Ruano D, Daza P. Breast cancer cell line MCF7 escapes from G1/S arrest induced by proteasome inhibition through a GSK-3beta dependent mechanism. Sci Rep 2015; 5: 10027.
    • (2015) Sci Rep , vol.5
    • Gavilan, E.1    Giraldez, S.2    Sanchez-Aguayo, I.3    Romero, F.4    Ruano, D.5    Daza, P.6
  • 52
    • 84861179304 scopus 로고    scopus 로고
    • Differential p38-dependent signalling in response to cellular stress and mitogenic stimulation in fibroblasts
    • Faust D, Schmitt C, Oesch F, Oesch-Bartlomowicz B, Schreck I, Weiss C et al. Differential p38-dependent signalling in response to cellular stress and mitogenic stimulation in fibroblasts. Cell Commun Signal 2012; 10: 6.
    • (2012) Cell Commun Signal , vol.10 , pp. 6
    • Faust, D.1    Schmitt, C.2    Oesch, F.3    Oesch-Bartlomowicz, B.4    Schreck, I.5    Weiss, C.6
  • 53
    • 84945570349 scopus 로고    scopus 로고
    • VR23: A quinoline-sulfonyl hybrid proteasome inhibitor that selectively kills cancer via cyclin E-mediated centro-some amplification
    • Pundir S, Vu HY, Solomon VR, McClure R, Lee H. VR23: a quinoline-sulfonyl hybrid proteasome inhibitor that selectively kills cancer via cyclin E-mediated centro-some amplification. Cancer Res 2015.
    • (2015) Cancer Res
    • Pundir, S.1    Vu, H.Y.2    Solomon, V.R.3    McClure, R.4    Lee, H.5
  • 54
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: Implications for oxidative stress
    • Keller JN, Hanni KB, Markesbery WR. Possible involvement of proteasome inhibition in aging: implications for oxidative stress. Mech Ageing Dev 2000; 113: 61–70.
    • (2000) Mech Ageing Dev , vol.113 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 55
    • 0141706672 scopus 로고    scopus 로고
    • Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells
    • Ling YH, Liebes L, Zou Y, Perez-Soler R. Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells. J Biol Chem 2003; 278: 33714–33723.
    • (2003) J Biol Chem , vol.278 , pp. 33714-33723
    • Ling, Y.H.1    Liebes, L.2    Zou, Y.3    Perez-Soler, R.4
  • 56
    • 0035006792 scopus 로고    scopus 로고
    • Proteasome inhibition in oxidative stress neurotoxicity: Implications for heat shock proteins
    • Ding Q, Keller JN. Proteasome inhibition in oxidative stress neurotoxicity: implications for heat shock proteins. J Neurochem 2001; 77: 1010–1017.
    • (2001) J Neurochem , vol.77 , pp. 1010-1017
    • Ding, Q.1    Keller, J.N.2
  • 57
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-kappaB signaling
    • Morgan MJ, Liu ZG. Crosstalk of reactive oxygen species and NF-kappaB signaling. Cell Res 2011; 21: 103–115.
    • (2011) Cell Res , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 58
    • 0035328584 scopus 로고    scopus 로고
    • Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: Implications for systemic nuclear factor-kappaB inhibition
    • Cusack JC Jr, Liu R, Houston M, Abendroth K, Elliott PJ, Adams J et al. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS-341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res 2001; 61: 3535–3540.
    • (2001) Cancer Res , vol.61 , pp. 3535-3540
    • Cusack, J.C.1    Liu, R.2    Houston, M.3    Abendroth, K.4    Elliott, P.J.5    Adams, J.6
  • 59
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T, Richardson P, Chauhan D, Palombella VJ, Elliott PJ, Adams J et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 2001; 61: 3071–3076.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3    Palombella, V.J.4    Elliott, P.J.5    Adams, J.6
  • 61
    • 0142054051 scopus 로고    scopus 로고
    • Bortezomib (PS-341): A novel, first-in-class proteasome inhibitor for the treatment of multiple myeloma and other cancers
    • Richardson PG, Hideshima T, Anderson KC. Bortezomib (PS-341): a novel, first-in-class proteasome inhibitor for the treatment of multiple myeloma and other cancers. Cancer Control 2003; 10: 361–369.
    • (2003) Cancer Control , vol.10 , pp. 361-369
    • Richardson, P.G.1    Hideshima, T.2    Anderson, K.C.3
  • 62
    • 33746840548 scopus 로고    scopus 로고
    • Proteasome inhibitors induce death but activate NF-kappaB on endometrial carcinoma cell lines and primary culture explants
    • Dolcet X, Llobet D, Encinas M, Pallares J, Cabero A, Schoenenberger JA et al. Proteasome inhibitors induce death but activate NF-kappaB on endometrial carcinoma cell lines and primary culture explants. JBiolChem2006; 281: 22118–22130.
    • (2006) Jbiolchem , vol.281 , pp. 22118-22130
    • Dolcet, X.1    Llobet, D.2    Encinas, M.3    Pallares, J.4    Cabero, A.5    Schoenenberger, J.A.6
  • 63
    • 70349243697 scopus 로고    scopus 로고
    • Bortezomib induces canonical nuclear factor-kappaB activation in multiple myeloma cells
    • Hideshima T, Ikeda H, Chauhan D, Okawa Y, Raje N, Podar K et al. Bortezomib induces canonical nuclear factor-kappaB activation in multiple myeloma cells. Blood 2009; 114: 1046–1052.
    • (2009) Blood , vol.114 , pp. 1046-1052
    • Hideshima, T.1    Ikeda, H.2    Chauhan, D.3    Okawa, Y.4    Raje, N.5    Podar, K.6
  • 64
    • 84883360510 scopus 로고    scopus 로고
    • Proteasome inhibition by bortezomib increases IL-8 expression in androgen-independent prostate cancer cells: The role of IKKalpha
    • Manna S, Singha B, Phyo SA, Gatla HR, Chang TP, Sanacora S et al. Proteasome inhibition by bortezomib increases IL-8 expression in androgen-independent prostate cancer cells: the role of IKKalpha. J Immunol 2013; 191: 2837–2846.
    • (2013) J Immunol , vol.191 , pp. 2837-2846
    • Manna, S.1    Singha, B.2    Phyo, S.A.3    Gatla, H.R.4    Chang, T.P.5    Sanacora, S.6
  • 65
    • 84893444785 scopus 로고    scopus 로고
    • Proteasome inhibition increases recruitment of IkappaB kinase beta (IKKbeta), S536P-p65, and transcription factor EGR1 to interleukin-8 (IL-8) promoter, resulting in increased IL-8 production in ovarian cancer cells
    • Singha B, Gatla HR, Manna S, Chang TP, Sanacora S, Poltoratsky V et al. Proteasome inhibition increases recruitment of IkappaB kinase beta (IKKbeta), S536P-p65, and transcription factor EGR1 to interleukin-8 (IL-8) promoter, resulting in increased IL-8 production in ovarian cancer cells. J Biol Chem 2014; 289: 2687–2700.
    • (2014) J Biol Chem , vol.289 , pp. 2687-2700
    • Singha, B.1    Gatla, H.R.2    Manna, S.3    Chang, T.P.4    Sanacora, S.5    Poltoratsky, V.6
  • 66
    • 33947206642 scopus 로고    scopus 로고
    • MG-132 sensitizes TRAIL-resistant prostate cancer cells by activating c-Fos/c-Jun heterodimers and repressing c-FLIP(L)
    • Li W, Zhang X, Olumi AF. MG-132 sensitizes TRAIL-resistant prostate cancer cells by activating c-Fos/c-Jun heterodimers and repressing c-FLIP(L). Cancer Res 2007; 67: 2247–2255.
    • (2007) Cancer Res , vol.67 , pp. 2247-2255
    • Li, W.1    Zhang, X.2    Olumi, A.F.3
  • 67
    • 0038240386 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP
    • Sayers TJ, Brooks AD, Koh CY, Ma W, Seki N, Raziuddin A et al. The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP. Blood 2003; 102: 303–310.
    • (2003) Blood , vol.102 , pp. 303-310
    • Sayers, T.J.1    Brooks, A.D.2    Koh, C.Y.3    Ma, W.4    Seki, N.5    Raziuddin, A.6
  • 69
    • 23944490171 scopus 로고    scopus 로고
    • Proteases, proteasomes and apoptosis: Breaking Ub is hard to do
    • Taylor RC, Adrain C, Martin SJ. Proteases, proteasomes and apoptosis: breaking Ub is hard to do. Cell Death Differ 2005; 12: 1213–1217.
    • (2005) Cell Death Differ , vol.12 , pp. 1213-1217
    • Taylor, R.C.1    Adrain, C.2    Martin, S.J.3
  • 70
    • 0028109918 scopus 로고
    • PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core
    • Heinemeyer W, Trondle N, Albrecht G, Wolf DH. PRE5 and PRE6, the last missing genes encoding 20S proteasome subunits from yeast? Indication for a set of 14 different subunits in the eukaryotic proteasome core. Biochemistry 1994; 33: 12229–12237.
    • (1994) Biochemistry , vol.33 , pp. 12229-12237
    • Heinemeyer, W.1    Trondle, N.2    Albrecht, G.3    Wolf, D.H.4
  • 71
    • 0030481129 scopus 로고    scopus 로고
    • Analysis of mammalian 20S proteasome biogenesis: The maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis
    • Schmidtke G, Kraft R, Kostka S, Henklein P, Frommel C, Lowe J et al. Analysis of mammalian 20S proteasome biogenesis: the maturation of beta-subunits is an ordered two-step mechanism involving autocatalysis. EMBO J 1996; 15: 6887–6898.
    • (1996) EMBO J , vol.15 , pp. 6887-6898
    • Schmidtke, G.1    Kraft, R.2    Kostka, S.3    Henklein, P.4    Frommel, C.5    Lowe, J.6
  • 72
    • 27244462417 scopus 로고    scopus 로고
    • Glutathiolation of the proteasome is enhanced by proteolytic inhibitors
    • Demasi M, Shringarpure R, Davies KJ. Glutathiolation of the proteasome is enhanced by proteolytic inhibitors. Arch Biochem Biophys 2001; 389: 254–263.
    • (2001) Arch Biochem Biophys , vol.389 , pp. 254-263
    • Demasi, M.1    Shringarpure, R.2    Davies, K.J.3
  • 73
    • 0036581160 scopus 로고    scopus 로고
    • Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR
    • Pfaffl MW, Horgan GW, Dempfle L. Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR. Nucleic Acids Res 2002; 30: e36.
    • (2002) Nucleic Acids Res , vol.30 , pp. e36
    • Pfaffl, M.W.1    Horgan, G.W.2    Dempfle, L.3
  • 74
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative C (T) method
    • Schmittgen TD, Livak KJ. Analyzing real-time PCR data by the comparative C (T) method. Nat Protoc 2008; 3: 1101–1108.
    • (2008) Nat Protoc , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.