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Volumn 30, Issue 11-12, 2008, Pages 1172-1184

Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches

Author keywords

[No Author keywords available]

Indexed keywords

ACLACINOMYCIN; ALPHA 1 ANTITRYPSIN; AMYLOID BETA PROTEIN; ARSENIC TRIOXIDE; ASCORBIC ACID; ATAXIN 1; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BORTEZOMIB; CARBOPLATIN; CELL PROTEIN; CEP 1612; COPPER ZINC SUPEROXIDE DISMUTASE; CVT 634; EPOXOMICIN; GEMCITABINE; HUNTINGTIN; LACTACYSTIN; LACTACYSTIN BETA LACTONE; MG 115; P 131; PARKIN; POLYGLUTAMINE; PRION PROTEIN; PROTEASOME; PROTEINASE INHIBITOR; SALINOSPORAMIDE A; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNINDEXED DRUG; BETA CATENIN;

EID: 58149159907     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20852     Document Type: Review
Times cited : (118)

References (110)
  • 1
    • 33750946999 scopus 로고    scopus 로고
    • Narrative review: Protein degradation and human diseases. The ubiquitin connection
    • Reinstein E, Ciechanover A. 2006. Narrative review: protein degradation and human diseases. The ubiquitin connection. Annals Int Med 145:676-684.
    • (2006) Annals Int Med , vol.145 , pp. 676-684
    • Reinstein, E.1    Ciechanover, A.2
  • 2
    • 34547936661 scopus 로고    scopus 로고
    • The proteasome and its role in nuclear protein maintenance
    • in press
    • Bader N, Jung T, Grune T. 2007. The proteasome and its role in nuclear protein maintenance. Exp Gerontol in press.
    • (2007) Exp Gerontol
    • Bader, N.1    Jung, T.2    Grune, T.3
  • 3
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer W, Gruhler A, Mohrle V, Mahe Y, Wolf DH. 1993. PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J Biol Chem 268:5115-5120.
    • (1993) J Biol Chem , vol.268 , pp. 5115-5120
    • Heinemeyer, W.1    Gruhler, A.2    Mohrle, V.3    Mahe, Y.4    Wolf, D.H.5
  • 4
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • Ciechanover A. 2006. The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology 66:S7-19.
    • (2006) Neurology , vol.66
    • Ciechanover, A.1
  • 5
    • 33744792036 scopus 로고    scopus 로고
    • Regulation of epithelial sodium channels by the ubiquitin-proteasome proteolytic pathway
    • Malik B, Price SR, Mitch WE, Yue Q, Eaton DC. 2006. Regulation of epithelial sodium channels by the ubiquitin-proteasome proteolytic pathway. Am J Physiol Renal Physiol 290:F1285-1294.
    • (2006) Am J Physiol Renal Physiol , vol.290
    • Malik, B.1    Price, S.R.2    Mitch, W.E.3    Yue, Q.4    Eaton, D.C.5
  • 6
    • 33745674468 scopus 로고    scopus 로고
    • Drug discovery in the ubiquitin-proteasome system
    • Nalepa G, Rolfe M, Harper JW. 2006. Drug discovery in the ubiquitin-proteasome system. Nat Rev Drug Discov 5:596-613.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 596-613
    • Nalepa, G.1    Rolfe, M.2    Harper, J.W.3
  • 7
    • 38449099679 scopus 로고    scopus 로고
    • Role of proteasomes in disease
    • Review
    • Dahlmann B. 2007. Role of proteasomes in disease. BMC Biochem 8: S3. Review.
    • (2007) BMC Biochem , vol.8
    • Dahlmann, B.1
  • 8
    • 29344447032 scopus 로고    scopus 로고
    • Intracellular protein degradation and its therapeutic implications
    • Hideshima T, Bradner JE, Chauhan D, Anderson KC. 2005. Intracellular protein degradation and its therapeutic implications. Clin Cancer Res 11:8530-8533.
    • (2005) Clin Cancer Res , vol.11 , pp. 8530-8533
    • Hideshima, T.1    Bradner, J.E.2    Chauhan, D.3    Anderson, K.C.4
  • 9
    • 33745816760 scopus 로고    scopus 로고
    • Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Goldberg AL, Mitch WE. 2006. Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. J Am Soc Nephrol 17:1807-1819.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 1807-1819
    • Lecker, S.H.1    Goldberg, A.L.2    Mitch, W.E.3
  • 10
    • 0037397606 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system and pathogenesis of human diseases: A novel platform for mechanism-based drug targeting
    • Ciechanover A. 2003. The ubiquitin proteolytic system and pathogenesis of human diseases: a novel platform for mechanism-based drug targeting. Biochem Soc Trans 31:474-481.
    • (2003) Biochem Soc Trans , vol.31 , pp. 474-481
    • Ciechanover, A.1
  • 12
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink AL. 1999. Chaperone-mediated protein folding. Physiol Rev 79:425-449.
    • (1999) Physiol Rev , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 13
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. 2002. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 14
    • 33746228127 scopus 로고    scopus 로고
    • Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins
    • Carvalho P, Goder V, Rapoport TA. 2006. Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126:361-373.
    • (2006) Cell , vol.126 , pp. 361-373
    • Carvalho, P.1    Goder, V.2    Rapoport, T.A.3
  • 16
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA. 2002. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3:246-255.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 17
    • 0034756104 scopus 로고    scopus 로고
    • From the cradle to the grave: Molecular chaperones that may choose between folding and degradation
    • Hohfeld J, Cyr DM, Patterson C. 2001. From the cradle to the grave: molecular chaperones that may choose between folding and degradation. EMBO Rep 2:885-890.
    • (2001) EMBO Rep , vol.2 , pp. 885-890
    • Hohfeld, J.1    Cyr, D.M.2    Patterson, C.3
  • 18
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman RL, Gordon C, Mayer RJ. 2005. Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Biol 6:599-609.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 20
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM, Eddins MJ. 2004. Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695:55-72.
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 21
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitinproteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. 2002. The ubiquitinproteasome 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
  • 22
    • 0031921466 scopus 로고    scopus 로고
    • Function and dysfunction of the presenilins
    • Price DL, Sisodia SS. 1998. Function and dysfunction of the presenilins. Annu Rev Neurosci 21:479-505.
    • (1998) Annu Rev Neurosci , vol.21 , pp. 479-505
    • Price, D.L.1    Sisodia, S.S.2
  • 23
  • 24
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • Kim T-W, Pettingell WH, Hallmark OG, Moir RD, Wasco W, Tanzi RE. 1997. Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells. J Biol Chem 272:11006-11010.
    • (1997) J Biol Chem , vol.272 , pp. 11006-11010
    • Kim, T.-W.1    Pettingell, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 25
    • 0033610863 scopus 로고    scopus 로고
    • Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation
    • Steiner H, Capell A, Pesold B, Citron M, Kloetzel PM, et al. 1998. Expression of Alzheimer's disease-associated presenilin-1 is controlled by proteolytic degradation and complex formation. J Biol Chem 273:32322-32331.
    • (1998) J Biol Chem , vol.273 , pp. 32322-32331
    • Steiner, H.1    Capell, A.2    Pesold, B.3    Citron, M.4    Kloetzel, P.M.5
  • 26
    • 0027193036 scopus 로고
    • Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
    • Morishima-Kawashima M, Hasegawa M, Takio K, Suzuki M, Titani K, Ihara Y. 1993. Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments. Neuron 10:1151-1160.
    • (1993) Neuron , vol.10 , pp. 1151-1160
    • Morishima-Kawashima, M.1    Hasegawa, M.2    Takio, K.3    Suzuki, M.4    Titani, K.5    Ihara, Y.6
  • 27
    • 0027407247 scopus 로고
    • Ubiquitin in neurodegenerative diseases
    • Lowe J, Mayer RJ, Landon M. 1993. Ubiquitin in neurodegenerative diseases. Brain Pathol 3:55-65.
    • (1993) Brain Pathol , vol.3 , pp. 55-65
    • Lowe, J.1    Mayer, R.J.2    Landon, M.3
  • 28
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen FW, de Kleijn DP, van den Hurk HH, Neubauer A, Sonnemans MA, et al. 1998a. Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279:242-247.
    • (1998) Science , vol.279 , pp. 242-247
    • van Leeuwen, F.W.1    de Kleijn, D.P.2    van den Hurk, H.H.3    Neubauer, A.4    Sonnemans, M.A.5
  • 30
    • 4344681293 scopus 로고    scopus 로고
    • Pathogenetic mechanisms of parkin in Parkinson's disease
    • Hattori N, Mizuno Y. 2004. Pathogenetic mechanisms of parkin in Parkinson's disease. Lancet 364:722-724.
    • (2004) Lancet , vol.364 , pp. 722-724
    • Hattori, N.1    Mizuno, Y.2
  • 31
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A, et al. 1997. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276:2045-2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 32
    • 0037131567 scopus 로고    scopus 로고
    • The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degrada-tion and Parkinson's disease susceptibility
    • Liu Y, Fallon L, Lashuel HA, Liu Z, Lansbury PT Jr. 2002. The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degrada-tion and Parkinson's disease susceptibility. Cell 111:209-218.
    • (2002) Cell , vol.111 , pp. 209-218
    • Liu, Y.1    Fallon, L.2    Lashuel, H.A.3    Liu, Z.4    Lansbury Jr., P.T.5
  • 33
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, et al. 1998. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392:605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5
  • 34
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene
    • Lücking CB, Dürr A, Bonifati V, Vaughan J, De Michele G, et al. 2000. Association between early-onset Parkinson's disease and mutations in the parkin gene. N Engl J Med 342:1560-1567.
    • (2000) N Engl J Med , vol.342 , pp. 1560-1567
    • Lücking, C.B.1    Dürr, A.2    Bonifati, V.3    Vaughan, J.4    De Michele, G.5
  • 35
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati V, Rizzu P, van Baren MJ, Schaap O, Breedveld GJ, et al. 2003. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299:256-259.
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    van Baren, M.J.3    Schaap, O.4    Breedveld, G.J.5
  • 36
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente EM, Abou-Sleiman PM, Caputo V, Muqit MM, Harvey K, et al. 2004. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304:1158-1160.
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5
  • 37
    • 0033788434 scopus 로고    scopus 로고
    • Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex
    • Ghee M, et al. 2000. Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex. J Neurochem 75:2221-2224.
    • (2000) J Neurochem , vol.75 , pp. 2221-2224
    • Ghee, M.1
  • 38
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam YA, et al. 2002. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal. Nature 416:763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1
  • 39
    • 2242472974 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions
    • Hasegawa M, et al. 2002. Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions. J Biol Chem 277:49071-49076.
    • (2002) J Biol Chem , vol.277 , pp. 49071-49076
    • Hasegawa, M.1
  • 40
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli L, et al. 2002. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 36:1007-1019.
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1
  • 41
    • 0141704202 scopus 로고    scopus 로고
    • L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system
    • Miller DW, et al. 2003. L166P mutant DJ-1, causative for recessive Parkinson's disease, is degraded through the ubiquitin-proteasome system. J Biol Chem 278:36588-36595.
    • (2003) J Biol Chem , vol.278 , pp. 36588-36595
    • Miller, D.W.1
  • 42
    • 0142139305 scopus 로고    scopus 로고
    • Role for the ubiquitin-proteasome system in Parkinson's disease and other neurodegenerative brain amyloidoses
    • Moore DJ, et al. 2003. Role for the ubiquitin-proteasome system in Parkinson's disease and other neurodegenerative brain amyloidoses. Neuromolecular Med 4:95-108.
    • (2003) Neuromolecular Med , vol.4 , pp. 95-108
    • Moore, D.J.1
  • 43
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung KK, et al. 2001. Parkin ubiquitinates the alpha-synuclein interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7:1144-1150.
    • (2001) Nat Med , vol.7 , pp. 1144-1150
    • Chung, K.K.1
  • 44
    • 0034085796 scopus 로고    scopus 로고
    • Synphilin-1 is present in Lewy bodies in Parkinson's disease
    • Wakabayashi K, et al. 2000. Synphilin-1 is present in Lewy bodies in Parkinson's disease. Ann Neurol 47:521-523.
    • (2000) Ann Neurol , vol.47 , pp. 521-523
    • Wakabayashi, K.1
  • 46
    • 34247390079 scopus 로고    scopus 로고
    • Polyglutamine Mediated Neurodegeneration: Use of Chaperones as Prevention Strategy
    • Paul S. 2007. Polyglutamine Mediated Neurodegeneration: Use of Chaperones as Prevention Strategy. Biochemistry (Moscow) 72:359-366.
    • (2007) Biochemistry (Moscow) , vol.72 , pp. 359-366
    • Paul, S.1
  • 47
    • 0034043493 scopus 로고    scopus 로고
    • Triplet repeat expansion in neuromuscular disease
    • Lieberman AP, Fischbeck KH. 2000. Triplet repeat expansion in neuromuscular disease. Muscle Nerve 23:843-850.
    • (2000) Muscle Nerve , vol.23 , pp. 843-850
    • Lieberman, A.P.1    Fischbeck, K.H.2
  • 48
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • Ross CA. 2002. Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders, Neuron 35:819-822.
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 49
    • 0038521282 scopus 로고    scopus 로고
    • Polyglutamines placed into context
    • La Spada AR, Taylor JP. 2003. Polyglutamines placed into context. Neuron 38:681-684.
    • (2003) Neuron , vol.38 , pp. 681-684
    • La Spada, A.R.1    Taylor, J.P.2
  • 50
    • 9444239187 scopus 로고    scopus 로고
    • Huntingtin is ubiquitinated and interacts with a specific ubiquitinconjugating enzyme
    • Kalchman MA, Graham RK, Xia G, Koide HB, et al. 1996. Huntingtin is ubiquitinated and interacts with a specific ubiquitinconjugating enzyme. J Biol Chem 271:19385-19394.
    • (1996) J Biol Chem , vol.271 , pp. 19385-19394
    • Kalchman, M.A.1    Graham, R.K.2    Xia, G.3    Koide, H.B.4
  • 51
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA mice
    • Cummings CJ, Reinstein E, Sun Y, Antalffy B, Jiang Y, et al. 1999. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA mice. Neuron 4:879-892.
    • (1999) Neuron , vol.4 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5
  • 53
    • 34247185404 scopus 로고    scopus 로고
    • Disease-associated prion protein oligomers inhibit the 26S proteasome
    • Kristiansen M, Deriziotis P, Dimcheff DE, et al. 2007. Disease-associated prion protein oligomers inhibit the 26S proteasome. Mol Cell 26:175-188.
    • (2007) Mol Cell , vol.26 , pp. 175-188
    • Kristiansen, M.1    Deriziotis, P.2    Dimcheff, D.E.3
  • 54
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen DR, Siddique T, Patterson D, Figlewicz DA, Sapp P, et al. 1993. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362:59-62.
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1    Siddique, T.2    Patterson, D.3    Figlewicz, D.A.4    Sapp, P.5
  • 55
    • 0031012849 scopus 로고    scopus 로고
    • UBE3A/E6-AP mutations cause Angelman syndrome
    • Kishino T, Lalande M, Wagstaff J. 1997. UBE3A/E6-AP mutations cause Angelman syndrome. Nat Genet 15:70-73.
    • (1997) Nat Genet , vol.15 , pp. 70-73
    • Kishino, T.1    Lalande, M.2    Wagstaff, J.3
  • 56
  • 57
    • 0030879482 scopus 로고    scopus 로고
    • Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons
    • Albrecht U, Sutcliffe JS, Cattanach BM, Beechey CV, Armstrong D, et al. 1997. Imprinted expression of the murine Angelman syndrome gene, Ube3a, in hippocampal and Purkinje neurons. Nat Genet 17:75-78.
    • (1997) Nat Genet , vol.17 , pp. 75-78
    • Albrecht, U.1    Sutcliffe, J.S.2    Cattanach, B.M.3    Beechey, C.V.4    Armstrong, D.5
  • 58
    • 0027946089 scopus 로고
    • Liddle's syndrome: Heritable human hypertension caused by mutations in the beta subunit of the epithelial sodium channel
    • Shimkets RA, Warnock DG, Bositis CM, Nelson-Williams C, Hansson JH, et al. 1994. Liddle's syndrome: heritable human hypertension caused by mutations in the beta subunit of the epithelial sodium channel. Cell 79:407-414.
    • (1994) Cell , vol.79 , pp. 407-414
    • Shimkets, R.A.1    Warnock, D.G.2    Bositis, C.M.3    Nelson-Williams, C.4    Hansson, J.H.5
  • 59
    • 0030731428 scopus 로고    scopus 로고
    • Regulation of stability and function of the epithelial Na± channel (ENaC) by ubiquitination
    • Staub O, Gautschi I, Ishikawa T, Breitschopf K, Ciechanover A, et al. 1997. Regulation of stability and function of the epithelial Na± channel (ENaC) by ubiquitination. EMBO J 16:6325-6336.
    • (1997) EMBO J , vol.16 , pp. 6325-6336
    • Staub, O.1    Gautschi, I.2    Ishikawa, T.3    Breitschopf, K.4    Ciechanover, A.5
  • 60
    • 0032957204 scopus 로고    scopus 로고
    • Biosynthesis and degradation of CFTR
    • Kopito RR. 1999. Biosynthesis and degradation of CFTR. Physiol Rev 79:S167-S173.
    • (1999) Physiol Rev , vol.79
    • Kopito, R.R.1
  • 61
    • 33747752509 scopus 로고    scopus 로고
    • Wilson's disease: An update. Nature Clinical Practice
    • Das SK, Ray K. 2006. Wilson's disease: an update. Nature Clinical Practice Neurology 2:482-493.
    • (2006) Neurology , vol.2 , pp. 482-493
    • Das, S.K.1    Ray, K.2
  • 63
    • 33645531744 scopus 로고    scopus 로고
    • Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation
    • Venuprasad K, Elly C, Gao M, et al. 2006. Convergence of Itch-induced ubiquitination with MEKK1-JNK signaling in Th2 tolerance and airway inflammation. J Clin Invest 116:1117-1126.
    • (2006) J Clin Invest , vol.116 , pp. 1117-1126
    • Venuprasad, K.1    Elly, C.2    Gao, M.3
  • 65
    • 0037076672 scopus 로고    scopus 로고
    • Autoubiquitination of the BRCA1-BARD1 RING ubiquitin ligase
    • Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ. 2002. Autoubiquitination of the BRCA1-BARD1 RING ubiquitin ligase. J Biol Chem 277:22085-22092.
    • (2002) J Biol Chem , vol.277 , pp. 22085-22092
    • Chen, A.1    Kleiman, F.E.2    Manley, J.L.3    Ouchi, T.4    Pan, Z.Q.5
  • 66
    • 0035805582 scopus 로고    scopus 로고
    • The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation
    • Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, et al. 2001. The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. J Biol Chem 276:14537-14540.
    • (2001) J Biol Chem , vol.276 , pp. 14537-14540
    • Hashizume, R.1    Fukuda, M.2    Maeda, I.3    Nishikawa, H.4    Oyake, D.5
  • 67
    • 0026630266 scopus 로고
    • APC mutations occur early during colorectal tumorigenesis
    • Powell SM, Zilz N, Beazer-Barclay Y, et al. 1992. APC mutations occur early during colorectal tumorigenesis. Nature 359:235-237.
    • (1992) Nature , vol.359 , pp. 235-237
    • Powell, S.M.1    Zilz, N.2    Beazer-Barclay, Y.3
  • 68
    • 0028987249 scopus 로고
    • Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • Munemitsu S, Albert I, Souza B, et al. 1995. Regulation of intracellular beta-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein. Proc Natl Acad Sci USA 92:3046-3050.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3046-3050
    • Munemitsu, S.1    Albert, I.2    Souza, B.3
  • 69
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • Werness BA, Levine AJ, Howley PM. 1990. Association of human papillomavirus types 16 and 18 E6 proteins with p53. Science 248:76-79.
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.A.1    Levine, A.J.2    Howley, P.M.3
  • 70
    • 0024809865 scopus 로고
    • Complex formation of human papillomavirus E7 proteins with the retinoblastoma tumor suppressor gene product
    • Munger K, Werness BA, Dyson N, et al. 1989. Complex formation of human papillomavirus E7 proteins with the retinoblastoma tumor suppressor gene product. Embo J 8:4099-4105.
    • (1989) Embo J , vol.8 , pp. 4099-4105
    • Munger, K.1    Werness, B.A.2    Dyson, N.3
  • 71
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M, Huibregtse JM, Vierstra RD, et al. 1993. The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75:495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3
  • 72
    • 8944239884 scopus 로고    scopus 로고
    • High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradation
    • Li X, Coffino P. 1996. High-risk human papillomavirus E6 protein has two distinct binding sites within p53, of which only one determines degradation. J Virol 70:4509-4516.
    • (1996) J Virol , vol.70 , pp. 4509-4516
    • Li, X.1    Coffino, P.2
  • 74
    • 0037236457 scopus 로고    scopus 로고
    • The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites" of the endocytosis pathway]
    • Benichou S, Benmerah A. 2003. The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites" of the endocytosis pathway]. Med Sci (Paris) 19:100-106.
    • (2003) Med Sci (Paris) , vol.19 , pp. 100-106
    • Benichou, S.1    Benmerah, A.2
  • 75
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • Coscoy L, Sanchez DJ, Ganem D. 2001. A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 155:1265-1273.
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 76
    • 0037155246 scopus 로고    scopus 로고
    • Functional organization of MIR2, a novel viral regulator of selective endocytosis
    • Sanchez DJ, Coscoy L, Ganem D. 2002. Functional organization of MIR2, a novel viral regulator of selective endocytosis. J Biol Chem 277:6124-6130.
    • (2002) J Biol Chem , vol.277 , pp. 6124-6130
    • Sanchez, D.J.1    Coscoy, L.2    Ganem, D.3
  • 77
    • 0037093467 scopus 로고    scopus 로고
    • Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation
    • Hewitt EW, Duncan L, Mufti D, Baker J, Stevenson PG, Lehner PJ. 2002. Ubiquitylation of MHC class I by the K3 viral protein signals internalization and TSG101-dependent degradation. Embo J 21:2418-2429.
    • (2002) Embo J , vol.21 , pp. 2418-2429
    • Hewitt, E.W.1    Duncan, L.2    Mufti, D.3    Baker, J.4    Stevenson, P.G.5    Lehner, P.J.6
  • 78
    • 12444275739 scopus 로고    scopus 로고
    • The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteosome-mediated degradation
    • Yu Y, Wang SE, Hayward GS. 2005. The KSHV immediate-early transcription factor RTA encodes ubiquitin E3 ligase activity that targets IRF7 for proteosome-mediated degradation. Immunity 22:59-70.
    • (2005) Immunity , vol.22 , pp. 59-70
    • Yu, Y.1    Wang, S.E.2    Hayward, G.S.3
  • 79
    • 38449084670 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in renal cell carcinoma
    • Corn PG. 2007. Role of the ubiquitin proteasome system in renal cell carcinoma. BMC Biochem 8: S4.
    • (2007) BMC Biochem , vol.8
    • Corn, P.G.1
  • 80
    • 0030962262 scopus 로고    scopus 로고
    • P53-dependent induction of apoptosis by proteasome inhibitors
    • Lopes UG, Erhardt P, Yao R, Cooper GM. 1997. P53-dependent induction of apoptosis by proteasome inhibitors. J Biol Chem 272: 12893-12896.
    • (1997) J Biol Chem , vol.272 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 81
    • 0035328584 scopus 로고    scopus 로고
    • Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS- 341: Implications for systemic nuclear factor-kappaB inhibition
    • Cusack JC Jr, Liu R, Houston M, Abendroth K, Elliott PJ, et al. 2001. Enhanced chemosensitivity to CPT-11 with proteasome inhibitor PS- 341: implications for systemic nuclear factor-kappaB inhibition. Cancer Res 61:3535-3540.
    • (2001) Cancer Res , vol.61 , pp. 3535-3540
    • Cusack Jr, J.C.1    Liu, R.2    Houston, M.3    Abendroth, K.4    Elliott, P.J.5
  • 83
    • 20344366589 scopus 로고    scopus 로고
    • Small-molecule inhibitors of proteasome activity
    • Gaczynska M, Osmulski PA. 2005. Small-molecule inhibitors of proteasome activity. Methods Mol Biol 301:3-22.
    • (2005) Methods Mol Biol , vol.301 , pp. 3-22
    • Gaczynska, M.1    Osmulski, P.A.2
  • 84
    • 33645961605 scopus 로고    scopus 로고
    • Natural products inhibiting the ubiquitin-proteasome proteolytic pathway, a target for drug development
    • Tsukamoto S, Yokosawa H. 2006. Natural products inhibiting the ubiquitin-proteasome proteolytic pathway, a target for drug development. Curr Med Chem 13:745-754.
    • (2006) Curr Med Chem , vol.13 , pp. 745-754
    • Tsukamoto, S.1    Yokosawa, H.2
  • 85
    • 33646841837 scopus 로고    scopus 로고
    • Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate
    • Kisselev AF, Callard A, Goldberg AL. 2006. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J Biol Chem 281:8582-8590.
    • (2006) J Biol Chem , vol.281 , pp. 8582-8590
    • Kisselev, A.F.1    Callard, A.2    Goldberg, A.L.3
  • 86
    • 29244454269 scopus 로고    scopus 로고
    • Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis
    • Nawrocki ST, Carew JS, Pino MS, et al. 2005. Bortezomib sensitizes pancreatic cancer cells to endoplasmic reticulum stress-mediated apoptosis. Cancer Res 65:11658-11666.
    • (2005) Cancer Res , vol.65 , pp. 11658-11666
    • Nawrocki, S.T.1    Carew, J.S.2    Pino, M.S.3
  • 87
    • 3442882798 scopus 로고    scopus 로고
    • Bortezomib as a potential treatment for prostate cancer
    • Papandreou CN, Logothetis CJ. 2004. Bortezomib as a potential treatment for prostate cancer. Cancer Res 64:5036-5043.
    • (2004) Cancer Res , vol.64 , pp. 5036-5043
    • Papandreou, C.N.1    Logothetis, C.J.2
  • 88
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. 2004. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 4:349-360.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 89
    • 0012433771 scopus 로고    scopus 로고
    • Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts
    • Nawrocki ST, Bruns CJ, Harbison MT, Bold RJ, Gotsch BS, et al. 2002. Effects of the proteasome inhibitor PS-341 on apoptosis and angiogenesis in orthotopic human pancreatic tumor xenografts. Mol Cancer Ther 1:1243-1253.
    • (2002) Mol Cancer Ther , vol.1 , pp. 1243-1253
    • Nawrocki, S.T.1    Bruns, C.J.2    Harbison, M.T.3    Bold, R.J.4    Gotsch, B.S.5
  • 90
    • 33749243499 scopus 로고    scopus 로고
    • Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells
    • Yang W, Monroe J, Zhang Y, George D, Bremer E, Li H. 2006. Proteasome inhibition induces both pro- and anti-cell death pathways in prostate cancer cells. Cancer Lett 243:217-227.
    • (2006) Cancer Lett , vol.243 , pp. 217-227
    • Yang, W.1    Monroe, J.2    Zhang, Y.3    George, D.4    Bremer, E.5    Li, H.6
  • 91
    • 38749133727 scopus 로고    scopus 로고
    • Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis
    • Thorpe JA, Christian PA, Schwarze SR. 2008. Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis. Prostate 68:200-209.
    • (2008) Prostate , vol.68 , pp. 200-209
    • Thorpe, J.A.1    Christian, P.A.2    Schwarze, S.R.3
  • 93
    • 1642486367 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces growth arrest and apoptosis of non-small cell lung cancer cells via the JNK/c-Jun/AP-1 signaling
    • Yang Y, Ikezoe T, Saito T, Kobayashi M, Koeffler HP, Taguchi H. 2004. Proteasome inhibitor PS-341 induces growth arrest and apoptosis of non-small cell lung cancer cells via the JNK/c-Jun/AP-1 signaling. Cancer Sci 95:176-180.
    • (2004) Cancer Sci , vol.95 , pp. 176-180
    • Yang, Y.1    Ikezoe, T.2    Saito, T.3    Kobayashi, M.4    Koeffler, H.P.5    Taguchi, H.6
  • 94
    • 3042673073 scopus 로고    scopus 로고
    • The Potential Role of Proteasome Inhibitors in the Treatment of Lung Cancer
    • Bunn PA Jr. 2004. The Potential Role of Proteasome Inhibitors in the Treatment of Lung Cancer. Clinical Cancer Research 10:4263S-4265S.
    • (2004) Clinical Cancer Research , vol.10
    • Bunn Jr., P.A.1
  • 95
    • 37549034694 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib in combination with gemcitabine and carboplatin in advanced non-small cell lung cancer: A California Cancer Consortium Phase I study
    • Davies AM, Ruel C, Lara PN, Lau DH, Gumerlock PH, et al. 2008. The proteasome inhibitor bortezomib in combination with gemcitabine and carboplatin in advanced non-small cell lung cancer: a California Cancer Consortium Phase I study. J Thorac Oncol 3: 68-74.
    • (2008) J Thorac Oncol , vol.3 , pp. 68-74
    • Davies, A.M.1    Ruel, C.2    Lara, P.N.3    Lau, D.H.4    Gumerlock, P.H.5
  • 96
    • 0034981649 scopus 로고    scopus 로고
    • 26S proteasome inhibition induces apoptosis and limits growth of human pancreatic cancer
    • Shah SA, Potter MW, McDade TP, Ricciardi R, Perugini RA, et al. 2001. 26S proteasome inhibition induces apoptosis and limits growth of human pancreatic cancer. J Cell Biochem 82:110-122.
    • (2001) J Cell Biochem , vol.82 , pp. 110-122
    • Shah, S.A.1    Potter, M.W.2    McDade, T.P.3    Ricciardi, R.4    Perugini, R.A.5
  • 98
    • 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, Podar K, Hideshima T, et al. 2005. A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from Bortezomib. Cancer Cell 8:407-419.
    • (2005) Cancer Cell , vol.8 , pp. 407-419
    • Chauhan, D.1    Catley, L.2    Li, G.3    Podar, K.4    Hideshima, T.5
  • 99
    • 34250194653 scopus 로고    scopus 로고
    • A phase I/II study of arsenic trioxide/bortezomib/ascorbic acid combination therapy for the treatment of relapsed or refractory multiple myeloma
    • Berenson JR, Matous J, Swift RA, Mapes R, Morrison B, Yeh HS. 2007. A phase I/II study of arsenic trioxide/bortezomib/ascorbic acid combination therapy for the treatment of relapsed or refractory multiple myeloma. Clin Cancer Res 13:1762-1768.
    • (2007) Clin Cancer Res , vol.13 , pp. 1762-1768
    • Berenson, J.R.1    Matous, J.2    Swift, R.A.3    Mapes, R.4    Morrison, B.5    Yeh, H.S.6
  • 100
    • 33847410207 scopus 로고    scopus 로고
    • The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells
    • Stapnes C, Døskeland AP, Hatfield K, Ersvaer E, Ryningen A, et al. 2007. The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells. Br J Haematol 136:814-828.
    • (2007) Br J Haematol , vol.136 , pp. 814-828
    • Stapnes, C.1    Døskeland, A.P.2    Hatfield, K.3    Ersvaer, E.4    Ryningen, A.5
  • 102
    • 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 61:3071-3076.
    • (2001) Cancer Res , vol.61 , pp. 3071-3076
    • Hideshima, T.1    Richardson, P.2    Chauhan, D.3
  • 103
    • 33747443493 scopus 로고    scopus 로고
    • Effect of Bortezomib on Human Neuroblastoma Cell Growth, Apoptosis, and Angiogenesis
    • Brignole C, Marimpietri D, Pastorino F, Nico B, Di Paolo D, et al. 2006. Effect of Bortezomib on Human Neuroblastoma Cell Growth, Apoptosis, and Angiogenesis. J Natl Cancer Inst 98:1142-1157.
    • (2006) J Natl Cancer Inst , vol.98 , pp. 1142-1157
    • Brignole, C.1    Marimpietri, D.2    Pastorino, F.3    Nico, B.4    Di Paolo, D.5
  • 104
    • 34547582308 scopus 로고    scopus 로고
    • Bortezomib inhibits angiogenesis and reduces tumor burden in a murine model of neuroblastoma
    • Hamner JB, Dickson PV, Sims TL, Zhou J, Spence Y, et al. 2007. Bortezomib inhibits angiogenesis and reduces tumor burden in a murine model of neuroblastoma. Surgery 142:185-191.
    • (2007) Surgery , vol.142 , pp. 185-191
    • Hamner, J.B.1    Dickson, P.V.2    Sims, T.L.3    Zhou, J.4    Spence, Y.5
  • 105
    • 9744278199 scopus 로고    scopus 로고
    • Proteasome inhibitors suppres formation of polyglutamine-induced nuclear inclusions in cultured postmitotic neurons
    • Kim WY, Horbinski C, Sigurdson W, Higgins D. 2004. Proteasome inhibitors suppres formation of polyglutamine-induced nuclear inclusions in cultured postmitotic neurons. J Neurochem 91:1044-1056.
    • (2004) J Neurochem , vol.91 , pp. 1044-1056
    • Kim, W.Y.1    Horbinski, C.2    Sigurdson, W.3    Higgins, D.4
  • 106
    • 15744392692 scopus 로고    scopus 로고
    • Proteasome inhibitors protect against degeneration of nigral dopaminergic neurons in hemiparkinsonian rats
    • Inden M, Kondo JI, Kitamura Y, Takata K, Nishimura K, Taniguchi T, et al. 2005. Proteasome inhibitors protect against degeneration of nigral dopaminergic neurons in hemiparkinsonian rats. J Pharmacol Sci 97:203-211.
    • (2005) J Pharmacol Sci , vol.97 , pp. 203-211
    • Inden, M.1    Kondo, J.I.2    Kitamura, Y.3    Takata, K.4    Nishimura, K.5    Taniguchi, T.6
  • 107
    • 0031950118 scopus 로고    scopus 로고
    • Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and potentiate A beta 42 recovery from human cells
    • Marambaud P, Ancolio K, Lopez-Perez E, Checler F. 1998. Proteasome inhibitors prevent the degradation of familial Alzheimer's disease-linked presenilin 1 and potentiate A beta 42 recovery from human cells. Mol Med 14:147-157.
    • (1998) Mol Med , vol.14 , pp. 147-157
    • Marambaud, P.1    Ancolio, K.2    Lopez-Perez, E.3    Checler, F.4
  • 109
    • 2642670312 scopus 로고    scopus 로고
    • Antiviral activity of the proteasome on incoming human immunodeficiency virus type 1
    • Schwartz O, Maréchal V, Friguet B, et al. 1998. Antiviral activity of the proteasome on incoming human immunodeficiency virus type 1. J Virol 72:3845-3850.
    • (1998) J Virol , vol.72 , pp. 3845-3850
    • Schwartz, O.1    Maréchal, V.2    Friguet, B.3


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