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Volumn 33, Issue 11, 2009, Pages 1440-1447

ER-Golgi network-A future target for anti-cancer therapy

Author keywords

Apoptosis; Cancer; Caspases; ER; ER stress; Golgi; Therapy

Indexed keywords

2 AMINO 6 BROMO 4 (1 CYANO 2 ETHOXY 2 OXOETHYL) 4H CHROMENE 3 CARBOXYLIC ACID ETHYL ESTER; ANTIBIOTIC AGENT; ANTINEOPLASTIC AGENT; BORTEZOMIB; BREFELDIN A; BREFLATE; DEATH RECEPTOR; EEYARESTATIN I; FAS ANTIBODY; FENRETINIDE; MONOCLONAL ANTIBODY; NSC 656202; STAUROSPORINE; TETROCARCIN A; THAPSIGARGIN; TUNICAMYCIN; UNCLASSIFIED DRUG;

EID: 68649102488     PISSN: 01452126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.leukres.2009.05.025     Document Type: Review
Times cited : (109)

References (103)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D., and Weinberg R.A. The hallmarks of cancer. Cell 100 1 (2000) 57-70
    • (2000) Cell , vol.100 , Issue.1 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 18244392443 scopus 로고    scopus 로고
    • Cell death independent of caspases: a review
    • Broker L.E., Kruyt F.A., and Giaccone G. Cell death independent of caspases: a review. Clin Cancer Res 11 9 (2005) 3155-3162
    • (2005) Clin Cancer Res , vol.11 , Issue.9 , pp. 3155-3162
    • Broker, L.E.1    Kruyt, F.A.2    Giaccone, G.3
  • 3
    • 9944240863 scopus 로고    scopus 로고
    • Splicing DNA-damage responses to tumour cell death
    • Crighton D., and Ryan K.M. Splicing DNA-damage responses to tumour cell death. Biochim Biophys Acta 1705 1 (2004) 3-15
    • (2004) Biochim Biophys Acta , vol.1705 , Issue.1 , pp. 3-15
    • Crighton, D.1    Ryan, K.M.2
  • 4
    • 33750632135 scopus 로고    scopus 로고
    • Apoptosis in the treatment of cancer: a promise kept?
    • Meng X.W., Lee S.H., and Kaufmann S.H. Apoptosis in the treatment of cancer: a promise kept?. Curr Opin Cell Biol 18 6 (2006) 668-676
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.6 , pp. 668-676
    • Meng, X.W.1    Lee, S.H.2    Kaufmann, S.H.3
  • 5
    • 0027451668 scopus 로고
    • p53-Dependent apoptosis modulates the cytotoxicity of anticancer agents
    • Lowe S.W., Ruley H.E., Jacks T., and Housman D.E. p53-Dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 74 6 (1993) 957-967
    • (1993) Cell , vol.74 , Issue.6 , pp. 957-967
    • Lowe, S.W.1    Ruley, H.E.2    Jacks, T.3    Housman, D.E.4
  • 6
    • 0033773114 scopus 로고    scopus 로고
    • Apoptosis in cancer: cause and cure
    • Kaufmann S.H., and Gores G.J. Apoptosis in cancer: cause and cure. Bioessays 22 11 (2000) 1007-1017
    • (2000) Bioessays , vol.22 , Issue.11 , pp. 1007-1017
    • Kaufmann, S.H.1    Gores, G.J.2
  • 7
    • 20344385260 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in cancer therapy
    • Ghobrial I.M., Witzig T.E., and Adjei A.A. Targeting apoptosis pathways in cancer therapy. CA Cancer J Clin 55 3 (2005) 178-194
    • (2005) CA Cancer J Clin , vol.55 , Issue.3 , pp. 178-194
    • Ghobrial, I.M.1    Witzig, T.E.2    Adjei, A.A.3
  • 8
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: from caspases to alternative mechanisms
    • Leist M., and Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2 8 (2001) 589-598
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.8 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 9
    • 0036910734 scopus 로고    scopus 로고
    • Programmed cell death: many ways for cells to die decently
    • Jaattela M. Programmed cell death: many ways for cells to die decently. Ann Med 34 6 (2002) 480-488
    • (2002) Ann Med , vol.34 , Issue.6 , pp. 480-488
    • Jaattela, M.1
  • 10
    • 0035409448 scopus 로고    scopus 로고
    • Programmed cell death and apoptosis: origins of the theory
    • Lockshin R.A., and Zakeri Z. Programmed cell death and apoptosis: origins of the theory. Nat Rev Mol Cell Biol 2 7 (2001) 545-550
    • (2001) Nat Rev Mol Cell Biol , vol.2 , Issue.7 , pp. 545-550
    • Lockshin, R.A.1    Zakeri, Z.2
  • 11
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • Okada H., and Mak T.W. Pathways of apoptotic and non-apoptotic death in tumour cells. Nat Rev Cancer 4 8 (2004) 592-603
    • (2004) Nat Rev Cancer , vol.4 , Issue.8 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 12
    • 7744235672 scopus 로고    scopus 로고
    • Death by design: apoptosis, necrosis and autophagy
    • Edinger A.L., and Thompson C.B. Death by design: apoptosis, necrosis and autophagy. Curr Opin Cell Biol 16 6 (2004) 663-669
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.6 , pp. 663-669
    • Edinger, A.L.1    Thompson, C.B.2
  • 13
    • 1842451620 scopus 로고    scopus 로고
    • Death without caspases, caspases without death
    • Abraham M.C., and Shaham S. Death without caspases, caspases without death. Trends Cell Biol 14 4 (2004) 184-193
    • (2004) Trends Cell Biol , vol.14 , Issue.4 , pp. 184-193
    • Abraham, M.C.1    Shaham, S.2
  • 14
    • 33745096533 scopus 로고    scopus 로고
    • Apoptosis effector mechanisms: a requiem performed in different keys
    • Hail Jr. N., Carter B.Z., Konopleva M., and Andreeff M. Apoptosis effector mechanisms: a requiem performed in different keys. Apoptosis 11 6 (2006) 889-904
    • (2006) Apoptosis , vol.11 , Issue.6 , pp. 889-904
    • Hail Jr., N.1    Carter, B.Z.2    Konopleva, M.3    Andreeff, M.4
  • 15
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: an innocent convict?
    • Levine B., and Yuan J. Autophagy in cell death: an innocent convict?. J Clin Invest 115 10 (2005) 2679-2688
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 16
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., and Jaattela M. Lysosomes and autophagy in cell death control. Nat Rev Cancer 5 11 (2005) 886-897
    • (2005) Nat Rev Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 17
    • 16844377506 scopus 로고    scopus 로고
    • Recent advances in understanding the cell death pathways activated by anticancer therapy
    • Kim R. Recent advances in understanding the cell death pathways activated by anticancer therapy. Cancer 103 8 (2005) 1551-1560
    • (2005) Cancer , vol.103 , Issue.8 , pp. 1551-1560
    • Kim, R.1
  • 18
    • 32544448056 scopus 로고    scopus 로고
    • Role of mitochondria as the gardens of cell death
    • Kim R., Emi M., and Tanabe K. Role of mitochondria as the gardens of cell death. Cancer Chemother Pharmacol 57 5 (2006) 545-553
    • (2006) Cancer Chemother Pharmacol , vol.57 , Issue.5 , pp. 545-553
    • Kim, R.1    Emi, M.2    Tanabe, K.3
  • 19
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri K.F., and Kroemer G. Organelle-specific initiation of cell death pathways. Nat Cell Biol 3 11 (2001) E255-E263
    • (2001) Nat Cell Biol , vol.3 , Issue.11
    • Ferri, K.F.1    Kroemer, G.2
  • 20
    • 0042266400 scopus 로고    scopus 로고
    • Death from within: apoptosis and the secretory pathway
    • Maag R.S., Hicks S.W., and Machamer C.E. Death from within: apoptosis and the secretory pathway. Curr Opin Cell Biol 15 4 (2003) 456-461
    • (2003) Curr Opin Cell Biol , vol.15 , Issue.4 , pp. 456-461
    • Maag, R.S.1    Hicks, S.W.2    Machamer, C.E.3
  • 21
    • 4444338911 scopus 로고    scopus 로고
    • Caspases involved in ER stress-mediated cell death
    • Momoi T. Caspases involved in ER stress-mediated cell death. J Chem Neuroanat 28 1-2 (2004) 101-105
    • (2004) J Chem Neuroanat , vol.28 , Issue.1-2 , pp. 101-105
    • Momoi, T.1
  • 22
    • 20544435937 scopus 로고    scopus 로고
    • Golgi structure in stress sensing and apoptosis
    • Hicks S.W., and Machamer C.E. Golgi structure in stress sensing and apoptosis. Biochim Biophys Acta 1744 3 (2005) 406-414
    • (2005) Biochim Biophys Acta , vol.1744 , Issue.3 , pp. 406-414
    • Hicks, S.W.1    Machamer, C.E.2
  • 23
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • Szegezdi E., Logue S.E., Gorman A.M., and Samali A. Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 7 9 (2006) 880-885
    • (2006) EMBO Rep , vol.7 , Issue.9 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 24
    • 0038464650 scopus 로고    scopus 로고
    • Regulation of cell death: the calcium-apoptosis link
    • Orrenius S., Zhivotovsky B., and Nicotera P. Regulation of cell death: the calcium-apoptosis link. Nat Rev Mol Cell Biol 4 7 (2003) 552-565
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.7 , pp. 552-565
    • Orrenius, S.1    Zhivotovsky, B.2    Nicotera, P.3
  • 25
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • Scorrano L., and Korsmeyer S.J. Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem Biophys Res Commun 304 3 (2003) 437-444
    • (2003) Biochem Biophys Res Commun , vol.304 , Issue.3 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 27
    • 0344925540 scopus 로고    scopus 로고
    • Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription
    • Chipuk J.E., Maurer U., Green D.R., and Schuler M. Pharmacologic activation of p53 elicits Bax-dependent apoptosis in the absence of transcription. Cancer Cell 4 5 (2003) 371-381
    • (2003) Cancer Cell , vol.4 , Issue.5 , pp. 371-381
    • Chipuk, J.E.1    Maurer, U.2    Green, D.R.3    Schuler, M.4
  • 28
    • 0041330430 scopus 로고    scopus 로고
    • p53's believe it or not: lessons on transcription-independent death
    • Chipuk J.E., and Green D.R. p53's believe it or not: lessons on transcription-independent death. J Clin Immunol 23 5 (2003) 355-361
    • (2003) J Clin Immunol , vol.23 , Issue.5 , pp. 355-361
    • Chipuk, J.E.1    Green, D.R.2
  • 29
    • 33745950626 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario
    • Chipuk J.E., Bouchier-Hayes L., and Green D.R. Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario. Cell Death Differ 13 8 (2006) 1396-1402
    • (2006) Cell Death Differ , vol.13 , Issue.8 , pp. 1396-1402
    • Chipuk, J.E.1    Bouchier-Hayes, L.2    Green, D.R.3
  • 30
    • 33846106906 scopus 로고    scopus 로고
    • Larger than life: mitochondria and the Bcl-2 family
    • Skommer J., Wlodkowic D., and Deptala A. Larger than life: mitochondria and the Bcl-2 family. Leuk Res 31 March (3) (2007) 277-286
    • (2007) Leuk Res , vol.31 , Issue.March 3 , pp. 277-286
    • Skommer, J.1    Wlodkowic, D.2    Deptala, A.3
  • 31
    • 0038697678 scopus 로고    scopus 로고
    • Golgi disassembly in apoptosis: cause or effect?
    • Machamer C.E. Golgi disassembly in apoptosis: cause or effect?. Trends Cell Biol 13 6 (2003) 279-281
    • (2003) Trends Cell Biol , vol.13 , Issue.6 , pp. 279-281
    • Machamer, C.E.1
  • 32
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: coping with stress
    • Rutkowski D.T., and Kaufman R.J. A trip to the ER: coping with stress. Trends Cell Biol 14 1 (2004) 20-28
    • (2004) Trends Cell Biol , vol.14 , Issue.1 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 33
    • 26444593029 scopus 로고    scopus 로고
    • Mitochondria and endoplasmic reticulum: the lethal interorganelle cross-talk
    • Walter L., and Hajnoczky G. Mitochondria and endoplasmic reticulum: the lethal interorganelle cross-talk. J Bioenerg Biomembr 37 3 (2005) 191-206
    • (2005) J Bioenerg Biomembr , vol.37 , Issue.3 , pp. 191-206
    • Walter, L.1    Hajnoczky, G.2
  • 34
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat Cell Biol 2 6 (2000) 326-332
    • (2000) Nat Cell Biol , vol.2 , Issue.6 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 35
    • 0033258544 scopus 로고    scopus 로고
    • Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
    • Katayama T., Imaizumi K., Sato N., Miyoshi K., Kudo T., Hitomi J., et al. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nat Cell Biol 1 8 (1999) 479-485
    • (1999) Nat Cell Biol , vol.1 , Issue.8 , pp. 479-485
    • Katayama, T.1    Imaizumi, K.2    Sato, N.3    Miyoshi, K.4    Kudo, T.5    Hitomi, J.6
  • 36
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals
    • Patil C., and Walter P. Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13 3 (2001) 349-355
    • (2001) Curr Opin Cell Biol , vol.13 , Issue.3 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 37
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough K.D., Martindale J.L., Klotz L.O., Aw T.Y., and Holbrook N.J. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 21 4 (2001) 1249-1259
    • (2001) Mol Cell Biol , vol.21 , Issue.4 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.O.3    Aw, T.Y.4    Holbrook, N.J.5
  • 38
    • 22244472001 scopus 로고    scopus 로고
    • Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells
    • Shiraishi T., Yoshida T., Nakata S., Horinaka M., Wakada M., Mizutani Y., et al. Tunicamycin enhances tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human prostate cancer cells. Cancer Res 65 14 (2005) 6364-6370
    • (2005) Cancer Res , vol.65 , Issue.14 , pp. 6364-6370
    • Shiraishi, T.1    Yoshida, T.2    Nakata, S.3    Horinaka, M.4    Wakada, M.5    Mizutani, Y.6
  • 39
    • 33646373219 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53
    • Li J., Lee B., and Lee A.S. Endoplasmic reticulum stress-induced apoptosis: multiple pathways and activation of p53-up-regulated modulator of apoptosis (PUMA) and NOXA by p53. J Biol Chem 281 11 (2006) 7260-7270
    • (2006) J Biol Chem , vol.281 , Issue.11 , pp. 7260-7270
    • Li, J.1    Lee, B.2    Lee, A.S.3
  • 40
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., et al. Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J Biol Chem 276 17 (2001) 13935-13940
    • (2001) J Biol Chem , vol.276 , Issue.17 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6
  • 41
    • 0033693855 scopus 로고    scopus 로고
    • IRE1 and efferent signaling from the endoplasmic reticulum
    • Urano F., Bertolotti A., and Ron D. IRE1 and efferent signaling from the endoplasmic reticulum. J Cell Sci 113 Pt 21 (2000) 3697-3702
    • (2000) J Cell Sci , vol.113 , Issue.PART 21 , pp. 3697-3702
    • Urano, F.1    Bertolotti, A.2    Ron, D.3
  • 43
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei K., and Davis R.J. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc Natl Acad Sci USA 100 5 (2003) 2432-2437
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.5 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 45
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T., Zhu H., Morishima N., Li E., Xu J., Yankner B.A., et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 403 6765 (2000) 98-103
    • (2000) Nature , vol.403 , Issue.6765 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6
  • 46
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis
    • Nakagawa T., and Yuan J. Cross-talk between two cysteine protease families. Activation of caspase-12 by calpain in apoptosis. J Cell Biol 150 4 (2000) 887-894
    • (2000) J Cell Biol , vol.150 , Issue.4 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 47
    • 27744500069 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis
    • Liu H., and Baliga R. Endoplasmic reticulum stress-associated caspase 12 mediates cisplatin-induced LLC-PK1 cell apoptosis. J Am Soc Nephrol 16 (2005) 1985-1992
    • (2005) J Am Soc Nephrol , vol.16 , pp. 1985-1992
    • Liu, H.1    Baliga, R.2
  • 48
    • 0037072937 scopus 로고    scopus 로고
    • An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12
    • Morishima N., Nakanishi K., Takenouchi H., Shibata T., and Yasuhiko Y. An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12. J Biol Chem 277 37 (2002) 34287-34294
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 34287-34294
    • Morishima, N.1    Nakanishi, K.2    Takenouchi, H.3    Shibata, T.4    Yasuhiko, Y.5
  • 50
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
    • Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 165 3 (2004) 347-356
    • (2004) J Cell Biol , vol.165 , Issue.3 , pp. 347-356
    • Hitomi, J.1    Katayama, T.2    Eguchi, Y.3    Kudo, T.4    Taniguchi, M.5    Koyama, Y.6
  • 51
    • 0037007141 scopus 로고    scopus 로고
    • The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum
    • Breckenridge D.G., Nguyen M., Kuppig S., Reth M., and Shore G.C. The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum. Proc Natl Acad Sci USA 99 7 (2002) 4331-4336
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.7 , pp. 4331-4336
    • Breckenridge, D.G.1    Nguyen, M.2    Kuppig, S.3    Reth, M.4    Shore, G.C.5
  • 52
    • 0344897663 scopus 로고    scopus 로고
    • Bcl-2 on the endoplasmic reticulum: protecting the mitochondria from a distance
    • Thomenius M.J., and Distelhorst C.W. Bcl-2 on the endoplasmic reticulum: protecting the mitochondria from a distance. J Cell Sci 116 Pt 22 (2003) 4493-4499
    • (2003) J Cell Sci , vol.116 , Issue.PART 22 , pp. 4493-4499
    • Thomenius, M.J.1    Distelhorst, C.W.2
  • 53
    • 3342984659 scopus 로고    scopus 로고
    • Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate
    • Chen R., Valencia I., Zhong F., McColl K.S., Roderick H.L., Bootman M.D., et al. Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate. J Cell Biol 166 2 (2004) 193-203
    • (2004) J Cell Biol , vol.166 , Issue.2 , pp. 193-203
    • Chen, R.1    Valencia, I.2    Zhong, F.3    McColl, K.S.4    Roderick, H.L.5    Bootman, M.D.6
  • 54
    • 0032425805 scopus 로고    scopus 로고
    • Electron microscopic tomography of rat-liver mitochondria and their interaction with the endoplasmic reticulum
    • Mannella C.A., Buttle K., Rath B.K., and Marko M. Electron microscopic tomography of rat-liver mitochondria and their interaction with the endoplasmic reticulum. Biofactors 8 3-4 (1998) 225-228
    • (1998) Biofactors , vol.8 , Issue.3-4 , pp. 225-228
    • Mannella, C.A.1    Buttle, K.2    Rath, B.K.3    Marko, M.4
  • 56
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis
    • Boehning D., Patterson R.L., Sedaghat L., Glebova N.O., Kurosaki T., and Snyder S.H. Cytochrome c binds to inositol (1,4,5) trisphosphate receptors, amplifying calcium-dependent apoptosis. Nat Cell Biol 5 12 (2003) 1051-1061
    • (2003) Nat Cell Biol , vol.5 , Issue.12 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 57
    • 85047689015 scopus 로고    scopus 로고
    • Calpains can do it alone: implications for cancer therapy
    • Guicciardi M.E., and Gores G.J. Calpains can do it alone: implications for cancer therapy. Cancer Biol Ther 2 2 (2003) 153-154
    • (2003) Cancer Biol Ther , vol.2 , Issue.2 , pp. 153-154
    • Guicciardi, M.E.1    Gores, G.J.2
  • 59
    • 1242316982 scopus 로고    scopus 로고
    • Polo-like kinase 3 is Golgi localized and involved in regulation of Golgi fragmentation during the cell cycle
    • Ruan Q., Wang Q., Xie S., Fang Y., Darzynkiewicz Z., Guan K., et al. Polo-like kinase 3 is Golgi localized and involved in regulation of Golgi fragmentation during the cell cycle. Exp Cell Res 294 (2004) 51-59
    • (2004) Exp Cell Res , vol.294 , pp. 51-59
    • Ruan, Q.1    Wang, Q.2    Xie, S.3    Fang, Y.4    Darzynkiewicz, Z.5    Guan, K.6
  • 60
    • 33744520878 scopus 로고    scopus 로고
    • Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis
    • Jiang N., Wang X., Jhanwar-Uniyal M., Darzynkiewicz Z., and Dai W. Polo box domain of Plk3 functions as a centrosome localization signal, overexpression of which causes mitotic arrest, cytokinesis defects, and apoptosis. J Biol Chem 281 (2006) 10577-10582
    • (2006) J Biol Chem , vol.281 , pp. 10577-10582
    • Jiang, N.1    Wang, X.2    Jhanwar-Uniyal, M.3    Darzynkiewicz, Z.4    Dai, W.5
  • 61
    • 36148950114 scopus 로고    scopus 로고
    • Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells
    • Wang L., Dai W., and Lu L. Stress-induced c-Jun activation mediated by Polo-like kinase 3 in corneal epithelial cells. J Biol Chem 282 (2007) 32121-32127
    • (2007) J Biol Chem , vol.282 , pp. 32121-32127
    • Wang, L.1    Dai, W.2    Lu, L.3
  • 62
    • 0036242249 scopus 로고    scopus 로고
    • Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity
    • Wang Q., Xie S., Chen J., Fukasawa K., Naik U., Traganos F., et al. Cell cycle arrest and apoptosis induced by human Polo-like kinase 3 is mediated through perturbation of microtubule integrity. Mol Cell Biol 22 (2002) 3450-3459
    • (2002) Mol Cell Biol , vol.22 , pp. 3450-3459
    • Wang, Q.1    Xie, S.2    Chen, J.3    Fukasawa, K.4    Naik, U.5    Traganos, F.6
  • 63
    • 20444444295 scopus 로고    scopus 로고
    • Function of polo-like kinase 3 in NF-kappaB-mediated proapoptotic response
    • Li Z., Niu J., Uwagawa T., Peng B., and Chiao P.J. Function of polo-like kinase 3 in NF-kappaB-mediated proapoptotic response. J Biol Chem 280 (2005) 16843-16850
    • (2005) J Biol Chem , vol.280 , pp. 16843-16850
    • Li, Z.1    Niu, J.2    Uwagawa, T.3    Peng, B.4    Chiao, P.J.5
  • 64
    • 30144435660 scopus 로고    scopus 로고
    • Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies
    • Syed N., Smith P., Sullivan A., Spender L.C., Dyer M., Karran L., et al. Transcriptional silencing of Polo-like kinase 2 (SNK/PLK2) is a frequent event in B-cell malignancies. Blood 107 (2006) 250-256
    • (2006) Blood , vol.107 , pp. 250-256
    • Syed, N.1    Smith, P.2    Sullivan, A.3    Spender, L.C.4    Dyer, M.5    Karran, L.6
  • 66
    • 0037175389 scopus 로고    scopus 로고
    • A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis
    • Chiu R., Novikov L., Mukherjee S., and Shields D. A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis. J Cell Biol 159 4 (2002) 637-648
    • (2002) J Cell Biol , vol.159 , Issue.4 , pp. 637-648
    • Chiu, R.1    Novikov, L.2    Mukherjee, S.3    Shields, D.4
  • 67
    • 0037017405 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
    • Lane J.D., Lucocq J., Pryde J., Barr F.A., Woodman P.G., Allan V.J., et al. Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis. J Cell Biol 156 3 (2002) 495-509
    • (2002) J Cell Biol , vol.156 , Issue.3 , pp. 495-509
    • Lane, J.D.1    Lucocq, J.2    Pryde, J.3    Barr, F.A.4    Woodman, P.G.5    Allan, V.J.6
  • 68
    • 2442453730 scopus 로고    scopus 로고
    • a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A., Tschopp J., and The PIDDosome. a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 304 5672 (2004) 843-846
    • (2004) Science , vol.304 , Issue.5672 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2    The PIDDosome3
  • 69
    • 19644394499 scopus 로고    scopus 로고
    • Caspase-resistant Golgin-160 disrupts apoptosis induced by secretory pathway stress and ligation of death receptors
    • Maag R.S., Mancini M., Rosen A., and Machamer C.E. Caspase-resistant Golgin-160 disrupts apoptosis induced by secretory pathway stress and ligation of death receptors. Mol Biol Cell 16 6 (2005) 3019-3027
    • (2005) Mol Biol Cell , vol.16 , Issue.6 , pp. 3019-3027
    • Maag, R.S.1    Mancini, M.2    Rosen, A.3    Machamer, C.E.4
  • 70
    • 0032526948 scopus 로고    scopus 로고
    • A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors
    • Hauser H.P., Bardroff M., Pyrowolakis G., and Jentsch S. A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J Cell Biol 141 6 (1998) 1415-1422
    • (1998) J Cell Biol , vol.141 , Issue.6 , pp. 1415-1422
    • Hauser, H.P.1    Bardroff, M.2    Pyrowolakis, G.3    Jentsch, S.4
  • 71
    • 0037203318 scopus 로고    scopus 로고
    • GD3 ganglioside and apoptosis
    • Malisan F., and Testi R. GD3 ganglioside and apoptosis. Biochim Biophys Acta 1585 2-3 (2002) 179-187
    • (2002) Biochim Biophys Acta , vol.1585 , Issue.2-3 , pp. 179-187
    • Malisan, F.1    Testi, R.2
  • 72
    • 0033810454 scopus 로고    scopus 로고
    • GD3 ganglioside directly targets mitochondria in a bcl-2-controlled fashion
    • Rippo M.R., Malisan F., Ravagnan L., Tomassini B., Condo I., Costantini P., et al. GD3 ganglioside directly targets mitochondria in a bcl-2-controlled fashion. FASEB J 14 13 (2000) 2047-2054
    • (2000) FASEB J , vol.14 , Issue.13 , pp. 2047-2054
    • Rippo, M.R.1    Malisan, F.2    Ravagnan, L.3    Tomassini, B.4    Condo, I.5    Costantini, P.6
  • 74
    • 1842680755 scopus 로고    scopus 로고
    • Membrane lipids and cell death: an overview
    • Cristea I.M., and Degli Esposti M. Membrane lipids and cell death: an overview. Chem Phys Lipids 129 2 (2004) 133-160
    • (2004) Chem Phys Lipids , vol.129 , Issue.2 , pp. 133-160
    • Cristea, I.M.1    Degli Esposti, M.2
  • 75
    • 0032500793 scopus 로고    scopus 로고
    • Cell surface trafficking of Fas: a rapid mechanism of p53-mediated apoptosis
    • Bennett M., Macdonald K., Chan S.W., Luzio J.P., Simari R., and Weissberg P. Cell surface trafficking of Fas: a rapid mechanism of p53-mediated apoptosis. Science 282 5387 (1998) 290-293
    • (1998) Science , vol.282 , Issue.5387 , pp. 290-293
    • Bennett, M.1    Macdonald, K.2    Chan, S.W.3    Luzio, J.P.4    Simari, R.5    Weissberg, P.6
  • 76
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems
    • Arvan P., Zhao X., Ramos-Castaneda J., and Chang A. Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems. Traffic 3 11 (2002) 771-780
    • (2002) Traffic , vol.3 , Issue.11 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 77
    • 26844570219 scopus 로고    scopus 로고
    • Lysosomes and endoplasmic reticulum: targets for improved, selective anticancer therapy
    • Linder S., and Shoshan M.C. Lysosomes and endoplasmic reticulum: targets for improved, selective anticancer therapy. Drug Resist Updat 8 4 (2005) 199-204
    • (2005) Drug Resist Updat , vol.8 , Issue.4 , pp. 199-204
    • Linder, S.1    Shoshan, M.C.2
  • 78
    • 30144437016 scopus 로고    scopus 로고
    • Targeting endoplasmic reticulum protein transport: a novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL
    • Carew J.S., Nawrocki S.T., Krupnik Y.V., Dunner K., McConkey D.J., Keating M.J., et al. Targeting endoplasmic reticulum protein transport: a novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL. Blood 107 1 (2006) 222-231
    • (2006) Blood , vol.107 , Issue.1 , pp. 222-231
    • Carew, J.S.1    Nawrocki, S.T.2    Krupnik, Y.V.3    Dunner, K.4    McConkey, D.J.5    Keating, M.J.6
  • 79
    • 2442480795 scopus 로고    scopus 로고
    • Multiple cell death pathways as regulators of tumour initiation and progression
    • Jaattela M. Multiple cell death pathways as regulators of tumour initiation and progression. Oncogene 23 16 (2004) 2746-2756
    • (2004) Oncogene , vol.23 , Issue.16 , pp. 2746-2756
    • Jaattela, M.1
  • 80
    • 11144314179 scopus 로고    scopus 로고
    • Increased mitochondrial biogenesis in primary leukemia cells: the role of endogenous nitric oxide and impact on sensitivity to fludarabine
    • Carew J.S., Nawrocki S.T., Xu R.H., Dunner K., McConkey D.J., Wierda W.G., et al. Increased mitochondrial biogenesis in primary leukemia cells: the role of endogenous nitric oxide and impact on sensitivity to fludarabine. Leukemia 18 12 (2004) 1934-1940
    • (2004) Leukemia , vol.18 , Issue.12 , pp. 1934-1940
    • Carew, J.S.1    Nawrocki, S.T.2    Xu, R.H.3    Dunner, K.4    McConkey, D.J.5    Wierda, W.G.6
  • 81
    • 0026623115 scopus 로고
    • ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes
    • Donaldson J.G., Cassel D., Kahn R.A., and Klausner R.D. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc Natl Acad Sci USA 89 14 (1992) 6408-6412
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.14 , pp. 6408-6412
    • Donaldson, J.G.1    Cassel, D.2    Kahn, R.A.3    Klausner, R.D.4
  • 82
    • 33745242294 scopus 로고    scopus 로고
    • Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs
    • Cheung H.H., Lynn Kelly N., Liston P., and Korneluk R.G. Involvement of caspase-2 and caspase-9 in endoplasmic reticulum stress-induced apoptosis: a role for the IAPs. Exp Cell Res 312 12 (2006) 2347-2357
    • (2006) Exp Cell Res , vol.312 , Issue.12 , pp. 2347-2357
    • Cheung, H.H.1    Lynn Kelly, N.2    Liston, P.3    Korneluk, R.G.4
  • 83
    • 0030587429 scopus 로고    scopus 로고
    • Brefeldin A is a potent inducer of apoptosis in human cancer cells independently of p53
    • Shao R.G., Shimizu T., and Pommier Y. Brefeldin A is a potent inducer of apoptosis in human cancer cells independently of p53. Exp Cell Res 227 2 (1996) 190-196
    • (1996) Exp Cell Res , vol.227 , Issue.2 , pp. 190-196
    • Shao, R.G.1    Shimizu, T.2    Pommier, Y.3
  • 84
    • 0033903708 scopus 로고    scopus 로고
    • Brefeldin A induces p53-independent apoptosis in primary cultures of human prostatic cancer cells
    • Wallen E., Sellers R.G., and Peehl D.M. Brefeldin A induces p53-independent apoptosis in primary cultures of human prostatic cancer cells. Urol 164 (2000) 836-841
    • (2000) Urol , vol.164 , pp. 836-841
    • Wallen, E.1    Sellers, R.G.2    Peehl, D.M.3
  • 85
    • 1842525726 scopus 로고    scopus 로고
    • Brefeldin-A induces apoptosis in human adenoid cystic carcinoma cultured cells
    • Salles F.T., Hespanhol A.M., Jaeger R.G., and Marques M.M. Brefeldin-A induces apoptosis in human adenoid cystic carcinoma cultured cells. Oral Oncol 40 6 (2004) 585-590
    • (2004) Oral Oncol , vol.40 , Issue.6 , pp. 585-590
    • Salles, F.T.1    Hespanhol, A.M.2    Jaeger, R.G.3    Marques, M.M.4
  • 86
    • 0036312001 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization
    • Boya P., Cohen I., Zamzami N., Vieira H.L., and Kroemer G. Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization. Cell Death Differ 9 4 (2002) 465-467
    • (2002) Cell Death Differ , vol.9 , Issue.4 , pp. 465-467
    • Boya, P.1    Cohen, I.2    Zamzami, N.3    Vieira, H.L.4    Kroemer, G.5
  • 87
    • 35748944567 scopus 로고    scopus 로고
    • Brefeldin A triggers apoptosis associated with mitochondrial breach and enhances HA14-1- and anti-Fas-mediated cell killing in follicular lymphoma cells
    • Wlodkowic D., Skommer J., and Pelkonen J. Brefeldin A triggers apoptosis associated with mitochondrial breach and enhances HA14-1- and anti-Fas-mediated cell killing in follicular lymphoma cells. Leukemia Res 31 12 (2007) 1687-1700
    • (2007) Leukemia Res , vol.31 , Issue.12 , pp. 1687-1700
    • Wlodkowic, D.1    Skommer, J.2    Pelkonen, J.3
  • 89
    • 0027231520 scopus 로고
    • Analysis of Brefeldin A in plasma by gas chromatography with electron capture
    • Phillips L.R., Supko J.G., and Malspeis L. Analysis of Brefeldin A in plasma by gas chromatography with electron capture. Anal Biochem 211 (1993) 16-22
    • (1993) Anal Biochem , vol.211 , pp. 16-22
    • Phillips, L.R.1    Supko, J.G.2    Malspeis, L.3
  • 90
    • 0032053505 scopus 로고    scopus 로고
    • Analysis of brefeldin A and the prodrug breflate in plasma by gas chromatography with mass selective detection
    • Phillips L.R., Wolfe T.L., Malspeis L., and Supko J.G. Analysis of brefeldin A and the prodrug breflate in plasma by gas chromatography with mass selective detection. J Pharm Biomed Anal 16 8 (1998) 1301-1309
    • (1998) J Pharm Biomed Anal , vol.16 , Issue.8 , pp. 1301-1309
    • Phillips, L.R.1    Wolfe, T.L.2    Malspeis, L.3    Supko, J.G.4
  • 91
    • 14644407525 scopus 로고    scopus 로고
    • The role of apoptosis in cancer development and treatment response
    • Brown J.M., and Attardi L.D. The role of apoptosis in cancer development and treatment response. Nat Rev Cancer 5 3 (2005) 231-237
    • (2005) Nat Rev Cancer , vol.5 , Issue.3 , pp. 231-237
    • Brown, J.M.1    Attardi, L.D.2
  • 92
    • 26444434342 scopus 로고    scopus 로고
    • Pharmacological manipulation of cell death: clinical applications in sight?
    • Green D.R., and Kroemer G. Pharmacological manipulation of cell death: clinical applications in sight?. J Clin Invest 115 10 (2005) 2610-2617
    • (2005) J Clin Invest , vol.115 , Issue.10 , pp. 2610-2617
    • Green, D.R.1    Kroemer, G.2
  • 93
    • 0032914747 scopus 로고    scopus 로고
    • Mechanism of Brefeldin A-induced growth inhibition and cell death in human prostatic carcinoma cells
    • Chapman J.R., Tazaki H., Mallouh C., and Konno S. Mechanism of Brefeldin A-induced growth inhibition and cell death in human prostatic carcinoma cells. Mol Urol 3 1 (1999) 11-16
    • (1999) Mol Urol , vol.3 , Issue.1 , pp. 11-16
    • Chapman, J.R.1    Tazaki, H.2    Mallouh, C.3    Konno, S.4
  • 94
    • 0036676970 scopus 로고    scopus 로고
    • Stressful death of T-ALL tumor cells after treatment with the anti-tumor agent Tetrocarcin-A
    • Tinhoffer I., Anether G., Senfter M., Pfaller K., Bernhard D., Hara M., et al. Stressful death of T-ALL tumor cells after treatment with the anti-tumor agent Tetrocarcin-A. FASEB J 16 (2002) 1295-1297
    • (2002) FASEB J , vol.16 , pp. 1295-1297
    • Tinhoffer, I.1    Anether, G.2    Senfter, M.3    Pfaller, K.4    Bernhard, D.5    Hara, M.6
  • 95
    • 0037827680 scopus 로고    scopus 로고
    • Tetrocarcin-A-induced ER stress mediates apoptosis in B-CLL cells via a Bcl-2-independent pathway
    • Anether G., Tinhoffer I., and Greil R. Tetrocarcin-A-induced ER stress mediates apoptosis in B-CLL cells via a Bcl-2-independent pathway. Blood 101 11 (2003) 4561-4567
    • (2003) Blood , vol.101 , Issue.11 , pp. 4561-4567
    • Anether, G.1    Tinhoffer, I.2    Greil, R.3
  • 96
    • 24644432531 scopus 로고    scopus 로고
    • The SERCA pump as a therapeutic target: making a "smart bomb" for prostate cancer
    • Denmeade S.R., and Isaacs J.T. The SERCA pump as a therapeutic target: making a "smart bomb" for prostate cancer. Cancer Biol & Ther 4 1 (2005) 14-22
    • (2005) Cancer Biol & Ther , vol.4 , Issue.1 , pp. 14-22
    • Denmeade, S.R.1    Isaacs, J.T.2
  • 97
    • 29244454269 scopus 로고    scopus 로고
    • Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis
    • Nawrocki S.T., Carew J.S., Pino M.S., Highshaw R.A., Dunner K., Huang P., et al. Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis. Cancer Res 65 24 (2005) 11658-11666
    • (2005) Cancer Res , vol.65 , Issue.24 , pp. 11658-11666
    • Nawrocki, S.T.1    Carew, J.S.2    Pino, M.S.3    Highshaw, R.A.4    Dunner, K.5    Huang, P.6
  • 98
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller D., and Dikic I. Targeting the ubiquitin system in cancer therapy. Nature 458 7237 (2009) 438-444
    • (2009) Nature , vol.458 , Issue.7237 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 99
    • 50249092779 scopus 로고    scopus 로고
    • Development of proteasome inhibitors in oncology and autoimmune diseases
    • Bennett M.K., and Kirk C.J. Development of proteasome inhibitors in oncology and autoimmune diseases. Curr Opin Drug Discov Dev 11 5 (2008) 616-625
    • (2008) Curr Opin Drug Discov Dev , vol.11 , Issue.5 , pp. 616-625
    • Bennett, M.K.1    Kirk, C.J.2
  • 100
    • 5344234076 scopus 로고    scopus 로고
    • The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications
    • Burger A.M., and Seth A.K. The ubiquitin-mediated protein degradation pathway in cancer: therapeutic implications. Eur J Cancer 40 15 (2004) 2217-2229
    • (2004) Eur J Cancer , vol.40 , Issue.15 , pp. 2217-2229
    • Burger, A.M.1    Seth, A.K.2
  • 101
    • 63149188611 scopus 로고    scopus 로고
    • Combining the endoplasmic reticulum stress-inducing agents bortezomib and fenretinide as a novel therapeutic strategy for metastatic melanoma
    • Hill D.S., Martin S., Armstrong J.L., Flockhart R., Tonison J.J., Simpson D.G., et al. Combining the endoplasmic reticulum stress-inducing agents bortezomib and fenretinide as a novel therapeutic strategy for metastatic melanoma. Clin Cancer Res 15 4 (2009) 1192-1198
    • (2009) Clin Cancer Res , vol.15 , Issue.4 , pp. 1192-1198
    • Hill, D.S.1    Martin, S.2    Armstrong, J.L.3    Flockhart, R.4    Tonison, J.J.5    Simpson, D.G.6
  • 102
    • 60549109872 scopus 로고    scopus 로고
    • ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells
    • Wang Q., Mora-Jensen H., Weniger M.A., Perez-Galan P., Wolford C., Hai T., et al. ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells. Proc Natl Acad Sci USA 106 7 (2009) 2200-2205
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.7 , pp. 2200-2205
    • Wang, Q.1    Mora-Jensen, H.2    Weniger, M.A.3    Perez-Galan, P.4    Wolford, C.5    Hai, T.6
  • 103
    • 34047192683 scopus 로고    scopus 로고
    • The endoplasmic reticulum: a target for new anticancer drugs
    • Boelens J., Lust S., Offner F., Bracke M.E., and Vanhoecke B.W. The endoplasmic reticulum: a target for new anticancer drugs. In Vivo 21 2 (2007) 215-226
    • (2007) In Vivo , vol.21 , Issue.2 , pp. 215-226
    • Boelens, J.1    Lust, S.2    Offner, F.3    Bracke, M.E.4    Vanhoecke, B.W.5


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