메뉴 건너뛰기




Volumn 34, Issue 1, 2010, Pages 85-92

Enhanced antimyeloma cytotoxicity by the combination of arsenic trioxide and bortezomib is further potentiated by p38 MAPK inhibition

Author keywords

ATO; Bortezomib; Myeloma; p38 MAPK

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ARSENIC TRIOXIDE; BIM PROTEIN; BORTEZOMIB; HEAT SHOCK PROTEIN 27; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN BCL 2; PROTEIN P27; PROTEIN P53; STAT3 PROTEIN; STRESS ACTIVATED PROTEIN KINASE; SYNDECAN 1;

EID: 73249129928     PISSN: 01452126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.leukres.2009.05.024     Document Type: Article
Times cited : (42)

References (49)
  • 2
    • 9944242716 scopus 로고    scopus 로고
    • p38 MAPK inhibition enhances PS-341 (bortezomib)-induced cytotoxicity against multiple myeloma cells
    • Hideshima T., Podar K., Chauhan D., et al. p38 MAPK inhibition enhances PS-341 (bortezomib)-induced cytotoxicity against multiple myeloma cells. Oncogene 23 (2004) 8766-877676
    • (2004) Oncogene , vol.23 , pp. 8766-877676
    • Hideshima, T.1    Podar, K.2    Chauhan, D.3
  • 3
    • 37249084060 scopus 로고    scopus 로고
    • P38 MAPK inhibition enhancing ATO-induced cytotoxicity against multiple myeloma cells
    • Wen J., Cheng H.Y., Feng Y., et al. P38 MAPK inhibition enhancing ATO-induced cytotoxicity against multiple myeloma cells. Br J Haematol 140 (2008) 169-18080
    • (2008) Br J Haematol , vol.140 , pp. 169-18080
    • Wen, J.1    Cheng, H.Y.2    Feng, Y.3
  • 4
    • 33746160660 scopus 로고    scopus 로고
    • Proteasome inhibitor bortezomib for the treatment of multiple myeloma
    • Cavo M. Proteasome inhibitor bortezomib for the treatment of multiple myeloma. Leukemia 20 (2006) 1341-135252
    • (2006) Leukemia , vol.20 , pp. 1341-135252
    • Cavo, M.1
  • 6
    • 0037973279 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed, refractory myeloma
    • Richardson P.G., Barlogie B., Berenson J., et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. N Engl J Med 348 (2003) 2609-261717
    • (2003) N Engl J Med , vol.348 , pp. 2609-261717
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 7
    • 0036739745 scopus 로고    scopus 로고
    • Clinical activity of arsenic trioxide for the treatment of multiple myeloma
    • Munshi N.C., Tricot G., Desikan R., et al. Clinical activity of arsenic trioxide for the treatment of multiple myeloma. Leukemia 16 (2002) 1835-18377
    • (2002) Leukemia , vol.16 , pp. 1835-18377
    • Munshi, N.C.1    Tricot, G.2    Desikan, R.3
  • 8
    • 34250194653 scopus 로고    scopus 로고
    • A phase I/II study of arsenic trioxide/bortezomib/ascorbic acid combination therapy for the treatment of relapsed or refractory multiple myeloma
    • Berenson J.R., Matous J., Swift R.A., Mapes R., Morrison B., and Yeh H.S. A phase I/II study of arsenic trioxide/bortezomib/ascorbic acid combination therapy for the treatment of relapsed or refractory multiple myeloma. Clin Cancer Res 13 (2007) 1762-17688
    • (2007) Clin Cancer Res , vol.13 , pp. 1762-17688
    • Berenson, J.R.1    Matous, J.2    Swift, R.A.3    Mapes, R.4    Morrison, B.5    Yeh, H.S.6
  • 9
    • 34447299646 scopus 로고    scopus 로고
    • Antimyeloma effects of arsenic trioxide are enhanced by melphalan, bortezomib and ascorbic acid
    • Campbell R.A., Sanchez E., Steinberg J.A., et al. Antimyeloma effects of arsenic trioxide are enhanced by melphalan, bortezomib and ascorbic acid. Br J Haematol 138 (2007) 467-47878
    • (2007) Br J Haematol , vol.138 , pp. 467-47878
    • Campbell, R.A.1    Sanchez, E.2    Steinberg, J.A.3
  • 10
    • 30444448398 scopus 로고    scopus 로고
    • IGF-1 receptor tyrosine kinase inhibition by the cyclolignan PPP induces G2/M-phase accumulation and apoptosis in multiple myeloma cells
    • Stromberg T., Ekman S., Girnita L., et al. IGF-1 receptor tyrosine kinase inhibition by the cyclolignan PPP induces G2/M-phase accumulation and apoptosis in multiple myeloma cells. Blood 107 (2006) 669-67878
    • (2006) Blood , vol.107 , pp. 669-67878
    • Stromberg, T.1    Ekman, S.2    Girnita, L.3
  • 11
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A., Rouse J., Doza Y.N., et al. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett 364 (1995) 229-23333
    • (1995) FEBS Lett , vol.364 , pp. 229-23333
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3
  • 12
    • 0033812246 scopus 로고    scopus 로고
    • The p38 MAP kinase inhibitor SB203580 enhances nuclear factor-kappa B transcriptional activity by a non-specific effect upon the ERK pathway
    • Birkenkamp K.U., Tuyt L.M., Lummen C., Wierenga A.T., Kruijer W., and Vellenga E. The p38 MAP kinase inhibitor SB203580 enhances nuclear factor-kappa B transcriptional activity by a non-specific effect upon the ERK pathway. Br J Pharmacol 131 (2000) 99-107
    • (2000) Br J Pharmacol , vol.131 , pp. 99-107
    • Birkenkamp, K.U.1    Tuyt, L.M.2    Lummen, C.3    Wierenga, A.T.4    Kruijer, W.5    Vellenga, E.6
  • 13
    • 0034775828 scopus 로고    scopus 로고
    • Quercetin and tamoxifen sensitize human melanoma cells to hyperthermia
    • Piantelli M., Tatone D., Castrilli G., et al. Quercetin and tamoxifen sensitize human melanoma cells to hyperthermia. Melanoma Res 11 (2001) 469-47676
    • (2001) Melanoma Res , vol.11 , pp. 469-47676
    • Piantelli, M.1    Tatone, D.2    Castrilli, G.3
  • 14
    • 11244304394 scopus 로고    scopus 로고
    • Docosahexaenoic acid enhances the susceptibility of human colorectal cancer cells to 5-fluorouracil
    • Calviello G., Di Nicuolo F., Serini S., et al. Docosahexaenoic acid enhances the susceptibility of human colorectal cancer cells to 5-fluorouracil. Cancer Chemother Pharmacol 55 (2005) 12-20
    • (2005) Cancer Chemother Pharmacol , vol.55 , pp. 12-20
    • Calviello, G.1    Di Nicuolo, F.2    Serini, S.3
  • 15
    • 34547106018 scopus 로고    scopus 로고
    • Understanding multiple myeloma pathogenesis in the bone marrow to identify new therapeutic targets
    • Hideshima T., Mitsiades C., Tonon G., Richardson P.G., and Anderson K.C. Understanding multiple myeloma pathogenesis in the bone marrow to identify new therapeutic targets. Nat Rev Cancer 7 (2007) 585-59898
    • (2007) Nat Rev Cancer , vol.7 , pp. 585-59898
    • Hideshima, T.1    Mitsiades, C.2    Tonon, G.3    Richardson, P.G.4    Anderson, K.C.5
  • 16
    • 0030610687 scopus 로고    scopus 로고
    • 3) in the treatment of acute promyelocytic leukemia (APL). II. Clinical efficacy and pharmacokinetics in relapsed patients
    • 3) in the treatment of acute promyelocytic leukemia (APL). II. Clinical efficacy and pharmacokinetics in relapsed patients. Blood 89 (1997) 3354-336060
    • (1997) Blood , vol.89 , pp. 3354-336060
    • Shen, Z.X.1    Chen, G.Q.2    Ni, J.H.3
  • 17
    • 0037111832 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies
    • Orlowski R.Z., Stinchcombe T.E., Mitchell B.S., et al. Phase I trial of the proteasome inhibitor PS-341 in patients with refractory hematologic malignancies. J Clin Oncol 20 (2002) 4420-44277
    • (2002) J Clin Oncol , vol.20 , pp. 4420-44277
    • Orlowski, R.Z.1    Stinchcombe, T.E.2    Mitchell, B.S.3
  • 18
    • 33645825623 scopus 로고    scopus 로고
    • Raloxifene-induced myeloma cell apoptosis: a study of nuclear factor-kappaB inhibition and gene expression signature
    • Olivier S., Close P., Castermans E., et al. Raloxifene-induced myeloma cell apoptosis: a study of nuclear factor-kappaB inhibition and gene expression signature. Mol Pharmacol 69 (2006) 1615-162323
    • (2006) Mol Pharmacol , vol.69 , pp. 1615-162323
    • Olivier, S.1    Close, P.2    Castermans, E.3
  • 19
    • 34548850030 scopus 로고    scopus 로고
    • Low-dose arsenic trioxide sensitizes glucocorticoid-resistant acute lymphoblastic leukemia cells to dexamethasone via an Akt-dependent pathway
    • Bornhauser B.C., Bonapace L., Lindholm D., et al. Low-dose arsenic trioxide sensitizes glucocorticoid-resistant acute lymphoblastic leukemia cells to dexamethasone via an Akt-dependent pathway. Blood 110 (2007) 2084-209191
    • (2007) Blood , vol.110 , pp. 2084-209191
    • Bornhauser, B.C.1    Bonapace, L.2    Lindholm, D.3
  • 20
    • 34250744640 scopus 로고    scopus 로고
    • Arsenic trioxide and proteasome inhibitor bortezomib synergistically induce apoptosis in leukemic cells: the role of protein kinase Cdelta
    • Yan H., Wang Y.C., Li D., et al. Arsenic trioxide and proteasome inhibitor bortezomib synergistically induce apoptosis in leukemic cells: the role of protein kinase Cdelta. Leukemia 21 (2007) 1488-149595
    • (2007) Leukemia , vol.21 , pp. 1488-149595
    • Yan, H.1    Wang, Y.C.2    Li, D.3
  • 21
    • 0038719671 scopus 로고    scopus 로고
    • JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells
    • Chauhan D., Li G., Hideshima T., et al. JNK-dependent release of mitochondrial protein, Smac, during apoptosis in multiple myeloma (MM) cells. J Biol Chem 278 (2003) 17593-175966
    • (2003) J Biol Chem , vol.278 , pp. 17593-175966
    • Chauhan, D.1    Li, G.2    Hideshima, T.3
  • 22
    • 0037441760 scopus 로고    scopus 로고
    • Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341
    • Hideshima T., Mitsiades C., Akiyama M., et al. Molecular mechanisms mediating antimyeloma activity of proteasome inhibitor PS-341. Blood 101 (2003) 1530-15344
    • (2003) Blood , vol.101 , pp. 1530-15344
    • Hideshima, T.1    Mitsiades, C.2    Akiyama, M.3
  • 23
    • 0034644522 scopus 로고    scopus 로고
    • Signal transduction by the JNK group of MAP kinases
    • Davis R.J. Signal transduction by the JNK group of MAP kinases. Cell 103 (2000) 239-25252
    • (2000) Cell , vol.103 , pp. 239-25252
    • Davis, R.J.1
  • 25
    • 33746178172 scopus 로고    scopus 로고
    • Role of the p38 mitogen-activated protein kinase pathway in the generation of arsenic trioxide-dependent cellular responses
    • Giafis N., Katsoulidis E., Sassano A., et al. Role of the p38 mitogen-activated protein kinase pathway in the generation of arsenic trioxide-dependent cellular responses. Cancer Res 66 (2006) 6763-677171
    • (2006) Cancer Res , vol.66 , pp. 6763-677171
    • Giafis, N.1    Katsoulidis, E.2    Sassano, A.3
  • 26
    • 0036782706 scopus 로고    scopus 로고
    • Transcription factors as targets for cancer therapy
    • Darnell Jr. J.E. Transcription factors as targets for cancer therapy. Nat Rev Cancer 2 (2002) 740-7499
    • (2002) Nat Rev Cancer , vol.2 , pp. 740-7499
    • Darnell Jr., J.E.1
  • 28
    • 34548693457 scopus 로고    scopus 로고
    • Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation and chemosensitization of human multiple myeloma cells
    • Pathak A.K., Bhutani M., Nair A.S., et al. Ursolic acid inhibits STAT3 activation pathway leading to suppression of proliferation and chemosensitization of human multiple myeloma cells. Mol Cancer Res 5 (2007) 943-95555
    • (2007) Mol Cancer Res , vol.5 , pp. 943-95555
    • Pathak, A.K.1    Bhutani, M.2    Nair, A.S.3
  • 29
    • 22044440019 scopus 로고    scopus 로고
    • Reduction in BCL-2 levels by 26S proteasome inhibition with bortezomib is associated with induction of apoptosis in small cell lung cancer
    • Mortenson M.M., Schlieman M.G., Virudachalam S., et al. Reduction in BCL-2 levels by 26S proteasome inhibition with bortezomib is associated with induction of apoptosis in small cell lung cancer. Lung Cancer 49 (2005) 163-17070
    • (2005) Lung Cancer , vol.49 , pp. 163-17070
    • Mortenson, M.M.1    Schlieman, M.G.2    Virudachalam, S.3
  • 30
    • 21244474683 scopus 로고    scopus 로고
    • Targeting BCL-2 overexpression in various human malignancies through NF-kappaB inhibition by the proteasome inhibitor bortezomib
    • Fahy B.N., Schlieman M.G., Mortenson M.M., Virudachalam S., and Bold R.J. Targeting BCL-2 overexpression in various human malignancies through NF-kappaB inhibition by the proteasome inhibitor bortezomib. Cancer Chemother Pharmacol 56 (2005) 46-54
    • (2005) Cancer Chemother Pharmacol , vol.56 , pp. 46-54
    • Fahy, B.N.1    Schlieman, M.G.2    Mortenson, M.M.3    Virudachalam, S.4    Bold, R.J.5
  • 31
    • 39749136204 scopus 로고    scopus 로고
    • BCL-2 family regulation by the 20S proteasome inhibitor bortezomib
    • Fennell D.A., Chacko A., and Mutti L. BCL-2 family regulation by the 20S proteasome inhibitor bortezomib. Oncogene 27 (2008) 1189-119797
    • (2008) Oncogene , vol.27 , pp. 1189-119797
    • Fennell, D.A.1    Chacko, A.2    Mutti, L.3
  • 32
    • 55249093243 scopus 로고    scopus 로고
    • Targeting MEK/MAPK signal transduction module potentiates ATO-induced apoptosis in multiple myeloma cells through multiple signaling pathways
    • Lunghi P., Giuliani N., and Mazzera L. Targeting MEK/MAPK signal transduction module potentiates ATO-induced apoptosis in multiple myeloma cells through multiple signaling pathways. Blood (2008)
    • (2008) Blood
    • Lunghi, P.1    Giuliani, N.2    Mazzera, L.3
  • 33
    • 0035851204 scopus 로고    scopus 로고
    • BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons
    • Harris C.A., and Johnson Jr. E.M. BH3-only Bcl-2 family members are coordinately regulated by the JNK pathway and require Bax to induce apoptosis in neurons. J Biol Chem 276 (2001) 37754-3776060
    • (2001) J Biol Chem , vol.276 , pp. 37754-3776060
    • Harris, C.A.1    Johnson Jr., E.M.2
  • 34
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked
    • Yang J., Liu X., Bhalla K., et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275 (1997) 1129-113232
    • (1997) Science , vol.275 , pp. 1129-113232
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 35
    • 8244262438 scopus 로고    scopus 로고
    • A recombinant adenovirus expressing p27Kip1 induces cell cycle arrest and loss of cyclin-Cdk activity in human breast cancer cells
    • Craig C., Wersto R., Kim M., et al. A recombinant adenovirus expressing p27Kip1 induces cell cycle arrest and loss of cyclin-Cdk activity in human breast cancer cells. Oncogene 14 (1997) 2283-22899
    • (1997) Oncogene , vol.14 , pp. 2283-22899
    • Craig, C.1    Wersto, R.2    Kim, M.3
  • 36
    • 0035128134 scopus 로고    scopus 로고
    • Suppression of mammary carcinoma growth in vitro and in vivo by inducible expression of the Cdk inhibitor p21
    • Shibata M.A., Yoshidome K., Shibata E., Jorcyk C.L., and Green J.E. Suppression of mammary carcinoma growth in vitro and in vivo by inducible expression of the Cdk inhibitor p21. Cancer Gene Ther 8 (2001) 23-35
    • (2001) Cancer Gene Ther , vol.8 , pp. 23-35
    • Shibata, M.A.1    Yoshidome, K.2    Shibata, E.3    Jorcyk, C.L.4    Green, J.E.5
  • 37
    • 26244463218 scopus 로고    scopus 로고
    • Constitutive activation of JAK3/STAT3 in colon carcinoma tumors and cell lines: inhibition of JAK3/STAT3 signaling induces apoptosis and cell cycle arrest of colon carcinoma cells
    • Lin Q., Lai R., Chirieac L.R., et al. Constitutive activation of JAK3/STAT3 in colon carcinoma tumors and cell lines: inhibition of JAK3/STAT3 signaling induces apoptosis and cell cycle arrest of colon carcinoma cells. Am J Pathol 167 (2005) 969-98080
    • (2005) Am J Pathol , vol.167 , pp. 969-98080
    • Lin, Q.1    Lai, R.2    Chirieac, L.R.3
  • 38
    • 40749156343 scopus 로고    scopus 로고
    • Combination of atorvastatin and celecoxib synergistically induces cell cycle arrest and apoptosis in colon cancer cells
    • Xiao H., Zhang Q., Lin Y., Reddy B.S., and Yang C.S. Combination of atorvastatin and celecoxib synergistically induces cell cycle arrest and apoptosis in colon cancer cells. Int J Cancer 122 (2008) 2115-212424
    • (2008) Int J Cancer , vol.122 , pp. 2115-212424
    • Xiao, H.1    Zhang, Q.2    Lin, Y.3    Reddy, B.S.4    Yang, C.S.5
  • 39
    • 33744494283 scopus 로고    scopus 로고
    • Inhibition of p38alpha MAPK enhances proteasome inhibitor-induced apoptosis of myeloma cells by modulating Hsp27, Bcl-X(L), Mcl-1 and p53 levels in vitro and inhibits tumor growth in vivo
    • Navas T.A., Nguyen A.N., Hideshima T., et al. Inhibition of p38alpha MAPK enhances proteasome inhibitor-induced apoptosis of myeloma cells by modulating Hsp27, Bcl-X(L), Mcl-1 and p53 levels in vitro and inhibits tumor growth in vivo. Leukemia 20 (2006) 1017-102727
    • (2006) Leukemia , vol.20 , pp. 1017-102727
    • Navas, T.A.1    Nguyen, A.N.2    Hideshima, T.3
  • 40
    • 0037246247 scopus 로고    scopus 로고
    • On the role of Hsp27 in regulating apoptosis
    • Concannon C.G., Gorman A.M., and Samali A. On the role of Hsp27 in regulating apoptosis. Apoptosis 8 (2003) 61-70
    • (2003) Apoptosis , vol.8 , pp. 61-70
    • Concannon, C.G.1    Gorman, A.M.2    Samali, A.3
  • 41
    • 0033944777 scopus 로고    scopus 로고
    • Heat shock proteins-modulators of apoptosis in tumour cells
    • Creagh E.M., Sheehan D., and Cotter T.G. Heat shock proteins-modulators of apoptosis in tumour cells. Leukemia 14 (2000) 1161-117373
    • (2000) Leukemia , vol.14 , pp. 1161-117373
    • Creagh, E.M.1    Sheehan, D.2    Cotter, T.G.3
  • 42
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J., Lambert H., Gingras-Breton G., Lavoie J.N., Huot J., and Landry J. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 110 Pt 3 (1997) 357-36868
    • (1997) J Cell Sci , vol.110 , Issue.PART 3 , pp. 357-36868
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 43
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J., Houle F., Marceau F., and Landry J. Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ Res 80 (1997) 383-39292
    • (1997) Circ Res , vol.80 , pp. 383-39292
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 44
    • 0029365005 scopus 로고
    • Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat-shock protein 27
    • Landry J., and Huot J. Modulation of actin dynamics during stress and physiological stimulation by a signaling pathway involving p38 MAP kinase and heat-shock protein 27. Biochem Cell Biol 73 (1995) 703-7077
    • (1995) Biochem Cell Biol , vol.73 , pp. 703-7077
    • Landry, J.1    Huot, J.2
  • 45
    • 0242496212 scopus 로고    scopus 로고
    • Molecular sequelae of proteasome inhibition in human multiple myeloma cells
    • Mitsiades N., Mitsiades C.S., Poulaki V., et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA 99 (2002) 14374-143799
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14374-143799
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 46
    • 0032526694 scopus 로고    scopus 로고
    • PRAK, a novel protein kinase regulated by the p38 MAP kinase
    • New L., Jiang Y., Zhao M., et al. PRAK, a novel protein kinase regulated by the p38 MAP kinase. EMBO J 17 (1998) 3372-338484
    • (1998) EMBO J , vol.17 , pp. 3372-338484
    • New, L.1    Jiang, Y.2    Zhao, M.3
  • 47
    • 0034282116 scopus 로고    scopus 로고
    • Heat-shock proteins as death determinants
    • Xanthoudakis S., and Nicholson D.W. Heat-shock proteins as death determinants. Nat Cell Biol 2 (2000) E163-E165
    • (2000) Nat Cell Biol , vol.2
    • Xanthoudakis, S.1    Nicholson, D.W.2
  • 48
    • 32944454483 scopus 로고    scopus 로고
    • Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors
    • Zaarur N., Gabai V.L., Porco Jr. J.A., Calderwood S., and Sherman M.Y. Targeting heat shock response to sensitize cancer cells to proteasome and Hsp90 inhibitors. Cancer Res 66 (2006) 1783-179191
    • (2006) Cancer Res , vol.66 , pp. 1783-179191
    • Zaarur, N.1    Gabai, V.L.2    Porco Jr., J.A.3    Calderwood, S.4    Sherman, M.Y.5
  • 49
    • 21544434331 scopus 로고    scopus 로고
    • p38 MAP kinase inhibitors: many are made, but few are chosen
    • Dominguez C., Powers D.A., and Tamayo N. p38 MAP kinase inhibitors: many are made, but few are chosen. Curr Opin Drug Discov Devel 8 (2005) 421-43030
    • (2005) Curr Opin Drug Discov Devel , vol.8 , pp. 421-43030
    • Dominguez, C.1    Powers, D.A.2    Tamayo, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.