메뉴 건너뛰기




Volumn 24, Issue 4, 2014, Pages 369-382

Proteasome inhibitor patents (2010-present)

Author keywords

Anticancer therapy; Bortezomib; Carfilzomib; Clinical trials; Drug discovery; Patents; Polyphenols; Proteasome inhibitors

Indexed keywords

GREEN TEA DERIVED POLYPHENOLIC COMPOUND; METAL COMPLEX; POLYPHENOL DERIVATIVE; PROTEASOME INHIBITOR; SALINOSPORAMIDE ANALOG; UNCLASSIFIED DRUG;

EID: 84896466672     PISSN: 13543776     EISSN: 17447674     Source Type: Journal    
DOI: 10.1517/13543776.2014.877444     Document Type: Review
Times cited : (6)

References (108)
  • 1
    • 0029353809 scopus 로고
    • The proteasome: A protein-degrading organelle?
    • Rubin DM, Finley D. The proteasome: a protein-degrading organelle? Curr Biol 1995;5:854-4
    • (1995) Curr Biol , vol.5 , pp. 854-864
    • Rubin, D.M.1    Finley, D.2
  • 2
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: Compartmentalizing protease
    • Baumeister W, Walz J, Proteolysis C. The proteasome: compartmentalizing protease. Cell 1998;92:367-80
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Proteolysis, C.3
  • 3
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll M, Ditzel L, Lowe J, et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997;386(6624):463-71
    • (1997) Nature , vol.386 , Issue.6624 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe, J.3
  • 4
    • 0036713383 scopus 로고    scopus 로고
    • Proteasome subunit Rpn1 binds ubiquitin-like protein domains
    • Elsasser S, Gali RR, Schwickart M, et al. Proteasome subunit Rpn1 binds ubiquitin-like protein domains. Nat Cell Biol 2002;4:725-30
    • (2002) Nat Cell Biol , vol.4 , pp. 725-730
    • Elsasser, S.1    Gali, R.R.2    Schwickart, M.3
  • 5
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 2004;5:177-87
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 6
    • 1542344946 scopus 로고    scopus 로고
    • Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon
    • Bose S, Stratford F, Broadfoot K, et al. Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon. Biochem J 2004;378:177-84
    • (2004) Biochem J , vol.378 , pp. 177-184
    • Bose, S.1    Stratford, F.2    Broadfoot, K.3
  • 7
    • 84896487374 scopus 로고    scopus 로고
    • 20S proteasome and its inhibitors: Crystallographic knowledge for drug development
    • Borissenko L, Groll M. 20S proteasome and its inhibitors: crystallographic knowledge for drug development. Chem Inform 2007;38:687-717
    • (2007) Chem Inform , vol.38 , pp. 687-717
    • Borissenko, L.1    Groll, M.2
  • 8
    • 78649350792 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and assays to determine responses to inhibitors
    • Tsvetkov L, Nanjundan M, Domino M, et al. The ubiquitin-proteasome system and assays to determine responses to inhibitors. Expert Opin Drug Discov 2010;5:1221-36
    • (2010) Expert Opin Drug Discov , vol.5 , pp. 1221-1236
    • Tsvetkov, L.1    Nanjundan, M.2    Domino, M.3
  • 9
    • 84856373151 scopus 로고    scopus 로고
    • Proteasome inhibitors: An expanding army attacking a unique target
    • Kisselev AF, van der Linden WA, Overkleeft HS. Proteasome inhibitors: an expanding army attacking a unique target. Chem Biol 2012;19:99-115
    • (2012) Chem Biol , vol.19 , pp. 99-115
    • Kisselev, A.F.1    Van Der Linden, W.A.2    Overkleeft, H.S.3
  • 10
    • 1042278905 scopus 로고    scopus 로고
    • Proteasome and peptidase function in MHC-class-I-mediated antigen presentation
    • Kloetzel PM, Ossendorp F. Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr Opin Immunol 2004;16:76-81
    • (2004) Curr Opin Immunol , vol.16 , pp. 76-81
    • Kloetzel, P.M.1    Ossendorp, F.2
  • 11
    • 44749085669 scopus 로고    scopus 로고
    • Thymoproteasome: Probable role in generating positively selecting peptides
    • Murata S, Takahama Y, Tanaka K. Thymoproteasome: probable role in generating positively selecting peptides. Curr Opin Immunol 2008;20:192-6
    • (2008) Curr Opin Immunol , vol.20 , pp. 192-196
    • Murata, S.1    Takahama, Y.2    Tanaka, K.3
  • 12
    • 0033920566 scopus 로고    scopus 로고
    • Protease inhibitor-induced apoptosis: Accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition
    • An W, Hwang S, Trepel J, et al. Protease inhibitor-induced apoptosis: accumulation of wt p53, p21WAF1/CIP1, and induction of apoptosis are independent markers of proteasome inhibition. Leukemia 2000; 14: 1276
    • (2000) Leukemia , vol.14 , pp. 1276
    • An, W.1    Hwang, S.2    Trepel, J.3
  • 13
    • 14544303662 scopus 로고    scopus 로고
    • Proteasome inhibition as a novel therapeutic target in human cancer
    • Rajkumar SV, Richardson PG, Hideshima T, et al. Proteasome inhibition as a novel therapeutic target in human cancer. J Clin Oncol 2005;23:630-9
    • (2005) J Clin Oncol , vol.23 , pp. 630-639
    • Rajkumar, S.V.1    Richardson, P.G.2    Hideshima, T.3
  • 14
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond J, Cohen G. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002;16:433
    • (2002) Leukemia , vol.16 , pp. 433
    • Almond, J.1    Cohen, G.2
  • 15
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches
    • Paul S. Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. Bioessays 2008;30:1172-84
    • (2008) Bioessays , vol.30 , pp. 1172-1184
    • Paul, S.1
  • 16
    • 77649162855 scopus 로고    scopus 로고
    • Sent to destroy: The ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease
    • Willis MS, Townley-Tilson WD, Kang EY, et al. Sent to destroy: the ubiquitin proteasome system regulates cell signaling and protein quality control in cardiovascular development and disease. Circ Res 2010;106:463-78
    • (2010) Circ Res , vol.106 , pp. 463-478
    • Willis, M.S.1    Townley-Tilson, W.D.2    Kang, E.Y.3
  • 17
    • 72949089694 scopus 로고    scopus 로고
    • Proteasome inhibition during myocardial infarction
    • Yu X, Kem DC. Proteasome inhibition during myocardial infarction. Cardiovasc Res 2010;85:312-20
    • (2010) Cardiovasc Res , vol.85 , pp. 312-320
    • Yu, X.1    Kem, D.C.2
  • 18
    • 78650840827 scopus 로고    scopus 로고
    • The role of proteasome inhibition with bortezomib in the treatment of antibody-mediated rejection after kidney-only or kidney-combined organ transplantation
    • Flechner SM, Fatica R, Askar M, et al. The role of proteasome inhibition with bortezomib in the treatment of antibody-mediated rejection after kidney-only or kidney-combined organ transplantation. Transplantation 2010;90:1486-92
    • (2010) Transplantation , vol.90 , pp. 1486-1492
    • Flechner, S.M.1    Fatica, R.2    Askar, M.3
  • 19
  • 20
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev AF, Goldberg AL. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001;8:739-58
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 21
    • 0037376230 scopus 로고    scopus 로고
    • Potential for proteasome inhibition in the treatment of cancer
    • Adams J. Potential for proteasome inhibition in the treatment of cancer. Drug Discov Today 2003;8(7):307-15
    • (2003) Drug Discov Today , vol.8 , Issue.7 , pp. 307-315
    • Adams, J.1
  • 22
    • 67650754085 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part I: Comprehensive understanding of the SAR of alpha-amino acid boronates
    • Zhu Y, Zhao X, Zhu X, et al. Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part I: comprehensive understanding of the SAR of alpha-amino acid boronates. J Med Chem 2009;52:4192-9
    • (2009) J Med Chem , vol.52 , pp. 4192-4199
    • Zhu, Y.1    Zhao, X.2    Zhu, X.3
  • 23
    • 84860436602 scopus 로고    scopus 로고
    • Advances in the understanding of mechanisms and therapeutic use of bortezomib
    • Mujtaba T, Dou Q. Advances in the understanding of mechanisms and therapeutic use of bortezomib. Discov Med 2011;12:471-80
    • (2011) Discov Med , vol.12 , pp. 471-480
    • Mujtaba, T.1    Dou, Q.2
  • 24
    • 4644248931 scopus 로고    scopus 로고
    • Phase II study of the proteasome inhibitor bortezomib (PS-341) in patients with metastatic neuroendocrine tumors
    • Shah MH, Young D, Kindler HL, et al. Phase II study of the proteasome inhibitor bortezomib (PS-341) in patients with metastatic neuroendocrine tumors. Clin Cancer Res 2004;10:6111-18
    • (2004) Clin Cancer Res , vol.10 , pp. 6111-6118
    • Shah, M.H.1    Young, D.2    Kindler, H.L.3
  • 25
    • 4644304196 scopus 로고    scopus 로고
    • Phase II trial of bortezomib for patients with advanced renal cell carcinoma
    • Kondagunta GV, Drucker B, Schwartz L, et al. Phase II trial of bortezomib for patients with advanced renal cell carcinoma. J Clin Oncol 2004;22:3720-5
    • (2004) J Clin Oncol , vol.22 , pp. 3720-3725
    • Kondagunta, G.V.1    Drucker, B.2    Schwartz, L.3
  • 26
    • 20444364475 scopus 로고    scopus 로고
    • A phase II study of bortezomib in the treatment of metastatic malignant melanoma
    • Markovic SN, Geyer SM, Dawkins F, et al. A phase II study of bortezomib in the treatment of metastatic malignant melanoma. Cancer 2005;103:2584-9
    • (2005) Cancer , vol.103 , pp. 2584-2589
    • Markovic, S.N.1    Geyer, S.M.2    Dawkins, F.3
  • 32
    • 84873893188 scopus 로고    scopus 로고
    • Carfilzomib: A novel treatment in relapsed and refractory multiple myeloma
    • Fostier K, De Becker A, Schots R. Carfilzomib: a novel treatment in relapsed and refractory multiple myeloma. Oncol Targets Ther 2012;5:237
    • (2012) Oncol Targets Ther , vol.5 , pp. 237
    • Fostier, K.1    De Becker, A.2    Schots, R.3
  • 33
    • 36148944490 scopus 로고    scopus 로고
    • Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma
    • Kuhn DJ, Chen Q, Voorhees PM, et al. Potent activity of carfilzomib, a novel, irreversible inhibitor of the ubiquitin-proteasome pathway, against preclinical models of multiple myeloma. Blood 2007;110:3281-90
    • (2007) Blood , vol.110 , pp. 3281-3290
    • Kuhn, D.J.1    Chen, Q.2    Voorhees, P.M.3
  • 34
    • 34447116376 scopus 로고    scopus 로고
    • Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome
    • Demo SD, Kirk CJ, Aujay MA, et al. Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. Cancer Res 2007;67:6383-91
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 41
    • 84896459114 scopus 로고    scopus 로고
    • US Food and Drug Administration
    • US Food and Drug Administration. Approved Drugs-Carfilzomib. 2012. Available from: http://www.fda. gov/Drugs/InformationOnDrugs/ApprovedDrugs/ ucm312945.htm
    • (2012) Approved Drugs-Carfilzomib.
  • 42
    • 33744924884 scopus 로고    scopus 로고
    • Microarray-assisted pathway analysis identifies mitogen-activated protein kinase signaling as a mediator of resistance to the green tea polyphenol epigallocatechin 3-gallate in her-2/neu-overexpressing breast cancer cells
    • Guo S, Lu J, Subramanian A, et al. Microarray-assisted pathway analysis identifies mitogen-activated protein kinase signaling as a mediator of resistance to the green tea polyphenol epigallocatechin 3-gallate in her-2/neu-overexpressing breast cancer cells. Cancer Res 2006;66:5322-9
    • (2006) Cancer Res , vol.66 , pp. 5322-5329
    • Guo, S.1    Lu, J.2    Subramanian, A.3
  • 43
    • 33745627071 scopus 로고    scopus 로고
    • Green tea, black tea and breast cancer risk: A meta-analysis of epidemiological studies
    • Sun CL, Yuan JM, Koh WP, et al. Green tea, black tea and breast cancer risk: a meta-analysis of epidemiological studies. Carcinogenesis 2006;27:1310-15
    • (2006) Carcinogenesis , vol.27 , pp. 1310-1315
    • Sun, C.L.1    Yuan, J.M.2    Koh, W.P.3
  • 44
    • 0035731418 scopus 로고    scopus 로고
    • Green tea and its catechins inhibit breast cancer xenografts
    • Sartippour MR, Heber D, Ma J, et al. Green tea and its catechins inhibit breast cancer xenografts. Nutr Cancer 2001;40:149-56
    • (2001) Nutr Cancer , vol.40 , pp. 149-156
    • Sartippour, M.R.1    Heber, D.2    Ma, J.3
  • 45
    • 0031878494 scopus 로고    scopus 로고
    • Inhibition of spontaneous formation of lung tumors and rhabdomyosarcomas in A/J mice by black and green tea
    • Landau JM, Wang ZY, Yang GY, et al. Inhibition of spontaneous formation of lung tumors and rhabdomyosarcomas in A/J mice by black and green tea. Carcinogenesis 1998;19:501-7
    • (1998) Carcinogenesis , vol.19 , pp. 501-507
    • Landau, J.M.1    Wang, Z.Y.2    Yang, G.Y.3
  • 46
    • 21144458334 scopus 로고    scopus 로고
    • Synergistic effect ofgreen tea catechins on cell growth and apoptosis induction in gastric carcinoma cells
    • Horie N, Hirabayashi N, Takahashi Y, et al. Synergistic effect ofgreen tea catechins on cell growth and apoptosis induction in gastric carcinoma cells. Biol Pharm Bull 2005;28:574-9
    • (2005) Biol Pharm Bull , vol.28 , pp. 574-579
    • Horie, N.1    Hirabayashi, N.2    Takahashi, Y.3
  • 47
    • 31544473720 scopus 로고    scopus 로고
    • Chemoprevention of human prostate cancer by oral administration of green tea catechins in volunteers with high-grade prostate intraepithelial neoplasia: A preliminary report from a one-year proof-of-principle study
    • Bettuzzi S, Brausi M, Rizzi F, et al. Chemoprevention of human prostate cancer by oral administration of green tea catechins in volunteers with high-grade prostate intraepithelial neoplasia: a preliminary report from a one-year proof-of-principle study. Cancer Res 2006;66:1234-40
    • (2006) Cancer Res , vol.66 , pp. 1234-1240
    • Bettuzzi, S.1    Brausi, M.2    Rizzi, F.3
  • 48
    • 0042738859 scopus 로고    scopus 로고
    • Inhibition of bladder tumor growth by the green tea derivative epigallocatechin-3-gallate
    • Kemberling J, Hampton JA, Keck RW, et al. Inhibition of bladder tumor growth by the green tea derivative epigallocatechin-3-gallate. J Urol 2003;170:773-6
    • (2003) J Urol , vol.170 , pp. 773-776
    • Kemberling, J.1    Hampton, J.A.2    Keck, R.W.3
  • 49
    • 0347417005 scopus 로고    scopus 로고
    • Docking studies and model development of tea polyphenol proteasome inhibitors: Applications to rational drug design
    • Smith DM, Daniel KG, Wang Z, et al. Docking studies and model development of tea polyphenol proteasome inhibitors: applications to rational drug design. Proteins 2003;54:58-70
    • (2003) Proteins , vol.54 , pp. 58-70
    • Smith, D.M.1    Daniel, K.G.2    Wang, Z.3
  • 50
    • 0035918278 scopus 로고    scopus 로고
    • Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo
    • Nam S, Smith DM, Dou QP. Ester bond-containing tea polyphenols potently inhibit proteasome activity in vitro and in vivo. J Biol Chem 2001;276:13322-30
    • (2001) J Biol Chem , vol.276 , pp. 13322-13330
    • Nam, S.1    Smith, D.M.2    Dou, Q.P.3
  • 51
    • 54849417391 scopus 로고    scopus 로고
    • Natural polyphenols as proteasome modulators and their role as anti-cancer compounds
    • Bonfili L, Cecarini V, Amici M, et al. Natural polyphenols as proteasome modulators and their role as anti-cancer compounds. FEBS J 2008;275:5512-26
    • (2008) FEBS J , vol.275 , pp. 5512-5526
    • Bonfili, L.1    Cecarini, V.2    Amici, M.3
  • 55
    • 33751275548 scopus 로고    scopus 로고
    • A novel anticancer gold(III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S proteasome in human breast cancer cell cultures and xenografts
    • Milacic V, Chen D, Ronconi L, et al. A novel anticancer gold(III) dithiocarbamate compound inhibits the activity of a purified 20S proteasome and 26S proteasome in human breast cancer cell cultures and xenografts. Cancer Res 2006;66:10478-86
    • (2006) Cancer Res , vol.66 , pp. 10478-10486
    • Milacic, V.1    Chen, D.2    Ronconi, L.3
  • 56
    • 64449085700 scopus 로고    scopus 로고
    • The tumor proteasome as a novel target for gold (III) complexes: Implications for breast cancer therapy
    • Milacic V, Dou QP. The tumor proteasome as a novel target for gold (III) complexes: implications for breast cancer therapy. Coord Chem Rev 2009;253:1649-60
    • (2009) Coord Chem Rev , vol.253 , pp. 1649-1660
    • Milacic, V.1    Dou, Q.P.2
  • 57
    • 54549114503 scopus 로고    scopus 로고
    • Ni (II), Cu (II), and Zn (II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells
    • Cvek B, Milacic V, Taraba J, et al. Ni (II), Cu (II), and Zn (II) diethyldithiocarbamate complexes show various activities against the proteasome in breast cancer cells. J Med Chem 2008;51:6256-8
    • (2008) J Med Chem , vol.51 , pp. 6256-6258
    • Cvek, B.1    Milacic, V.2    Taraba, J.3
  • 58
    • 67649969204 scopus 로고    scopus 로고
    • Comparative activities of nickel (II) and zinc (II) complexes of asymmetric [NN O] ligands as 26S proteasome inhibitors
    • Frezza M, Hindo SS, Tomco D, et al. Comparative activities of nickel (II) and zinc (II) complexes of asymmetric [NN O] ligands as 26S proteasome inhibitors. Inorg Chem 2009;48:5928-37
    • (2009) Inorg Chem , vol.48 , pp. 5928-5937
    • Frezza, M.1    Hindo, S.S.2    Tomco, D.3
  • 59
    • 1542270307 scopus 로고    scopus 로고
    • Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells
    • Daniel KG, Gupta P, Harbach RH, et al. Organic copper complexes as a new class of proteasome inhibitors and apoptosis inducers in human cancer cells. Biochem Pharmacol 2004;67:1139-51
    • (2004) Biochem Pharmacol , vol.67 , pp. 1139-1151
    • Daniel, K.G.1    Gupta, P.2    Harbach, R.H.3
  • 60
    • 84901648175 scopus 로고    scopus 로고
    • Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells
    • Daniel KG, Chen D, Orlu S, et al. Clioquinol and pyrrolidine dithiocarbamate complex with copper to form proteasome inhibitors and apoptosis inducers in human breast cancer cells. Breast Cancer Res 2005;7:R897-908
    • (2005) Breast Cancer Res , vol.7
    • Daniel, K.G.1    Chen, D.2    Orlu, S.3
  • 61
    • 73949101373 scopus 로고    scopus 로고
    • Novel 8-hydroxylquinoline analogs induce copper-dependent proteasome inhibition and cell death in human breast cancer cells
    • Milacic V, Jiao P, Zhang B, et al. Novel 8-hydroxylquinoline analogs induce copper-dependent proteasome inhibition and cell death in human breast cancer cells. Int J Oncol 2009;35:1481-91
    • (2009) Int J Oncol , vol.35 , pp. 1481-1491
    • Milacic, V.1    Jiao, P.2    Zhang, B.3
  • 62
    • 70349911835 scopus 로고    scopus 로고
    • Metals in anticancer therapy: Copper (II) complexes as inhibitors of the 20S proteasome
    • Hindo SS, Frezza M, Tomco D, et al. Metals in anticancer therapy: copper (II) complexes as inhibitors of the 20S proteasome. Eur J Med Chem 2009;44:4353-61
    • (2009) Eur J Med Chem , vol.44 , pp. 4353-4361
    • Hindo, S.S.1    Frezza, M.2    Tomco, D.3
  • 63
    • 84868486281 scopus 로고    scopus 로고
    • Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid schiff base-copper complexes
    • Zuo J, Bi C, Fan Y, et al. Cellular and computational studies of proteasome inhibition and apoptosis induction in human cancer cells by amino acid schiff base-copper complexes. J Inorg Biochem 2013;118:83-93
    • (2013) J Inorg Biochem , vol.118 , pp. 83-93
    • Zuo, J.1    Bi, C.2    Fan, Y.3
  • 64
    • 24544480850 scopus 로고
    • Studies on derivatives of 8-hydroxyquinoline (oxine). The sensitivity and selectivity of 5-nitroso-oxine and 2-methyl-5-nitroso-oxine towards the group IIIB metals
    • Hollingshead RGW. Studies on derivatives of 8-hydroxyquinoline (oxine). The sensitivity and selectivity of 5-nitroso-oxine and 2-methyl-5-nitroso-oxine towards the group IIIB metals. Anal Chim Acta 1955;12:401-7
    • (1955) Anal Chim Acta , vol.12 , pp. 401-407
    • Hollingshead, R.G.W.1
  • 67
    • 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 RH, Buchanan GO, Mincer TJ, et al. Salinosporamide A: a highly cytotoxic proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew Chem Int Ed 2003;42:355-7
    • (2003) Angew Chem Int Ed , vol.42 , pp. 355-357
    • Feling, R.H.1    Buchanan, G.O.2    Mincer, T.J.3
  • 68
    • 62149103377 scopus 로고    scopus 로고
    • Discovery and development of the anticancer agent salinosporamide A (NPI-0052)
    • Fenical W, Jensen PR, Palladino MA, et al. Discovery and development of the anticancer agent salinosporamide A (NPI-0052). Bioorg Med Chem 2009;17:2175-80
    • (2009) Bioorg Med Chem , vol.17 , pp. 2175-2180
    • Fenical, W.1    Jensen, P.R.2    Palladino, M.A.3
  • 69
    • 77952564354 scopus 로고    scopus 로고
    • From natural product to clinical trials: NPI-0052 (salinosporamide A), a marine actinomycete-derived anticancer agent. Chapter 12
    • Lam KS, Lloyd GK, Neuteboom STC, et al. From natural product to clinical trials: NPI-0052 (salinosporamide A), a marine actinomycete-derived anticancer agent. Chapter 12. Nat Prod Chem Drug Discov 2010;355-73
    • (2010) Nat Prod Chem Drug Discov , pp. 355-373
    • Lam, K.S.1    Lloyd, G.K.2    Stc, N.3
  • 73
    • 38949125853 scopus 로고    scopus 로고
    • Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma
    • Chauhan D, Singh A, Brahmandam M, et al. Combination of proteasome inhibitors bortezomib and NPI-0052 trigger in vivo synergistic cytotoxicity in multiple myeloma. Blood 2008;111:1654-64
    • (2008) Blood , vol.111 , pp. 1654-1664
    • Chauhan, D.1    Singh, A.2    Brahmandam, M.3
  • 74
    • 33748300908 scopus 로고    scopus 로고
    • The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia
    • Ruiz S, Krupnik Y, Keating M, et al. The proteasome inhibitor NPI-0052 is a more effective inducer of apoptosis than bortezomib in lymphocytes from patients with chronic lymphocytic leukemia. Mol Cancer Ther 2006;5:1836-43
    • (2006) Mol Cancer Ther , vol.5 , pp. 1836-1843
    • Ruiz, S.1    Krupnik, Y.2    Keating, M.3
  • 75
    • 34347375499 scopus 로고    scopus 로고
    • NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells
    • Miller CP, Ban K, Dujka ME, et al. NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemia cells. Blood 2007;110:267-77
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3
  • 76
    • 66149121016 scopus 로고    scopus 로고
    • Caspase-8 dependent histone acetylation by a novel proteasome inhibitor, NPI-0052: A mechanism for synergy in leukemia cells
    • Miller CP, Rudra S, Keating MJ, et al. Caspase-8 dependent histone acetylation by a novel proteasome inhibitor, NPI-0052: a mechanism for synergy in leukemia cells. Blood 2009;113:4289-99
    • (2009) Blood , vol.113 , pp. 4289-4299
    • Miller, C.P.1    Rudra, S.2    Keating, M.J.3
  • 77
    • 77957991639 scopus 로고    scopus 로고
    • Design synthesis and biological evaluation of dibromotyrosine analogues inspired by marine natural products as inhibitors of human prostate cancer proliferation, invasion, and migration
    • Sallam AA, Ramasahayam S, Meyer SA, et al. Design, synthesis, and biological evaluation of dibromotyrosine analogues inspired by marine natural products as inhibitors of human prostate cancer proliferation, invasion, and migration. Bioorg Med Chem 2010;18:7446-57
    • (2010) Bioorg Med Chem , vol.18 , pp. 7446-7457
    • Sallam, A.A.1    Ramasahayam, S.2    Meyer, S.A.3
  • 78
    • 60049083840 scopus 로고    scopus 로고
    • Discovery, design, and synthesis of anti-metastatic lead phenylmethylene hydantoins inspired by marine natural products
    • Mudit M, Khanfar M, Muralidharan A, et al. Discovery, design, and synthesis of anti-metastatic lead phenylmethylene hydantoins inspired by marine natural products. Bioorg Med Chem 2009;17:1731-8
    • (2009) Bioorg Med Chem , vol.17 , pp. 1731-1738
    • Mudit, M.1    Khanfar, M.2    Muralidharan, A.3
  • 82
    • 0028286026 scopus 로고
    • Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers
    • Scanlan MJ, Raj B, Calvo B, et al. Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers. Proc Natl Acad Sci 1994;91:5657-61
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 5657-5661
    • Scanlan, M.J.1    Raj, B.2    Calvo, B.3
  • 83
    • 0037199968 scopus 로고    scopus 로고
    • Hierarchical organization of modularaity in metabolic networks
    • Ravasz E, Somera AL, Mongru DA, et al. Hierarchical organization of modularaity in metabolic networks. Science 2002;297:1551-5
    • (2002) Science , vol.297 , pp. 1551-1555
    • Ravasz, E.1    Somera, A.L.2    Mongru, D.A.3
  • 84
    • 0034609791 scopus 로고    scopus 로고
    • The large-scale organization of metabolic networks
    • Jeong H, Tombor B, Albert R, et al. The large-scale organization of metabolic networks. Nature 2000;407:651-4
    • (2000) Nature , vol.407 , pp. 651-654
    • Jeong, H.1    Tombor, B.2    Albert, R.3
  • 85
    • 0742305866 scopus 로고    scopus 로고
    • Network biology: Understanding the cell's functional organization
    • Barabasi AL, Oltvai ZN. Network biology: understanding the cell's functional organization. Nat Rev Genet 2004;5:101-13
    • (2004) Nat Rev Genet , vol.5 , pp. 101-113
    • Barabasi, A.L.1    Oltvai, Z.N.2
  • 86
    • 0037316239 scopus 로고    scopus 로고
    • Reconstruction of metabolic networks from genome data and analysis of their global structure for various organisms
    • Ma H, Zeng AP. Reconstruction of metabolic networks from genome data and analysis of their global structure for various organisms. Bioinformatics 2003;19:270-7
    • (2003) Bioinformatics , vol.19 , pp. 270-277
    • Ma, H.1    Zeng, A.P.2
  • 88
    • 0036176510 scopus 로고    scopus 로고
    • Mechanisms of cancer drug resistance
    • Gottesman MM. Mechanisms of cancer drug resistance. Annu Rev Med 2002;53:615-27
    • (2002) Annu Rev Med , vol.53 , pp. 615-627
    • Gottesman, M.M.1
  • 89
    • 16844368698 scopus 로고    scopus 로고
    • Annual review of medicine. Tumour stem cells and drug resistance
    • Dean M, Fojo T, Bates S. Annual review of medicine. Tumour stem cells and drug resistance. Nat Rev Cancer 2005;5:275-84
    • (2005) Nat Rev Cancer , vol.5 , pp. 275-284
    • Dean, M.1    Fojo, T.2    Bates, S.3
  • 92
    • 41949110089 scopus 로고    scopus 로고
    • CEP-18770: A novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib
    • Piva R, Ruggeri B, Williams M, et al. CEP-18770: a novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib. Blood 2008;111:2765-75
    • (2008) Blood , vol.111 , pp. 2765-2775
    • Piva, R.1    Ruggeri, B.2    Williams, M.3
  • 93
    • 84872109533 scopus 로고    scopus 로고
    • A first in human phase i study of the proteasome inhibitor CEP-18770 in patients with advanced solid tumours and multiple myeloma
    • Gallerani E, Zucchetti M, Brunelli D, et al. A first in human phase I study of the proteasome inhibitor CEP-18770 in patients with advanced solid tumours and multiple myeloma. Eur J Cancer 2013;49(2):290-6
    • (2013) Eur J Cancer , vol.49 , Issue.2 , pp. 290-296
    • Gallerani, E.1    Zucchetti, M.2    Brunelli, D.3
  • 95
    • 35548979078 scopus 로고    scopus 로고
    • Inhibition of Jak/STAT signaling ameliorates mice experimental nephrotic syndrome
    • Li R, Yang N, Zhang L, et al. Inhibition of Jak/STAT signaling ameliorates mice experimental nephrotic syndrome. Am J Nephrol 2007;27:580-9
    • (2007) Am J Nephrol , vol.27 , pp. 580-589
    • Li, R.1    Yang, N.2    Zhang, L.3
  • 96
    • 15944387964 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib sensitizes cells to killing by death receptor ligand TRAIL via BH3-only proteins Bik and Bim
    • Nikrad M, Johnson T, Puthalalath H, et al. The proteasome inhibitor bortezomib sensitizes cells to killing by death receptor ligand TRAIL via BH3-only proteins Bik and Bim. Mol Cancer Ther 2005;4:443-9
    • (2005) Mol Cancer Ther , vol.4 , pp. 443-449
    • Nikrad, M.1    Johnson, T.2    Puthalalath, H.3
  • 97
    • 0642349188 scopus 로고    scopus 로고
    • Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts
    • Williams S, Pettaway C, Song R, et al. Differential effects of the proteasome inhibitor bortezomib on apoptosis and angiogenesis in human prostate tumor xenografts. Mol Cancer Ther 2003;2:835-43
    • (2003) Mol Cancer Ther , vol.2 , pp. 835-843
    • Williams, S.1    Pettaway, C.2    Song, R.3
  • 98
    • 78049528598 scopus 로고    scopus 로고
    • Mechanisms of peripheral neuropathy associated with bortezomib and vincristine in patients with newly diagnosed multiple myeloma: A prospective analysis of data from the HOVON-65/GMMG-HD4 trial
    • Broyl A, Corthals SL, Jongen JL, et al. Mechanisms of peripheral neuropathy associated with bortezomib and vincristine in patients with newly diagnosed multiple myeloma: a prospective analysis of data from the HOVON-65/GMMG-HD4 trial. Lancet Oncol 2010;11:1057-65
    • (2010) Lancet Oncol , vol.11 , pp. 1057-1065
    • Broyl, A.1    Corthals, S.L.2    Jongen, J.L.3
  • 99
    • 29244454269 scopus 로고    scopus 로고
    • Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis
    • Nawrocki ST, Carew JS, Pino MS, et al. Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis. Cancer Res 2005;65:11658-66
    • (2005) Cancer Res , vol.65 , pp. 11658-11666
    • Nawrocki, S.T.1    Carew, J.S.2    Pino, M.S.3
  • 100
    • 28444436266 scopus 로고    scopus 로고
    • Risk factors and kinetics of thrombocytopenia associated with bortezomib for relapsed, refractory multiple myeloma
    • Lonial S, Waller EK, Richardson PG, et al. Risk factors and kinetics of thrombocytopenia associated with bortezomib for relapsed, refractory multiple myeloma. Blood 2005;106:3777-84
    • (2005) Blood , vol.106 , pp. 3777-3784
    • Lonial, S.1    Waller, E.K.2    Richardson, P.G.3
  • 101
    • 33750197980 scopus 로고    scopus 로고
    • Response to bortezomib and activation of osteoblasts in multiple myeloma
    • Zangari M, Yaccoby S, Cavallo F, et al. Response to bortezomib and activation of osteoblasts in multiple myeloma. Clin Lymphoma Myeloma 2006;7:109-14
    • (2006) Clin Lymphoma Myeloma , vol.7 , pp. 109-114
    • Zangari, M.1    Yaccoby, S.2    Cavallo, F.3
  • 102
    • 79960105001 scopus 로고    scopus 로고
    • Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. Pombe
    • Takeda K, Mori A, Yanagida M. Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. pombe. PloS One 2011;6:e22021
    • (2011) PloS One , vol.6
    • Takeda, K.1    Mori, A.2    Yanagida, M.3
  • 103
    • 45849152092 scopus 로고    scopus 로고
    • A novel role for a familiar protein in apoptosis induced by proteasome inhibition
    • McConkey DJ. A novel role for a familiar protein in apoptosis induced by proteasome inhibition. Cancer Cell 2008;14:1-2
    • (2008) Cancer Cell , vol.14 , pp. 1-2
    • McConkey, D.J.1
  • 104
    • 42949125866 scopus 로고    scopus 로고
    • Target specificity and off-target effects as determinants of cancer drug efficacy
    • Shoshan MC, Linder S. Target specificity and off-target effects as determinants of cancer drug efficacy. Expert Opin Drug Metab Toxicol 2008;4(3):273-80
    • (2008) Expert Opin Drug Metab Toxicol , vol.4 , Issue.3 , pp. 273-280
    • Shoshan, M.C.1    Linder, S.2
  • 105
    • 77649237033 scopus 로고    scopus 로고
    • Building on bortezomib: Second-generation proteasome inhibitors as anti-cancer therapy
    • Dick LR, Fleming PE. Building on bortezomib: second-generation proteasome inhibitors as anti-cancer therapy. Drug Discov Today 2010;15:243-9
    • (2010) Drug Discov Today , vol.15 , pp. 243-249
    • Dick, L.R.1    Fleming, P.E.2
  • 106
    • 79955498420 scopus 로고    scopus 로고
    • Nonproteasomal targets of the proteasome inhibitors bortezomib and carfilzomib: A link to clinical adverse events
    • Arastu-Kapur S, Anderl JL, Kraus M, et al. Nonproteasomal targets of the proteasome inhibitors bortezomib and carfilzomib: a link to clinical adverse events. Clin Cancer Res 2011;17:2734-43
    • (2011) Clin Cancer Res , vol.17 , pp. 2734-2743
    • Arastu-Kapur, S.1    Anderl, J.L.2    Kraus, M.3
  • 107
    • 77953163141 scopus 로고    scopus 로고
    • Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib
    • Chen S, Blank JL, Peters T, et al. Genome-wide siRNA screen for modulators of cell death induced by proteasome inhibitor bortezomib. Cancer Res 2010;70:4318-26
    • (2010) Cancer Res , vol.70 , pp. 4318-4326
    • Chen, S.1    Blank, J.L.2    Peters, T.3
  • 108
    • 45849099115 scopus 로고    scopus 로고
    • Argyrin A reveals a critical role for the tumor suppressor protein p27 in mediating antitumor activities in response to proteasome inhibition
    • Nickeleit I, Zender S, Sasse F, et al. Argyrin A reveals a critical role for the tumor suppressor protein p27 in mediating antitumor activities in response to proteasome inhibition. Cancer Cell 2008;14:23-35
    • (2008) Cancer Cell , vol.14 , pp. 23-35
    • Nickeleit, I.1    Zender, S.2    Sasse, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.