메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Combined Inhibition of p97 and the Proteasome Causes Lethal Disruption of the Secretory Apparatus in Multiple Myeloma Cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BORTEZOMIB; CELL PROTEIN; PROTEASOME; PROTEIN P97;

EID: 84884268185     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0074415     Document Type: Article
Times cited : (44)

References (57)
  • 1
    • 84864773480 scopus 로고    scopus 로고
    • DangER: Protein ovERload. Targeting protein degradation to treat myeloma
    • doi:10.3324/haematol.2012.064923. PubMed: 22580998
    • Aronson LI, Davies FE, (2012) DangER: protein ovERload. Targeting protein degradation to treat myeloma. Haematologica 97: 1119-1130. doi:10.3324/haematol.2012.064923. PubMed: 22580998.
    • (2012) Haematologica , vol.97 , pp. 1119-1130
    • Aronson, L.I.1    Davies, F.E.2
  • 2
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • doi:10.1146/annurev.biochem.73.011303.074134. PubMed: 15952902
    • Schröder M, Kaufman RJ, (2005) The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789. doi:10.1146/annurev.biochem.73.011303.074134. PubMed: 15952902.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schröder, M.1    Kaufman, R.J.2
  • 3
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • doi:10.1038/nrm2546. PubMed: 19002207
    • Vembar SS, Brodsky JL, (2008) One step at a time: endoplasmic reticulum-associated degradation. Nat Rev Mol Cell Biol 9: 944-957. doi:10.1038/nrm2546. PubMed: 19002207.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 4
    • 79952264011 scopus 로고    scopus 로고
    • Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress
    • doi:10.1038/ncb0311-184. PubMed: 21364565
    • Tabas I, Ron D, (2011) Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 13: 184-190. doi:10.1038/ncb0311-184. PubMed: 21364565.
    • (2011) Nat Cell Biol , vol.13 , pp. 184-190
    • Tabas, I.1    Ron, D.2
  • 5
    • 63849281664 scopus 로고    scopus 로고
    • The proteasome load versus capacity balance determines apoptotic sensitivity of multiple myeloma cells to proteasome inhibition
    • doi:10.1182/blood-2008-08-172734. PubMed: 19164601
    • Bianchi G, Oliva L, Cascio P, Pengo N, Fontana F, et al. (2009) The proteasome load versus capacity balance determines apoptotic sensitivity of multiple myeloma cells to proteasome inhibition. Blood 113: 3040-3049. doi:10.1182/blood-2008-08-172734. PubMed: 19164601.
    • (2009) Blood , vol.113 , pp. 3040-3049
    • Bianchi, G.1    Oliva, L.2    Cascio, P.3    Pengo, N.4    Fontana, F.5
  • 6
    • 33644871448 scopus 로고    scopus 로고
    • Progressively impaired proteasomal capacity during terminal plasma cell differentiation
    • doi:10.1038/sj.emboj.7601009. PubMed: 16498407
    • Cenci S, Mezghrani A, Cascio P, Bianchi G, Cerruti F, et al. (2006) Progressively impaired proteasomal capacity during terminal plasma cell differentiation. EMBO J 25: 1104-1113. doi:10.1038/sj.emboj.7601009. PubMed: 16498407.
    • (2006) EMBO J , vol.25 , pp. 1104-1113
    • Cenci, S.1    Mezghrani, A.2    Cascio, P.3    Bianchi, G.4    Cerruti, F.5
  • 7
    • 78149311525 scopus 로고    scopus 로고
    • The life span of short-lived plasma cells is partly determined by a block on activation of apoptotic caspases acting in combination with endoplasmic reticulum stress
    • doi:10.1182/blood-2009-10-250423. PubMed: 20651073
    • Auner HW, Beham-Schmid C, Dillon N, Sabbattini P, (2010) The life span of short-lived plasma cells is partly determined by a block on activation of apoptotic caspases acting in combination with endoplasmic reticulum stress. Blood 116: 3445-3455. doi:10.1182/blood-2009-10-250423. PubMed: 20651073.
    • (2010) Blood , vol.116 , pp. 3445-3455
    • Auner, H.W.1    Beham-Schmid, C.2    Dillon, N.3    Sabbattini, P.4
  • 8
    • 78650087357 scopus 로고    scopus 로고
    • Emerging therapies for the treatment of relapsed or refractory multiple myeloma
    • doi:10.1111/j.1600-0609.2010.01542.x. PubMed: 20942854
    • Dimopoulos MA, San-Miguel JF, Anderson KC, (2011) Emerging therapies for the treatment of relapsed or refractory multiple myeloma. Eur J Haematol 86: 1-15. doi:10.1111/j.1600-0609.2010.01542.x. PubMed: 20942854.
    • (2011) Eur J Haematol , vol.86 , pp. 1-15
    • Dimopoulos, M.A.1    San-Miguel, J.F.2    Anderson, K.C.3
  • 9
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • doi:10.1182/blood-2005-08-3531. PubMed: 16507771
    • Obeng EA, Carlson LM, Gutman DM, Harrington WJ Jr., Lee KP, et al. (2006) Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 107: 4907-4916. doi:10.1182/blood-2005-08-3531. PubMed: 16507771.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5
  • 10
    • 0043193876 scopus 로고    scopus 로고
    • Proteasome inhibitors disrupt the unfolded protein response in myeloma cells
    • doi:10.1073/pnas.1334037100. PubMed: 12902539
    • Lee AH, Iwakoshi NN, Anderson KC, Glimcher LH, (2003) Proteasome inhibitors disrupt the unfolded protein response in myeloma cells. Proc Natl Acad Sci U S A 100: 9946-9951. doi:10.1073/pnas.1334037100. PubMed: 12902539.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9946-9951
    • Lee, A.H.1    Iwakoshi, N.N.2    Anderson, K.C.3    Glimcher, L.H.4
  • 11
    • 60549109872 scopus 로고    scopus 로고
    • ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells
    • doi:10.1073/pnas.0807611106. PubMed: 19164757
    • Wang Q, Mora-Jensen H, Weniger MA, Perez-Galan P, Wolford C, et al. (2009) ERAD inhibitors integrate ER stress with an epigenetic mechanism to activate BH3-only protein NOXA in cancer cells. Proc Natl Acad Sci U S A 106: 2200-2205. doi:10.1073/pnas.0807611106. PubMed: 19164757.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2200-2205
    • Wang, Q.1    Mora-Jensen, H.2    Weniger, M.A.3    Perez-Galan, P.4    Wolford, C.5
  • 12
    • 33847714599 scopus 로고    scopus 로고
    • Extensive immunoglobulin production sensitizes myeloma cells for proteasome inhibition
    • doi:10.1158/0008-5472.CAN-06-2258. PubMed: 17308121
    • Meister S, Schubert U, Neubert K, Herrmann K, Burger R, et al. (2007) Extensive immunoglobulin production sensitizes myeloma cells for proteasome inhibition. Cancer Res 67: 1783-1792. doi:10.1158/0008-5472.CAN-06-2258. PubMed: 17308121.
    • (2007) Cancer Res , vol.67 , pp. 1783-1792
    • Meister, S.1    Schubert, U.2    Neubert, K.3    Herrmann, K.4    Burger, R.5
  • 13
    • 67651146528 scopus 로고    scopus 로고
    • Effect of autophagy on multiple myeloma cell viability
    • doi:10.1158/1535-7163.MCT-08-1177. PubMed: 19509276
    • Hoang B, Benavides A, Shi Y, Frost P, Lichtenstein A, (2009) Effect of autophagy on multiple myeloma cell viability. Mol Cancer Ther 8: 1974-1984. doi:10.1158/1535-7163.MCT-08-1177. PubMed: 19509276.
    • (2009) Mol Cancer Ther , vol.8 , pp. 1974-1984
    • Hoang, B.1    Benavides, A.2    Shi, Y.3    Frost, P.4    Lichtenstein, A.5
  • 14
    • 78650041246 scopus 로고    scopus 로고
    • Tipifarnib sensitizes cells to proteasome inhibition by blocking degradation of bortezomib-induced aggresomes
    • doi:10.1182/blood-2010-03-272393. PubMed: 20844234
    • David E, Kaufman JL, Flowers CR, Schafer-Hales K, Torre C, et al. (2010) Tipifarnib sensitizes cells to proteasome inhibition by blocking degradation of bortezomib-induced aggresomes. Blood 116: 5285-5288. doi:10.1182/blood-2010-03-272393. PubMed: 20844234.
    • (2010) Blood , vol.116 , pp. 5285-5288
    • David, E.1    Kaufman, J.L.2    Flowers, C.R.3    Schafer-Hales, K.4    Torre, C.5
  • 15
    • 67349212864 scopus 로고    scopus 로고
    • Characterization of the ubiquitin-proteasome system in bortezomib-adapted cells
    • doi:10.1038/leu.2009.8. PubMed: 19225532
    • Rückrich T, Kraus M, Gogel J, Beck A, Ovaa H, et al. (2009) Characterization of the ubiquitin-proteasome system in bortezomib-adapted cells. Leukemia 23: 1098-1105. doi:10.1038/leu.2009.8. PubMed: 19225532.
    • (2009) Leukemia , vol.23 , pp. 1098-1105
    • Rückrich, T.1    Kraus, M.2    Gogel, J.3    Beck, A.4    Ovaa, H.5
  • 16
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • doi:10.1111/j.1600-0854.2008.00729.x. PubMed: 18315532
    • Nakatsukasa K, Brodsky JL, (2008) The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9: 861-870. doi:10.1111/j.1600-0854.2008.00729.x. PubMed: 18315532.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 17
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • doi:10.1083/jcb.200302169. PubMed: 12847084
    • Ye Y, Meyer HH, Rapoport TA, (2003) Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162: 71-84. doi:10.1083/jcb.200302169. PubMed: 12847084.
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 18
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • doi:10.1016/j.molcel.2009.09.016. PubMed: 19818707
    • Ernst R, Mueller B, Ploegh HL, Schlieker C, (2009) The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol Cell 36: 28-38. doi:10.1016/j.molcel.2009.09.016. PubMed: 19818707.
    • (2009) Mol Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 19
    • 33750528166 scopus 로고    scopus 로고
    • Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells
    • doi:10.1091/mbc.E06-05-0432. PubMed: 16914519
    • Wójcik C, Rowicka M, Kudlicki A, Nowis D, McConnell E, et al. (2006) Valosin-containing protein (p97) is a regulator of endoplasmic reticulum stress and of the degradation of N-end rule and ubiquitin-fusion degradation pathway substrates in mammalian cells. Mol Biol Cell 17: 4606-4618. doi:10.1091/mbc.E06-05-0432. PubMed: 16914519.
    • (2006) Mol Biol Cell , vol.17 , pp. 4606-4618
    • Wójcik, C.1    Rowicka, M.2    Kudlicki, A.3    Nowis, D.4    McConnell, E.5
  • 20
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • doi:10.1038/414652a. PubMed: 11740563
    • Ye Y, Meyer HH, Rapoport TA, (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414: 652-656. doi:10.1038/414652a. PubMed: 11740563.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 21
    • 26444621357 scopus 로고    scopus 로고
    • Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • doi:10.1073/pnas.0505006102. PubMed: 16186510
    • Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, et al. (2005) Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A 102: 14132-14138. doi:10.1073/pnas.0505006102. PubMed: 16186510.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14132-14138
    • Ye, Y.1    Shibata, Y.2    Kikkert, M.3    van Voorden, S.4    Wiertz, E.5
  • 22
    • 84861970930 scopus 로고    scopus 로고
    • p97 complexes as signal integration hubs
    • doi:10.1186/1741-7007-10-48. PubMed: 22694940
    • Meyer H, (2012) p97 complexes as signal integration hubs. BMC Biol 10: 48. doi:10.1186/1741-7007-10-48. PubMed: 22694940.
    • (2012) BMC Biol , vol.10 , pp. 48
    • Meyer, H.1
  • 23
    • 33751343672 scopus 로고    scopus 로고
    • p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis
    • doi:10.1016/j.devcel.2006.10.016. PubMed: 17141156
    • Uchiyama K, Totsukawa G, Puhka M, Kaneko Y, Jokitalo E, et al. (2006) p37 is a p97 adaptor required for Golgi and ER biogenesis in interphase and at the end of mitosis. Dev Cell 11: 803-816. doi:10.1016/j.devcel.2006.10.016. PubMed: 17141156.
    • (2006) Dev Cell , vol.11 , pp. 803-816
    • Uchiyama, K.1    Totsukawa, G.2    Puhka, M.3    Kaneko, Y.4    Jokitalo, E.5
  • 24
    • 78650733298 scopus 로고    scopus 로고
    • Cdc48/p97 mediates UV-dependent turnover of RNA Pol II
    • doi:10.1016/j.molcel.2010.12.017. PubMed: 21211725
    • Verma R, Oania R, Fang R, Smith GT, Deshaies RJ, (2011) Cdc48/p97 mediates UV-dependent turnover of RNA Pol II. Mol Cell 41: 82-92. doi:10.1016/j.molcel.2010.12.017. PubMed: 21211725.
    • (2011) Mol Cell , vol.41 , pp. 82-92
    • Verma, R.1    Oania, R.2    Fang, R.3    Smith, G.T.4    Deshaies, R.J.5
  • 25
    • 84855206731 scopus 로고    scopus 로고
    • Recent advances in p97/VCP/Cdc48 cellular functions
    • doi:10.1016/j.bbamcr.2011.07.001. PubMed: 21781992
    • Yamanaka K, Sasagawa Y, Ogura T, (2012) Recent advances in p97/VCP/Cdc48 cellular functions. Biochim Biophys Acta 1823: 130-137. doi:10.1016/j.bbamcr.2011.07.001. PubMed: 21781992.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 130-137
    • Yamanaka, K.1    Sasagawa, Y.2    Ogura, T.3
  • 26
    • 79953171555 scopus 로고    scopus 로고
    • Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways
    • doi:10.1073/pnas.1015312108. PubMed: 21383145
    • Chou TF, Brown SJ, Minond D, Nordin BE, Li K, et al. (2011) Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways. Proc Natl Acad Sci U S A 108: 4834-4839. doi:10.1073/pnas.1015312108. PubMed: 21383145.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 4834-4839
    • Chou, T.F.1    Brown, S.J.2    Minond, D.3    Nordin, B.E.4    Li, K.5
  • 27
    • 80052353713 scopus 로고    scopus 로고
    • Development of p97 AAA ATPase inhibitors
    • doi:10.4161/auto.7.9.16489. PubMed: 21606684
    • Chou TF, Deshaies RJ, (2011) Development of p97 AAA ATPase inhibitors. Autophagy 7: 1091-1092. doi:10.4161/auto.7.9.16489. PubMed: 21606684.
    • (2011) Autophagy , vol.7 , pp. 1091-1092
    • Chou, T.F.1    Deshaies, R.J.2
  • 28
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin I
    • doi:10.1074/jbc.M708347200. PubMed: 18199748
    • Wang Q, Li L, Ye Y, (2008) Inhibition of p97-dependent protein degradation by Eeyarestatin I. J Biol Chem 283: 7445-7454. doi:10.1074/jbc.M708347200. PubMed: 18199748.
    • (2008) J Biol Chem , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 29
    • 78649742954 scopus 로고    scopus 로고
    • The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group
    • doi:10.1371/journal.pone.0015479. PubMed: 21124757
    • Wang Q, Shinkre BA, Lee JG, Weniger MA, Liu Y, et al. (2010) The ERAD inhibitor Eeyarestatin I is a bifunctional compound with a membrane-binding domain and a p97/VCP inhibitory group. PLOS ONE 5: e15479. doi:10.1371/journal.pone.0015479. PubMed: 21124757.
    • (2010) PLOS ONE , vol.5
    • Wang, Q.1    Shinkre, B.A.2    Lee, J.G.3    Weniger, M.A.4    Liu, Y.5
  • 30
    • 84871382622 scopus 로고    scopus 로고
    • Sorafenib-mediated targeting of the AAA(+) ATPase p97/VCP leads to disruption of the secretory pathway, endoplasmic reticulum stress, and hepatocellular cancer cell death
    • doi:10.1158/1535-7163.MCT-12-0516. PubMed: 23041544
    • Yi P, Higa A, Taouji S, Bexiga MG, Marza E, et al. (2012) Sorafenib-mediated targeting of the AAA(+) ATPase p97/VCP leads to disruption of the secretory pathway, endoplasmic reticulum stress, and hepatocellular cancer cell death. Mol Cancer Ther 11: 2610-2620. doi:10.1158/1535-7163.MCT-12-0516. PubMed: 23041544.
    • (2012) Mol Cancer Ther , vol.11 , pp. 2610-2620
    • Yi, P.1    Higa, A.2    Taouji, S.3    Bexiga, M.G.4    Marza, E.5
  • 31
    • 84867517513 scopus 로고    scopus 로고
    • Sorafenib has potent antitumor activity against multiple myeloma in vitro, ex vivo, and in vivo in the 5T33MM mouse model
    • doi:10.1158/0008-5472.CAN-12-0658. PubMed: 22952216
    • Kharaziha P, De Raeve H, Fristedt C, Li Q, Gruber A, et al. (2012) Sorafenib has potent antitumor activity against multiple myeloma in vitro, ex vivo, and in vivo in the 5T33MM mouse model. Cancer Res 72: 5348-5362. doi:10.1158/0008-5472.CAN-12-0658. PubMed: 22952216.
    • (2012) Cancer Res , vol.72 , pp. 5348-5362
    • Kharaziha, P.1    De Raeve, H.2    Fristedt, C.3    Li, Q.4    Gruber, A.5
  • 32
    • 84880040665 scopus 로고    scopus 로고
    • P97/CDC-48: Proteostasis control in tumor cell biology
    • PubMed: 23726843
    • Fessart D, Marza E, Taouji S, Delom F, Chevet E, (2013) P97/CDC-48: Proteostasis control in tumor cell biology. Cancer Lett, 337: 26-34. PubMed: 23726843.
    • (2013) Cancer Lett , vol.337 , pp. 26-34
    • Fessart, D.1    Marza, E.2    Taouji, S.3    Delom, F.4    Chevet, E.5
  • 33
    • 57149130824 scopus 로고    scopus 로고
    • AAA ATPase p97/VCP: Cellular functions, disease and therapeutic potential
    • doi:10.1111/j.1582-4934.2008.00462.x. PubMed: 18798739
    • Vij N, (2008) AAA ATPase p97/VCP: cellular functions, disease and therapeutic potential. J Cell Mol Med 12: 2511-2518. doi:10.1111/j.1582-4934.2008.00462.x. PubMed: 18798739.
    • (2008) J Cell Mol Med , vol.12 , pp. 2511-2518
    • Vij, N.1
  • 34
    • 36549086530 scopus 로고    scopus 로고
    • Trafficking through the early secretory pathway of mammalian cells
    • doi:10.1007/978-1-59745-466-7_19. PubMed: 17951695
    • Ward TH, (2007) Trafficking through the early secretory pathway of mammalian cells. Methods Mol Biol 390: 281-296. doi:10.1007/978-1-59745-466-7_19. PubMed: 17951695.
    • (2007) Methods Mol Biol , vol.390 , pp. 281-296
    • Ward, T.H.1
  • 35
    • 76149093156 scopus 로고    scopus 로고
    • Biogenesis of secretory organelles during B cell differentiation
    • doi:10.1189/jlb.1208774. PubMed: 19889725
    • Kirk SJ, Cliff JM, Thomas JA, Ward TH, (2010) Biogenesis of secretory organelles during B cell differentiation. J Leukoc Biol 87: 245-255. doi:10.1189/jlb.1208774. PubMed: 19889725.
    • (2010) J Leukoc Biol , vol.87 , pp. 245-255
    • Kirk, S.J.1    Cliff, J.M.2    Thomas, J.A.3    Ward, T.H.4
  • 36
    • 84878322959 scopus 로고    scopus 로고
    • Nelfinavir augments proteasome inhibition by bortezomib in myeloma cells and overcomes bortezomib and carfilzomib resistance. Blood
    • Kraus M, Bader J, Overkleeft H, Driessen C, (2013) Nelfinavir augments proteasome inhibition by bortezomib in myeloma cells and overcomes bortezomib and carfilzomib resistance. Blood. Cancer J 3: e103.
    • (2013) Cancer J , vol.3
    • Kraus, M.1    Bader, J.2    Overkleeft, H.3    Driessen, C.4
  • 37
    • 84863170102 scopus 로고    scopus 로고
    • KLF9 is a novel transcriptional regulator of bortezomib- and LBH589-induced apoptosis in multiple myeloma cells
    • doi:10.1182/blood-2011-04-346676. PubMed: 22144178
    • Mannava S, Zhuang D, Nair JR, Bansal R, Wawrzyniak JA, et al. (2012) KLF9 is a novel transcriptional regulator of bortezomib- and LBH589-induced apoptosis in multiple myeloma cells. Blood 119: 1450-1458. doi:10.1182/blood-2011-04-346676. PubMed: 22144178.
    • (2012) Blood , vol.119 , pp. 1450-1458
    • Mannava, S.1    Zhuang, D.2    Nair, J.R.3    Bansal, R.4    Wawrzyniak, J.A.5
  • 38
    • 83355169702 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases
    • doi:10.1074/jbc.M111.274332. PubMed: 22006919
    • Wang F, Song W, Brancati G, Segatori L, (2011) Inhibition of endoplasmic reticulum-associated degradation rescues native folding in loss of function protein misfolding diseases. J Biol Chem 286: 43454-43464. doi:10.1074/jbc.M111.274332. PubMed: 22006919.
    • (2011) J Biol Chem , vol.286 , pp. 43454-43464
    • Wang, F.1    Song, W.2    Brancati, G.3    Segatori, L.4
  • 39
    • 84863919796 scopus 로고    scopus 로고
    • Long-term analysis of the IFM 99 trials for myeloma: Cytogenetic abnormalities [t(4;14), del(17p), 1q gains] play a major role in defining long-term survival
    • doi:10.1200/JCO.2011.36.5726. PubMed: 22547600
    • Avet-Loiseau H, Attal M, Campion L, Caillot D, Hulin C, et al. (2012) Long-term analysis of the IFM 99 trials for myeloma: cytogenetic abnormalities [t(4;14), del(17p), 1q gains] play a major role in defining long-term survival. J Clin Oncol 30: 1949-1952. doi:10.1200/JCO.2011.36.5726. PubMed: 22547600.
    • (2012) J Clin Oncol , vol.30 , pp. 1949-1952
    • Avet-Loiseau, H.1    Attal, M.2    Campion, L.3    Caillot, D.4    Hulin, C.5
  • 40
    • 79951507143 scopus 로고    scopus 로고
    • Mutated RAS and constitutively activated Akt delineate distinct oncogenic pathways, which independently contribute to multiple myeloma cell survival
    • doi:10.1182/blood-2010-05-284422. PubMed: 21149634
    • Steinbrunn T, Stühmer T, Gattenlöhner S, Rosenwald A, Mottok A, et al. (2011) Mutated RAS and constitutively activated Akt delineate distinct oncogenic pathways, which independently contribute to multiple myeloma cell survival. Blood 117: 1998-2004. doi:10.1182/blood-2010-05-284422. PubMed: 21149634.
    • (2011) Blood , vol.117 , pp. 1998-2004
    • Steinbrunn, T.1    Stühmer, T.2    Gattenlöhner, S.3    Rosenwald, A.4    Mottok, A.5
  • 41
    • 70350708810 scopus 로고    scopus 로고
    • Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome
    • doi:10.1182/blood-2009-05-223677. PubMed: 19671918
    • Parlati F, Lee SJ, Aujay M, Suzuki E, Levitsky K, et al. (2009) Carfilzomib can induce tumor cell death through selective inhibition of the chymotrypsin-like activity of the proteasome. Blood 114: 3439-3447. doi:10.1182/blood-2009-05-223677. PubMed: 19671918.
    • (2009) Blood , vol.114 , pp. 3439-3447
    • Parlati, F.1    Lee, S.J.2    Aujay, M.3    Suzuki, E.4    Levitsky, K.5
  • 42
    • 22244452016 scopus 로고    scopus 로고
    • Proteasome inhibitors trigger NOXA-mediated apoptosis in melanoma and myeloma cells
    • doi:10.1158/0008-5472.CAN-05-0676. PubMed: 16024630
    • Qin JZ, Ziffra J, Stennett L, Bodner B, Bonish BK, et al. (2005) Proteasome inhibitors trigger NOXA-mediated apoptosis in melanoma and myeloma cells. Cancer Res 65: 6282-6293. doi:10.1158/0008-5472.CAN-05-0676. PubMed: 16024630.
    • (2005) Cancer Res , vol.65 , pp. 6282-6293
    • Qin, J.Z.1    Ziffra, J.2    Stennett, L.3    Bodner, B.4    Bonish, B.K.5
  • 43
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • doi:10.1371/journal.pbio.0040423. PubMed: 17132049
    • Bernales S, McDonald KL, Walter P, (2006) Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLOS Biol 4: e423. doi:10.1371/journal.pbio.0040423. PubMed: 17132049.
    • (2006) PLOS Biol , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 44
    • 5444222234 scopus 로고    scopus 로고
    • XBP1: A link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum
    • doi:10.1083/jcb.200406136. PubMed: 15466483
    • Sriburi R, Jackowski S, Mori K, Brewer JW, (2004) XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum. J Cell Biol 167: 35-41. doi:10.1083/jcb.200406136. PubMed: 15466483.
    • (2004) J Cell Biol , vol.167 , pp. 35-41
    • Sriburi, R.1    Jackowski, S.2    Mori, K.3    Brewer, J.W.4
  • 45
    • 18444395232 scopus 로고    scopus 로고
    • Blimp-1 orchestrates plasma cell differentiation by extinguishing the mature B cell gene expression program
    • doi:10.1016/S1074-7613(02)00335-7. PubMed: 12150891
    • Shaffer AL, Lin KI, Kuo TC, Yu X, Hurt EM, et al. (2002) Blimp-1 orchestrates plasma cell differentiation by extinguishing the mature B cell gene expression program. Immunity 17: 51-62. doi:10.1016/S1074-7613(02)00335-7. PubMed: 12150891.
    • (2002) Immunity , vol.17 , pp. 51-62
    • Shaffer, A.L.1    Lin, K.I.2    Kuo, T.C.3    Yu, X.4    Hurt, E.M.5
  • 46
    • 0034669945 scopus 로고    scopus 로고
    • Loss of PTEN expression leading to high Akt activation in human multiple myelomas
    • PubMed: 11071655
    • Hyun T, Yam A, Pece S, Xie X, Zhang J, et al. (2000) Loss of PTEN expression leading to high Akt activation in human multiple myelomas. Blood 96: 3560-3568. PubMed: 11071655.
    • (2000) Blood , vol.96 , pp. 3560-3568
    • Hyun, T.1    Yam, A.2    Pece, S.3    Xie, X.4    Zhang, J.5
  • 47
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • doi:10.1038/nrm2199. PubMed: 17565364
    • Ron D, Walter P, (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8: 519-529. doi:10.1038/nrm2199. PubMed: 17565364.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 48
    • 0034737639 scopus 로고    scopus 로고
    • Identification of caspase 3-mediated cleavage and functional alteration of eukaryotic initiation factor 2alpha in apoptosis
    • doi:10.1074/jbc.275.13.9314. PubMed: 10734073
    • Marissen WE, Guo Y, Thomas AA, Matts RL, Lloyd RE, (2000) Identification of caspase 3-mediated cleavage and functional alteration of eukaryotic initiation factor 2alpha in apoptosis. J Biol Chem 275: 9314-9323. doi:10.1074/jbc.275.13.9314. PubMed: 10734073.
    • (2000) J Biol Chem , vol.275 , pp. 9314-9323
    • Marissen, W.E.1    Guo, Y.2    Thomas, A.A.3    Matts, R.L.4    Lloyd, R.E.5
  • 49
    • 0035834676 scopus 로고    scopus 로고
    • Translation inhibition in apoptosis: Caspase-dependent PKR activation and eIF2-alpha phosphorylation
    • doi:10.1074/jbc.M103674200. PubMed: 11555640
    • Saelens X, Kalai M, Vandenabeele P, (2001) Translation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylation. J Biol Chem 276: 41620-41628. doi:10.1074/jbc.M103674200. PubMed: 11555640.
    • (2001) J Biol Chem , vol.276 , pp. 41620-41628
    • Saelens, X.1    Kalai, M.2    Vandenabeele, P.3
  • 50
    • 20144365870 scopus 로고    scopus 로고
    • Initiation factor modifications in the preapoptotic phase
    • doi:10.1038/sj.cdd.4401591. PubMed: 15900314
    • Morley SJ, Coldwell MJ, Clemens MJ, (2005) Initiation factor modifications in the preapoptotic phase. Cell Death Differ 12: 571-584. doi:10.1038/sj.cdd.4401591. PubMed: 15900314.
    • (2005) Cell Death Differ , vol.12 , pp. 571-584
    • Morley, S.J.1    Coldwell, M.J.2    Clemens, M.J.3
  • 51
    • 33750068623 scopus 로고    scopus 로고
    • mTOR, translation initiation and cancer
    • doi:10.1038/sj.onc.1209888. PubMed: 17041626
    • Mamane Y, Petroulakis E, LeBacquer O, Sonenberg N, (2006) mTOR, translation initiation and cancer. Oncogene 25: 6416-6422. doi:10.1038/sj.onc.1209888. PubMed: 17041626.
    • (2006) Oncogene , vol.25 , pp. 6416-6422
    • Mamane, Y.1    Petroulakis, E.2    LeBacquer, O.3    Sonenberg, N.4
  • 52
    • 21044446935 scopus 로고    scopus 로고
    • Molecular characterization of PS-341 (bortezomib) resistance: Implications for overcoming resistance using lysophosphatidic acid acyltransferase (LPAAT)-beta inhibitors
    • doi:10.1038/sj.onc.1208522. PubMed: 15735676
    • Hideshima T, Chauhan D, Ishitsuka K, Yasui H, Raje N, et al. (2005) Molecular characterization of PS-341 (bortezomib) resistance: implications for overcoming resistance using lysophosphatidic acid acyltransferase (LPAAT)-beta inhibitors. Oncogene 24: 3121-3129. doi:10.1038/sj.onc.1208522. PubMed: 15735676.
    • (2005) Oncogene , vol.24 , pp. 3121-3129
    • Hideshima, T.1    Chauhan, D.2    Ishitsuka, K.3    Yasui, H.4    Raje, N.5
  • 53
    • 79955461011 scopus 로고    scopus 로고
    • Subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma: A randomised, phase 3, non-inferiority study
    • doi:10.1016/S1470-2045(11)70081-X. PubMed: 21507715
    • Moreau P, Pylypenko H, Grosicki S, Karamanesht I, Leleu X, et al. (2011) Subcutaneous versus intravenous administration of bortezomib in patients with relapsed multiple myeloma: a randomised, phase 3, non-inferiority study. Lancet Oncol 12: 431-440. doi:10.1016/S1470-2045(11)70081-X. PubMed: 21507715.
    • (2011) Lancet Oncol , vol.12 , pp. 431-440
    • Moreau, P.1    Pylypenko, H.2    Grosicki, S.3    Karamanesht, I.4    Leleu, X.5
  • 54
    • 79955498420 scopus 로고    scopus 로고
    • Nonproteasomal targets of the proteasome inhibitors bortezomib and carfilzomib: A link to clinical adverse events
    • doi:10.1158/1078-0432.CCR-10-1950. PubMed: 21364033
    • Arastu-Kapur S, Anderl JL, Kraus M, Parlati F, Shenk KD, et al. (2011) Nonproteasomal targets of the proteasome inhibitors bortezomib and carfilzomib: a link to clinical adverse events. Clin Cancer Res 17: 2734-2743. doi:10.1158/1078-0432.CCR-10-1950. PubMed: 21364033.
    • (2011) Clin Cancer Res , vol.17 , pp. 2734-2743
    • Arastu-Kapur, S.1    Anderl, J.L.2    Kraus, M.3    Parlati, F.4    Shenk, K.D.5
  • 55
    • 84055172732 scopus 로고    scopus 로고
    • Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma
    • doi:10.1371/journal.pone.0029073. PubMed: 22216170
    • Valle CW, Min T, Bodas M, Mazur S, Begum S, et al. (2011) Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma. PLOS ONE 6: e29073. doi:10.1371/journal.pone.0029073. PubMed: 22216170.
    • (2011) PLOS ONE , vol.6
    • Valle, C.W.1    Min, T.2    Bodas, M.3    Mazur, S.4    Begum, S.5
  • 56
    • 33746541576 scopus 로고    scopus 로고
    • HDAC6-p97/VCP controlled polyubiquitin chain turnover
    • doi:10.1038/sj.emboj.7601210. PubMed: 16810319
    • Boyault C, Gilquin B, Zhang Y, Rybin V, Garman E, et al. (2006) HDAC6-p97/VCP controlled polyubiquitin chain turnover. EMBO J 25: 3357-3366. doi:10.1038/sj.emboj.7601210. PubMed: 16810319.
    • (2006) EMBO J , vol.25 , pp. 3357-3366
    • Boyault, C.1    Gilquin, B.2    Zhang, Y.3    Rybin, V.4    Garman, E.5
  • 57
    • 79951630982 scopus 로고    scopus 로고
    • The case for therapeutic proteostasis modulators
    • doi:10.1517/14728222.2011.553610. PubMed: 21250874
    • Vij N, (2011) The case for therapeutic proteostasis modulators. Expert Opin Ther Targets 15: 233-236. doi:10.1517/14728222.2011.553610. PubMed: 21250874.
    • (2011) Expert Opin Ther Targets , vol.15 , pp. 233-236
    • Vij, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.