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Volumn 13, Issue 13, 2012, Pages 1665-1675

Proteasome inhibitors: A new perspective for treating autoimmune diseases

Author keywords

Autoimmunity; Immunoproteasome; Novel therapeutics; Proteasome inhibitors; Treatment; Ubiquitin proteasome system

Indexed keywords

1, 4 NAPHTHOQUINONE DERIVATIVE; AUTOANTIBODY; AZATHIOPRINE; BELIMUMAB; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARFILZOMIB; CYCLOPHOSPHAMIDE; DELANZOMIB; DEXAMETHASONE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INORGANIC COMPOUND; MACROCYCLIC COMPOUND; MYCOPHENOLIC ACID 2 MORPHOLINOETHYL ESTER; NEDD8 INHIBITOR; NEDD8 PROTEIN; ONX 0914; PROTEASOME; PROTEASOME INHIBITOR; RITUXIMAB; SALINOSPORAMIDE A; TOCILIZUMAB; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN E1 INHIBITOR; UNCLASSIFIED DRUG; VORINOSTAT;

EID: 84870227323     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/138945012803530053     Document Type: Article
Times cited : (20)

References (101)
  • 1
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Ann Rev Biochem 2009; 78: 477-513.
    • (2009) Ann Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 2
    • 78149299837 scopus 로고    scopus 로고
    • Proteasome inhibitors: Dozens of molecules and still counting
    • De Bettignies G, Coux O. Proteasome inhibitors: dozens of molecules and still counting. Biochimie 2010; 92: 1530-1545.
    • (2010) Biochimie , vol.92 , pp. 1530-1545
    • de Bettignies, G.1    Coux, O.2
  • 3
    • 33750946999 scopus 로고    scopus 로고
    • Narrative review: Protein degradation and human diseases: The ubiquitin connection
    • Reinstein E, Ciechanover A. Narrative review: protein degradation and human diseases: the ubiquitin connection. Ann Intern Med 2006; 145: 676-684.
    • (2006) Ann Intern Med , vol.145 , pp. 676-684
    • Reinstein, E.1    Ciechanover, A.2
  • 4
    • 0342265782 scopus 로고
    • A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes
    • Etlinger JD, Goldberg AL. A soluble ATP-dependent proteolytic system responsible for the degradation of abnormal proteins in reticulocytes. Proc Natl Acad Sci USA 1977; 74: 54-58.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 54-58
    • Etlinger, J.D.1    Goldberg, A.L.2
  • 5
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools- proteasome inhibitors offer therapeutic promise
    • Goldberg AL, Rock K. Not just research tools- proteasome inhibitors offer therapeutic promise. Nat Med 2002; 8: 338-340.
    • (2002) Nat Med , vol.8 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 6
    • 2342667387 scopus 로고    scopus 로고
    • The development of proteasome inhibitors as anticancer drugs
    • Adams J. The development of proteasome inhibitors as anticancer drugs. Cancer Cell 2004; 5: 1964-1979.
    • (2004) Cancer Cell , vol.5 , pp. 1964-1979
    • Adams, J.1
  • 7
    • 80054850810 scopus 로고    scopus 로고
    • Macrocyclic proteasome inhibitors
    • Krahn D, Ottmann C, Kaiser M. Macrocyclic proteasome inhibitors. Curr Med Chem 2011; 18: 5052-5060.
    • (2011) Curr Med Chem , vol.18 , pp. 5052-5060
    • Krahn, D.1    Ottmann, C.2    Kaiser, M.3
  • 8
    • 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: 243-249.
    • (2010) Drug Discov Today , vol.15 , pp. 243-249
    • Dick, L.R.1    Fleming, P.E.2
  • 9
    • 84870255603 scopus 로고    scopus 로고
    • The putative role of endoplasmic reticulum aminopeptidases in autoimmunity: Insights from genomic-wide association studies
    • doi:10.1016/J.autrev.2012.04.007
    • Fierabracci A, Milillo AM, Locatelli F, Fruci D. The putative role of endoplasmic reticulum aminopeptidases in autoimmunity: insights from genomic-wide association studies. Autoimmun Rev 2012; doi:10.1016/J.autrev.2012.04.007.
    • (2012) Autoimmun Rev
    • Fierabracci, A.1    Milillo, A.M.2    Locatelli, F.3    Fruci, D.4
  • 10
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll M, Ditzel L, Lowe, et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 1997; 386: 463-471.
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1    Ditzel, L.2    Lowe3
  • 11
    • 0032514684 scopus 로고    scopus 로고
    • Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digest of enolase I
    • Nussbaum AK, Dick TP, Keilholz W, et al. Cleavage motifs of the yeast 20S proteasome beta subunits deduced from digest of enolase I. Proc Natl Acad Sci USA 1998; 95: 12504-12509.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12504-12509
    • Nussbaum, A.K.1    Dick, T.P.2    Keilholz, W.3
  • 12
    • 77955602593 scopus 로고    scopus 로고
    • The immunoproteasome cleans up after inflammation
    • Van Deventer S, Neefjes J. The immunoproteasome cleans up after inflammation. Cell 2010; 142: 517-518.
    • (2010) Cell , vol.142 , pp. 517-518
    • van Deventer, S.1    Neefjes, J.2
  • 13
    • 0035067590 scopus 로고    scopus 로고
    • Interferon-gamma inducible exchanges of 20S proteasome active site subunits: Why?
    • Groettrup M, Khan S, Schwarz K, Schmidtke G. Interferon-gamma inducible exchanges of 20S proteasome active site subunits: why? Biochimie 2001; 83: 367-372.
    • (2001) Biochimie , vol.83 , pp. 367-372
    • Groettrup, M.1    Khan, S.2    Schwarz, K.3    Schmidtke, G.4
  • 14
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino GN, Slòaughter CA. The proteasome, a novel protease regulated by multiple mechanisms. J Biol Chem 1999; 274: 22123-22126.
    • (1999) J Biol Chem , vol.274 , pp. 22123-22126
    • Demartino, G.N.1    Slòaughter, C.A.2
  • 15
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • Griffin TA, Nandi D, Cruz M, et al. Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits. J Exp Med 1998; 187: 97-104.
    • (1998) J Exp Med , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3
  • 16
    • 34249883977 scopus 로고    scopus 로고
    • Regulation of CD8+ T cell development by thymus-specific proteasomes
    • Murata S, Sasaki K, Kishimoto T, et al. Regulation of CD8+ T cell development by thymus-specific proteasomes. Science 2007; 316: 1349-1353.
    • (2007) Science , vol.316 , pp. 1349-1353
    • Murata, S.1    Sasaki, K.2    Kishimoto, T.3
  • 17
    • 79953678603 scopus 로고    scopus 로고
    • Proteasome inhibition and its therapeutic potential in multiple myeloma
    • Chari A, Mazymber A, Jagannath S. Proteasome inhibition and its therapeutic potential in multiple myeloma. Biologics 2010; 4: 273-287.
    • (2010) Biologics , vol.4 , pp. 273-287
    • Chari, A.1    Mazymber, A.2    Jagannath, S.3
  • 18
    • 84870230497 scopus 로고    scopus 로고
    • Pulmonary manifestations of systemic autoimmune diseases
    • Cojocaru M, Cojocaru IM, Silosi I, Vrabie CD. Pulmonary manifestations of systemic autoimmune diseases. Maedica 2011; 6:224-229.
    • (2011) Maedica , vol.6 , pp. 224-229
    • Cojocaru, M.1    Cojocaru, I.M.2    Silosi, I.3    Vrabie, C.D.4
  • 19
    • 80055082247 scopus 로고    scopus 로고
    • Experimental strategies in autoimmunity: Antagonists of cytokines and their receptors, nanocarriers, inhibitors of immunoproteasome, leukocyte migration and protein kinases
    • Fierabracci A, Ayroldi E. Experimental strategies in autoimmunity: antagonists of cytokines and their receptors, nanocarriers, inhibitors of immunoproteasome, leukocyte migration and protein kinases. Curr Pharm Des 2011; 17:3094-3107.
    • (2011) Curr Pharm Des , vol.17 , pp. 3094-3107
    • Fierabracci, A.1    Ayroldi, E.2
  • 21
    • 44849112235 scopus 로고    scopus 로고
    • Current treatment of lupus nephritis
    • Houssiau FA, Ginzler EM. Current treatment of lupus nephritis. Lupus 2008; 17: 426-430.
    • (2008) Lupus , vol.17 , pp. 426-430
    • Houssiau, F.A.1    Ginzler, E.M.2
  • 22
    • 84856103470 scopus 로고    scopus 로고
    • Novel, orally active, proteasome inhibitor, delanzomib (CEP-18770), ameliorates disease symptoms and glomerulonephritis in two preclinical mouse models of SLE
    • Seavey MM, Lu LD, Stump KL, Wallace NH, Ruggeri BA. Novel, orally active, proteasome inhibitor, delanzomib (CEP-18770), ameliorates disease symptoms and glomerulonephritis in two preclinical mouse models of SLE. Int Immunopharmacol 2012; 12: 257-270.
    • (2012) Int Immunopharmacol , vol.12 , pp. 257-270
    • Seavey, M.M.1    Lu, L.D.2    Stump, K.L.3    Wallace, N.H.4    Ruggeri, B.A.5
  • 23
    • 46749088320 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis
    • Neubert K, Meister S, Moser K. The proteasome inhibitor bortezomib depletes plasma cells and protects mice with lupus-like disease from nephritis. Nat Med 2008; 14: 748-755.
    • (2008) Nat Med , vol.14 , pp. 748-755
    • Neubert, K.1    Meister, S.2    Moser, K.3
  • 24
    • 0022273898 scopus 로고
    • Murine models of systemic lupus erythematosus
    • Theofilopoulos AN, Dixon FJ. Murine models of systemic lupus erythematosus. Adv Immunol 1985; 37: 269-290.
    • (1985) Adv Immunol , vol.37 , pp. 269-290
    • Theofilopoulos, A.N.1    Dixon, F.J.2
  • 25
    • 39449137543 scopus 로고    scopus 로고
    • Proteasome inhibition drastically but reversibly impairs murine lymphocyte development
    • Maseda D, Meister S, Neubert K, Hermann M, Voll RE. Proteasome inhibition drastically but reversibly impairs murine lymphocyte development. Cell Death Differ 2008; 15: 600-612.
    • (2008) Cell Death Differ , vol.15 , pp. 600-612
    • Maseda, D.1    Meister, S.2    Neubert, K.3    Hermann, M.4    Voll, R.E.5
  • 26
    • 84856153814 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib prevents lupus nephritis in the NZB/W F1 mouse model by preservation of glomerular and tubulointerstitial architecture
    • Hainz N, Thomas S, Neuvert K, et al. The proteasome inhibitor bortezomib prevents lupus nephritis in the NZB/W F1 mouse model by preservation of glomerular and tubulointerstitial architecture. Nepron Exp Nephrol 2012; 120: e47-e58.
    • (2012) Nepron Exp Nephrol , vol.120
    • Hainz, N.1    Thomas, S.2    Neuvert, K.3
  • 27
    • 79551667105 scopus 로고    scopus 로고
    • Myeloperoxidasespecific plasma cell depletion by bortezomib protects from antineutrophil cytoplasmic autoantibodies-induced glomerulonephritis
    • Bontscho J, Schreiber A, Manz RA, et al. Myeloperoxidasespecific plasma cell depletion by bortezomib protects from antineutrophil cytoplasmic autoantibodies-induced glomerulonephritis. J Am Soc Nephrol 2011; 22; 336-348.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 336-348
    • Bontscho, J.1    Schreiber, A.2    Manz, R.A.3
  • 30
    • 78149492075 scopus 로고    scopus 로고
    • State of the art: Rheumatoid arthritis
    • McInnes IB, O'Dell JR. State of the art: rheumatoid arthritis. Ann Rheum Dis 2010; 69: 1898-1906.
    • (2010) Ann Rheum Dis , vol.69 , pp. 1898-1906
    • McInnes, I.B.1    O'Dell, J.R.2
  • 31
    • 33749023888 scopus 로고    scopus 로고
    • Mechanisms of disease: The molecular and cellular basis of joint destruction in rheumatoid arthritis
    • Müller-Ladner U, Pap T, Gay RE, Neidhart M, Gay S. Mechanisms of disease: the molecular and cellular basis of joint destruction in rheumatoid arthritis. Nat Clin Pract Rheumatol 2005; 1: 102-110.
    • (2005) Nat Clin Pract Rheumatol , vol.1 , pp. 102-110
    • Müller-Ladner, U.1    Pap, T.2    Gay, R.E.3    Neidhart, M.4    Gay, S.5
  • 32
    • 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: 739-758.
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 33
    • 0017743014 scopus 로고
    • Arthritis in rats after systemic injection of streptococcal cells or cell walls
    • Cromartie WJ, Craddock JC, Schwab JH, Anderie SK, Yang CH. Arthritis in rats after systemic injection of streptococcal cells or cell walls. J Exp Med 1977; 146: 1585-1602.
    • (1977) J Exp Med , vol.146 , pp. 1585-1602
    • Cromartie, W.J.1    Craddock, J.C.2    Schwab, J.H.3    Anderie, S.K.4    Yang, C.H.5
  • 34
    • 13044316560 scopus 로고
    • Role of the proteasome and NF-kB in streptococcal cell wall-induced polyarthritis
    • Palombella VJ, Conner EM, Fuseler JW, et al. Role of the proteasome and NF-kB in streptococcal cell wall-induced polyarthritis. Proc Natl Acad Sci USA 1988; 95: 15671-1566.
    • (1988) Proc Natl Acad Sci USA , vol.95 , pp. 15671-21566
    • Palombella, V.J.1    Conner, E.M.2    Fuseler, J.W.3
  • 35
    • 70449727070 scopus 로고    scopus 로고
    • Bortezomib attenuates murine collagen-induced arthritis
    • Lee SW, Kim JH, Park YB, Lee SK. Bortezomib attenuates murine collagen-induced arthritis. Ann Rheum Dis 2009; 68: 1761-1767.
    • (2009) Ann Rheum Dis , vol.68 , pp. 1761-1767
    • Lee, S.W.1    Kim, J.H.2    Park, Y.B.3    Lee, S.K.4
  • 36
    • 84859131427 scopus 로고    scopus 로고
    • Proteasome inhibitor bortezomib ameliorates intestinal injury in mice
    • Yanaba K, Asana Y, Sugaya M, Kadono T, Sato S. Proteasome inhibitor bortezomib ameliorates intestinal injury in mice. PloS One 2012; 7: e34587.
    • (2012) PloS One , vol.7
    • Yanaba, K.1    Asana, Y.2    Sugaya, M.3    Kadono, T.4    Sato, S.5
  • 37
    • 77954008149 scopus 로고    scopus 로고
    • Targeting the proteasome; partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis
    • Schmidt N, Gonzales E, Visekruna A, et al. Targeting the proteasome; partial inhibition of the proteasome by bortezomib or deletion of the immunosubunit LMP7 attenuates experimental colitis. Gut 2010; 59: 896-906.
    • (2010) Gut , vol.59 , pp. 896-906
    • Schmidt, N.1    Gonzales, E.2    Visekruna, A.3
  • 38
    • 2442563304 scopus 로고    scopus 로고
    • Clinical epidemiology of inflammatory bowel disease: Incidence, prevalence and environmental influences
    • Loftus EV Jr. Clinical epidemiology of inflammatory bowel disease: incidence, prevalence and environmental influences. Gastroenterology 2004; 126: 1504-1517.
    • (2004) Gastroenterology , vol.126 , pp. 1504-1517
    • Loftus Jr., E.V.1
  • 39
    • 0027451455 scopus 로고
    • Enhanced secretion of tumour necrosis factor-alpha, IL-6 and IL-1 beta by isolated lamina propria mononuclear cells from patients with ulcerative colitis and Crohn's disease
    • Reinecker HC, Steffen M, Witthoeft T, et al. Enhanced secretion of tumour necrosis factor-alpha, IL-6 and IL-1 beta by isolated lamina propria mononuclear cells from patients with ulcerative colitis and Crohn's disease. Clin Exp Immunol 1993; 94: 174-181.
    • (1993) Clin Exp Immunol , vol.94 , pp. 174-181
    • Reinecker, H.C.1    Steffen, M.2    Witthoeft, T.3
  • 40
    • 84876015508 scopus 로고    scopus 로고
    • Management of inflammatory bowel disease in adults
    • Katz JA. Management of inflammatory bowel disease in adults. J Dig Dis 2007; 8: 65-71.
    • (2007) J Dig Dis , vol.8 , pp. 65-71
    • Katz, J.A.1
  • 41
    • 67650754085 scopus 로고    scopus 로고
    • Design, synthesis, biological evaluation, and structure-activity relationship (SAR) discussion of dipeptidyl boronate proteasome inhibitors, part 1: 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 1: comprehensive understanding of the SAR of alpha-amino acid boronates. J Med Chem 2009; 52: 4192-4199.
    • (2009) J Med Chem , vol.52 , pp. 4192-4199
    • Zhu, Y.1    Zhao, X.2    Zhu, X.3
  • 42
    • 0034991967 scopus 로고    scopus 로고
    • Classification of demyelinating disease at the interface between etiology and pathogenesis
    • Lassmann H. Classification of demyelinating disease at the interface between etiology and pathogenesis. Curr Opin Neurol 2001; 14: 253-258.
    • (2001) Curr Opin Neurol , vol.14 , pp. 253-258
    • Lassmann, H.1
  • 44
    • 55249102985 scopus 로고    scopus 로고
    • Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation
    • Fissolo N, Kraus M, Reich M, et al. Dual inhibition of proteasomal and lysosomal proteolysis ameliorates autoimmune central nervous system inflammation. Eur J Immunol 2008; 38: 2401-2411.
    • (2008) Eur J Immunol , vol.38 , pp. 2401-2411
    • Fissolo, N.1    Kraus, M.2    Reich, M.3
  • 45
    • 0033695299 scopus 로고    scopus 로고
    • Proteolysis in MHC class II antigen presentation: Who's in charge?
    • Villadangos JA, Ploegh HL. Proteolysis in MHC class II antigen presentation: who's in charge? Immunity 2000; 12: 233-239.
    • (2000) Immunity , vol.12 , pp. 233-239
    • Villadangos, J.A.1    Ploegh, H.L.2
  • 46
    • 77954354166 scopus 로고    scopus 로고
    • The auto-antigen repertoire in myasthenia gravis
    • Vrolix K, Fraussen J, Molenaar PC, et al. The auto-antigen repertoire in myasthenia gravis. Autoimmunity 2010; 43: 380-400.
    • (2010) Autoimmunity , vol.43 , pp. 380-400
    • Vrolix, K.1    Fraussen, J.2    Molenaar, P.C.3
  • 47
    • 0035105784 scopus 로고    scopus 로고
    • Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies
    • Hoch W, McConville J, Helms S, Newsom-Davis J, Melms A, Vincent A. Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies. Nat Med 2001; 7: 365-368.
    • (2001) Nat Med , vol.7 , pp. 365-368
    • Hoch, W.1    McConville, J.2    Helms, S.3    Newsom-Davis, J.4    Melms, A.5    Vincent, A.6
  • 48
    • 79951838009 scopus 로고    scopus 로고
    • Proteasome inhibition with bortezomib depletes plasma cells and autoantibodies in experimental autoimmune myasthenia gravis
    • Gomez AM, Vrolix K, Martínez-Martínez P, et al. Proteasome inhibition with bortezomib depletes plasma cells and autoantibodies in experimental autoimmune myasthenia gravis. J Immunol 2011; 186: 2503-2513.
    • (2011) J Immunol , vol.186 , pp. 2503-2513
    • Gomez, A.M.1    Vrolix, K.2    Martínez-Martínez, P.3
  • 49
    • 77956198116 scopus 로고    scopus 로고
    • Prevention of experimental colitis by a selective inhibitor of the immunoproteasome
    • Basler M, Dajee M, Moll C, Groettrup M, Kirk CJ. Prevention of experimental colitis by a selective inhibitor of the immunoproteasome. J Immunol 2010; 185: 634-641.
    • (2010) J Immunol , vol.185 , pp. 634-641
    • Basler, M.1    Dajee, M.2    Moll, C.3    Groettrup, M.4    Kirk, C.J.5
  • 50
    • 67650388103 scopus 로고    scopus 로고
    • A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis
    • Muchamuel T, Basler M, Aujay A, et al. A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis. Nat Med 2009; 15: 781-787.
    • (2009) Nat Med , vol.15 , pp. 781-787
    • Muchamuel, T.1    Basler, M.2    Aujay, A.3
  • 51
    • 33744539521 scopus 로고    scopus 로고
    • Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells
    • Obeng EA, Carlson LM, Gutman DM, Harrington WJ Jr, Lee KP, Boise LH. Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells. Blood 2006; 107: 4907-4916.
    • (2006) Blood , vol.107 , pp. 4907-4916
    • Obeng, E.A.1    Carlson, L.M.2    Gutman, D.M.3    Harrington Jr., W.J.4    Lee, K.P.5    Boise, L.H.6
  • 52
    • 84863012127 scopus 로고    scopus 로고
    • Beneficial effect of novel proteasome inhibitors in murine lupus via dual inhibition of type 1 interferon and autoantibody-secreting cells
    • Ichikawa HT, Conley T, Muchamuel T, et al. Beneficial effect of novel proteasome inhibitors in murine lupus via dual inhibition of type 1 interferon and autoantibody-secreting cells. Arthritis Rheum 2012; 64: 493-503.
    • (2012) Arthritis Rheum , vol.64 , pp. 493-503
    • Ichikawa, H.T.1    Conley, T.2    Muchamuel, T.3
  • 53
    • 34548183776 scopus 로고    scopus 로고
    • Neurotoxicity of bortezomib therapy in multiple myeloma: A single-center experience and review of the literature
    • Badros A, Goloubeva O, Dalal JS, et al. Neurotoxicity of bortezomib therapy in multiple myeloma: a single-center experience and review of the literature. Cancer 2007; 110: 1042-1049.
    • (2007) Cancer , vol.110 , pp. 1042-1049
    • Badros, A.1    Goloubeva, O.2    Dalal, J.S.3
  • 54
    • 84859959246 scopus 로고    scopus 로고
    • Prophylactic and therapeutic efficacies of a selective inhibitor of the immunoproteasome for Hashimoto's thyroiditis, but not for Graves' hyperthyroidism, in mice
    • Nagayama Y, Nakahara M, Shimamura M, et al. Prophylactic and therapeutic efficacies of a selective inhibitor of the immunoproteasome for Hashimoto's thyroiditis, but not for Graves' hyperthyroidism, in mice. Clin Exp Immunol 2012; 168: 268-273.
    • (2012) Clin Exp Immunol , vol.168 , pp. 268-273
    • Nagayama, Y.1    Nakahara, M.2    Shimamura, M.3
  • 55
    • 84875539389 scopus 로고    scopus 로고
    • Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling
    • doi 10.1007/s10637-012-9804-z
    • Zanotto-Filho A, Braganhol E, Battastini AMO, Moreira JCF. Proteasome inhibitor MG132 induces selective apoptosis in glioblastoma cells through inhibition of PI3K/Akt and NFkappaB pathways, mitochondrial dysfunction, and activation of p38-JNK1/2 signaling. Invest New Drugs 2012; doi 10.1007/s10637-012-9804-z.
    • (2012) Invest New Drugs
    • Zanotto-Filho, A.1    Braganhol, E.2    Battastini, A.M.O.3    Moreira, J.C.F.4
  • 56
    • 3242692570 scopus 로고    scopus 로고
    • Inhibition of the proteasome reduces transfet-induced diabetes in nonobese diabetic mice
    • Petrovic J, Hall H, Mehr R, Glas R, Höglund P. Inhibition of the proteasome reduces transfet-induced diabetes in nonobese diabetic mice. Scan J Immunol 2004; 60: 134-142.
    • (2004) Scan J Immunol , vol.60 , pp. 134-142
    • Petrovic, J.1    Hall, H.2    Mehr, R.3    Glas, R.4    Höglund, P.5
  • 57
    • 0031899972 scopus 로고    scopus 로고
    • Evidence for involvement of the proteasome complex (26S) and NFkappaB in IL-1 beta-induced nitric oxide and prostaglandin production by rat islets and RINm5F cells
    • Kwon G, Corbett JA, Hauser S, et al. Evidence for involvement of the proteasome complex (26S) and NFkappaB in IL-1 beta-induced nitric oxide and prostaglandin production by rat islets and RINm5F cells. Diabetes 1998; 47: 583-591.
    • (1998) Diabetes , vol.47 , pp. 583-591
    • Kwon, G.1    Corbett, J.A.2    Hauser, S.3
  • 58
    • 61849110417 scopus 로고    scopus 로고
    • The effect of proteasome inhibitor MG132 on experimental inflammatory bowel disease
    • Inoue S, Nakase H, Matsuura M, et al. The effect of proteasome inhibitor MG132 on experimental inflammatory bowel disease. Clin Exp Immunol 2009; 156: 172-182.
    • (2009) Clin Exp Immunol , vol.156 , pp. 172-182
    • Inoue, S.1    Nakase, H.2    Matsuura, M.3
  • 59
    • 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. Attenuation of pain and inflammation in adjuvant-induced arthritis by the proteasome inhibitor MG132. Arthritis Rheum 2010; 62: 2160-2169.
    • (2010) Arthritis Rheum , vol.62 , pp. 2160-2169
    • Ahmed, A.S.1    Li, J.2    Ahmed, M.3
  • 60
    • 51149105272 scopus 로고    scopus 로고
    • Update on the management of lupus nephritis: Let the treatment fit the patient
    • Bertsias G, Boumpas DT. Update on the management of lupus nephritis: let the treatment fit the patient. Nat Clin Pract Rheumatol 2008; 4: 464-472.
    • (2008) Nat Clin Pract Rheumatol , vol.4 , pp. 464-472
    • Bertsias, G.1    Boumpas, D.T.2
  • 61
    • 33748441252 scopus 로고    scopus 로고
    • Alternative and classical NF-kappa B signaling retain autoreactive B cells in the splenic marginal zone and result in lupus-like disease
    • Enzler T, Bonizzi G, Silverman GJ, et al. Alternative and classical NF-kappa B signaling retain autoreactive B cells in the splenic marginal zone and result in lupus-like disease. Immunity 2006; 25: 403-415.
    • (2006) Immunity , vol.25 , pp. 403-415
    • Enzler, T.1    Bonizzi, G.2    Silverman, G.J.3
  • 62
    • 0037973279 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed, refractory myeloma
    • Richardson PG, Barlogie B, Berenson J, et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. N Engl J Med 2003; 348: 2609-2617.
    • (2003) N Engl J Med , vol.348 , pp. 2609-2617
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 63
    • 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: 2765-2775.
    • (2008) Blood , vol.111 , pp. 2765-2775
    • Piva, R.1    Ruggeri, B.2    Williams, M.3
  • 64
    • 77953154024 scopus 로고    scopus 로고
    • The development and pharmacology of proteasome inhibitors for the management and treatment of cancer
    • Ruggeri B, Miknyoczki S, Dorsey B, Hui AM. The development and pharmacology of proteasome inhibitors for the management and treatment of cancer. Adv Pharmacol 2009; 57:91-135.
    • (2009) Adv Pharmacol , vol.57 , pp. 91-135
    • Ruggeri, B.1    Miknyoczki, S.2    Dorsey, B.3    Hui, A.M.4
  • 65
    • 84860768745 scopus 로고    scopus 로고
    • Probing the specificity and activity profiles of the proteasome inhibitors bortezomib and delanzomib
    • Berkers CR, Leestemaker Y, Schuurman KG, et al. Probing the specificity and activity profiles of the proteasome inhibitors bortezomib and delanzomib. Mol Pharm 2012; 9: 1126-1135.
    • (2012) Mol Pharm , vol.9 , pp. 1126-1135
    • Berkers, C.R.1    Leestemaker, Y.2    Schuurman, K.G.3
  • 66
    • 53049106912 scopus 로고    scopus 로고
    • Molecular basis of bortezomib resistance: Proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein
    • Oerlemans R, Franke NE, Assaraf YG, et al. Molecular basis of bortezomib resistance: proteasome subunit beta5 (PSMB5) gene mutation and overexpression of PSMB5 protein. Blood 2008; 112: 2489-2499.
    • (2008) Blood , vol.112 , pp. 2489-2499
    • Oerlemans, R.1    Franke, N.E.2    Assaraf, Y.G.3
  • 67
    • 33644845743 scopus 로고    scopus 로고
    • Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome
    • Groll M, Berkers CR, Ploegh LH, Ovaa H. Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome. Structure 2006; 14: 451-456.
    • (2006) Structure , vol.14 , pp. 451-456
    • Groll, M.1    Berkers, C.R.2    Ploegh, L.H.3    Ovaa, H.4
  • 68
    • 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: 6383-6391.
    • (2007) Cancer Res , vol.67 , pp. 6383-6391
    • Demo, S.D.1    Kirk, C.J.2    Aujay, M.A.3
  • 69
    • 27644562277 scopus 로고    scopus 로고
    • A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib
    • Chauhan D, Catley L, Li G, et al. A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib. Cancer Cell 2005; 8: 407-419.
    • (2005) Cancer Cell , vol.8 , pp. 407-419
    • Chauhan, D.1    Catley, L.2    Li, G.3
  • 70
    • 64749098830 scopus 로고    scopus 로고
    • An inhibitor of NEED8-activating enxyme as a new approach to treat cancer
    • Soucy TA, Smith PG, Milhollen MA, et al. An inhibitor of NEED8-activating enxyme as a new approach to treat cancer. Nature 2009; 458: 732-736.
    • (2009) Nature , vol.458 , pp. 732-736
    • Soucy, T.A.1    Smith, P.G.2    Milhollen, M.A.3
  • 72
    • 84862815656 scopus 로고    scopus 로고
    • Design and synthesis of naphthoquinone derivatives as antiproliferative agents and 20S proteasome inhibitors
    • Xu K, Xiao Z, Tang YB, et al. Design and synthesis of naphthoquinone derivatives as antiproliferative agents and 20S proteasome inhibitors. Bioorg Med Chem Lett 2012; 22: 2772-2774.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 2772-2774
    • Xu, K.1    Xiao, Z.2    Tang, Y.B.3
  • 73
    • 84858010952 scopus 로고    scopus 로고
    • Discovery and synthesis of hydronaphthoquinones as novel proteasome inhibitors
    • Ge Y, Kazi A, Marsilio F, et al. Discovery and synthesis of hydronaphthoquinones as novel proteasome inhibitors. J Med Chem 2012; 55: 1978-1998.
    • (2012) J Med Chem , vol.55 , pp. 1978-1998
    • Ge, Y.1    Kazi, A.2    Marsilio, F.3
  • 74
    • 84858978749 scopus 로고    scopus 로고
    • Identification and mechanistic studies of a novel ubiquitin E1 inhibitor
    • Ungermannova D, Parker SJ, Nasveschu KCG, et al. Identification and mechanistic studies of a novel ubiquitin E1 inhibitor. J Biomol Screen 2012; 17: 421-434.
    • (2012) J Biomol Screen , vol.17 , pp. 421-434
    • Ungermannova, D.1    Parker, S.J.2    Nasveschu, K.C.G.3
  • 75
    • 34948881265 scopus 로고    scopus 로고
    • Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through downmodulation of NF-kB regulated gene products
    • Ahn KS, Sethi G, Chao TH, et al. Salinosporamide A (NPI-0052) potentiates apoptosis, suppresses osteoclastogenesis, and inhibits invasion through downmodulation of NF-kB regulated gene products. Blood 2007; 110: 2286-2295.
    • (2007) Blood , vol.110 , pp. 2286-2295
    • Ahn, K.S.1    Sethi, G.2    Chao, T.H.3
  • 77
    • 77949432502 scopus 로고    scopus 로고
    • Clinical trial of the novel structure proteasome inhibitor NPI-0052 in patients with relapsed and relapsed/refractory multiple myeloma (r/R MM)
    • Hofmeister CC, Richardson P, Zimmerman T, et al. Clinical trial of the novel structure proteasome inhibitor NPI-0052 in patients with relapsed and relapsed/refractory multiple myeloma (r/R MM). J Clin Oncol 2009; 27: 15s.
    • (2009) J Clin Oncol , vol.27
    • Hofmeister, C.C.1    Richardson, P.2    Zimmerman, T.3
  • 78
    • 84871407100 scopus 로고    scopus 로고
    • Phase I clinical trial of the novel proteasome inhibitor marizomib with the histone deacetylase inhibitor vorinostat in patients with melanoma, pancreatic and lung cancer based on in vitro assessments of the combination
    • doi10.1007/s10637-011-9766-6
    • Millward M, Price T, Townsend A, et al. Phase I clinical trial of the novel proteasome inhibitor marizomib with the histone deacetylase inhibitor vorinostat in patients with melanoma, pancreatic and lung cancer based on in vitro assessments of the combination. Invest New Drugs 2011; doi10.1007/s10637-011-9766-6.
    • (2011) Invest New Drugs
    • Millward, M.1    Price, T.2    Townsend, A.3
  • 79
    • 84859492923 scopus 로고    scopus 로고
    • HDAC inhibitor therapy in autoimmunity and transplantation
    • Hancok WW, Akimova T, Beier UH, Liu Y, Wang L. HDAC inhibitor therapy in autoimmunity and transplantation. Ann Rheum Dis 2012; 71 (Suppl. 2): 146-154.
    • (2012) Ann Rheum Dis , vol.71 , Issue.SUPPL. 2 , pp. 146-154
    • Hancok, W.W.1    Akimova, T.2    Beier, U.H.3    Liu, Y.4    Wang, L.5
  • 80
    • 0033597126 scopus 로고    scopus 로고
    • Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway
    • Gong L, Yeh ET. Identification of the activating and conjugating enzymes of the NEDD8 conjugation pathway. J Biol Chem 1999; 274: 12036-12042.
    • (1999) J Biol Chem , vol.274 , pp. 12036-12042
    • Gong, L.1    Yeh, E.T.2
  • 81
    • 84862637714 scopus 로고    scopus 로고
    • Molecular and cellular effects of NEED8-activating enzyme inhibition in myeloma
    • McMillin DW, Jacobs HM, Delmore J, et al. Molecular and cellular effects of NEED8-activating enzyme inhibition in myeloma. Mol Cancer Ther 2012; 11: 942-951.
    • (2012) Mol Cancer Ther , vol.11 , pp. 942-951
    • McMillin, D.W.1    Jacobs, H.M.2    Delmore, J.3
  • 82
    • 0036305816 scopus 로고    scopus 로고
    • Argyrins, immunosuppressive cyclic peptides from myxobacteria. I. Production, isolation, phyco-chemical and biological properties
    • Sasse F, Steinmetz H, Schupp T, et al. Argyrins, immunosuppressive cyclic peptides from myxobacteria. I. Production, isolation, phyco-chemical and biological properties. J Antibiot 2002; 55: 543-551.
    • (2002) J Antibiot , vol.55 , pp. 543-551
    • Sasse, F.1    Steinmetz, H.2    Schupp, T.3
  • 83
    • 0036671772 scopus 로고    scopus 로고
    • Argyrins, immunosuppressive cyclic peptides from myxobacteria. II. Structure elucidation and stereochemistry
    • Vollbrecht L, Steinmetz H, Hofle G, et al. Argyrins, immunosuppressive cyclic peptides from myxobacteria. II. Structure elucidation and stereochemistry. J Antibiot 2002; 55: 715-721.
    • (2002) J Antibiot , vol.55 , pp. 715-721
    • Vollbrecht, L.1    Steinmetz, H.2    Hofle, G.3
  • 84
    • 0034105791 scopus 로고    scopus 로고
    • TMC-95A, B, C, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities
    • Koguchi Y, Kohno J, Nishio M, et al. TMC-95A, B, C, novel proteasome inhibitors produced by Apiospora montagnei Sacc. TC 1093. Taxonomy, production, isolation, and biological activities. J Antibiot 2000; 53: 105-109.
    • (2000) J Antibiot , vol.53 , pp. 105-109
    • Koguchi, Y.1    Kohno, J.2    Nishio, M.3
  • 85
    • 0034712160 scopus 로고    scopus 로고
    • Structures of TMC-95A-D: Novel proteasome inhibitors from Apiospora montagnei sacc. TC 1093
    • Kohno J, Koguchi Y, Nishio M, et al. Structures of TMC-95A-D: novel proteasome inhibitors from Apiospora montagnei sacc. TC 1093. J Org Chem 2000; 65: 990-995.
    • (2000) J Org Chem , vol.65 , pp. 990-995
    • Kohno, J.1    Koguchi, Y.2    Nishio, M.3
  • 86
    • 84860350522 scopus 로고    scopus 로고
    • Noncovalent inhibition of 20S proteasome by pegylated dimerized inhibitors
    • Maréchal X, Pujol A, Richy N, et al. Noncovalent inhibition of 20S proteasome by pegylated dimerized inhibitors. Eur J Med Chem 2012; 52: 322-327.
    • (2012) Eur J Med Chem , vol.52 , pp. 322-327
    • Maréchal, X.1    Pujol, A.2    Richy, N.3
  • 87
    • 0030805604 scopus 로고    scopus 로고
    • Cyclosporin A is an uncompetitive inhibitor of proteasome activity and prevents NF-kappaB activation
    • Myer S, Kohler NG, Joly A. Cyclosporin A is an uncompetitive inhibitor of proteasome activity and prevents NF-kappaB activation. FEBS Lett 1997; 413: 354-358.
    • (1997) FEBS Lett , vol.413 , pp. 354-358
    • Myer, S.1    Kohler, N.G.2    Joly, A.3
  • 88
    • 78650188894 scopus 로고    scopus 로고
    • Scytonemides A and B, cyclic peptides with 20S proteasome inhibitory activity from the cultured cyanobacterium Scytonema hofmanii
    • Krunic A, Vallat A, Mo S, et al. Scytonemides A and B, cyclic peptides with 20S proteasome inhibitory activity from the cultured cyanobacterium Scytonema hofmanii. J Nat Prod 2010; 73: 1927-1932.
    • (2010) J Nat Prod , vol.73 , pp. 1927-1932
    • Krunic, A.1    Vallat, A.2    Mo, S.3
  • 89
    • 42049085712 scopus 로고    scopus 로고
    • A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism
    • Groll M, Schellenberg B, Bachmann AS, et al. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature 2008; 452; 755-758.
    • (2008) Nature , vol.452 , pp. 755-758
    • Groll, M.1    Schellenberg, B.2    Bachmann, A.S.3
  • 90
    • 2642616988 scopus 로고    scopus 로고
    • Syringolin, a novel peptide elicitor from pseudomonas syringae pv. Syringae that induces resistance to Pyricularia oryzae in rice
    • Waspi U, Blanc D, Winkler T, Ruedi P, Dudler R. Syringolin, a novel peptide elicitor from pseudomonas syringae pv. Syringae that induces resistance to Pyricularia oryzae in rice. Mol Plant Microne In 1998; 11: 727-733.
    • (1998) Mol Plant Microne In , vol.11 , pp. 727-733
    • Waspi, U.1    Blanc, D.2    Winkler, T.3    Ruedi, P.4    Dudler, R.5
  • 91
    • 0032952478 scopus 로고    scopus 로고
    • Identification and structure of a family of syringolin variants: Unusual cyclic peptides from Pseudomonas syringae that elicit defense responses in rice
    • Waspi U, Hassa P, Staempfli AA, Molleyres LP, Winkler T, Dudler R. Identification and structure of a family of syringolin variants: unusual cyclic peptides from Pseudomonas syringae that elicit defense responses in rice. Microbiol Res 1999; 154: 89-93.
    • (1999) Microbiol Res , vol.154 , pp. 89-93
    • Waspi, U.1    Hassa, P.2    Staempfli, A.A.3    Molleyres, L.P.4    Winkler, T.5    Dudler, R.6
  • 92
    • 84870227412 scopus 로고    scopus 로고
    • Novel proteasome-inhibitory syrbactin analogs inducing endoplasmic reticulum stress and apoptosis in hematological tumor cell lines
    • Anshu A, Thomas S, Agarwal P, Ibarra-Rivera TR, Pirrung MC, Schonthal AH. Novel proteasome-inhibitory syrbactin analogs inducing endoplasmic reticulum stress and apoptosis in hematological tumor cell lines. Biochem Pharmacol 2010; 80: 170-198.
    • (2010) Biochem Pharmacol , vol.80 , pp. 170-198
    • Anshu, A.1    Thomas, S.2    Agarwal, P.3    Ibarra-Rivera, T.R.4    Pirrung, M.C.5    Schonthal, A.H.6
  • 93
    • 84555191774 scopus 로고    scopus 로고
    • Syringolin B-Inspired proteasome inhibitor analogue TIR-203 exhibits enhanced biological activity in multiple myeloma and neuroblastoma
    • Opoku-Ansah, Ibarra-Rivera TR, Pirrung MC, Bachmann AS. Syringolin B-Inspired proteasome inhibitor analogue TIR-203 exhibits enhanced biological activity in multiple myeloma and neuroblastoma. Pharm Biol 2012; 50: 25-29.
    • (2012) Pharm Biol , vol.50 , pp. 25-29
    • Opoku, A.1    Ibarra-Rivera, T.R.2    Pirrung, M.C.3    Bachmann, A.S.4
  • 94
    • 0023798582 scopus 로고
    • Glidobactins A, B, and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity
    • Oka M, Nishiyama Y, Ohta S, et al. Glidobactins A, B, and C, new antitumor antibiotics. I. Production, isolation, chemical properties and biological activity. J Antibiot 1988; 41: 1331-1337.
    • (1988) J Antibiot , vol.41 , pp. 1331-1337
    • Oka, M.1    Nishiyama, Y.2    Ohta, S.3
  • 96
    • 78751485542 scopus 로고    scopus 로고
    • Proteasome inhibitory activity of thiazole antibiotics
    • Pandit B, Gartel AL. Proteasome inhibitory activity of thiazole antibiotics. Cancer Biol Ther 2011; 11: 43-47.
    • (2011) Cancer Biol Ther , vol.11 , pp. 43-47
    • Pandit, B.1    Gartel, A.L.2
  • 97
    • 67649394729 scopus 로고    scopus 로고
    • Discovery of a novel proteasome inhibitor selective for cancer cells over non-transformed cells
    • Kazi A, Lawrence H, Guida WC, et al. Discovery of a novel proteasome inhibitor selective for cancer cells over non-transformed cells. Cell Cycle 2009; 8: 1940-1951.
    • (2009) Cell Cycle , vol.8 , pp. 1940-1951
    • Kazi, A.1    Lawrence, H.2    Guida, W.C.3
  • 98
    • 79952485141 scopus 로고    scopus 로고
    • Synthesis and proteasome inhibition of lithocolic acid derivatives
    • Dang Z, Lin A, Ho P, et al. Synthesis and proteasome inhibition of lithocolic acid derivatives. Biorg Med Chem Lett 2011; 21: 1926-1928.
    • (2011) Biorg Med Chem Lett , vol.21 , pp. 1926-1928
    • Dang, Z.1    Lin, A.2    Ho, P.3
  • 99
    • 84858683642 scopus 로고    scopus 로고
    • Targeting the ubiquitinproteasome pathway with inorganic compounds to fight cancer: A challenge for the future
    • Dalla Via L, Nardon C, Fregona D. Targeting the ubiquitinproteasome pathway with inorganic compounds to fight cancer: a challenge for the future. Future Med Chem 2012; 4: 525-543.
    • (2012) Future Med Chem , vol.4 , pp. 525-543
    • Dalla Via, L.1    Nardon, C.2    Fregona, D.3
  • 100
    • 35148887169 scopus 로고    scopus 로고
    • Inhibition of the proteasome activity by gallium (III) complexes contributes to their anti-prostate tumor effects
    • Chen D, Frezza M, Shakya R, et al. Inhibition of the proteasome activity by gallium (III) complexes contributes to their anti-prostate tumor effects. Cancer Res 2007; 67: 9258-9265.
    • (2007) Cancer Res , vol.67 , pp. 9258-9265
    • Chen, D.1    Frezza, M.2    Shakya, R.3
  • 101
    • 77951660776 scopus 로고    scopus 로고
    • Latest insights into the anticancer activity of Au(III)-dithiocarbamato complexes
    • Ronconi L, Aldinucci D, Dou QP, Fregona D. Latest insights into the anticancer activity of Au(III)-dithiocarbamato complexes. Anticancer Agents Med Chem 2010; 10: 283-292.
    • (2010) Anticancer Agents Med Chem , vol.10 , pp. 283-292
    • Ronconi, L.1    Aldinucci, D.2    Dou, Q.P.3    Fregona, D.4


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