메뉴 건너뛰기




Volumn 5, Issue 14, 2006, Pages 1477-1480

New directions for neurodegenerative disease therapy: Using chemical compounds to boost the formation of mutant protein inclusions

Author keywords

Aggregation; Huntington's disease; Inclusion body; Misfolded protein; Neurodegenerative diseases; Parkinson's disease

Indexed keywords

5 [4 (4 CHLOROBENZOYL) 1 PIPERAZINYL] 8 NITROQUINOLINE; ALPHA SYNUCLEIN; CHEMICAL COMPOUND; HUNTINGTIN; MUTANT PROTEIN; NITROQUINOLINE DERIVATIVE; POLYGLUTAMINE; UNCLASSIFIED DRUG;

EID: 33746265074     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.5.14.2929     Document Type: Review
Times cited : (28)

References (43)
  • 1
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol Rev 2002; 82:373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 2
    • 23144443884 scopus 로고    scopus 로고
    • Protein quality control: Chaperones culling corrupt conformations
    • McClellan AJ, Tam S, Kaganovich D, Frydman J. Protein quality control: Chaperones culling corrupt conformations. Nat Cell Biol 2005; 7:736-41.
    • (2005) Nat Cell Biol , vol.7 , pp. 736-741
    • McClellan, A.J.1    Tam, S.2    Kaganovich, D.3    Frydman, J.4
  • 5
    • 0142186172 scopus 로고    scopus 로고
    • Aging and molecular chaperones
    • Soti C, Csermely P. Aging and molecular chaperones. Exp Gerontol 2003; 38:1037-40.
    • (2003) Exp Gerontol , vol.38 , pp. 1037-1040
    • Soti, C.1    Csermely, P.2
  • 6
    • 27644596641 scopus 로고    scopus 로고
    • Opinion: What is the role of protein aggregation in neurodegeneration?
    • Ross CA, Poirier MA. Opinion: What is the role of protein aggregation in neurodegeneration? Nat Rev Mol Cell Biol 2005; 6:891-8.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 891-898
    • Ross, C.A.1    Poirier, M.A.2
  • 7
    • 0031918640 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length
    • Becher MW, Kotzuk JA, Sharp AH, Davies SW, Bates GP, Price DL, Ross CA. Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length. Neurobiol Dis 1998; 4:387-97.
    • (1998) Neurobiol Dis , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3    Davies, S.W.4    Bates, G.P.5    Price, D.L.6    Ross, C.A.7
  • 9
  • 11
    • 0033391428 scopus 로고    scopus 로고
    • Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice
    • Cummings CJ, Reinstein E, Sun Y, Antalffy B, Jiang Y, Ciechanover A, Orr HT, Beaudet AL, Zoghbi HY. Mutation of the E6-AP ubiquitin ligase reduces nuclear inclusion frequency while accelerating polyglutamine-induced pathology in SCA1 mice. Neuron 1999; 24:879-92.
    • (1999) Neuron , vol.24 , pp. 879-892
    • Cummings, C.J.1    Reinstein, E.2    Sun, Y.3    Antalffy, B.4    Jiang, Y.5    Ciechanover, A.6    Orr, H.T.7    Beaudet, A.L.8    Zoghbi, H.Y.9
  • 13
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement IA, Skinner PJ, Kaytor MD, Yi H, Hersch SM, Clark HB, Zoghbi HY, Orr HT. Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice. Cell 1998; 95:41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 15
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 1998; 95:55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 19
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004; 431:805-10.
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 21
    • 4344583898 scopus 로고    scopus 로고
    • Involvement of macroautophagy in the dissolution of neuronal inclusions
    • Rideout HJ, Lang-Rollin I, Stefanis L. Involvement of macroautophagy in the dissolution of neuronal inclusions. Int J Biochem Cell Biol 2004; 36:2551-62.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2551-2562
    • Rideout, H.J.1    Lang-Rollin, I.2    Stefanis, L.3
  • 26
    • 0034612220 scopus 로고    scopus 로고
    • Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy
    • USA
    • Heiser V, Scherzinger E, Boeddrich A, Nordhoff E, Lurz R, Schugardt N, Lehrach H, Wanker EE. Inhibition of huntingtin fibrillogenesis by specific antibodies and small molecules: Implications for Huntington's disease therapy. Proc Natl Acad Sci USA 2000; 97:6739-44.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 6739-6744
    • Heiser, V.1    Scherzinger, E.2    Boeddrich, A.3    Nordhoff, E.4    Lurz, R.5    Schugardt, N.6    Lehrach, H.7    Wanker, E.E.8
  • 28
    • 12944335007 scopus 로고    scopus 로고
    • Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation
    • Wang J, Gines S, MacDonald ME, Gusella JF. Reversal of a full-length mutant huntingtin neuronal cell phenotype by chemical inhibitors of polyglutamine-mediated aggregation. BMC Neurosci 2005; 6:1.
    • (2005) BMC Neurosci , vol.6 , pp. 1
    • Wang, J.1    Gines, S.2    MacDonald, M.E.3    Gusella, J.F.4
  • 30
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004; 10:S10-7.
    • (2004) Nat Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 32
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001; 292:1552-5.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 33
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett EJ, Bence NF, Jayakumar R, Kopito RR. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 2005; 17:351-65.
    • (2005) Mol Cell , vol.17 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 35
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana NR, Zemskov EA, Wang G, Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum Mol Genet 2001; 10:1049-59.
    • (2001) Hum Mol Genet , vol.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 36
    • 1842766144 scopus 로고    scopus 로고
    • Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins
    • Venkatraman P, Wetzel R, Tanaka M, Nukina N, Goldberg AL. Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 2004; 14:95-104.
    • (2004) Mol Cell , vol.14 , pp. 95-104
    • Venkatraman, P.1    Wetzel, R.2    Tanaka, M.3    Nukina, N.4    Goldberg, A.L.5
  • 37
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef LG, Lindsten K, Masucci MG, Dantuma NP. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum Mol Genet 2002; 11:2689-700.
    • (2002) Hum Mol Genet , vol.11 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 38
    • 3142604036 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases
    • Ross CA, Pickart CM. The ubiquitin-proteasome pathway in Parkinson's disease and other neurodegenerative diseases. Trends Cell Biol 2004; 14:703-11.
    • (2004) Trends Cell Biol , vol.14 , pp. 703-711
    • Ross, C.A.1    Pickart, C.M.2
  • 39
    • 0032525130 scopus 로고    scopus 로고
    • Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
    • Gilon T, Chomsky O, Kulka RG. Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae. EMBO J 1998; 17:2759-66.
    • (1998) EMBO J , vol.17 , pp. 2759-2766
    • Gilon, T.1    Chomsky, O.2    Kulka, R.G.3
  • 41
    • 0035859226 scopus 로고    scopus 로고
    • α-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
    • McLean PJ, Kawamata H, Hyman BT. α-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons. Neuroscience 2001; 104:901-12.
    • (2001) Neuroscience , vol.104 , pp. 901-912
    • McLean, P.J.1    Kawamata, H.2    Hyman, B.T.3
  • 43
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • Muchowski PJ, Wacker JL. Modulation of neurodegeneration by molecular chaperones. Nat Rev Neurosci 2005; 6:11-22.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.