메뉴 건너뛰기




Volumn 1, Issue 2, 2006, Pages 91-116

Proteasome inhibitors and modulators of heat shock protein function

Author keywords

Bortezomib; HSP90 inhibitors; Multiple myeloma; Non Hodgkin's lymphoma; p38 inhibitors; Ubiquitin proteasome pathway

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ALKYLATING AGENT; ALPHA',BETA' EPOXYKETONE; ANTHRACYCLINE DERIVATIVE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CALPAIN; CAMPTOTHECIN; CASPASE INHIBITOR; CHYMOTRYPSIN; EPIGALLOCATECHIN GALLATE; EPOXOMICIN; GREEN TEA EXTRACT; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90 INHIBITOR; HISTONE DEACETYLASE INHIBITOR; IRINOTECAN; KETONE DERIVATIVE; KNK 437; LACTACYSTIN; LACTACYSTIN BETA LACTONE; LEUPEPTIN; MG 115; NPI 0052; PLATINUM DERIVATIVE; POLYPHENOL DERIVATIVE; PROTEASOME INHIBITOR; SALINOSPORAMIDE A; SCIO 469; TAXANE DERIVATIVE; TRIPEPTIDE DERIVATIVE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; UNINDEXED DRUG; VINCA ALKALOID; VORINOSTAT;

EID: 33746542134     PISSN: 1872115X     EISSN: 1872115X     Source Type: Journal    
DOI: 10.1016/j.uct.2006.05.008     Document Type: Review
Times cited : (7)

References (243)
  • 1
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution
    • Lowe J., Stock D., Jap B., Zwickl P., Baumeister W., and Huber R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution. Science 268 (1995) 533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 2
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 Å resolution
    • Groll M., Ditzel L., Lowe J., et al. Structure of 20S proteasome from yeast at 2.4 Å resolution. Nature 386 (1997) 463-471
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3
  • 3
    • 0036103598 scopus 로고    scopus 로고
    • The structure of the mammalian 20S proteasome at 2.75 Å resolution
    • Unno M., Mizushima T., Morimoto Y., et al. The structure of the mammalian 20S proteasome at 2.75 Å resolution. Structure (Camb) 10 (2002) 609-618
    • (2002) Structure (Camb) , vol.10 , pp. 609-618
    • Unno, M.1    Mizushima, T.2    Morimoto, Y.3
  • 4
    • 0024370674 scopus 로고
    • The multicatalytic proteinase. Multiple proteolytic activities
    • Rivett A.J. The multicatalytic proteinase. Multiple proteolytic activities. J Biol Chem 264 (1989) 12215-12219
    • (1989) J Biol Chem , vol.264 , pp. 12215-12219
    • Rivett, A.J.1
  • 5
    • 0030595329 scopus 로고    scopus 로고
    • Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly
    • Chen P., and Hochstrasser M. Autocatalytic subunit processing couples active site formation in the 20S proteasome to completion of assembly. Cell 86 (1996) 961-972
    • (1996) Cell , vol.86 , pp. 961-972
    • Chen, P.1    Hochstrasser, M.2
  • 6
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev A.F., Akopian T.N., Castillo V., and Goldberg A.L. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell 4 (1999) 395-402
    • (1999) Mol Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 7
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • Orlowski M., Cardozo C., and Michaud C. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 32 (1993) 1563-1572
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 8
    • 0033756543 scopus 로고    scopus 로고
    • Opening doors into the proteasome
    • Pickart C.M., and VanDemark A.P. Opening doors into the proteasome. Nat Struct Biol 7 (2000) 999-1001
    • (2000) Nat Struct Biol , vol.7 , pp. 999-1001
    • Pickart, C.M.1    VanDemark, A.P.2
  • 9
    • 0033766480 scopus 로고    scopus 로고
    • A gated channel into the proteasome core particle
    • Groll M., Bajorek M., Kohler A., et al. A gated channel into the proteasome core particle. Nat Struct Biol 7 (2000) 1062-1067
    • (2000) Nat Struct Biol , vol.7 , pp. 1062-1067
    • Groll, M.1    Bajorek, M.2    Kohler, A.3
  • 10
    • 1042302128 scopus 로고    scopus 로고
    • Potential roles of protein oxidation and the immunoproteasome in MHC class I antigen presentation: the 'PrOxI' hypothesis
    • Teoh C.Y., and Davies K.J. Potential roles of protein oxidation and the immunoproteasome in MHC class I antigen presentation: the 'PrOxI' hypothesis. Arch Biochem Biophys 423 (2004) 88-96
    • (2004) Arch Biochem Biophys , vol.423 , pp. 88-96
    • Teoh, C.Y.1    Davies, K.J.2
  • 11
    • 0028241569 scopus 로고
    • Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex
    • Fruh K., Gossen M., Wang K., Bujard H., Peterson P.A., and Yang Y. Displacement of housekeeping proteasome subunits by MHC-encoded LMPs: a newly discovered mechanism for modulating the multicatalytic proteinase complex. EMBO J 13 (1994) 3236-3244
    • (1994) EMBO J , vol.13 , pp. 3236-3244
    • Fruh, K.1    Gossen, M.2    Wang, K.3    Bujard, H.4    Peterson, P.A.5    Yang, Y.6
  • 12
    • 2442515965 scopus 로고    scopus 로고
    • Proteasome function in antigen presentation: immunoproteasome complexes, peptide production, and interactions with viral proteins
    • Rivett A.J., and Hearn A.R. Proteasome function in antigen presentation: immunoproteasome complexes, peptide production, and interactions with viral proteins. Curr Protein Pept Sci 5 (2004) 153-161
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 153-161
    • Rivett, A.J.1    Hearn, A.R.2
  • 13
    • 0032539909 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death
    • Ciechanover A., and Schwartz A.L. The ubiquitin-proteasome pathway: the complexity and myriad functions of proteins death. Proc Natl Acad Sci USA 95 (1998) 2727-2730
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2727-2730
    • Ciechanover, A.1    Schwartz, A.L.2
  • 14
  • 15
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68 (1999) 1015-1068
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 16
    • 9644289334 scopus 로고    scopus 로고
    • The proteasome and MHC class I antigen processing
    • Kloetzel P.M. The proteasome and MHC class I antigen processing. Biochim Biophys Acta 1695 (2004) 225-233
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 225-233
    • Kloetzel, P.M.1
  • 18
    • 0033996762 scopus 로고    scopus 로고
    • The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signaling
    • Karin M., and Delhase M. The I kappa B kinase (IKK) and NF-kappa B: key elements of proinflammatory signaling. Semin Immunol 12 (2000) 85-98
    • (2000) Semin Immunol , vol.12 , pp. 85-98
    • Karin, M.1    Delhase, M.2
  • 19
    • 1542718628 scopus 로고    scopus 로고
    • Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy, a comprehensive review
    • Sreedhar A.S., and Csermely P. Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy, a comprehensive review. Pharmacol Ther 101 (2004) 227-257
    • (2004) Pharmacol Ther , vol.101 , pp. 227-257
    • Sreedhar, A.S.1    Csermely, P.2
  • 21
    • 0642377466 scopus 로고    scopus 로고
    • More than folding: localized functions of cytosolic chaperones
    • Young J.C., Barral J.M., and Ulrich Hartl F. More than folding: localized functions of cytosolic chaperones. Trends Biochem Sci 28 (2003) 541-547
    • (2003) Trends Biochem Sci , vol.28 , pp. 541-547
    • Young, J.C.1    Barral, J.M.2    Ulrich Hartl, F.3
  • 22
    • 15944373162 scopus 로고    scopus 로고
    • Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo
    • Tang D., Khaleque M.A., Jones E.L., et al. Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo. Cell Stress Chaperones 10 (2005) 46-58
    • (2005) Cell Stress Chaperones , vol.10 , pp. 46-58
    • Tang, D.1    Khaleque, M.A.2    Jones, E.L.3
  • 23
    • 20844437570 scopus 로고    scopus 로고
    • Proteome-wide analysis of head and neck squamous cell carcinomas using laser-capture microdissection and tandem mass spectrometry
    • Baker H., Patel V., Molinolo A.A., et al. Proteome-wide analysis of head and neck squamous cell carcinomas using laser-capture microdissection and tandem mass spectrometry. Oral Oncol 41 (2005) 183-199
    • (2005) Oral Oncol , vol.41 , pp. 183-199
    • Baker, H.1    Patel, V.2    Molinolo, A.A.3
  • 24
    • 0030967506 scopus 로고    scopus 로고
    • Specific expression of HSP-27 in human tumor cell lines in vitro
    • Morino M., Tsuzuki T., Ishikawa Y., et al. Specific expression of HSP-27 in human tumor cell lines in vitro. In Vivo 11 (1997) 179-184
    • (1997) In Vivo , vol.11 , pp. 179-184
    • Morino, M.1    Tsuzuki, T.2    Ishikawa, Y.3
  • 25
    • 23644449396 scopus 로고    scopus 로고
    • Heat shock proteins in renal cell carcinomas
    • Lichtenfels R., Seliger B., and Atkins D. Heat shock proteins in renal cell carcinomas. Contrib Nephrol 148 (2005) 35-56
    • (2005) Contrib Nephrol , vol.148 , pp. 35-56
    • Lichtenfels, R.1    Seliger, B.2    Atkins, D.3
  • 26
    • 0029179962 scopus 로고
    • Distribution of HSP-27 and HER-2/neu in in situ and invasive ductal breast carcinomas
    • Storm F.K., Gilchrist K.W., Warner T.F., and Mahvi D.M. Distribution of HSP-27 and HER-2/neu in in situ and invasive ductal breast carcinomas. Ann Surg Oncol 2 (1995) 43-48
    • (1995) Ann Surg Oncol , vol.2 , pp. 43-48
    • Storm, F.K.1    Gilchrist, K.W.2    Warner, T.F.3    Mahvi, D.M.4
  • 27
    • 0028970484 scopus 로고
    • Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix
    • Ralhan R., and Kaur J. Differential expression of Mr 70,000 heat shock protein in normal, premalignant, and malignant human uterine cervix. Clin Cancer Res 1 (1995) 1217-1222
    • (1995) Clin Cancer Res , vol.1 , pp. 1217-1222
    • Ralhan, R.1    Kaur, J.2
  • 28
    • 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) 383-392
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 29
    • 0037086661 scopus 로고    scopus 로고
    • Heat-shock protein 70 attenuates nitric oxide-induced apoptosis in RAW macrophages by preventing cytochrome c release
    • Klein S.D., and Brune B. Heat-shock protein 70 attenuates nitric oxide-induced apoptosis in RAW macrophages by preventing cytochrome c release. Biochem J 362 (2002) 635-641
    • (2002) Biochem J , vol.362 , pp. 635-641
    • Klein, S.D.1    Brune, B.2
  • 30
    • 0034682748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation
    • Li C.Y., Lee J.S., Ko Y.G., Kim J.I., and Seo J.S. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J Biol Chem 275 (2000) 25665-25671
    • (2000) J Biol Chem , vol.275 , pp. 25665-25671
    • Li, C.Y.1    Lee, J.S.2    Ko, Y.G.3    Kim, J.I.4    Seo, J.S.5
  • 31
    • 21644489785 scopus 로고    scopus 로고
    • Up-regulation of the association between heat shock protein 90 and endothelial nitric oxide synthase prevents high glucose-induced apoptosis in human endothelial cells
    • Lin L.Y., Lin C.Y., Ho F.M., and Liau C.S. Up-regulation of the association between heat shock protein 90 and endothelial nitric oxide synthase prevents high glucose-induced apoptosis in human endothelial cells. J Cell Biochem 94 (2005) 194-201
    • (2005) J Cell Biochem , vol.94 , pp. 194-201
    • Lin, L.Y.1    Lin, C.Y.2    Ho, F.M.3    Liau, C.S.4
  • 33
    • 0027366354 scopus 로고
    • The small heat shock protein HSP-27 is correlated with growth and drug resistance in human breast cancer cell lines
    • Oesterreich S., Weng C.N., Qiu M., Hilsenbeck S.G., Osborne C.K., and Fuqua S.A. The small heat shock protein HSP-27 is correlated with growth and drug resistance in human breast cancer cell lines. Cancer Res 53 (1993) 4443-4448
    • (1993) Cancer Res , vol.53 , pp. 4443-4448
    • Oesterreich, S.1    Weng, C.N.2    Qiu, M.3    Hilsenbeck, S.G.4    Osborne, C.K.5    Fuqua, S.A.6
  • 34
    • 0032033123 scopus 로고    scopus 로고
    • Cell surface expression of 70 kDa heat shock protein in human oral dysplasia and squamous cell carcinoma: correlation with clinicopathological features
    • Kaur J., Das S.N., Srivastava A., and Ralhan R. Cell surface expression of 70 kDa heat shock protein in human oral dysplasia and squamous cell carcinoma: correlation with clinicopathological features. Oral Oncol 34 (1998) 93-98
    • (1998) Oral Oncol , vol.34 , pp. 93-98
    • Kaur, J.1    Das, S.N.2    Srivastava, A.3    Ralhan, R.4
  • 35
    • 0031733457 scopus 로고    scopus 로고
    • Prognostic significance of heat shock proteins HSP-70 and HSP-90 in endometrial carcinomas
    • Nanbu K., Konishi I., Mandai M., et al. Prognostic significance of heat shock proteins HSP-70 and HSP-90 in endometrial carcinomas. Cancer Detect Prev 22 (1998) 549-555
    • (1998) Cancer Detect Prev , vol.22 , pp. 549-555
    • Nanbu, K.1    Konishi, I.2    Mandai, M.3
  • 36
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman B.C., and Yamamoto K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296 (2002) 2232-2235
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 37
    • 0037853218 scopus 로고    scopus 로고
    • ErbB2 degradation mediated by the co-chaperone protein CHIP
    • Zhou P., Fernandes N., Dodge I.L., et al. ErbB2 degradation mediated by the co-chaperone protein CHIP. J Biol Chem 278 (2003) 13829-13837
    • (2003) J Biol Chem , vol.278 , pp. 13829-13837
    • Zhou, P.1    Fernandes, N.2    Dodge, I.L.3
  • 38
    • 0035899897 scopus 로고    scopus 로고
    • Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
    • Demand J., Alberti S., Patterson C., and Hohfeld J. Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr Biol 11 (2001) 1569-1577
    • (2001) Curr Biol , vol.11 , pp. 1569-1577
    • Demand, J.1    Alberti, S.2    Patterson, C.3    Hohfeld, J.4
  • 39
    • 0035142877 scopus 로고    scopus 로고
    • The HSC-70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham G.C., Patterson C., Zhang W., Younger J.M., and Cyr D.M. The HSC-70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3 (2001) 100-105
    • (2001) Nat Cell Biol , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 40
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., et al. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol 19 (1999) 4535-4545
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3
  • 41
    • 0344039806 scopus 로고    scopus 로고
    • GRP-E-like regulation of the HSC-70 chaperone by the anti-apoptotic protein BAG-1
    • Hohfeld J., and Jentsch S. GRP-E-like regulation of the HSC-70 chaperone by the anti-apoptotic protein BAG-1. EMBO J 16 (1997) 6209-6216
    • (1997) EMBO J , vol.16 , pp. 6209-6216
    • Hohfeld, J.1    Jentsch, S.2
  • 42
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/HSC-70 complex: convergent functional evolution of HSP-70 nucleotide exchange factors
    • Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U., and Moarefi I. Structure of a Bag/HSC-70 complex: convergent functional evolution of HSP-70 nucleotide exchange factors. Science 291 (2001) 1553-1557
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 43
    • 0039172708 scopus 로고    scopus 로고
    • The ubiquitin-related BAG-1 provides a link between the molecular chaperones HSC-70/HSP-70 and the proteasome
    • Luders J., Demand J., and Hohfeld J. The ubiquitin-related BAG-1 provides a link between the molecular chaperones HSC-70/HSP-70 and the proteasome. J Biol Chem 275 (2000) 4613-4617
    • (2000) J Biol Chem , vol.275 , pp. 4613-4617
    • Luders, J.1    Demand, J.2    Hohfeld, J.3
  • 44
    • 2942716692 scopus 로고    scopus 로고
    • Functional proteomic screens reveal an essential extracellular role for HSP-90 alpha in cancer cell invasiveness
    • Eustace B.K., Sakurai T., Stewart J.K., et al. Functional proteomic screens reveal an essential extracellular role for HSP-90 alpha in cancer cell invasiveness. Nat Cell Biol 6 (2004) 507-514
    • (2004) Nat Cell Biol , vol.6 , pp. 507-514
    • Eustace, B.K.1    Sakurai, T.2    Stewart, J.K.3
  • 45
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP-90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation
    • Whitesell L., Mimnaugh E.G., De Costa B., Myers C.E., and Neckers L.M. Inhibition of heat shock protein HSP-90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc Natl Acad Sci USA 91 (1994) 8324-8328
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De Costa, B.3    Myers, C.E.4    Neckers, L.M.5
  • 46
    • 0029737509 scopus 로고    scopus 로고
    • Mutant conformation of p53 translated in vitro or in vivo requires functional HSP-90
    • Blagosklonny M.V., Toretsky J., Bohen S., and Neckers L. Mutant conformation of p53 translated in vitro or in vivo requires functional HSP-90. Proc Natl Acad Sci USA 93 (1996) 8379-8383
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8379-8383
    • Blagosklonny, M.V.1    Toretsky, J.2    Bohen, S.3    Neckers, L.4
  • 47
    • 0026786503 scopus 로고
    • Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex
    • Vinitsky A., Michaud C., Powers J.C., and Orlowski M. Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31 (1992) 9421-9428
    • (1992) Biochemistry , vol.31 , pp. 9421-9428
    • Vinitsky, A.1    Michaud, C.2    Powers, J.C.3    Orlowski, M.4
  • 48
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., and Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268 (1995) 726-731
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 49
    • 0026065338 scopus 로고
    • Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells
    • Omura S., Fujimoto T., Otoguro K., et al. Lactacystin, a novel microbial metabolite, induces neuritogenesis of neuroblastoma cells. J Antibiot (Tokyo) 44 (1991) 113-116
    • (1991) J Antibiot (Tokyo) , vol.44 , pp. 113-116
    • Omura, S.1    Fujimoto, T.2    Otoguro, K.3
  • 51
    • 15644363581 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells
    • Dick L.R., Cruikshank A.A., Destree A.T., et al. Mechanistic studies on the inactivation of the proteasome by lactacystin in cultured cells. J Biol Chem 272 (1997) 182-188
    • (1997) J Biol Chem , vol.272 , pp. 182-188
    • Dick, L.R.1    Cruikshank, A.A.2    Destree, A.T.3
  • 52
  • 53
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski R.Z., Eswara J.R., Lafond-Walker A., Grever M.R., Orlowski M., and Dang C.V. Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res 58 (1998) 4342-4348
    • (1998) Cancer Res , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3    Grever, M.R.4    Orlowski, M.5    Dang, C.V.6
  • 55
    • 0036735298 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model
    • LeBlanc R., Catley L.P., Hideshima T., et al. Proteasome inhibitor PS-341 inhibits human myeloma cell growth in vivo and prolongs survival in a murine model. Cancer Res 62 (2002) 4996-5000
    • (2002) Cancer Res , vol.62 , pp. 4996-5000
    • LeBlanc, R.1    Catley, L.P.2    Hideshima, T.3
  • 56
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: a novel class of potent and effective anti-tumor agents
    • Adams J., Palombella V.J., Sausville E.A., et al. Proteasome inhibitors: a novel class of potent and effective anti-tumor agents. Cancer Res 59 (1999) 2615-2622
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 57
    • 13844322559 scopus 로고    scopus 로고
    • Synthetic peracetate tea polyphenols as potent proteasome inhibitors and apoptosis inducers in human cancer cells
    • Kuhn D., Lam W.H., Kazi A., et al. Synthetic peracetate tea polyphenols as potent proteasome inhibitors and apoptosis inducers in human cancer cells. Front Biosci 10 (2005) 1010-1023
    • (2005) Front Biosci , vol.10 , pp. 1010-1023
    • Kuhn, D.1    Lam, W.H.2    Kazi, A.3
  • 60
    • 0037626648 scopus 로고    scopus 로고
    • Signal transduction pathways: targets for green and black tea polyphenols
    • Park A.M., and Dong Z. Signal transduction pathways: targets for green and black tea polyphenols. J Biochem Mol Biol 36 (2003) 66-77
    • (2003) J Biochem Mol Biol , vol.36 , pp. 66-77
    • Park, A.M.1    Dong, Z.2
  • 61
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam S., Smith D.M., and Dou Q.P. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 276 (2001) 13322-13330
    • (2001) J Biol Chem , vol.276 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 63
    • 4644290038 scopus 로고    scopus 로고
    • A potential prodrug for a green tea polyphenol proteasome inhibitor: evaluation of the peracetate ester of (-)-epigallocatechin gallate [(-)-EGCG]
    • Lam W.H., Kazi A., Kuhn D.J., et al. A potential prodrug for a green tea polyphenol proteasome inhibitor: evaluation of the peracetate ester of (-)-epigallocatechin gallate [(-)-EGCG]. Bioorg Med Chem 12 (2004) 5587-5593
    • (2004) Bioorg Med Chem , vol.12 , pp. 5587-5593
    • Lam, W.H.1    Kazi, A.2    Kuhn, D.J.3
  • 64
    • 23344435097 scopus 로고    scopus 로고
    • Tripeptide mimetics inhibit the 20S proteasome by covalent bonding to the active site threonines
    • Braun H.A., Umbreen S., Groll M., et al. Tripeptide mimetics inhibit the 20S proteasome by covalent bonding to the active site threonines. J Biol Chem 280 (2005) 28394-28401
    • (2005) J Biol Chem , vol.280 , pp. 28394-28401
    • Braun, H.A.1    Umbreen, S.2    Groll, M.3
  • 65
    • 0037455147 scopus 로고    scopus 로고
    • Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora
    • Feling R.H., Buchanan G.O., Mincer T.J., Kauffman C.A., Jensen P.R., and Fenical W. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew Chem Int Ed Engl 42 (2003) 355-357
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 355-357
    • Feling, R.H.1    Buchanan, G.O.2    Mincer, T.J.3    Kauffman, C.A.4    Jensen, P.R.5    Fenical, W.6
  • 66
    • 20044397059 scopus 로고    scopus 로고
    • Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor
    • Macherla V.R., Mitchell S.S., Manam R.R., et al. Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor. J Med Chem 48 (2005) 3684-3687
    • (2005) J Med Chem , vol.48 , pp. 3684-3687
    • Macherla, V.R.1    Mitchell, S.S.2    Manam, R.R.3
  • 67
    • 33846693828 scopus 로고    scopus 로고
    • Preclinical evaluation of a novel and orally active proteasome inhibitor as a therapy in relapsed/refractory multiple myeloma
    • [Abstract 3122]
    • Chauhan D., Catley L., Li G., et al. Preclinical evaluation of a novel and orally active proteasome inhibitor as a therapy in relapsed/refractory multiple myeloma. J Clin Oncol 23 (2005) 222s [Abstract 3122]
    • (2005) J Clin Oncol , vol.23
    • Chauhan, D.1    Catley, L.2    Li, G.3
  • 68
    • 0027050714 scopus 로고
    • Epoxomicin, a new anti-tumor agent of microbial origin
    • Hanada M., Sugawara K., Kaneta K., et al. Epoxomicin, a new anti-tumor agent of microbial origin. J Antibiot (Tokyo) 45 (1992) 1746-1752
    • (1992) J Antibiot (Tokyo) , vol.45 , pp. 1746-1752
    • Hanada, M.1    Sugawara, K.2    Kaneta, K.3
  • 69
    • 0030012069 scopus 로고    scopus 로고
    • Design and synthesis of novel protease inhibitors. Tripeptide [alpha]′,[beta]′-epoxyketones as nanomolar inactivators of the proteasome
    • Spaltenstein A., Leban J.J., Huang J.J., et al. Design and synthesis of novel protease inhibitors. Tripeptide [alpha]′,[beta]′-epoxyketones as nanomolar inactivators of the proteasome. Tetrahedron Lett 37 (1996) 1343-1346
    • (1996) Tetrahedron Lett , vol.37 , pp. 1343-1346
    • Spaltenstein, A.1    Leban, J.J.2    Huang, J.J.3
  • 70
    • 0033517032 scopus 로고    scopus 로고
    • Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology
    • Sin N., Kim K.B., Elofsson M., et al. Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg Med Chem Lett 9 (1999) 2283-2288
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 2283-2288
    • Sin, N.1    Kim, K.B.2    Elofsson, M.3
  • 71
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc Natl Acad Sci USA 96 (1999) 10403-10408
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 72
    • 0033230405 scopus 로고    scopus 로고
    • Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha′,beta′-epoxyketones
    • Elofsson M., Splittgerber U., Myung J., Mohan R., and Crews C.M. Towards subunit-specific proteasome inhibitors: synthesis and evaluation of peptide alpha′,beta′-epoxyketones. Chem Biol 6 (1999) 811-822
    • (1999) Chem Biol , vol.6 , pp. 811-822
    • Elofsson, M.1    Splittgerber, U.2    Myung, J.3    Mohan, R.4    Crews, C.M.5
  • 73
    • 0020674228 scopus 로고
    • Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex
    • Wilk S., and Orlowski M. Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex. J Neurochem 40 (1983) 842-849
    • (1983) J Neurochem , vol.40 , pp. 842-849
    • Wilk, S.1    Orlowski, M.2
  • 74
    • 0032539702 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids
    • Adams J., Behnke M., Chen S., et al. Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg Med Chem Lett 8 (1998) 333-338
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 333-338
    • Adams, J.1    Behnke, M.2    Chen, S.3
  • 75
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams J. Development of the proteasome inhibitor PS-341. Oncologist 7 (2002) 9-16
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 76
    • 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
  • 77
    • 0034192390 scopus 로고    scopus 로고
    • Inducible chemoresistance to 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) in colorectal cancer cells and a xenograft model is overcome by inhibition of nuclear factor-kappaB activation
    • Cusack Jr. J.C., Liu R., and Baldwin Jr. A.S. Inducible chemoresistance to 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) in colorectal cancer cells and a xenograft model is overcome by inhibition of nuclear factor-kappaB activation. Cancer Res 60 (2000) 2323-2330
    • (2000) Cancer Res , vol.60 , pp. 2323-2330
    • Cusack Jr., J.C.1    Liu, R.2    Baldwin Jr., A.S.3
  • 78
    • 0035341494 scopus 로고    scopus 로고
    • Enhancement of radiosensitivity by proteasome inhibition: implications for a role of NF-kappaB
    • Russo S.M., Tepper J.E., Baldwin Jr. A.S., et al. Enhancement of radiosensitivity by proteasome inhibition: implications for a role of NF-kappaB. Int J Radiat Oncol Biol Phys 50 (2001) 183-193
    • (2001) Int J Radiat Oncol Biol Phys , vol.50 , pp. 183-193
    • Russo, S.M.1    Tepper, J.E.2    Baldwin Jr., A.S.3
  • 79
    • 0037342894 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 markedly enhances sensitivity of multiple myeloma tumor cells to chemotherapeutic agents
    • Ma M.H., Yang H.H., Parker K., et al. The proteasome inhibitor PS-341 markedly enhances sensitivity of multiple myeloma tumor cells to chemotherapeutic agents. Clin Cancer Res 9 (2003) 1136-1144
    • (2003) Clin Cancer Res , vol.9 , pp. 1136-1144
    • Ma, M.H.1    Yang, H.H.2    Parker, K.3
  • 80
    • 0035725855 scopus 로고    scopus 로고
    • Analysis of expression of nuclear factor kappa B (NF-kappa B) in multiple myeloma: downregulation of NF-kappa B induces apoptosis
    • Ni H., Ergin M., Huang Q., et al. Analysis of expression of nuclear factor kappa B (NF-kappa B) in multiple myeloma: downregulation of NF-kappa B induces apoptosis. Br J Haematol 115 (2001) 279-286
    • (2001) Br J Haematol , vol.115 , pp. 279-286
    • Ni, H.1    Ergin, M.2    Huang, Q.3
  • 81
    • 0035300479 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells
    • Hideshima T., Richardson P., Chauhan D., et al. The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 61 (2001) 3071-3076
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 82
    • 2442429306 scopus 로고    scopus 로고
    • JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins
    • Tsuruta F., Sunayama J., Mori Y., et al. JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. EMBO J 23 (2004) 1889-1899
    • (2004) EMBO J , vol.23 , pp. 1889-1899
    • Tsuruta, F.1    Sunayama, J.2    Mori, Y.3
  • 83
    • 0037516876 scopus 로고    scopus 로고
    • Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells
    • Dewson G., Snowden R.T., Almond J.B., Dyer M.J., and Cohen G.M. Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells. Oncogene 22 (2003) 2643-2654
    • (2003) Oncogene , vol.22 , pp. 2643-2654
    • Dewson, G.1    Snowden, R.T.2    Almond, J.B.3    Dyer, M.J.4    Cohen, G.M.5
  • 84
    • 0037441760 scopus 로고    scopus 로고
    • Molecular mechanisms mediating anti-myeloma activity of proteasome inhibitor PS-341
    • Hideshima T., Mitsiades C., Akiyama M., et al. Molecular mechanisms mediating anti-myeloma activity of proteasome inhibitor PS-341. Blood 101 (2003) 1530-1534
    • (2003) Blood , vol.101 , pp. 1530-1534
    • Hideshima, T.1    Mitsiades, C.2    Akiyama, M.3
  • 85
    • 0032513215 scopus 로고    scopus 로고
    • Proteasome inhibitors activate stress kinases and induce HSP-72. Diverse effects on apoptosis
    • Meriin A.B., Gabai V.L., Yaglom J., Shifrin V.I., and Sherman M.Y. Proteasome inhibitors activate stress kinases and induce HSP-72. Diverse effects on apoptosis. J Biol Chem 273 (1998) 6373-6379
    • (1998) J Biol Chem , vol.273 , pp. 6373-6379
    • Meriin, A.B.1    Gabai, V.L.2    Yaglom, J.3    Shifrin, V.I.4    Sherman, M.Y.5
  • 86
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G. The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 3 (1997) 614-620
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 87
    • 0031465443 scopus 로고    scopus 로고
    • Conversion of Bcl-2 to a Bax-like death effector by caspases
    • Cheng E.H., Kirsch D.G., Clem R.J., et al. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science 278 (1997) 1966-1968
    • (1997) Science , vol.278 , pp. 1966-1968
    • Cheng, E.H.1    Kirsch, D.G.2    Clem, R.J.3
  • 90
    • 0032145442 scopus 로고    scopus 로고
    • "Loop" domain is necessary for taxol-induced mobility shift and phosphorylation of Bcl-2 as well as for inhibiting taxol-induced cytosolic accumulation of cytochrome c and apoptosis
    • Fang G., Chang B.S., Kim C.N., Perkins C., Thompson C.B., and Bhalla K.N. "Loop" domain is necessary for taxol-induced mobility shift and phosphorylation of Bcl-2 as well as for inhibiting taxol-induced cytosolic accumulation of cytochrome c and apoptosis. Cancer Res 58 (1998) 3202-3208
    • (1998) Cancer Res , vol.58 , pp. 3202-3208
    • Fang, G.1    Chang, B.S.2    Kim, C.N.3    Perkins, C.4    Thompson, C.B.5    Bhalla, K.N.6
  • 91
    • 0037427122 scopus 로고    scopus 로고
    • NF-kappaB transcription factor induces drug resistance through MDR1 expression in cancer cells
    • Bentires-Alj M., Barbu V., Fillet M., et al. NF-kappaB transcription factor induces drug resistance through MDR1 expression in cancer cells. Oncogene 22 (2003) 90-97
    • (2003) Oncogene , vol.22 , pp. 90-97
    • Bentires-Alj, M.1    Barbu, V.2    Fillet, M.3
  • 92
    • 0032862993 scopus 로고    scopus 로고
    • The human multidrug resistance P-glycoprotein is inactive when its maturation is inhibited: potential for a role in cancer chemotherapy
    • Loo T.W., and Clarke D.M. The human multidrug resistance P-glycoprotein is inactive when its maturation is inhibited: potential for a role in cancer chemotherapy. FASEB J 13 (1999) 1724-1732
    • (1999) FASEB J , vol.13 , pp. 1724-1732
    • Loo, T.W.1    Clarke, D.M.2
  • 94
    • 0037726036 scopus 로고    scopus 로고
    • Transcriptional repression of ErbB2 by histone deacetylase inhibitors detected by a genomically integrated ErbB2 promoter-reporting cell screen
    • Scott G.K., Marden C., Xu F., Kirk L., and Benz C.C. Transcriptional repression of ErbB2 by histone deacetylase inhibitors detected by a genomically integrated ErbB2 promoter-reporting cell screen. Mol Cancer Ther 1 (2002) 385-392
    • (2002) Mol Cancer Ther , vol.1 , pp. 385-392
    • Scott, G.K.1    Marden, C.2    Xu, F.3    Kirk, L.4    Benz, C.C.5
  • 95
    • 9144220841 scopus 로고    scopus 로고
    • Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications
    • Mitsiades C.S., Mitsiades N.S., McMullan C.J., et al. Transcriptional signature of histone deacetylase inhibition in multiple myeloma: biological and clinical implications. Proc Natl Acad Sci USA 101 (2004) 540-545
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 540-545
    • Mitsiades, C.S.1    Mitsiades, N.S.2    McMullan, C.J.3
  • 96
    • 0036681989 scopus 로고    scopus 로고
    • Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are anti-proliferative against human tumors
    • Fournel M., Trachy-Bourget M.C., Yan P.T., et al. Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are anti-proliferative against human tumors. Cancer Res 62 (2002) 4325-4330
    • (2002) Cancer Res , vol.62 , pp. 4325-4330
    • Fournel, M.1    Trachy-Bourget, M.C.2    Yan, P.T.3
  • 97
    • 18544367699 scopus 로고    scopus 로고
    • Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells
    • Kwon S.H., Ahn S.H., Kim Y.K., et al. Apicidin, a histone deacetylase inhibitor, induces apoptosis and Fas/Fas ligand expression in human acute promyelocytic leukemia cells. J Biol Chem 277 (2002) 2073-2080
    • (2002) J Biol Chem , vol.277 , pp. 2073-2080
    • Kwon, S.H.1    Ahn, S.H.2    Kim, Y.K.3
  • 98
    • 4444239987 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberic bishydroxamate regulates the expression of multiple apoptotic mediators and induces mitochondria-dependent apoptosis of melanoma cells
    • Zhang X.D., Gillespie S.K., Borrow J.M., and Hersey P. The histone deacetylase inhibitor suberic bishydroxamate regulates the expression of multiple apoptotic mediators and induces mitochondria-dependent apoptosis of melanoma cells. Mol Cancer Ther 3 (2004) 425-435
    • (2004) Mol Cancer Ther , vol.3 , pp. 425-435
    • Zhang, X.D.1    Gillespie, S.K.2    Borrow, J.M.3    Hersey, P.4
  • 99
    • 17744416444 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor activates the Waf1/Cip1 gene promoter through the Sp1 sites
    • Sowa Y., Orita T., Minamikawa S., et al. Histone deacetylase inhibitor activates the Waf1/Cip1 gene promoter through the Sp1 sites. Biochem Biophys Res Commun 241 (1997) 142-150
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 142-150
    • Sowa, Y.1    Orita, T.2    Minamikawa, S.3
  • 100
    • 6344229760 scopus 로고    scopus 로고
    • Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor-induced apoptosis through the generation of reactive oxygen species
    • Denlinger C.E., Rundall B.K., and Jones D.R. Proteasome inhibition sensitizes non-small cell lung cancer to histone deacetylase inhibitor-induced apoptosis through the generation of reactive oxygen species. J Thorac Cardiovasc Surg 128 (2004) 740-748
    • (2004) J Thorac Cardiovasc Surg , vol.128 , pp. 740-748
    • Denlinger, C.E.1    Rundall, B.K.2    Jones, D.R.3
  • 101
  • 102
    • 2542523228 scopus 로고    scopus 로고
    • Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors
    • Pei X.Y., Dai Y., and Grant S. Synergistic induction of oxidative injury and apoptosis in human multiple myeloma cells by the proteasome inhibitor bortezomib and histone deacetylase inhibitors. Clin Cancer Res 10 (2004) 3839-3852
    • (2004) Clin Cancer Res , vol.10 , pp. 3839-3852
    • Pei, X.Y.1    Dai, Y.2    Grant, S.3
  • 103
    • 23944469381 scopus 로고    scopus 로고
    • The fully human anti-CD30 antibody 5F11 activates NF-κB and sensitizes lymphoma cells to bortezomib-induced apoptosis
    • Boll B., Hansen H., Heuck F., et al. The fully human anti-CD30 antibody 5F11 activates NF-κB and sensitizes lymphoma cells to bortezomib-induced apoptosis. Blood 106 (2005) 1839-1842
    • (2005) Blood , vol.106 , pp. 1839-1842
    • Boll, B.1    Hansen, H.2    Heuck, F.3
  • 104
    • 9244251096 scopus 로고    scopus 로고
    • 2-terminal kinase activation, Fas up-regulation, and poly(ADP-ribose) polymerase cleavage in SN38-mediated cytotoxicity against multiple myeloma
    • 2-terminal kinase activation, Fas up-regulation, and poly(ADP-ribose) polymerase cleavage in SN38-mediated cytotoxicity against multiple myeloma. Cancer Res 64 (2004) 8746-8753
    • (2004) Cancer Res , vol.64 , pp. 8746-8753
    • Catley, L.1    Tai, Y.T.2    Shringarpure, R.3
  • 105
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: a novel class of potent and effective anti-tumor agents
    • Adams J., Palombella V.J., Sausville E.A., et al. Proteasome inhibitors: a novel class of potent and effective anti-tumor agents. Cancer Res 59 (1999) 2615-2622
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 106
    • 0036023407 scopus 로고    scopus 로고
    • A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies
    • Aghajanian C., Soignet S., Dizon D.S., et al. A phase I trial of the novel proteasome inhibitor PS341 in advanced solid tumor malignancies. Clin Cancer Res 8 (2002) 2505-2511
    • (2002) Clin Cancer Res , vol.8 , pp. 2505-2511
    • Aghajanian, C.1    Soignet, S.2    Dizon, D.S.3
  • 107
    • 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) 4420-4427
    • (2002) J Clin Oncol , vol.20 , pp. 4420-4427
    • Orlowski, R.Z.1    Stinchcombe, T.E.2    Mitchell, B.S.3
  • 108
    • 2942692143 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer
    • Papandreou C.N., Daliani D.D., Nix D., et al. Phase I trial of the proteasome inhibitor bortezomib in patients with advanced solid tumors with observations in androgen-independent prostate cancer. J Clin Oncol 22 (2004) 2108-2121
    • (2004) J Clin Oncol , vol.22 , pp. 2108-2121
    • Papandreou, C.N.1    Daliani, D.D.2    Nix, D.3
  • 109
    • 2542481724 scopus 로고    scopus 로고
    • Phase I study of bortezomib in refractory or relapsed acute leukemias
    • Cortes J., Thomas D., Koller C., et al. Phase I study of bortezomib in refractory or relapsed acute leukemias. Clin Cancer Res 10 (2004) 3371-3376
    • (2004) Clin Cancer Res , vol.10 , pp. 3371-3376
    • Cortes, J.1    Thomas, D.2    Koller, C.3
  • 110
    • 16544389047 scopus 로고    scopus 로고
    • Phase I study of the proteasome inhibitor bortezomib in pediatric patients with refractory solid tumors: a Children's Oncology Group study (ADVL0015)
    • Blaney S.M., Bernstein M., Neville K., et al. Phase I study of the proteasome inhibitor bortezomib in pediatric patients with refractory solid tumors: a Children's Oncology Group study (ADVL0015). J Clin Oncol 22 (2004) 4804-4809
    • (2004) J Clin Oncol , vol.22 , pp. 4804-4809
    • Blaney, S.M.1    Bernstein, M.2    Neville, K.3
  • 113
    • 0642378063 scopus 로고    scopus 로고
    • Overcoming drug resistance in multiple myeloma: the emergence of therapeutic approaches to induce apoptosis
    • Yang H.H., Ma M.H., Vescio R.A., and Berenson J.R. Overcoming drug resistance in multiple myeloma: the emergence of therapeutic approaches to induce apoptosis. J Clin Oncol 21 (2003) 4239-4247
    • (2003) J Clin Oncol , vol.21 , pp. 4239-4247
    • Yang, H.H.1    Ma, M.H.2    Vescio, R.A.3    Berenson, J.R.4
  • 114
    • 0037443551 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications
    • Mitsiades N., Mitsiades C.S., Richardson P.G., et al. The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications. Blood 101 (2003) 2377-2380
    • (2003) Blood , vol.101 , pp. 2377-2380
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 115
    • 0013132084 scopus 로고    scopus 로고
    • A phase I and pharmacodynamic study of the proteasome inhibitor PS-341 in combination with doxorubicin
    • [Abstract 368]
    • Thomas J.P., Arzoomanian R., Alberti D., et al. A phase I and pharmacodynamic study of the proteasome inhibitor PS-341 in combination with doxorubicin. J Clin Oncol 21 (2002) 93a [Abstract 368]
    • (2002) J Clin Oncol , vol.21
    • Thomas, J.P.1    Arzoomanian, R.2    Alberti, D.3
  • 116
    • 3543146046 scopus 로고    scopus 로고
    • Phase I trial of the proteasome inhibitor bortezomib in combination with pegylated liposomal doxorubicin in patients with refractory solid tumors
    • [Abstract 868]
    • Dees E.C., O'Neil B., Humes E., et al. Phase I trial of the proteasome inhibitor bortezomib in combination with pegylated liposomal doxorubicin in patients with refractory solid tumors. J Clin Oncol 22 (2003) 217 [Abstract 868]
    • (2003) J Clin Oncol , vol.22 , pp. 217
    • Dees, E.C.1    O'Neil, B.2    Humes, E.3
  • 117
    • 33746487680 scopus 로고    scopus 로고
    • Preliminary evidence of efficacy and tolerance for weekly intravenous bortezomib plus mitoxantrone in patients with advanced androgen-independent prostate cancer (AIPCa)
    • [Abstract 4567]
    • Siefker-Radtke A.O., Poulter V., Mathew P., Tu S., Logothetis C.J., and Papandreou C.N. Preliminary evidence of efficacy and tolerance for weekly intravenous bortezomib plus mitoxantrone in patients with advanced androgen-independent prostate cancer (AIPCa). J Clin Oncol 23 (2005) 394s [Abstract 4567]
    • (2005) J Clin Oncol , vol.23
    • Siefker-Radtke, A.O.1    Poulter, V.2    Mathew, P.3    Tu, S.4    Logothetis, C.J.5    Papandreou, C.N.6
  • 118
    • 33646796542 scopus 로고    scopus 로고
    • ®) in combination with paclitaxel in advanced solid tumor patients (pts)
    • [Abstract 3104]
    • ®) in combination with paclitaxel in advanced solid tumor patients (pts). J Clin Oncol 23 (2005) 217s [Abstract 3104]
    • (2005) J Clin Oncol , vol.23
    • Shapiro, C.L.1    Ramaswamy, B.2    Young, D.3
  • 119
    • 33646807660 scopus 로고    scopus 로고
    • Phase I trial of bortezomib (PS-341) in combination with docetaxel in patients with advanced solid tumors
    • [Abstract 3052]
    • Messersmith W.A., Baker S.D., Dinh K., et al. Phase I trial of bortezomib (PS-341) in combination with docetaxel in patients with advanced solid tumors. J Clin Oncol 23 (2004) 208 [Abstract 3052]
    • (2004) J Clin Oncol , vol.23 , pp. 208
    • Messersmith, W.A.1    Baker, S.D.2    Dinh, K.3
  • 120
    • 0142139039 scopus 로고    scopus 로고
    • Phase I study of bortezomib in combination with docetaxel in anthracycline-pretreated advanced breast cancer
    • [Abstract 63]
    • Albanell J., Baselga J., Guix M., et al. Phase I study of bortezomib in combination with docetaxel in anthracycline-pretreated advanced breast cancer. J Clin Oncol 22 (2003) 16 [Abstract 63]
    • (2003) J Clin Oncol , vol.22 , pp. 16
    • Albanell, J.1    Baselga, J.2    Guix, M.3
  • 121
    • 0142169725 scopus 로고    scopus 로고
    • Phase I/II trial of bortezomib (PS-341) plus docetaxel in patients with advanced androgen-independent prostate cancer
    • [Abstract 1705]
    • Roth B.J., Dreicer R., Berg W., et al. Phase I/II trial of bortezomib (PS-341) plus docetaxel in patients with advanced androgen-independent prostate cancer. J Clin Oncol 22 (2003) 424 [Abstract 1705]
    • (2003) J Clin Oncol , vol.22 , pp. 424
    • Roth, B.J.1    Dreicer, R.2    Berg, W.3
  • 122
    • 0347981405 scopus 로고    scopus 로고
    • Phase I trial of PS-341 and carboplatin in recurrent ovarian cancer
    • [Abstract 1815]
    • Aghajanian C., Dizon D., Yan X.J., et al. Phase I trial of PS-341 and carboplatin in recurrent ovarian cancer. J Clin Oncol 22 (2003) 452 [Abstract 1815]
    • (2003) J Clin Oncol , vol.22 , pp. 452
    • Aghajanian, C.1    Dizon, D.2    Yan, X.J.3
  • 123
    • 11344263355 scopus 로고    scopus 로고
    • The proteasome inhibitor, bortezomib, in combination with gemcitabine (Gem) and carboplatin (Carbo) in advanced non-small cell lung cancer (NSCLC): final results of a phase I California Cancer Consortium study
    • [Abstract 7106]
    • Davies A.M., Lara P.N., Lau D.H., et al. The proteasome inhibitor, bortezomib, in combination with gemcitabine (Gem) and carboplatin (Carbo) in advanced non-small cell lung cancer (NSCLC): final results of a phase I California Cancer Consortium study. J Clin Oncol 23 (2004) 639 [Abstract 7106]
    • (2004) J Clin Oncol , vol.23 , pp. 639
    • Davies, A.M.1    Lara, P.N.2    Lau, D.H.3
  • 124
    • 33646820246 scopus 로고    scopus 로고
    • A phase 1B, open-label, dose-escalation study of bortezomib in combination with gemcitabine (Gem) and cisplatin (Cis) in the first-line treatment of patients with advanced solid tumors: preliminary results of a phase IB study
    • [Abstract 2103]
    • Voortman J., Smit E., Kuenen B., et al. A phase 1B, open-label, dose-escalation study of bortezomib in combination with gemcitabine (Gem) and cisplatin (Cis) in the first-line treatment of patients with advanced solid tumors: preliminary results of a phase IB study. J Clin Oncol 23 (2005) 160s [Abstract 2103]
    • (2005) J Clin Oncol , vol.23
    • Voortman, J.1    Smit, E.2    Kuenen, B.3
  • 125
    • 0346720624 scopus 로고    scopus 로고
    • Phase I dose-escalation study of the proteasome inhibitor, bortezomib, plus irinotecan in patients with advanced solid tumors
    • [Abstract 915]
    • Ryan D.P., O'Neil B., Lima C.R., et al. Phase I dose-escalation study of the proteasome inhibitor, bortezomib, plus irinotecan in patients with advanced solid tumors. J Clin Oncol 22 (2003) 228 [Abstract 915]
    • (2003) J Clin Oncol , vol.22 , pp. 228
    • Ryan, D.P.1    O'Neil, B.2    Lima, C.R.3
  • 126
    • 2342637810 scopus 로고    scopus 로고
    • Phase I dose escalation study of bortezomib and gemcitabine safety and tolerability in patients with advanced solid tumors
    • [Abstract 839]
    • Appleman L.J., Ryan D.P., Clark J.W., et al. Phase I dose escalation study of bortezomib and gemcitabine safety and tolerability in patients with advanced solid tumors. J Clin Oncol 22 (2003) 209 [Abstract 839]
    • (2003) J Clin Oncol , vol.22 , pp. 209
    • Appleman, L.J.1    Ryan, D.P.2    Clark, J.W.3
  • 127
    • 27744505806 scopus 로고    scopus 로고
    • Phase I study of PS-341 (bortezomib) with 5-fluorouracil/leucovorin (5-FU/LV) in advanced solid tumors: a California Cancer Consortium study
    • [Abstract 2057]
    • Iqbal S., Cole S., Yang D., et al. Phase I study of PS-341 (bortezomib) with 5-fluorouracil/leucovorin (5-FU/LV) in advanced solid tumors: a California Cancer Consortium study. J Clin Oncol 23 (2004) 141 [Abstract 2057]
    • (2004) J Clin Oncol , vol.23 , pp. 141
    • Iqbal, S.1    Cole, S.2    Yang, D.3
  • 128
    • 33646820868 scopus 로고    scopus 로고
    • Phase I trial of bortezomib and capecitabine in patients with metastatic breast cancer previously treated with taxanes and/or anthracyclines
    • [Abstract 755]
    • Possinger K., Schippinger W., Kiewe P., et al. Phase I trial of bortezomib and capecitabine in patients with metastatic breast cancer previously treated with taxanes and/or anthracyclines. J Clin Oncol 23 (2005) 66s [Abstract 755]
    • (2005) J Clin Oncol , vol.23
    • Possinger, K.1    Schippinger, W.2    Kiewe, P.3
  • 129
    • 33746484217 scopus 로고    scopus 로고
    • Proteasome inhibitor bortezomib and re-irradiation (rRT) with scheduled treatment break in patients (pts) with head/neck squamous carcinoma (HNSCC)
    • [Abstract 5592]
    • Conley B.A., Donovan E., Muir C., et al. Proteasome inhibitor bortezomib and re-irradiation (rRT) with scheduled treatment break in patients (pts) with head/neck squamous carcinoma (HNSCC). J Clin Oncol 23 (2005) 522s [Abstract 5592]
    • (2005) J Clin Oncol , vol.23
    • Conley, B.A.1    Donovan, E.2    Muir, C.3
  • 130
    • 21344464047 scopus 로고    scopus 로고
    • Bortezomib in combination with melphalan in the treatment of relapsed or refractory multiple myeloma: a phase I/II study
    • [Abstract 209]
    • Berenson J., Yang H., Swift R., et al. Bortezomib in combination with melphalan in the treatment of relapsed or refractory multiple myeloma: a phase I/II study. Blood 104 (2004) 64a [Abstract 209]
    • (2004) Blood , vol.104
    • Berenson, J.1    Yang, H.2    Swift, R.3
  • 131
    • 21944446824 scopus 로고    scopus 로고
    • A phase I/II national, multi-center, open-label study of bortezomib plus melphalan and prednisone (V-MP) in elderly untreated multiple myeloma patients
    • [Abstract 3462]
    • Mateos M.V., Blade J., Diaz Mediavilla J., et al. A phase I/II national, multi-center, open-label study of bortezomib plus melphalan and prednisone (V-MP) in elderly untreated multiple myeloma patients. Blood 104 (2004) 943a [Abstract 3462]
    • (2004) Blood , vol.104
    • Mateos, M.V.1    Blade, J.2    Diaz Mediavilla, J.3
  • 132
    • 0037097595 scopus 로고    scopus 로고
    • Apoptotic signaling induced by immunomodulatory thalidomide analogs in human multiple myeloma cells: therapeutic implications
    • Mitsiades N., Mitsiades C.S., Poulaki V., et al. Apoptotic signaling induced by immunomodulatory thalidomide analogs in human multiple myeloma cells: therapeutic implications. Blood 99 (2002) 4525-4530
    • (2002) Blood , vol.99 , pp. 4525-4530
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 133
    • 23944475760 scopus 로고    scopus 로고
    • ® plus thalidomide (V + T) in advanced and refractory multiple myeloma
    • [Abstract 1480]
    • ® plus thalidomide (V + T) in advanced and refractory multiple myeloma. Blood 104 (2004) 413a [Abstract 1480]
    • (2004) Blood , vol.104
    • Zangari, M.1    Barlogie, B.2    Hollmig, K.3
  • 134
    • 21344458719 scopus 로고    scopus 로고
    • ®, thalidomide, dexamethasone) as primary therapy for newly-diagnosed multiple myeloma
    • [Abstract 210]
    • ®, thalidomide, dexamethasone) as primary therapy for newly-diagnosed multiple myeloma. Blood 104 (2004) 64a [Abstract 210]
    • (2004) Blood , vol.104
    • Alexanian, R.1    Wang, L.M.2    Weber, D.M.3    Delasalle, K.B.4
  • 135
    • 0344737064 scopus 로고    scopus 로고
    • Repression of mitogen-activated protein kinase (MAPK) phosphatase-1 by anthracyclines contributes to their antiapoptotic activation of p44/42-MAPK
    • Small G.W., Somasundaram S., Moore D.T., Shi Y.Y., and Orlowski R.Z. Repression of mitogen-activated protein kinase (MAPK) phosphatase-1 by anthracyclines contributes to their antiapoptotic activation of p44/42-MAPK. J Pharmacol Exp Ther 307 (2003) 861-869
    • (2003) J Pharmacol Exp Ther , vol.307 , pp. 861-869
    • Small, G.W.1    Somasundaram, S.2    Moore, D.T.3    Shi, Y.Y.4    Orlowski, R.Z.5
  • 136
    • 9444249941 scopus 로고    scopus 로고
    • Evidence that mitogen-activated protein kinase phosphatase-1 induction by proteasome inhibitors plays an antiapoptotic role
    • Small G.W., Shi Y.Y., Edmund N.A., Somasundaram S., Moore D.T., and Orlowski R.Z. Evidence that mitogen-activated protein kinase phosphatase-1 induction by proteasome inhibitors plays an antiapoptotic role. Mol Pharmacol 66 (2004) 1478-1490
    • (2004) Mol Pharmacol , vol.66 , pp. 1478-1490
    • Small, G.W.1    Shi, Y.Y.2    Edmund, N.A.3    Somasundaram, S.4    Moore, D.T.5    Orlowski, R.Z.6
  • 137
    • 20144387627 scopus 로고    scopus 로고
    • Phase 1 trial of the proteasome inhibitor bortezomib and pegylated liposomal doxorubicin in patients with advanced hematologic malignancies
    • Orlowski R.Z., Voorhees P.M., Garcia R.A., et al. Phase 1 trial of the proteasome inhibitor bortezomib and pegylated liposomal doxorubicin in patients with advanced hematologic malignancies. Blood 105 (2005) 3058-3065
    • (2005) Blood , vol.105 , pp. 3058-3065
    • Orlowski, R.Z.1    Voorhees, P.M.2    Garcia, R.A.3
  • 138
    • 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) 2609-2617
    • (2003) N Engl J Med , vol.348 , pp. 2609-2617
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 139
    • 21344435052 scopus 로고    scopus 로고
    • PAD combination therapy (PS-341/bortezomib, doxorubicin and dexamethasone) for previously untreated patients with multiple myeloma
    • Oakervee H.E., Popat R., Curry N., et al. PAD combination therapy (PS-341/bortezomib, doxorubicin and dexamethasone) for previously untreated patients with multiple myeloma. Br J Haematol 129 (2005) 755-762
    • (2005) Br J Haematol , vol.129 , pp. 755-762
    • Oakervee, H.E.1    Popat, R.2    Curry, N.3
  • 140
    • 33846873224 scopus 로고    scopus 로고
    • ®) + Adriamycin™ + thalidomide + dexamethasone (VATD) as an effective regimen in patients with refractory or relapsed multiple myeloma
    • [Abstract 2399]
    • ®) + Adriamycin™ + thalidomide + dexamethasone (VATD) as an effective regimen in patients with refractory or relapsed multiple myeloma. Blood 104 (2004) 659a [Abstract 2399]
    • (2004) Blood , vol.104
    • Hollmig, K.1    Stover, J.2    Talamo, G.3
  • 141
    • 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) 14374-14379
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14374-14379
    • Mitsiades, N.1    Mitsiades, C.S.2    Poulaki, V.3
  • 142
    • 32844464998 scopus 로고    scopus 로고
    • Dose escalating trial of 17-AAG with bortezomib (BZ) in patients with relapsed refractory multiple myeloma (MM)
    • [Abstract 6682]
    • Chanan-Khan A., Alsina M., Carroll M., et al. Dose escalating trial of 17-AAG with bortezomib (BZ) in patients with relapsed refractory multiple myeloma (MM). J Clin Oncol 24 (2005) 605s [Abstract 6682]
    • (2005) J Clin Oncol , vol.24
    • Chanan-Khan, A.1    Alsina, M.2    Carroll, M.3
  • 143
    • 16844374736 scopus 로고    scopus 로고
    • Phase I/II study of bortezomib alone and bortezomib with dose-adjusted EPOCH chemotherapy in relapsed or refractory aggressive B-cell lymphoma
    • [Abstract 1385]
    • Dunleavy K., Janik J., Gea-Banacloche J., et al. Phase I/II study of bortezomib alone and bortezomib with dose-adjusted EPOCH chemotherapy in relapsed or refractory aggressive B-cell lymphoma. Blood 104 (2004) 389a [Abstract 1385]
    • (2004) Blood , vol.104
    • Dunleavy, K.1    Janik, J.2    Gea-Banacloche, J.3
  • 144
    • 27244451663 scopus 로고    scopus 로고
    • ®) in combination with idarubicin and cytarabine in patients with acute myeloid leukemia
    • [Abstract 1799]
    • ®) in combination with idarubicin and cytarabine in patients with acute myeloid leukemia. Blood 104 (2004) 498a [Abstract 1799]
    • (2004) Blood , vol.104
    • Attar, E.C.1    DeAngelo, D.J.2    Ballen, K.K.3
  • 145
    • 32844471527 scopus 로고    scopus 로고
    • A phase I trial of bortezomib in combination with fludarabine in patients with lymphoproliferative neoplasms
    • [Abstract 6647]
    • Koc O.N., Bahlis N.J., Liu L., et al. A phase I trial of bortezomib in combination with fludarabine in patients with lymphoproliferative neoplasms. J Clin Oncol 23 (2005) 596s [Abstract 6647]
    • (2005) J Clin Oncol , vol.23
    • Koc, O.N.1    Bahlis, N.J.2    Liu, L.3
  • 146
    • 2442510143 scopus 로고    scopus 로고
    • Phase II trial of PS-341 in patients with renal cell cancer: A University of Chicago phase II consortium study
    • Davis N.B., Taber D.A., Ansari R.H., et al. Phase II trial of PS-341 in patients with renal cell cancer: A University of Chicago phase II consortium study. J Clin Oncol 22 (2004) 115-119
    • (2004) J Clin Oncol , vol.22 , pp. 115-119
    • Davis, N.B.1    Taber, D.A.2    Ansari, R.H.3
  • 147
    • 4644304196 scopus 로고    scopus 로고
    • Phase II trial of bortezomib for patients with advanced renal cell carcinoma
    • Kondagunta G.V., Drucker B., Schwartz L., et al. Phase II trial of bortezomib for patients with advanced renal cell carcinoma. J Clin Oncol 22 (2004) 3720-3725
    • (2004) J Clin Oncol , vol.22 , pp. 3720-3725
    • Kondagunta, G.V.1    Drucker, B.2    Schwartz, L.3
  • 148
    • 4644248931 scopus 로고    scopus 로고
    • Phase II study of the proteasome inhibitor bortezomib (PS-341) in patients with metastatic neuroendocrine tumors
    • Shah M.H., Young D., Kindler H.L., et al. Phase II study of the proteasome inhibitor bortezomib (PS-341) in patients with metastatic neuroendocrine tumors. Clin Cancer Res 10 (2004) 6111-6118
    • (2004) Clin Cancer Res , vol.10 , pp. 6111-6118
    • Shah, M.H.1    Young, D.2    Kindler, H.L.3
  • 149
    • 20444364475 scopus 로고    scopus 로고
    • A phase II study of bortezomib in the treatment of metastatic malignant melanoma
    • Markovic S.N., Geyer S.M., Dawkins F., et al. A phase II study of bortezomib in the treatment of metastatic malignant melanoma. Cancer 103 (2005) 2584-2589
    • (2005) Cancer , vol.103 , pp. 2584-2589
    • Markovic, S.N.1    Geyer, S.M.2    Dawkins, F.3
  • 150
    • 15744364211 scopus 로고    scopus 로고
    • A multicenter phase II study of bortezomib in recurrent or metastatic sarcomas
    • Maki R.G., Kraft A.S., Scheu K., et al. A multicenter phase II study of bortezomib in recurrent or metastatic sarcomas. Cancer 103 (2005) 1431-1438
    • (2005) Cancer , vol.103 , pp. 1431-1438
    • Maki, R.G.1    Kraft, A.S.2    Scheu, K.3
  • 151
    • 33746487067 scopus 로고    scopus 로고
    • Phase II study of bortezomib for castrate metastatic prostate cancer (PC)
    • [Abstract 4633]
    • Morris M.J., Beekman K.W., Kelly W.K., et al. Phase II study of bortezomib for castrate metastatic prostate cancer (PC). J Clin Oncol 23 (2005) 411s [Abstract 4633]
    • (2005) J Clin Oncol , vol.23
    • Morris, M.J.1    Beekman, K.W.2    Kelly, W.K.3
  • 152
    • 33646838191 scopus 로고    scopus 로고
    • Phase 2 study of bortezomib in advanced or metastatic urothelial cancer. A trial of the Princess Margaret Hospital [PMH] phase II consortium
    • [Abstract 4677]
    • Sridhar S.S., Stadler W., Le L., et al. Phase 2 study of bortezomib in advanced or metastatic urothelial cancer. A trial of the Princess Margaret Hospital [PMH] phase II consortium. J Clin Oncol 23 (2005) 422s [Abstract 4677]
    • (2005) J Clin Oncol , vol.23
    • Sridhar, S.S.1    Stadler, W.2    Le, L.3
  • 153
    • 26644437865 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 (Bortezomib) in platinum (plat)-treated extensive-stage small cell lung cancer (E-SCLC): a SWOG (0327) phase II trial
    • [Abstract 7047]
    • Johl J., Chansky K., Lara P.N., Davies A.M., Bold R., and Gandara D.R. The proteasome inhibitor PS-341 (Bortezomib) in platinum (plat)-treated extensive-stage small cell lung cancer (E-SCLC): a SWOG (0327) phase II trial. J Clin Oncol 23 (2005) 632s [Abstract 7047]
    • (2005) J Clin Oncol , vol.23
    • Johl, J.1    Chansky, K.2    Lara, P.N.3    Davies, A.M.4    Bold, R.5    Gandara, D.R.6
  • 154
    • 18844461545 scopus 로고    scopus 로고
    • A phase II study of the proteasome inhibitor PS-341 in patients with metastatic breast cancer
    • [Abstract 546]
    • Brown J., Von Roenn J., O'Regan R., et al. A phase II study of the proteasome inhibitor PS-341 in patients with metastatic breast cancer. J Clin Oncol 23 (2004) 13 [Abstract 546]
    • (2004) J Clin Oncol , vol.23 , pp. 13
    • Brown, J.1    Von Roenn, J.2    O'Regan, R.3
  • 155
    • 33645465044 scopus 로고    scopus 로고
    • A phase II trial of PS-341 in metastatic breast cancer (MBC)
    • [Abstract 3102]
    • Cristofanilli M., Gonzalez-Angulo A.M., Nealy K.N., et al. A phase II trial of PS-341 in metastatic breast cancer (MBC). J Clin Oncol 22 (2004) 220 [Abstract 3102]
    • (2004) J Clin Oncol , vol.22 , pp. 220
    • Cristofanilli, M.1    Gonzalez-Angulo, A.M.2    Nealy, K.N.3
  • 156
    • 23044446004 scopus 로고    scopus 로고
    • A phase II trial of the proteosome inhibitor PS-341 in patients with metastatic colorectal cancer
    • [Abstract 3109]
    • Mackay H., Major P., Townsley C., et al. A phase II trial of the proteosome inhibitor PS-341 in patients with metastatic colorectal cancer. J Clin Oncol 23 (2004) 222 [Abstract 3109]
    • (2004) J Clin Oncol , vol.23 , pp. 222
    • Mackay, H.1    Major, P.2    Townsley, C.3
  • 157
    • 1242281150 scopus 로고    scopus 로고
    • Phase II clinical/pharmacodynamic trial of the proteasome inhibitor PS-341 in advanced non-small cell lung cancer
    • [Abstract 810]
    • Stevenson J., Nho C.W., Schick J., et al. Phase II clinical/pharmacodynamic trial of the proteasome inhibitor PS-341 in advanced non-small cell lung cancer. J Clin Oncol 22 (2003) 202 [Abstract 810]
    • (2003) J Clin Oncol , vol.22 , pp. 202
    • Stevenson, J.1    Nho, C.W.2    Schick, J.3
  • 158
    • 33746547574 scopus 로고    scopus 로고
    • Weekly docetaxel and bortezomib in the treatment of patients with advanced hormone refractory prostate cancer (HRPC): a Minnie Pearl Cancer Research Network phase II trial
    • [Abstract 4735]
    • Meluch A.A., Spigel D.S., Greco F.A., et al. Weekly docetaxel and bortezomib in the treatment of patients with advanced hormone refractory prostate cancer (HRPC): a Minnie Pearl Cancer Research Network phase II trial. J Clin Oncol 23 (2005) 436s [Abstract 4735]
    • (2005) J Clin Oncol , vol.23
    • Meluch, A.A.1    Spigel, D.S.2    Greco, F.A.3
  • 159
    • 16244396294 scopus 로고    scopus 로고
    • Phase I/II trial of bortezomib plus docetaxel in patients with advanced androgen-independent prostate cancer
    • [Abstract 4654]
    • Dreicer R., Roth B., Petrylak D., et al. Phase I/II trial of bortezomib plus docetaxel in patients with advanced androgen-independent prostate cancer. J Clin Oncol 23 (2004) 418 [Abstract 4654]
    • (2004) J Clin Oncol , vol.23 , pp. 418
    • Dreicer, R.1    Roth, B.2    Petrylak, D.3
  • 160
    • 23844449093 scopus 로고    scopus 로고
    • Bortezomib ± docetaxel in previously treated patients with advanced non-small cell lung cancer (NSCLC): a phase 2 study
    • [Abstract 7034]
    • Fanucchi M.P., Fossella F., Fidias P., et al. Bortezomib ± docetaxel in previously treated patients with advanced non-small cell lung cancer (NSCLC): a phase 2 study. J Clin Oncol 23 (2005) 629s [Abstract 7034]
    • (2005) J Clin Oncol , vol.23
    • Fanucchi, M.P.1    Fossella, F.2    Fidias, P.3
  • 161
    • 18844421493 scopus 로고    scopus 로고
    • Bortezomib ± irinotecan in relapsed/refractory colorectal cancer (CRC): interim analysis results from phase (ph) 2b study
    • [Abstract 3591]
    • Dragovich T., Lenz H.J., Rocha Lima C.M.S., et al. Bortezomib ± irinotecan in relapsed/refractory colorectal cancer (CRC): interim analysis results from phase (ph) 2b study. J Clin Oncol 23 (2004) 268 [Abstract 3591]
    • (2004) J Clin Oncol , vol.23 , pp. 268
    • Dragovich, T.1    Lenz, H.J.2    Rocha Lima, C.M.S.3
  • 162
    • 10344236596 scopus 로고    scopus 로고
    • Phase I/II trial of bortezomib in patients with unresectable hepatocellular carcinoma (HCC)
    • [Abstract 4089]
    • Hegewisch-Becker S., Sterneck M., Schubert U., et al. Phase I/II trial of bortezomib in patients with unresectable hepatocellular carcinoma (HCC). J Clin Oncol 23 (2004) 334 [Abstract 4089]
    • (2004) J Clin Oncol , vol.23 , pp. 334
    • Hegewisch-Becker, S.1    Sterneck, M.2    Schubert, U.3
  • 163
    • 3042775299 scopus 로고    scopus 로고
    • Clinical course of patients with relapsed multiple myeloma
    • Kumar S.K., Therneau T.M., Gertz M.A., et al. Clinical course of patients with relapsed multiple myeloma. Mayo Clin Proc 79 (2004) 867-874
    • (2004) Mayo Clin Proc , vol.79 , pp. 867-874
    • Kumar, S.K.1    Therneau, T.M.2    Gertz, M.A.3
  • 164
    • 2342620088 scopus 로고    scopus 로고
    • Chromosome 13 deletion/hypodiploidy and prognosis in multiple myeloma patients
    • Fassas A.B., and Tricot G. Chromosome 13 deletion/hypodiploidy and prognosis in multiple myeloma patients. Leuk Lymphoma 45 (2004) 1083-1091
    • (2004) Leuk Lymphoma , vol.45 , pp. 1083-1091
    • Fassas, A.B.1    Tricot, G.2
  • 165
    • 5644250621 scopus 로고    scopus 로고
    • A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma
    • Jagannath S., Barlogie B., Berenson J., et al. A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma. Br J Haematol 127 (2004) 165-172
    • (2004) Br J Haematol , vol.127 , pp. 165-172
    • Jagannath, S.1    Barlogie, B.2    Berenson, J.3
  • 166
    • 23944486566 scopus 로고    scopus 로고
    • ®, Doxil in combination with low-dose thalidomide as salvage therapy for patients with relapsed or refractory multiple myeloma and Waldenström's macroglobulinemia: encouraging preliminary results
    • [Abstract 2421]
    • ®, Doxil in combination with low-dose thalidomide as salvage therapy for patients with relapsed or refractory multiple myeloma and Waldenström's macroglobulinemia: encouraging preliminary results. Blood 104 (2004) 665a [Abstract 2421]
    • (2004) Blood , vol.104
    • Chanan-Khan, A.A.1    Miller, K.C.2    McCarthy, P.3
  • 169
    • 21344469223 scopus 로고    scopus 로고
    • Bortezomib therapy alone and in combination with dexamethasone for previously untreated symptomatic multiple myeloma
    • Jagannath S., Durie B.G., Wolf J., et al. Bortezomib therapy alone and in combination with dexamethasone for previously untreated symptomatic multiple myeloma. Br J Haematol 129 (2005) 776-783
    • (2005) Br J Haematol , vol.129 , pp. 776-783
    • Jagannath, S.1    Durie, B.G.2    Wolf, J.3
  • 170
    • 27944439118 scopus 로고    scopus 로고
    • ®) plus dexamethasone as induction treatment prior to autologous stem cell transplantation in patients with newly diagnosed multiple myeloma: preliminary results of an IFM phase II study
    • [Abstract 6653]
    • ®) plus dexamethasone as induction treatment prior to autologous stem cell transplantation in patients with newly diagnosed multiple myeloma: preliminary results of an IFM phase II study. J Clin Oncol 23 (2005) 598s [Abstract 6653]
    • (2005) J Clin Oncol , vol.23
    • Harousseau, J.1    Attal, M.2    Coiteux, V.3
  • 171
    • 32844474901 scopus 로고    scopus 로고
    • Bortezomib and pegylated liposomal doxorubicin as initial therapy for adult patients with symptomatic multiple myeloma: CALGB study 10301
    • [Abstract 730]
    • Orlowski R.Z., Peterson B.L., Caligiuri M.A., Kelly M., and Larson R.A. Bortezomib and pegylated liposomal doxorubicin as initial therapy for adult patients with symptomatic multiple myeloma: CALGB study 10301. Haematologica 90 s1 (2005) 151 [Abstract 730]
    • (2005) Haematologica , vol.90 , Issue.SUPPL.1 , pp. 151
    • Orlowski, R.Z.1    Peterson, B.L.2    Caligiuri, M.A.3    Kelly, M.4    Larson, R.A.5
  • 172
    • 21844473161 scopus 로고    scopus 로고
    • Total therapy 3 (TT 3) for newly diagnosed myeloma, incorporating Velcade into remission induction with DT PACE: early results regarding efficacy, PBSC mobilization and toxicities
    • [Abstract 538]
    • Barlogie B., Hollmig K., Zangari M., et al. Total therapy 3 (TT 3) for newly diagnosed myeloma, incorporating Velcade into remission induction with DT PACE: early results regarding efficacy, PBSC mobilization and toxicities. Blood 104 (2004) 156a [Abstract 538]
    • (2004) Blood , vol.104
    • Barlogie, B.1    Hollmig, K.2    Zangari, M.3
  • 173
    • 31644451689 scopus 로고    scopus 로고
    • Bortezomib given in sequence with anthracycline and thalidomide-containing regimens does not adversely affect stem cell mobilization and engraftment in patients with multiple myeloma undergoing autologous hematopoietic stem cell transplantation
    • [Abstract 541]
    • Uy G.L., Fisher N.M., Devine S.M., et al. Bortezomib given in sequence with anthracycline and thalidomide-containing regimens does not adversely affect stem cell mobilization and engraftment in patients with multiple myeloma undergoing autologous hematopoietic stem cell transplantation. Blood 104 (2004) 157a [Abstract 541]
    • (2004) Blood , vol.104
    • Uy, G.L.1    Fisher, N.M.2    Devine, S.M.3
  • 174
    • 20044376092 scopus 로고    scopus 로고
    • Phase II clinical experience with the novel proteasome inhibitor bortezomib in patients with indolent non-Hodgkin's lymphoma and mantle cell lymphoma
    • O'Connor O.A., Wright J., Moskowitz C., et al. Phase II clinical experience with the novel proteasome inhibitor bortezomib in patients with indolent non-Hodgkin's lymphoma and mantle cell lymphoma. J Clin Oncol 23 (2005) 676-684
    • (2005) J Clin Oncol , vol.23 , pp. 676-684
    • O'Connor, O.A.1    Wright, J.2    Moskowitz, C.3
  • 175
    • 20044396543 scopus 로고    scopus 로고
    • Phase II study of proteasome inhibitor bortezomib in relapsed or refractory B-cell non-Hodgkin's lymphoma
    • Goy A., Younes A., McLaughlin P., et al. Phase II study of proteasome inhibitor bortezomib in relapsed or refractory B-cell non-Hodgkin's lymphoma. J Clin Oncol 23 (2005) 667-675
    • (2005) J Clin Oncol , vol.23 , pp. 667-675
    • Goy, A.1    Younes, A.2    McLaughlin, P.3
  • 176
    • 16844367553 scopus 로고    scopus 로고
    • Phase II trial of bortezomib in mantle cell lymphoma
    • [Abstract 608]
    • Belch A., Kouroukis C.T., Crump M., et al. Phase II trial of bortezomib in mantle cell lymphoma. Blood 104 (2004) 175a [Abstract 608]
    • (2004) Blood , vol.104
    • Belch, A.1    Kouroukis, C.T.2    Crump, M.3
  • 177
    • 23844519367 scopus 로고    scopus 로고
    • Bortezomib in patients with relapsed or refractory mantle cell lymphoma (MCL): preliminary results of the PINNACLE study
    • [Abstract 6563]
    • Goy A., Bernstein S., Kahl B., et al. Bortezomib in patients with relapsed or refractory mantle cell lymphoma (MCL): preliminary results of the PINNACLE study. J Clin Oncol 23 (2005) 575s [Abstract 6563]
    • (2005) J Clin Oncol , vol.23
    • Goy, A.1    Bernstein, S.2    Kahl, B.3
  • 178
    • 23644452770 scopus 로고    scopus 로고
    • ®) in patients (pts) with relapsed/refractory non-Hodgkin's lymphoma (NHL) and Hodgkin's disease (HD)
    • [Abstract 1386]
    • ®) in patients (pts) with relapsed/refractory non-Hodgkin's lymphoma (NHL) and Hodgkin's disease (HD). Blood 104 (2004) 389a [Abstract 1386]
    • (2004) Blood , vol.104
    • Strauss, S.J.1    Maharaj, L.2    Stec, J.3
  • 179
    • 20044369803 scopus 로고    scopus 로고
    • ®) in a phase II study of patients with previously untreated or treated Waldenström's macroglobulinemia (WM)
    • [Abstract 3278]
    • ®) in a phase II study of patients with previously untreated or treated Waldenström's macroglobulinemia (WM). Blood 104 (2004) 896a [Abstract 3278]
    • (2004) Blood , vol.104
    • Chen, C.I.1    White, D.2    Kouroukis, C.T.3
  • 180
    • 18844465632 scopus 로고    scopus 로고
    • Constitutive nuclear factor-kappaB-RelA activation is required for proliferation and survival of Hodgkin's disease tumor cells
    • Bargou R.C., Emmerich F., Krappmann D., et al. Constitutive nuclear factor-kappaB-RelA activation is required for proliferation and survival of Hodgkin's disease tumor cells. J Clin Invest 100 (1997) 2961-2969
    • (1997) J Clin Invest , vol.100 , pp. 2961-2969
    • Bargou, R.C.1    Emmerich, F.2    Krappmann, D.3
  • 181
    • 21044439454 scopus 로고    scopus 로고
    • ®) for the treatment of relapsed classical Hodgkin's disease
    • [Abstract 2638]
    • ®) for the treatment of relapsed classical Hodgkin's disease. Blood 104 (2004) 722a [Abstract 2638]
    • (2004) Blood , vol.104
    • Younes, A.1    Pro, B.2    Romaguera, J.3    Dang, N.4
  • 182
    • 16844375813 scopus 로고    scopus 로고
    • Phase 2 study of three doses of single agent bortezomib in patients with fludarabine-refractory B-cell CLL
    • [Abstract 4841]
    • Faderl S., Rai K.R., Gribben J., et al. Phase 2 study of three doses of single agent bortezomib in patients with fludarabine-refractory B-cell CLL. Blood 104 (2004) [Abstract 4841]
    • (2004) Blood , vol.104
    • Faderl, S.1    Rai, K.R.2    Gribben, J.3
  • 183
    • 24544475064 scopus 로고    scopus 로고
    • ®, formerly PS-341) for patients with imatinib-refractory chronic myeloid leukemia (CML) in chronic (CP) or accelerated phase (AP)
    • [Abstract 4971]
    • ®, formerly PS-341) for patients with imatinib-refractory chronic myeloid leukemia (CML) in chronic (CP) or accelerated phase (AP). Blood 102 (2003) [Abstract 4971]
    • (2003) Blood , vol.102
    • Cortes, J.1    Giles, F.2    O'Brien, S.3
  • 184
    • 20444433230 scopus 로고    scopus 로고
    • Bortezomib or high-dose dexamethasone for relapsed multiple myeloma
    • Richardson P.G., Sonneveld P., Schuster M.W., et al. Bortezomib or high-dose dexamethasone for relapsed multiple myeloma. N Engl J Med 352 (2005) 2487-2498
    • (2005) N Engl J Med , vol.352 , pp. 2487-2498
    • Richardson, P.G.1    Sonneveld, P.2    Schuster, M.W.3
  • 185
    • 30944436753 scopus 로고    scopus 로고
    • Bortezomib appears to overcome poor prognosis conferred by chromosome 13 deletion in phase 2 and 3 trials
    • [Abstract 6501]
    • Jagannath S., Richardson P.G., Sonneveld P., et al. Bortezomib appears to overcome poor prognosis conferred by chromosome 13 deletion in phase 2 and 3 trials. J Clin Oncol 24 (2005) 560s [Abstract 6501]
    • (2005) J Clin Oncol , vol.24
    • Jagannath, S.1    Richardson, P.G.2    Sonneveld, P.3
  • 186
    • 20044381304 scopus 로고    scopus 로고
    • Bortezomib in recurrent and/or refractory multiple myeloma. Initial clinical experience in patients with impared renal function
    • Jagannath S., Barlogie B., Berenson J.R., et al. Bortezomib in recurrent and/or refractory multiple myeloma. Initial clinical experience in patients with impared renal function. Cancer 103 (2005) 1195-1200
    • (2005) Cancer , vol.103 , pp. 1195-1200
    • Jagannath, S.1    Barlogie, B.2    Berenson, J.R.3
  • 187
    • 32844455809 scopus 로고    scopus 로고
    • Reversal of advanced renal dysfunction on bortezomib treatment in multiple myeloma patients
    • [Abstract 6714]
    • Mohrbacher A., and Levine A.M. Reversal of advanced renal dysfunction on bortezomib treatment in multiple myeloma patients. J Clin Oncol 23 (2005) 612s [Abstract 6714]
    • (2005) J Clin Oncol , vol.23
    • Mohrbacher, A.1    Levine, A.M.2
  • 188
    • 33746502818 scopus 로고    scopus 로고
    • Response to bortezomib (BOR) and bone metabolism in multiple myeloma patients
    • [Abstract 6536]
    • Zangari M., Esseltine D.L., Najarian K., et al. Response to bortezomib (BOR) and bone metabolism in multiple myeloma patients. J Clin Oncol 23 (2005) 569s [Abstract 6536]
    • (2005) J Clin Oncol , vol.23
    • Zangari, M.1    Esseltine, D.L.2    Najarian, K.3
  • 189
    • 0036017391 scopus 로고    scopus 로고
    • Protein degradation and the generation of MHC class I-presented peptides
    • Rock K.L., York I.A., Saric T., and Goldberg A.L. Protein degradation and the generation of MHC class I-presented peptides. Adv Immunol 80 (2002) 1-70
    • (2002) Adv Immunol , vol.80 , pp. 1-70
    • Rock, K.L.1    York, I.A.2    Saric, T.3    Goldberg, A.L.4
  • 190
    • 0031974234 scopus 로고    scopus 로고
    • Induction of primary, human antigen-specific cytotoxic T lymphocytes in vitro using dendritic cells pulsed with peptides
    • Wong C., Morse M., and Nair S.K. Induction of primary, human antigen-specific cytotoxic T lymphocytes in vitro using dendritic cells pulsed with peptides. J Immunother 21 (1998) 32-40
    • (1998) J Immunother , vol.21 , pp. 32-40
    • Wong, C.1    Morse, M.2    Nair, S.K.3
  • 191
    • 0034650796 scopus 로고    scopus 로고
    • Induction of anti-tumor immunity by proteasome-inhibited syngeneic fibroblasts pulsed with a modified TAA peptide
    • El-Shami K.M., Tirosh B., Popovic D., et al. Induction of anti-tumor immunity by proteasome-inhibited syngeneic fibroblasts pulsed with a modified TAA peptide. Int J Cancer 85 (2000) 236-242
    • (2000) Int J Cancer , vol.85 , pp. 236-242
    • El-Shami, K.M.1    Tirosh, B.2    Popovic, D.3
  • 192
    • 2542599273 scopus 로고    scopus 로고
    • Inhibition of acute graft-versus-host disease with retention of graft-versus-tumor effects by the proteasome inhibitor bortezomib
    • Sun K., Welniak L.A., Panoskaltsis-Mortari A., et al. Inhibition of acute graft-versus-host disease with retention of graft-versus-tumor effects by the proteasome inhibitor bortezomib. Proc Natl Acad Sci USA 101 (2004) 8120-8125
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8120-8125
    • Sun, K.1    Welniak, L.A.2    Panoskaltsis-Mortari, A.3
  • 193
    • 33746560969 scopus 로고    scopus 로고
    • A novel orally available proteasome inhibitor NPI-0052 induces killing in multiple myeloma cells resistant to conventional and bortezomib therapies
    • [Abstract 2405]
    • Chauhan D., Li G., Podar K., et al. A novel orally available proteasome inhibitor NPI-0052 induces killing in multiple myeloma cells resistant to conventional and bortezomib therapies. Blood 104 (2004) 661a [Abstract 2405]
    • (2004) Blood , vol.104
    • Chauhan, D.1    Li, G.2    Podar, K.3
  • 194
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • Takayama S., Reed J.C., and Homma S. Heat-shock proteins as regulators of apoptosis. Oncogene 22 (2003) 9041-9047
    • (2003) Oncogene , vol.22 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 195
    • 0141484615 scopus 로고    scopus 로고
    • A high-affinity conformation of HSP-90 confers tumour selectivity on HSP-90 inhibitors
    • Kamal A., Thao L., Sensintaffar J., et al. A high-affinity conformation of HSP-90 confers tumour selectivity on HSP-90 inhibitors. Nature 425 (2003) 407-410
    • (2003) Nature , vol.425 , pp. 407-410
    • Kamal, A.1    Thao, L.2    Sensintaffar, J.3
  • 196
    • 3042553538 scopus 로고    scopus 로고
    • Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor HSP-90
    • Vilenchik M., Solit D., Basso A., et al. Targeting wide-range oncogenic transformation via PU24FCl, a specific inhibitor of tumor HSP-90. Chem Biol 11 (2004) 787-797
    • (2004) Chem Biol , vol.11 , pp. 787-797
    • Vilenchik, M.1    Solit, D.2    Basso, A.3
  • 197
    • 0026211346 scopus 로고
    • Expression of heat shock protein 70 and c-Myc protein in human breast cancer: an immunohistochemical study
    • Tauchi K., Tsutsumi Y., Hori S., Yoshimura S., Osamura R.Y., and Watanabe K. Expression of heat shock protein 70 and c-Myc protein in human breast cancer: an immunohistochemical study. Jpn J Clin Oncol 21 (1991) 256-263
    • (1991) Jpn J Clin Oncol , vol.21 , pp. 256-263
    • Tauchi, K.1    Tsutsumi, Y.2    Hori, S.3    Yoshimura, S.4    Osamura, R.Y.5    Watanabe, K.6
  • 198
    • 0027503365 scopus 로고
    • Heat shock protein HSP-70 in patients with axillary lymph node-negative breast cancer: prognostic implications
    • Ciocca D.R., Clark G.M., Tandon A.K., Fuqua S.A., Welch W.J., and McGuire W.L. Heat shock protein HSP-70 in patients with axillary lymph node-negative breast cancer: prognostic implications. J Natl Cancer Inst 85 (1993) 570-574
    • (1993) J Natl Cancer Inst , vol.85 , pp. 570-574
    • Ciocca, D.R.1    Clark, G.M.2    Tandon, A.K.3    Fuqua, S.A.4    Welch, W.J.5    McGuire, W.L.6
  • 199
    • 0033994048 scopus 로고    scopus 로고
    • Overexpression of the heat shock protein HSP-70 family and p53 protein and prognosis for patients with gastric cancer
    • Maehara Y., Oki E., Abe T., et al. Overexpression of the heat shock protein HSP-70 family and p53 protein and prognosis for patients with gastric cancer. Oncology 58 (2000) 144-151
    • (2000) Oncology , vol.58 , pp. 144-151
    • Maehara, Y.1    Oki, E.2    Abe, T.3
  • 200
    • 0033001952 scopus 로고    scopus 로고
    • Preoperative treatment of rectal cancer with radiation, chemotherapy and hyperthermia: analysis of treatment efficacy and heat-shock response
    • Rau B., Gaestel M., Wust P., et al. Preoperative treatment of rectal cancer with radiation, chemotherapy and hyperthermia: analysis of treatment efficacy and heat-shock response. Radiat Res 151 (1999) 479-488
    • (1999) Radiat Res , vol.151 , pp. 479-488
    • Rau, B.1    Gaestel, M.2    Wust, P.3
  • 201
    • 0030750217 scopus 로고    scopus 로고
    • Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients
    • Santarosa M., Favaro D., Quaia M., and Galligioni E. Expression of heat shock protein 72 in renal cell carcinoma: possible role and prognostic implications in cancer patients. Eur J Cancer 33 (1997) 873-877
    • (1997) Eur J Cancer , vol.33 , pp. 873-877
    • Santarosa, M.1    Favaro, D.2    Quaia, M.3    Galligioni, E.4
  • 202
    • 0029586916 scopus 로고
    • Expression of the heat shock protein HSP-27 in human ovarian cancer
    • Langdon S.P., Rabiasz G.J., Hirst G.L., et al. Expression of the heat shock protein HSP-27 in human ovarian cancer. Clin Cancer Res 1 (1995) 1603-1609
    • (1995) Clin Cancer Res , vol.1 , pp. 1603-1609
    • Langdon, S.P.1    Rabiasz, G.J.2    Hirst, G.L.3
  • 203
    • 0034671358 scopus 로고    scopus 로고
    • Heat shock protein expression independently predicts clinical outcome in prostate cancer
    • Cornford P.A., Dodson A.R., Parsons K.F., et al. Heat shock protein expression independently predicts clinical outcome in prostate cancer. Cancer Res 60 (2000) 7099-7105
    • (2000) Cancer Res , vol.60 , pp. 7099-7105
    • Cornford, P.A.1    Dodson, A.R.2    Parsons, K.F.3
  • 204
    • 0026664393 scopus 로고
    • High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells
    • Yufu Y., Nishimura J., and Nawata H. High constitutive expression of heat shock protein 90 alpha in human acute leukemia cells. Leuk Res 16 (1992) 597-605
    • (1992) Leuk Res , vol.16 , pp. 597-605
    • Yufu, Y.1    Nishimura, J.2    Nawata, H.3
  • 205
    • 0842329639 scopus 로고    scopus 로고
    • Induction of HSP-90 protein expression in malignant melanomas and melanoma metastases
    • Becker B., Multhoff G., Farkas B., et al. Induction of HSP-90 protein expression in malignant melanomas and melanoma metastases. Exp Dermatol 13 (2004) 27-32
    • (2004) Exp Dermatol , vol.13 , pp. 27-32
    • Becker, B.1    Multhoff, G.2    Farkas, B.3
  • 206
    • 0029849363 scopus 로고    scopus 로고
    • Expression and roles of heat shock proteins in human breast cancer
    • Yano M., Naito Z., Tanaka S., and Asano G. Expression and roles of heat shock proteins in human breast cancer. Jpn J Cancer Res 87 (1996) 908-915
    • (1996) Jpn J Cancer Res , vol.87 , pp. 908-915
    • Yano, M.1    Naito, Z.2    Tanaka, S.3    Asano, G.4
  • 207
    • 0033988478 scopus 로고    scopus 로고
    • Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy
    • Trieb K., Gerth R., Holzer G., Grohs J.G., Berger P., and Kotz R. Antibodies to heat shock protein 90 in osteosarcoma patients correlate with response to neoadjuvant chemotherapy. Br J Cancer 82 (2000) 85-87
    • (2000) Br J Cancer , vol.82 , pp. 85-87
    • Trieb, K.1    Gerth, R.2    Holzer, G.3    Grohs, J.G.4    Berger, P.5    Kotz, R.6
  • 208
    • 14844282315 scopus 로고    scopus 로고
    • Correlation between clinicopathology and expression of heat shock protein 70 and glucose-regulated protein 94 in human colonic adenocarcinoma
    • Wang X.P., Qiu F.R., Liu G.Z., and Chen R.F. Correlation between clinicopathology and expression of heat shock protein 70 and glucose-regulated protein 94 in human colonic adenocarcinoma. World J Gastroenterol 11 (2005) 1056-1059
    • (2005) World J Gastroenterol , vol.11 , pp. 1056-1059
    • Wang, X.P.1    Qiu, F.R.2    Liu, G.Z.3    Chen, R.F.4
  • 209
    • 0032058966 scopus 로고    scopus 로고
    • Autoantibodies to the 90 kDa heat shock protein and poor survival in breast cancer patients
    • Conroy S.E., Sasieni P.D., Fentiman I., and Latchman D.S. Autoantibodies to the 90 kDa heat shock protein and poor survival in breast cancer patients. Eur J Cancer 34 (1998) 942-943
    • (1998) Eur J Cancer , vol.34 , pp. 942-943
    • Conroy, S.E.1    Sasieni, P.D.2    Fentiman, I.3    Latchman, D.S.4
  • 210
    • 0030667932 scopus 로고    scopus 로고
    • In vivo functions of the Saccharomyces cerevisiae HSP-90 chaperone
    • Nathan D.F., Vos M.H., and Lindquist S. In vivo functions of the Saccharomyces cerevisiae HSP-90 chaperone. Proc Natl Acad Sci USA 94 (1997) 12949-12956
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12949-12956
    • Nathan, D.F.1    Vos, M.H.2    Lindquist, S.3
  • 212
    • 0346996448 scopus 로고    scopus 로고
    • Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts
    • Zhao C., and Wang E. Heat shock protein 90 suppresses tumor necrosis factor alpha induced apoptosis by preventing the cleavage of Bid in NIH3T3 fibroblasts. Cell Signal 16 (2004) 313-321
    • (2004) Cell Signal , vol.16 , pp. 313-321
    • Zhao, C.1    Wang, E.2
  • 213
    • 0034718540 scopus 로고    scopus 로고
    • Modulation of Akt kinase activity by binding to HSP-90
    • Sato S., Fujita N., and Tsuruo T. Modulation of Akt kinase activity by binding to HSP-90. Proc Natl Acad Sci USA 97 (2000) 10832-10837
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 10832-10837
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 214
    • 0034664030 scopus 로고    scopus 로고
    • Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90
    • Pandey P., Saleh A., Nakazawa A., et al. Negative regulation of cytochrome c-mediated oligomerization of Apaf-1 and activation of procaspase-9 by heat shock protein 90. EMBO J 19 (2000) 4310-4322
    • (2000) EMBO J , vol.19 , pp. 4310-4322
    • Pandey, P.1    Saleh, A.2    Nakazawa, A.3
  • 215
    • 4143095430 scopus 로고    scopus 로고
    • Altered HSP-90 function in cancer: a unique therapeutic opportunity
    • Bagatell R., and Whitesell L. Altered HSP-90 function in cancer: a unique therapeutic opportunity. Mol Cancer Ther 3 (2004) 1021-1030
    • (2004) Mol Cancer Ther , vol.3 , pp. 1021-1030
    • Bagatell, R.1    Whitesell, L.2
  • 216
    • 2642521990 scopus 로고    scopus 로고
    • Therapeutic and diagnostic implications of HSP-90 activation
    • Kamal A., Boehm M.F., and Burrows F.J. Therapeutic and diagnostic implications of HSP-90 activation. Trends Mol Med 10 (2004) 283-290
    • (2004) Trends Mol Med , vol.10 , pp. 283-290
    • Kamal, A.1    Boehm, M.F.2    Burrows, F.J.3
  • 217
    • 0023940887 scopus 로고
    • Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A
    • Uehara Y., Murakami Y., Mizuno S., and Kawai S. Inhibition of transforming activity of tyrosine kinase oncogenes by herbimycin A. Virology 164 (1988) 294-298
    • (1988) Virology , vol.164 , pp. 294-298
    • Uehara, Y.1    Murakami, Y.2    Mizuno, S.3    Kawai, S.4
  • 218
    • 0031590456 scopus 로고    scopus 로고
    • Geldanamycin-induced destabilization of Raf-1 involves the proteasome
    • Schulte T.W., An W.G., and Neckers L.M. Geldanamycin-induced destabilization of Raf-1 involves the proteasome. Biochem Biophys Res Commun 239 (1997) 655-659
    • (1997) Biochem Biophys Res Commun , vol.239 , pp. 655-659
    • Schulte, T.W.1    An, W.G.2    Neckers, L.M.3
  • 219
    • 0030878952 scopus 로고    scopus 로고
    • Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo
    • Whitesell L., Sutphin P., An W.G., Schulte T., Blagosklonny M.V., and Neckers L. Geldanamycin-stimulated destabilization of mutated p53 is mediated by the proteasome in vivo. Oncogene 14 (1997) 2809-2816
    • (1997) Oncogene , vol.14 , pp. 2809-2816
    • Whitesell, L.1    Sutphin, P.2    An, W.G.3    Schulte, T.4    Blagosklonny, M.V.5    Neckers, L.6
  • 220
  • 221
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-Allylamino-17-demethoxygeldanamycin binds to HSP-90 and shares important biologic activities with geldanamycin
    • Schulte T.W., and Neckers L.M. The benzoquinone ansamycin 17-Allylamino-17-demethoxygeldanamycin binds to HSP-90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 42 (1998) 273-279
    • (1998) Cancer Chemother Pharmacol , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 222
    • 23044441106 scopus 로고    scopus 로고
    • Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies
    • Banerji U., O'Donnell A., Scurr M., et al. Phase I pharmacokinetic and pharmacodynamic study of 17-allylamino, 17-demethoxygeldanamycin in patients with advanced malignancies. J Clin Oncol 23 (2005) 4152-4161
    • (2005) J Clin Oncol , vol.23 , pp. 4152-4161
    • Banerji, U.1    O'Donnell, A.2    Scurr, M.3
  • 223
    • 1942485334 scopus 로고    scopus 로고
    • 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models
    • Burger A.M., Fiebig H.H., Stinson S.F., and Sausville E.A. 17-(Allylamino)-17-demethoxygeldanamycin activity in human melanoma models. Anticancer Drugs 15 (2004) 377-387
    • (2004) Anticancer Drugs , vol.15 , pp. 377-387
    • Burger, A.M.1    Fiebig, H.H.2    Stinson, S.F.3    Sausville, E.A.4
  • 224
    • 0033579175 scopus 로고    scopus 로고
    • DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90
    • Kelland L.R., Sharp S.Y., Rogers P.M., Myers T.G., and Workman P. DT-Diaphorase expression and tumor cell sensitivity to 17-allylamino, 17-demethoxygeldanamycin, an inhibitor of heat shock protein 90. J Natl Cancer Inst 91 (1999) 1940-1949
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1940-1949
    • Kelland, L.R.1    Sharp, S.Y.2    Rogers, P.M.3    Myers, T.G.4    Workman, P.5
  • 225
    • 0036091221 scopus 로고    scopus 로고
    • 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts
    • Solit D.B., Zheng F.F., Drobnjak M., et al. 17-Allylamino-17-demethoxygeldanamycin induces the degradation of androgen receptor and HER-2/neu and inhibits the growth of prostate cancer xenografts. Clin Cancer Res 8 (2002) 986-993
    • (2002) Clin Cancer Res , vol.8 , pp. 986-993
    • Solit, D.B.1    Zheng, F.F.2    Drobnjak, M.3
  • 226
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell R., Khan O., Paine-Murrieta G., Taylor C.W., Akinaga S., and Whitesell L. Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 7 (2001) 2076-2084
    • (2001) Clin Cancer Res , vol.7 , pp. 2076-2084
    • Bagatell, R.1    Khan, O.2    Paine-Murrieta, G.3    Taylor, C.W.4    Akinaga, S.5    Whitesell, L.6
  • 227
    • 4444311881 scopus 로고    scopus 로고
    • Simultaneous inhibition of HSP-90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances anti-tumor activity
    • Mimnaugh E.G., Xu W., Vos M., et al. Simultaneous inhibition of HSP-90 and the proteasome promotes protein ubiquitination, causes endoplasmic reticulum-derived cytosolic vacuolization, and enhances anti-tumor activity. Mol Cancer Ther 3 (2004) 551-566
    • (2004) Mol Cancer Ther , vol.3 , pp. 551-566
    • Mimnaugh, E.G.1    Xu, W.2    Vos, M.3
  • 228
    • 9744236616 scopus 로고    scopus 로고
    • Enhanced tumor cell radiosensitivity and abrogation of G2 and S phase arrest by the HSP-90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin
    • Bull E.E., Dote H., Brady K.J., et al. Enhanced tumor cell radiosensitivity and abrogation of G2 and S phase arrest by the HSP-90 inhibitor 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin. Clin Cancer Res 10 (2004) 8077-8084
    • (2004) Clin Cancer Res , vol.10 , pp. 8077-8084
    • Bull, E.E.1    Dote, H.2    Brady, K.J.3
  • 229
    • 3242670482 scopus 로고    scopus 로고
    • Anti-angiogenic properties of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin: an orally bioavailable heat shock protein 90 modulator
    • Kaur G., Belotti D., Burger A.M., et al. Anti-angiogenic properties of 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin: an orally bioavailable heat shock protein 90 modulator. Clin Cancer Res 10 (2004) 4813-4821
    • (2004) Clin Cancer Res , vol.10 , pp. 4813-4821
    • Kaur, G.1    Belotti, D.2    Burger, A.M.3
  • 230
    • 0028605318 scopus 로고
    • A protein kinase involved in the regulation of inflammatory cytokine biosynthesis
    • Lee J.C., Laydon J.T., McDonnell P.C., et al. A protein kinase involved in the regulation of inflammatory cytokine biosynthesis. Nature 372 (1994) 739-746
    • (1994) Nature , vol.372 , pp. 739-746
    • Lee, J.C.1    Laydon, J.T.2    McDonnell, P.C.3
  • 231
    • 17644437502 scopus 로고    scopus 로고
    • Regulation of stress-induced cytokine production by pyridinylimidazoles: inhibition of CSBP kinase
    • Gallagher T.F., Seibel G.L., Kassis S., et al. Regulation of stress-induced cytokine production by pyridinylimidazoles: inhibition of CSBP kinase. Bioorg Med Chem 5 (1997) 49-64
    • (1997) Bioorg Med Chem , vol.5 , pp. 49-64
    • Gallagher, T.F.1    Seibel, G.L.2    Kassis, S.3
  • 232
    • 14044272999 scopus 로고    scopus 로고
    • Small heat shock proteins HSP-27 and alphaB-crystallin: cytoprotective and oncogenic functions
    • Parcellier A., Schmitt E., Brunet M., Hammann A., Solary E., and Garrido C. Small heat shock proteins HSP-27 and alphaB-crystallin: cytoprotective and oncogenic functions. Antioxid Redox Signal 7 (2005) 404-413
    • (2005) Antioxid Redox Signal , vol.7 , pp. 404-413
    • Parcellier, A.1    Schmitt, E.2    Brunet, M.3    Hammann, A.4    Solary, E.5    Garrido, C.6
  • 233
    • 3543060077 scopus 로고    scopus 로고
    • Expression of heat shock protein 27 in human renal cell carcinoma
    • Sarto C., Valsecchi C., Magni F., et al. Expression of heat shock protein 27 in human renal cell carcinoma. Proteomics 4 (2004) 2252-2260
    • (2004) Proteomics , vol.4 , pp. 2252-2260
    • Sarto, C.1    Valsecchi, C.2    Magni, F.3
  • 234
    • 19444376495 scopus 로고    scopus 로고
    • HSP-27 protects AML cells against VP-16-induced apoptosis through modulation of p38 and c-Jun
    • Schepers H., Geugien M., van der Toorn M., et al. HSP-27 protects AML cells against VP-16-induced apoptosis through modulation of p38 and c-Jun. Exp Hematol 33 (2005) 660-670
    • (2005) Exp Hematol , vol.33 , pp. 660-670
    • Schepers, H.1    Geugien, M.2    van der Toorn, M.3
  • 235
    • 0037246247 scopus 로고    scopus 로고
    • On the role of HSP-27 in regulating apoptosis
    • Concannon C.G., Gorman A.M., and Samali A. On the role of HSP-27 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
  • 236
    • 0036636175 scopus 로고    scopus 로고
    • Up-regulation of HSP-27 plays a role in the resistance of human colon carcinoma HT29 cells to photooxidative stress
    • Wang H.P., Hanlon J.G., Rainbow A.J., Espiritu M., and Singh G. Up-regulation of HSP-27 plays a role in the resistance of human colon carcinoma HT29 cells to photooxidative stress. Photochem Photobiol 76 (2002) 98-104
    • (2002) Photochem Photobiol , vol.76 , pp. 98-104
    • Wang, H.P.1    Hanlon, J.G.2    Rainbow, A.J.3    Espiritu, M.4    Singh, G.5
  • 237
    • 23844517377 scopus 로고    scopus 로고
    • Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis
    • de Graauw M., Tijdens I., Cramer R., Corless S., Timms J.F., and van de Water B. Heat shock protein 27 is the major differentially phosphorylated protein involved in renal epithelial cellular stress response and controls focal adhesion organization and apoptosis. J Biol Chem (2005)
    • (2005) J Biol Chem
    • de Graauw, M.1    Tijdens, I.2    Cramer, R.3    Corless, S.4    Timms, J.F.5    van de Water, B.6
  • 239
    • 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) 8766-8776
    • (2004) Oncogene , vol.23 , pp. 8766-8776
    • Hideshima, T.1    Podar, K.2    Chauhan, D.3
  • 240
    • 20344381691 scopus 로고    scopus 로고
    • A phase I pharmacokinetic (PK) and pharmacodynamic (PD) trial of weekly 17-allylamino-17 demethoxygeldanamycin (17AAG, NSC-704057) in patients with advanced tumors
    • [Abstract 3031]
    • Ramanathan R.K., Trump D.L., Eiseman J.L., et al. A phase I pharmacokinetic (PK) and pharmacodynamic (PD) trial of weekly 17-allylamino-17 demethoxygeldanamycin (17AAG, NSC-704057) in patients with advanced tumors. J Clin Oncol 22 (2004) 14s [Abstract 3031]
    • (2004) J Clin Oncol , vol.22
    • Ramanathan, R.K.1    Trump, D.L.2    Eiseman, J.L.3
  • 241
    • 22144496224 scopus 로고    scopus 로고
    • A phase I trial of 17-allylamino-geldanamycin (17AAG) in patients with advanced cancer
    • [Abstract 3030]
    • Erlichman C., Toft D., Reid J., et al. A phase I trial of 17-allylamino-geldanamycin (17AAG) in patients with advanced cancer. J Clin Oncol 22 (2004) 14s [Abstract 3030]
    • (2004) J Clin Oncol , vol.22
    • Erlichman, C.1    Toft, D.2    Reid, J.3
  • 242
    • 18244378478 scopus 로고    scopus 로고
    • Phase 1 pharmacokinetic and pharmacodynamic trial of docetaxel and 17AAG (17-allylamino-17-demethoxygeldanamycin)
    • [Abstract 3032]
    • Solit D.B., Egorin M., Valentin G., et al. Phase 1 pharmacokinetic and pharmacodynamic trial of docetaxel and 17AAG (17-allylamino-17-demethoxygeldanamycin). J Clin Oncol 22 (2004) 14s [Abstract 3032]
    • (2004) J Clin Oncol , vol.22
    • Solit, D.B.1    Egorin, M.2    Valentin, G.3
  • 243
    • 33645835232 scopus 로고    scopus 로고
    • Phase 1 trial of 17-AAG in patients with relapsed and refractory multiple myeloma (MM)
    • [Abstract 3050]
    • Mitsiades C., Chanan-Khan A., Alsina M., et al. Phase 1 trial of 17-AAG in patients with relapsed and refractory multiple myeloma (MM). J Clin Oncol 23 (2005) 16s [Abstract 3050]
    • (2005) J Clin Oncol , vol.23
    • Mitsiades, C.1    Chanan-Khan, A.2    Alsina, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.