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Volumn 15, Issue 3, 2012, Pages 249-260

The ubiquitin proteasome system and efficacy of proteasome inhibitors in diseases

Author keywords

26S proteasome; Proteasome inhibitors; Ubiquitin proteasome system

Indexed keywords

AM 114; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CALPAIN; CARFILZOMIB; DELANZOMIB; EPOXOMICIN; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LACTACYSTIN; LACTACYSTIN BETA LACTONE; PROTEASOME; PROTEASOME INHIBITOR; SALINOSPORAMIDE A; TP 110; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84862529832     PISSN: 17561841     EISSN: 1756185X     Source Type: Journal    
DOI: 10.1111/j.1756-185X.2012.01737.x     Document Type: Review
Times cited : (43)

References (111)
  • 1
    • 0029347062 scopus 로고
    • New insights into proteasome function: from Archaebacteria to drug development
    • Goldberg AL, Stein R, Adams J (1995) New insights into proteasome function: from Archaebacteria to drug development. Chem Biol 2, 503-8.
    • (1995) Chem Biol , vol.2 , pp. 503-508
    • Goldberg, A.L.1    Stein, R.2    Adams, J.3
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and function of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg AL (1996) Structure and function of the 20S and 26S proteasomes. Annu Rev Biochem 65, 801-47.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 4
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted Short-lived protein
    • Chau V, Tobia JW, Bachmair A et al. (1989) A multiubiquitin chain is confined to specific lysine in a targeted Short-lived protein. Science (Washington DC) 243, 1576-83.
    • (1989) Science (Washington DC) , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobia, J.W.2    Bachmair, A.3
  • 5
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82, 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 6
    • 0034065822 scopus 로고    scopus 로고
    • Ubiquitin-mediated proteolysis: biological regulation via destruction
    • Ciechanover A, Orian A, Schwartz AL (2000) Ubiquitin-mediated proteolysis: biological regulation via destruction. BioEssays 22, 442-51.
    • (2000) BioEssays , vol.22 , pp. 442-451
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 8
    • 1542297619 scopus 로고    scopus 로고
    • Urban renewal in the nucleus: is protein turnover by proteasomes absolutely required for nuclear receptor-regulated transcription?
    • Nawaz Z, O'Malley BW (2004) Urban renewal in the nucleus: is protein turnover by proteasomes absolutely required for nuclear receptor-regulated transcription? Molec Endocrinol 18, 493-9.
    • (2004) Molec Endocrinol , vol.18 , pp. 493-499
    • Nawaz, Z.1    O'Malley, B.W.2
  • 9
    • 0034062989 scopus 로고    scopus 로고
    • Proteasome inhibition: a new strategy in cancer treatment
    • Adams J, Palombella VJ, Elliott PJ (2000) Proteasome inhibition: a new strategy in cancer treatment. Invest New Drugs 18, 109-21.
    • (2000) Invest New Drugs , vol.18 , pp. 109-121
    • Adams, J.1    Palombella, V.J.2    Elliott, P.J.3
  • 10
    • 0036680037 scopus 로고    scopus 로고
    • Preclinical and clinical evaluation of proteasome inhibitor PS-341 for the treatment of cancer
    • Adams J (2002) Preclinical and clinical evaluation of proteasome inhibitor PS-341 for the treatment of cancer. Curr Opin Chem Biol 6, 493-500.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 493-500
    • Adams, J.1
  • 12
    • 0030867774 scopus 로고    scopus 로고
    • The ubiquitin system
    • Varshavsky A (1997) The ubiquitin system. Trend Biochem Sci 22, 383-7.
    • (1997) Trend Biochem Sci , vol.22 , pp. 383-387
    • Varshavsky, A.1
  • 13
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B
    • Palombella VJ, Rando OJ, Goldberg AL et al. (1994) The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B. Cell 78, 773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3
  • 14
    • 13044316560 scopus 로고    scopus 로고
    • Role of the proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis
    • Palombella VJ, Conner EM, Fuseler JW et al. (1998) Role of the proteasome and NF-kappaB in streptococcal cell wall-induced polyarthritis. Proc Natl Acad Sci USA 95, 15671-6.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15671-15676
    • Palombella, V.J.1    Conner, E.M.2    Fuseler, J.W.3
  • 15
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz AL, Ciechanover A (1999) The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu Rev Med 50, 57-74.
    • (1999) Annu Rev Med , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 16
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40, 427-46.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 17
    • 1842486790 scopus 로고    scopus 로고
    • Ubiquitin and breast cancer
    • Ohta T, Fukuda M (2004) Ubiquitin and breast cancer. Oncogene 23, 2079-88.
    • (2004) Oncogene , vol.23 , pp. 2079-2088
    • Ohta, T.1    Fukuda, M.2
  • 18
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes
    • Etlinger JD, Goldberg AL (1977) A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc Natl Acad Sci U S A 74, 54-8.
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 19
    • 0018187738 scopus 로고
    • A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes
    • Ciechanover A, Hod Y, Hershko A (1978) A heat-stable polypeptide component of an ATP-dependent proteolytic system from reticulocytes. Biochem Biophys Res Commun 81, 1100-5.
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 1100-1105
    • Ciechanover, A.1    Hod, Y.2    Hershko, A.3
  • 20
    • 3242671372 scopus 로고    scopus 로고
    • A field guide to ubiquitylation
    • Fang S, Weissman AM (2004) A field guide to ubiquitylation. Cell Mol Life Sci 61, 1546-61.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1546-1561
    • Fang, S.1    Weissman, A.M.2
  • 21
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko A, Heller H, Elias S, Ciechanover A (1983) Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem 258, 8206-14.
    • (1983) J Biol Chem , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 23
    • 33745726659 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in cardiac physiology and pathology
    • Powell SR (2006) The ubiquitin-proteasome system in cardiac physiology and pathology. Am J Physiol Heart Circ Physiol 291, H1-19.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291
    • Powell, S.R.1
  • 24
    • 0029687633 scopus 로고    scopus 로고
    • Regulatory features of multicatalytic and 26S proteases
    • Hoffman L, Rechsteiner M (1996) Regulatory features of multicatalytic and 26S proteases. Curr Top Cell Regul 34, 1-32.
    • (1996) Curr Top Cell Regul , vol.34 , pp. 1-32
    • Hoffman, L.1    Rechsteiner, M.2
  • 25
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D, Zwickl P, Baumeister W (1999) The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 68, 1015-68.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 26
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kins: proteases in the machine age
    • Pickart CM, Cohen RE (2004) Proteasomes and their kins: proteases in the machine age. Nat Rev Mol Cell Biol 5, 177-87.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 27
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78, 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 29
    • 67749095289 scopus 로고    scopus 로고
    • Insights into the molecular architecture of the 26S proteasome
    • Nickell S, Beck F, Scheres SH et al. (2009) Insights into the molecular architecture of the 26S proteasome. Proc Natl Acad Sci USA 106, 11943-7.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11943-11947
    • Nickell, S.1    Beck, F.2    Scheres, S.H.3
  • 30
    • 0033615348 scopus 로고    scopus 로고
    • The proteasome: a macromolecular assembly designed for controlled proteolysis
    • Zwickl P, Voges D, Baumeister W (1999) The proteasome: a macromolecular assembly designed for controlled proteolysis. Philos Trans R Soc Lond B Biol Sci 354, 1501-11.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 1501-1511
    • Zwickl, P.1    Voges, D.2    Baumeister, W.3
  • 31
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel PM (2001) Antigen processing by the proteasome. Nat Rev Mol Cell Biol 2, 179-87.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 32
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino GN, Slaughter CA (1999) The proteasome, a novel protease regulated by multiple mechanisms. J Biol Chem 274, 22123-6.
    • (1999) J Biol Chem , vol.274 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 33
    • 0032488846 scopus 로고    scopus 로고
    • The proteasome: paradigm of a self-compartmentalizing protease
    • Baumeister W, Walz J, Zuhl F, Seemuller E (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92, 367-80.
    • (1998) Cell , vol.92 , pp. 367-380
    • Baumeister, W.1    Walz, J.2    Zuhl, F.3    Seemuller, E.4
  • 34
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N, Murakami Y, Minami Y, Shimbara N, Hendil KB, Tanaka K (2000) Hybrid proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 275, 14336-45.
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Shimbara, N.4    Hendil, K.B.5    Tanaka, K.6
  • 35
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: on protein death and cell life
    • Ciechanover A (1998) The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 17, 7151-60.
    • (1998) EMBO J , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 36
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: from research tools to drug candidates
    • Kisselev AF, Goldberg AL (2001) Proteasome inhibitors: from research tools to drug candidates. Chem Biol 8, 739-58.
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 37
    • 0027516156 scopus 로고
    • Proteasomes: multicatalytic proteinase complexes
    • Rivett AJ (1993) Proteasomes: multicatalytic proteinase complexes. Biochem J 291, 1-10.
    • (1993) Biochem J , vol.291 , pp. 1-10
    • Rivett, A.J.1
  • 38
    • 0029071646 scopus 로고
    • Functions of the proteasome: the lysis at the end of the tunnel
    • Goldberg AL (1995) Functions of the proteasome: the lysis at the end of the tunnel. Science 268, 522-3.
    • (1995) Science , vol.268 , pp. 522-523
    • Goldberg, A.L.1
  • 39
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L et al. (1994) Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78, 761-71.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3
  • 40
    • 0038649638 scopus 로고    scopus 로고
    • The proteasome - an emerging therapeutic target in cancer
    • Mitchell BS (2003) The proteasome - an emerging therapeutic target in cancer. N Engl J Med 348, 2597-8.
    • (2003) N Engl J Med , vol.348 , pp. 2597-2598
    • Mitchell, B.S.1
  • 41
    • 0034296394 scopus 로고    scopus 로고
    • Basic medical research award. The ubiquitin system
    • Hershko A, Ciechanover A, Varshavsky A (2000) Basic medical research award. The ubiquitin system. Nat Med 6, 1073-81.
    • (2000) Nat Med , vol.6 , pp. 1073-1081
    • Hershko, A.1    Ciechanover, A.2    Varshavsky, A.3
  • 42
    • 0033178142 scopus 로고    scopus 로고
    • Proteasome inhibitors as potential novel anticancer agents
    • Dou QP, Li B (1999) Proteasome inhibitors as potential novel anticancer agents. Drug Resist Update 2, 215-23.
    • (1999) Drug Resist Update , vol.2 , pp. 215-223
    • Dou, Q.P.1    Li, B.2
  • 43
    • 0032429122 scopus 로고    scopus 로고
    • Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts
    • An B, Goldfarb RH, Siman R, Dou QP (1998) Novel dipeptidyl proteasome inhibitors overcome Bcl-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ 5, 1062-75.
    • (1998) Cell Death Differ , vol.5 , pp. 1062-1075
    • An, B.1    Goldfarb, R.H.2    Siman, R.3    Dou, Q.P.4
  • 45
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: valuable new tools for cell biologists
    • Lee DH, Goldberg AL (1998) Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol 8, 397-403.
    • (1998) Trends Cell Biol , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 46
    • 0034635952 scopus 로고    scopus 로고
    • Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression
    • Li B, Dou QP (2000) Bax degradation by the ubiquitin/proteasome-dependent pathway: involvement in tumor survival and progression. Proc Natl Acad Sci USA 97, 3850-5.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3850-3855
    • Li, B.1    Dou, Q.P.2
  • 47
    • 0035215395 scopus 로고    scopus 로고
    • Proteasome inhibition in cancer: development of PS-341
    • Adams J (2001) Proteasome inhibition in cancer: development of PS-341. Semin Oncol 28, 613-19.
    • (2001) Semin Oncol , vol.28 , pp. 613-619
    • Adams, J.1
  • 48
    • 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. (2001) The proteasome inhibitor PS-341 inhibits growth, induces apoptosis, and overcomes drug resistance in human multiple myeloma cells. Cancer Res 61, 3071-6.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 49
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-kB in preventing TNF-induced cell death
    • Beg AA, Baltimore D (1996) An essential role for NF-kB in preventing TNF-induced cell death. Science (Washington DC), 274, 782-4.
    • (1996) Science (Washington DC) , vol.274 , pp. 782-784
    • Beg, A.A.1    Baltimore, D.2
  • 51
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kB
    • Wang CY, Mayo MW, Baldwin AS (1996) TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-kB. Science (Washington DC), 274, 784-7.
    • (1996) Science (Washington DC) , vol.274 , pp. 784-787
    • Wang, C.Y.1    Mayo, M.W.2    Baldwin, A.S.3
  • 52
    • 0030885421 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kB control
    • Chu ZL, McKinsey TA, Liu L, Gentry JJ, Malim MH, Ballard DW (1997) Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-kB control. Proc Natl Acad Sci USA 94, 10057-62.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10057-10062
    • Chu, Z.L.1    McKinsey, T.A.2    Liu, L.3    Gentry, J.J.4    Malim, M.H.5    Ballard, D.W.6
  • 53
    • 0343262654 scopus 로고    scopus 로고
    • Crystal structure of epoxomicin: 20S proteasome reveals a molecular bassifor selectivity of alpha 'beta' - epoxyketone proteasome inhibitors
    • Groll M, Kim KB, Kairies N, Huber R, Crews CM (2000) Crystal structure of epoxomicin: 20S proteasome reveals a molecular bassifor selectivity of alpha 'beta' - epoxyketone proteasome inhibitors. J Am Chem Soc 122, 1237-8.
    • (2000) J Am Chem Soc , vol.122 , pp. 1237-1238
    • Groll, M.1    Kim, K.B.2    Kairies, N.3    Huber, R.4    Crews, C.M.5
  • 54
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activit
    • Meng L, Mohan R, Kwok BH, Elofsson M, Sin N, Crews CM (1999) Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activit. Proc Natl Acad Sci USA 96, 10403-8.
    • (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
  • 56
    • 0033965742 scopus 로고    scopus 로고
    • Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells
    • Drexler HC, Risau W, Konerding MA (2000) Inhibition of proteasome function induces programmed cell death in proliferating endothelial cells. FASEB J 14, 65-77.
    • (2000) FASEB J , vol.14 , pp. 65-77
    • Drexler, H.C.1    Risau, W.2    Konerding, M.A.3
  • 57
    • 0032539702 scopus 로고    scopus 로고
    • Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids
    • Adams J, Behnke M, Chen S et al. (1998) Potent and selective inhibitors of the proteasome: dipeptidyl boronic acids. Bioorg Med Chem Lett 8, 333-8.
    • (1998) Bioorg Med Chem Lett , vol.8 , pp. 333-338
    • Adams, J.1    Behnke, M.2    Chen, S.3
  • 58
    • 0036181371 scopus 로고    scopus 로고
    • Development of the proteasome inhibitor PS-341
    • Adams J (2002) Development of the proteasome inhibitor PS-341. Oncologist 7, 9-16.
    • (2002) Oncologist , vol.7 , pp. 9-16
    • Adams, J.1
  • 59
    • 0032189685 scopus 로고    scopus 로고
    • Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor
    • Orlowski RZ, Eswara JR, Lafond-Walker A et al. (1998) Tumor growth inhibition induced in a murine model of human Burkitt's lymphoma by a proteasome inhibitor. Cancer Res 58, 4342-8.
    • (1998) Cancer Res , vol.58 , pp. 4342-4348
    • Orlowski, R.Z.1    Eswara, J.R.2    Lafond-Walker, A.3
  • 60
    • 0031034160 scopus 로고    scopus 로고
    • Activation of the cell death program by inhibition of proteasome function
    • Drexler HC (1997) Activation of the cell death program by inhibition of proteasome function. Proc Natl Acad Sci USA 94, 855-60.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 855-860
    • Drexler, H.C.1
  • 61
    • 0031906567 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis
    • Delic J, Masdehors P, Omura S et al. (1998) The proteasome inhibitor lactacystin induces apoptosis and sensitizes chemo- and radioresistant human chronic lymphocytic leukaemia lymphocytes to TNF-alpha-initiated apoptosis. Br J Cancer 77, 1103-7.
    • (1998) Br J Cancer , vol.77 , pp. 1103-1107
    • Delic, J.1    Masdehors, P.2    Omura, S.3
  • 62
    • 0033152760 scopus 로고    scopus 로고
    • Proteasome inhibitors: A novel class of potent and effective antitumor agents
    • Adams J, Palombella VJ, Sausville EA et al. (1999) Proteasome inhibitors: A novel class of potent and effective antitumor agents. Cancer Res 59, 2615-22.
    • (1999) Cancer Res , vol.59 , pp. 2615-2622
    • Adams, J.1    Palombella, V.J.2    Sausville, E.A.3
  • 63
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: a novel target for cancer chemotherapy
    • Almond JB, Cohen GM (2002) The proteasome: a novel target for cancer chemotherapy. Leukemia 16, 433-43.
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 64
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J (2004) The development of proteasome inhibitors as anticancer drugs. Cancer Cell 5, 417-21.
    • (2004) Cancer Cell , vol.5 , pp. 417-421
    • Adams, J.1
  • 65
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella VJ, Rando OJ, Goldberg AL, Maniatis T (1994) The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78, 773-85.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 66
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl HL (1999) Activators and target genes of Rel/NF-κB transcription factors. Oncogene 18, 6853-66.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 67
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NFkappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B
    • Traenckner EB, Wilk S, Baeuerle PA (1994) A proteasome inhibitor prevents activation of NFkappa B and stabilizes a newly phosphorylated form of I kappa B-alpha that is still bound to NF-kappa B. EMBO J 13, 5433-41.
    • (1994) EMBO J , vol.13 , pp. 5433-5441
    • Traenckner, E.B.1    Wilk, S.2    Baeuerle, P.A.3
  • 68
    • 0028788180 scopus 로고
    • Degradation process of ligand-stimulated plateletderived growth factor beta-receptor involvesubiquitin-proteasome proteolytic pathway
    • Mori S, Tanaka K, Omura S, Saito Y (1995) Degradation process of ligand-stimulated plateletderived growth factor beta-receptor involvesubiquitin-proteasome proteolytic pathway. J Biol Chem 270, 29447-52.
    • (1995) J Biol Chem , vol.270 , pp. 29447-29452
    • Mori, S.1    Tanaka, K.2    Omura, S.3    Saito, Y.4
  • 71
    • 0030938526 scopus 로고    scopus 로고
    • Peptidyl aldehyde inhibitors of proteasome induce apoptosis rapidly in mouse lymphoma RVC cells
    • Tanimoto Y, Onishi Y, Hashimoto S et al. (1997) Peptidyl aldehyde inhibitors of proteasome induce apoptosis rapidly in mouse lymphoma RVC cells. J Biochem 121, 542-9.
    • (1997) J Biochem , vol.121 , pp. 542-549
    • Tanimoto, Y.1    Onishi, Y.2    Hashimoto, S.3
  • 72
    • 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. (2007) Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. Cancer Res 67, 6383-91.
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 73
    • 77953834412 scopus 로고    scopus 로고
    • MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level
    • Yong Hwan H (2010) MG132 as a proteasome inhibitor induces cell growth inhibition and cell death in A549 lung cancer cells via influencing reactive oxygen species and GSH level. Hum Exp Toxicol 29, 607-14.
    • (2010) Hum Exp Toxicol , vol.29 , pp. 607-614
    • Yong Hwan, H.1
  • 74
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268, 726-31.
    • (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
  • 75
    • 3042577683 scopus 로고    scopus 로고
    • Approval summary for bortezomib for injection in the treatment of multiple myeloma
    • Bross PF, Kane R, Farrell AT et al. (2004) Approval summary for bortezomib for injection in the treatment of multiple myeloma. Clin Cancer Res 10, 3954-64.
    • (2004) Clin Cancer Res , vol.10 , pp. 3954-3964
    • Bross, P.F.1    Kane, R.2    Farrell, A.T.3
  • 76
    • 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. (2004) A phase 2 study of two doses of bortezomib in relapsed or refractory myeloma. Br J Haematol 127, 165-72.
    • (2004) Br J Haematol , vol.127 , pp. 165-172
    • Jagannath, S.1    Barlogie, B.2    Berenson, J.3
  • 77
    • 0035736099 scopus 로고    scopus 로고
    • The proteasome: a new target for novel drug therapies
    • Elliott PJ, Ross JS (2001) The proteasome: a new target for novel drug therapies. Am J Clin Pathol 116, 637-46.
    • (2001) Am J Clin Pathol , vol.116 , pp. 637-646
    • Elliott, P.J.1    Ross, J.S.2
  • 78
    • 0012810697 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway of intracellular proteolysis
    • Doherty FJ, Dawson S, Mayer RJ (2002) The ubiquitin-proteasome pathway of intracellular proteolysis. Essays Biochem 38, 51-63.
    • (2002) Essays Biochem , vol.38 , pp. 51-63
    • Doherty, F.J.1    Dawson, S.2    Mayer, R.J.3
  • 79
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools - proteasome inhibitors offer therapeutic promise
    • Goldberg AL, Rock K (2002) Not just research tools - proteasome inhibitors offer therapeutic promise. Nat Med 8, 338-40.
    • (2002) Nat Med , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 80
    • 0033760253 scopus 로고    scopus 로고
    • The role of the proteasome in autoimmunity
    • Hayashi T, Faustman D (2000) The role of the proteasome in autoimmunity. Diabetes Metab Res Rev 16, 325-37.
    • (2000) Diabetes Metab Res Rev , vol.16 , pp. 325-337
    • Hayashi, T.1    Faustman, D.2
  • 81
    • 0036870323 scopus 로고    scopus 로고
    • On the role of proteasomes in cell biology and proteasome inhibition as a novel frontier in the development of immunosuppressants
    • Wu J (2002) On the role of proteasomes in cell biology and proteasome inhibition as a novel frontier in the development of immunosuppressants. Am J Transplant 2, 904-12.
    • (2002) Am J Transplant , vol.2 , pp. 904-912
    • Wu, J.1
  • 82
    • 13144294030 scopus 로고    scopus 로고
    • Inhibition of NF-κB activation in vitro and in vivo: role of 26S proteasome
    • Grisham MB, Palombella VJ, Elliott PJ et al. (1999) Inhibition of NF-κB activation in vitro and in vivo: role of 26S proteasome. Methods Enzymol 300, 345-63.
    • (1999) Methods Enzymol , vol.300 , pp. 345-363
    • Grisham, M.B.1    Palombella, V.J.2    Elliott, P.J.3
  • 83
    • 28844484584 scopus 로고    scopus 로고
    • Development and characterization of proteasome inhibitors
    • Bo Kim K, Fonseca FN, Crews CM (2005) Development and characterization of proteasome inhibitors. Methods Enzymol 399, 585-609.
    • (2005) Methods Enzymol , vol.399 , pp. 585-609
    • Bo Kim, K.1    Fonseca, F.N.2    Crews, C.M.3
  • 84
    • 0142199959 scopus 로고    scopus 로고
    • Feeding the machine: mechanisms of proteasomecatalyzed degradation of ubiquitinated proteins
    • Crews CM (2003) Feeding the machine: mechanisms of proteasomecatalyzed degradation of ubiquitinated proteins. Curr Opin Chem Biol 7, 534-9.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 534-539
    • Crews, C.M.1
  • 85
    • 0036839571 scopus 로고    scopus 로고
    • Is NF-κB a useful therapeutic target in rheumatoid arthritis?
    • Feldmann M, Andreakos E, Smith C et al. (2002) Is NF-κB a useful therapeutic target in rheumatoid arthritis?. Ann Rheum Dis 61(Suppl.2), ii13-8.84.
    • (2002) Ann Rheum Dis , vol.61 , Issue.SUPPL. 2
    • Feldmann, M.1    Andreakos, E.2    Smith, C.3
  • 86
    • 0029010658 scopus 로고
    • The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression
    • Read MA, Neish AS, Luscinskas FW, Palombella VJ, Maniatis T, Collins T (1995) The proteasome pathway is required for cytokine-induced endothelial-leukocyte adhesion molecule expression. Immunity 2, 493-506.
    • (1995) Immunity , vol.2 , pp. 493-506
    • Read, M.A.1    Neish, A.S.2    Luscinskas, F.W.3    Palombella, V.J.4    Maniatis, T.5    Collins, T.6
  • 87
    • 0017743014 scopus 로고
    • Arthritis in rats after systemic injection of streptococcal cells or cell walls
    • Cromartie WJ, Craddock JG, Schwab JH, Anderle SK, Yang CH (1977) Arthritis in rats after systemic injection of streptococcal cells or cell walls. J Exp Med 146, 1585-602.
    • (1977) J Exp Med , vol.146 , pp. 1585-1602
    • Cromartie, W.J.1    Craddock, J.G.2    Schwab, J.H.3    Anderle, S.K.4    Yang, C.H.5
  • 88
    • 0032505870 scopus 로고    scopus 로고
    • NF-κB activation provides the potential link between inflammation and hyperplasia in the arthritic joint
    • Miagkov AV, Kovalenko DV, Brown CE et al. (1998) NF-κB activation provides the potential link between inflammation and hyperplasia in the arthritic joint. Proc Natl Acad Sci USA 95, 13859-64.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13859-13864
    • Miagkov, A.V.1    Kovalenko, D.V.2    Brown, C.E.3
  • 89
    • 34250368734 scopus 로고    scopus 로고
    • Proteasome inhibition attenuates infarct size and preserves cardiac function in a murine model of myocardial ischemia-reperfusion injury
    • Stansfield WE, Moss NC, Willis MS, Tang R, Selzman CH (2007) Proteasome inhibition attenuates infarct size and preserves cardiac function in a murine model of myocardial ischemia-reperfusion injury. Ann Thorac Surg 84, 120-5.
    • (2007) Ann Thorac Surg , vol.84 , pp. 120-125
    • Stansfield, W.E.1    Moss, N.C.2    Willis, M.S.3    Tang, R.4    Selzman, C.H.5
  • 90
    • 38849159333 scopus 로고    scopus 로고
    • Bone building with bortezomib
    • Roodman GD (2008) Bone building with bortezomib. J Clin Invest 118, 462-4.
    • (2008) J Clin Invest , vol.118 , pp. 462-464
    • Roodman, G.D.1
  • 91
    • 0032889283 scopus 로고    scopus 로고
    • Reovirus-Induced Apoptosis Is Preceded by Increased Cellular Calpain Activity and Is Blocked by Calpain Inhibitors
    • Debiasi RL, Squier MKT, Pike B et al. (1999) Reovirus-Induced Apoptosis Is Preceded by Increased Cellular Calpain Activity and Is Blocked by Calpain Inhibitors. J Virology 73, 695.
    • (1999) J Virology , vol.73 , pp. 695
    • Debiasi, R.L.1    Squier, M.K.T.2    Pike, B.3
  • 92
    • 1542292775 scopus 로고    scopus 로고
    • Salinosporamide A, an antitumor proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora
    • Feling RH, Buchanan GO, Mincer TJ, Kauffman CA, Jensen PR, Fenical W (2003) Salinosporamide A, an antitumor proteasome inhibitor from a novel microbial source, a marine bacterium of the new genus Salinospora. Angew Chem Int Ed 115, 369-71.
    • (2003) Angew Chem Int Ed , vol.115 , pp. 369-371
    • Feling, R.H.1    Buchanan, G.O.2    Mincer, T.J.3    Kauffman, C.A.4    Jensen, P.R.5    Fenical, W.6
  • 93
    • 20044397059 scopus 로고    scopus 로고
    • Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor
    • Macherla VR, Mitchell SS, Manam RR et al. (2005) Structure-activity relationship studies of salinosporamide A (NPI-0052), a novel marine derived proteasome inhibitor. J Med Chem 48, 3684-7.
    • (2005) J Med Chem , vol.48 , pp. 3684-3687
    • Macherla, V.R.1    Mitchell, S.S.2    Manam, R.R.3
  • 94
    • 33846253586 scopus 로고    scopus 로고
    • Comparison of biochemical and biological effects of ML858 (salinosporamide A) and bortezomib
    • Williamson MJ, Blank JL, Bruzzese FJ et al. (2006) Comparison of biochemical and biological effects of ML858 (salinosporamide A) and bortezomib. Mol Cancer Ther 5, 3052-61.
    • (2006) Mol Cancer Ther , vol.5 , pp. 3052-3061
    • Williamson, M.J.1    Blank, J.L.2    Bruzzese, F.J.3
  • 95
    • 39749143840 scopus 로고    scopus 로고
    • Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer
    • Dorsey BD, Iqbal M, Chatterjee S et al. (2008) Discovery of a potent, selective, and orally active proteasome inhibitor for the treatment of cancer. J Med Chem 51, 1068-7298.
    • (2008) J Med Chem , vol.51 , pp. 1068-7298
    • Dorsey, B.D.1    Iqbal, M.2    Chatterjee, S.3
  • 96
    • 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. (2008) CEP-18770: a novel, orally active proteasome inhibitor with a tumor-selective pharmacologic profile competitive with bortezomib. Blood 111, 2765-75.
    • (2008) Blood , vol.111 , pp. 2765-2775
    • Piva, R.1    Ruggeri, B.2    Williams, M.3
  • 97
    • 0033621851 scopus 로고    scopus 로고
    • P27Kip1 Accumulation by Inhibition of proteasome Function Induces Apoptosis in Oral Squamous Cell Carcinoma Cells
    • Kudo Y, Takata T, Ogawa I et al. (2000) P27Kip1 Accumulation by Inhibition of proteasome Function Induces Apoptosis in Oral Squamous Cell Carcinoma Cells. Clin Cancer Res 6, 916.
    • (2000) Clin Cancer Res , vol.6 , pp. 916
    • Kudo, Y.1    Takata, T.2    Ogawa, I.3
  • 98
    • 0035215010 scopus 로고    scopus 로고
    • Postischemic (6h) treatment with rht-PA and proteasome inhibitor PS-519 reduces infarction in a rat model of embolic focal cerebral ischemia
    • Zhang L, Zhang ZG, Zhang R, Chopp M, Adams J, Elliott PJ (2001) Postischemic (6h) treatment with rht-PA and proteasome inhibitor PS-519 reduces infarction in a rat model of embolic focal cerebral ischemia. Stroke 32, 2926-31.
    • (2001) Stroke , vol.32 , pp. 2926-2931
    • Zhang, L.1    Zhang, Z.G.2    Zhang, R.3    Chopp, M.4    Adams, J.5    Elliott, P.J.6
  • 99
    • 0037215550 scopus 로고    scopus 로고
    • Delayed treatment with MLN519 reduces infarction and associated neurological deficit caused by focal ischemic brain injury in rats via anti-inflammatory mechanisms involving NF-kB activation, gliosis and leukocyte infiltration
    • Williams AJ, Hale S, Moffett J, Adams J, Elliott PJ, Tortella FC (2003) Delayed treatment with MLN519 reduces infarction and associated neurological deficit caused by focal ischemic brain injury in rats via anti-inflammatory mechanisms involving NF-kB activation, gliosis and leukocyte infiltration. J Cereb Blood Flow Metabol 23, 75-87.
    • (2003) J Cereb Blood Flow Metabol , vol.23 , pp. 75-87
    • Williams, A.J.1    Hale, S.2    Moffett, J.3    Adams, J.4    Elliott, P.J.5    Tortella, F.C.6
  • 101
    • 0033863764 scopus 로고    scopus 로고
    • Treatment of established relapsing experimental autoimmune encephalomyelitis with the proteasome inhibitor PS-519
    • Vanderlugt CL, Rahbe SM, Elliott PJ, Dal Canto MC, Miller SD (2000) Treatment of established relapsing experimental autoimmune encephalomyelitis with the proteasome inhibitor PS-519. J Autoimmun 14, 205-11.
    • (2000) J Autoimmun , vol.14 , pp. 205-211
    • Vanderlugt, C.L.1    Rahbe, S.M.2    Elliott, P.J.3    Dal Canto, M.C.4    Miller, S.D.5
  • 102
    • 43949095463 scopus 로고    scopus 로고
    • Proteasome inhibition as a novel therapy in treating rheumatoid arthritis
    • Brun J (2008) Proteasome inhibition as a novel therapy in treating rheumatoid arthritis. Medical Hypothesis 71, 65-72.
    • (2008) Medical Hypothesis , vol.71 , pp. 65-72
    • Brun, J.1
  • 103
    • 64949101030 scopus 로고    scopus 로고
    • TP 110, a New proteasome inhibitor, down regulates IAPs in human multiple myeloma cells
    • Iijima M, Momose I, Ikeda D (2009) TP 110, a New proteasome inhibitor, down regulates IAPs in human multiple myeloma cells. Anti cancer Res 29, 977-85.
    • (2009) Anti cancer Res , vol.29 , pp. 977-985
    • Iijima, M.1    Momose, I.2    Ikeda, D.3
  • 104
    • 78049497262 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib drastically affects inflammation and bone disease in adjuvant induced arthritis in rats
    • Yannaki E, Papadopoulou A, Athanasiou E, Kaloyannidis P (2010) The proteasome inhibitor bortezomib drastically affects inflammation and bone disease in adjuvant induced arthritis in rats. Arthritis Rheum 62, 3277-88.
    • (2010) Arthritis Rheum , vol.62 , pp. 3277-3288
    • Yannaki, E.1    Papadopoulou, A.2    Athanasiou, E.3    Kaloyannidis, P.4
  • 105
    • 77954236941 scopus 로고    scopus 로고
    • Attenuation of Pain and inflammation in Adjuvant-Induced Arthritis by the Proteasome Inhibitor MG132
    • Ahmed AS, Li J, Ahmed M et al. (2010) Attenuation of Pain and inflammation in Adjuvant-Induced Arthritis by the Proteasome Inhibitor MG132. Arthrits Rheum 62, 2160-9.
    • (2010) Arthrits Rheum , vol.62 , pp. 2160-2169
    • Ahmed, A.S.1    Li, J.2    Ahmed, M.3
  • 106
    • 79953705982 scopus 로고    scopus 로고
    • Proteasome inhibition aggravates tumor necrosis factor-mediated bone resorption in a mouse model of inflammatory arthritis
    • Polzer K, Neubert K, Meister S et al. (2011) Proteasome inhibition aggravates tumor necrosis factor-mediated bone resorption in a mouse model of inflammatory arthritis. Arthritis Rheum 63, 670-80.
    • (2011) Arthritis Rheum , vol.63 , pp. 670-680
    • Polzer, K.1    Neubert, K.2    Meister, S.3
  • 107
    • 34948881265 scopus 로고    scopus 로고
    • Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-kappa B-regulated gene products
    • Ahn KS, Sethi G, Chao TH et al. (2007) Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through down-modulation of NF-kappa B-regulated gene products. Blood, 110, 2286-95.
    • (2007) Blood , vol.110 , pp. 2286-2295
    • Ahn, K.S.1    Sethi, G.2    Chao, T.H.3
  • 108
    • 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 leukemic cells
    • Miller CP, Ban K, Dujka ME et al. (2007) NPI-0052, a novel proteasome inhibitor, induces caspase-8 and ROS-dependent apoptosis alone and in combination with HDAC inhibitors in leukemic cells. Blood, 110, 267-77.
    • (2007) Blood , vol.110 , pp. 267-277
    • Miller, C.P.1    Ban, K.2    Dujka, M.E.3
  • 109
    • 33745276531 scopus 로고    scopus 로고
    • A Boronic-Chalcone Derivative Exhibits Potent Anticancer Activity through Inhibition of the proteasome
    • Achanta G, Modzelewska A, Feng L, Khan SR, Huang P (2006) A Boronic-Chalcone Derivative Exhibits Potent Anticancer Activity through Inhibition of the proteasome. Mol Pharmacol 70, 426-33.
    • (2006) Mol Pharmacol , vol.70 , pp. 426-433
    • Achanta, G.1    Modzelewska, A.2    Feng, L.3    Khan, S.R.4    Huang, P.5
  • 111
    • 84862519625 scopus 로고    scopus 로고
    • Signal transduction pathways in Rheumatoid arthritis
    • Nalini G, Vasanthi P, Rajasekhar G (2010) Signal transduction pathways in Rheumatoid arthritis. SRJM 3, 18-21.
    • (2010) SRJM , vol.3 , pp. 18-21
    • Nalini, G.1    Vasanthi, P.2    Rajasekhar, G.3


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